Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 06:00, 19 November 2007 (UTC)
[edit]Proteins without matches (12)
[edit]Proteins with a High Potential Match (6)
[edit]Redirected Proteins (7)
[edit]Manual Inspection (Page not found) (18)
[edit]
Protein Status Grid - Date: 06:00, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 06:00, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on ALAD... {November 18, 2007 9:35:48 PM PST}
- SEARCH REDIRECT: Control Box Found: ALAD {November 18, 2007 9:36:27 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:36:28 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:36:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:36:28 PM PST}
- UPDATED: Updated protein page: ALAD {November 18, 2007 9:36:34 PM PST}
- INFO: Beginning work on APRT... {November 18, 2007 9:36:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:37:07 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_APRT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ore.
| PDB = {{PDB2|1ore}}, {{PDB2|1zn7}}, {{PDB2|1zn8}}, {{PDB2|1zn9}}
| Name = Adenine phosphoribosyltransferase
| HGNCid = 626
| Symbol = APRT
| AltSymbols =; AMP; DKFZp686D13177; MGC125856; MGC125857; MGC129961
| OMIM = 102600
| ECnumber =
| Homologene = 413
| MGIid = 88061
| GeneAtlas_image1 = PBB_GE_APRT_213892_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_APRT_203219_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003999 |text = adenine phosphoribosyltransferase activity}} {{GNF_GO|id=GO:0016208 |text = AMP binding}} {{GNF_GO|id=GO:0016757 |text = transferase activity, transferring glycosyl groups}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006166 |text = purine ribonucleoside salvage}} {{GNF_GO|id=GO:0006168 |text = adenine salvage}} {{GNF_GO|id=GO:0009116 |text = nucleoside metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 353
| Hs_Ensembl = ENSG00000198931
| Hs_RefseqProtein = NP_000476
| Hs_RefseqmRNA = NM_000485
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 87403378
| Hs_GenLoc_end = 87405843
| Hs_Uniprot = P07741
| Mm_EntrezGene = 11821
| Mm_Ensembl = ENSMUSG00000006589
| Mm_RefseqmRNA = NM_009698
| Mm_RefseqProtein = NP_033828
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 125460727
| Mm_GenLoc_end = 125462950
| Mm_Uniprot = Q564P4
}}
}}
'''Adenine phosphoribosyltransferase''', also known as '''APRT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: APRT adenine phosphoribosyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=353| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Adenine phosphoribosyltransferase belongs to the purine/pyrimidine phosphoribosyltransferase family. A conserved feature of this gene is the distribution of CpG dinucleotides. This enzyme catalyzes the formation of AMP and inorganic pyrophosphate from adenine and 5-phosphoribosyl-1-pyrophosphate (PRPP). It also produces adenine as a by-product of the polyamine biosynthesis pathway. A homozygous deficiency in this enzyme causes 2,8-dihydroxyadenine urolithiasis. Two transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: APRT adenine phosphoribosyltransferase| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=353| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Tischfield JA, Engle SJ, Gupta PK, ''et al.'' |title=Germline and somatic mutation at the APRT locus of mice and man. |journal=Adv. Exp. Med. Biol. |volume=370 |issue= |pages= 661-4 |year= 1995 |pmid= 7660991 |doi= }}
*{{cite journal | author=Takeuchi H, Kaneko Y, Fujita J, Yoshida O |title=A case of a compound heterozygote for adenine phosphoribosyltransferase deficiency (APRT*J/APRT*Q0) leading to 2,8-dihydroxyadenine urolithiasis: review of the reported cases with 2,8-dihydroxyadenine stones in Japan. |journal=J. Urol. |volume=149 |issue= 4 |pages= 824-6 |year= 1993 |pmid= 8455250 |doi= }}
*{{cite journal | author=Ludwig H, Kuzmits R, Pietschmann H, Müller MM |title=Enzymes of the purine interconversion system in chronic lymphatic leukemia: decreased purine nucleoside phosphorylase and adenosine deaminase activity. |journal=Blut |volume=39 |issue= 5 |pages= 309-15 |year= 1980 |pmid= 116697 |doi= }}
*{{cite journal | author=Johnson LA, Gordon RB, Emmerson BT |title=Adenine phosphoribosyltransferase: a simple spectrophotometric assay and the incidence of mutation in the normal population. |journal=Biochem. Genet. |volume=15 |issue= 3-4 |pages= 265-72 |year= 1977 |pmid= 869896 |doi= }}
*{{cite journal | author=Kamatani N, Hakoda M, Otsuka S, ''et al.'' |title=Only three mutations account for almost all defective alleles causing adenine phosphoribosyltransferase deficiency in Japanese patients. |journal=J. Clin. Invest. |volume=90 |issue= 1 |pages= 130-5 |year= 1992 |pmid= 1353080 |doi= }}
*{{cite journal | author=Chen J, Sahota A, Laxdal T, ''et al.'' |title=Identification of a single missense mutation in the adenine phosphoribosyltransferase (APRT) gene from five Icelandic patients and a British patient. |journal=Am. J. Hum. Genet. |volume=49 |issue= 6 |pages= 1306-11 |year= 1992 |pmid= 1746557 |doi= }}
*{{cite journal | author=Mimori A, Hidaka Y, Wu VC, ''et al.'' |title=A mutant allele common to the type I adenine phosphoribosyltransferase deficiency in Japanese subjects. |journal=Am. J. Hum. Genet. |volume=48 |issue= 1 |pages= 103-7 |year= 1991 |pmid= 1985452 |doi= }}
*{{cite journal | author=Chen J, Sahota A, Stambrook PJ, Tischfield JA |title=Polymerase chain reaction amplification and sequence analysis of human mutant adenine phosphoribosyltransferase genes: the nature and frequency of errors caused by Taq DNA polymerase. |journal=Mutat. Res. |volume=249 |issue= 1 |pages= 169-76 |year= 1991 |pmid= 2067530 |doi= }}
*{{cite journal | author=Gathof BS, Sahota A, Gresser U, ''et al.'' |title=Identification of a splice mutation at the adenine phosphoribosyltransferase locus in a German family. |journal=Klin. Wochenschr. |volume=69 |issue= 24 |pages= 1152-5 |year= 1992 |pmid= 2135300 |doi= }}
*{{cite journal | author=Kamatani N, Kuroshima S, Hakoda M, ''et al.'' |title=Crossovers within a short DNA sequence indicate a long evolutionary history of the APRT*J mutation. |journal=Hum. Genet. |volume=85 |issue= 6 |pages= 600-4 |year= 1990 |pmid= 2227951 |doi= }}
*{{cite journal | author=Kamatani N, Kuroshima S, Terai C, ''et al.'' |title=Detection of an amino acid substitution in the mutant enzyme for a special type of adenine phosphoribosyltransferase (APRT) deficiency by sequence-specific protein cleavage. |journal=Am. J. Hum. Genet. |volume=45 |issue= 2 |pages= 325-31 |year= 1989 |pmid= 2502918 |doi= }}
*{{cite journal | author=Hidaka Y, Tarlé SA, Fujimori S, ''et al.'' |title=Human adenine phosphoribosyltransferase deficiency. Demonstration of a single mutant allele common to the Japanese. |journal=J. Clin. Invest. |volume=81 |issue= 3 |pages= 945-50 |year= 1988 |pmid= 3343350 |doi= }}
*{{cite journal | author=Wilson JM, O'Toole TE, Argos P, ''et al.'' |title=Human adenine phosphoribosyltransferase. Complete amino acid sequence of the erythrocyte enzyme. |journal=J. Biol. Chem. |volume=261 |issue= 29 |pages= 13677-83 |year= 1986 |pmid= 3531209 |doi= }}
*{{cite journal | author=Broderick TP, Schaff DA, Bertino AM, ''et al.'' |title=Comparative anatomy of the human APRT gene and enzyme: nucleotide sequence divergence and conservation of a nonrandom CpG dinucleotide arrangement. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 10 |pages= 3349-53 |year= 1987 |pmid= 3554238 |doi= }}
*{{cite journal | author=Hidaka Y, Palella TD, O'Toole TE, ''et al.'' |title=Human adenine phosphoribosyltransferase. Identification of allelic mutations at the nucleotide level as a cause of complete deficiency of the enzyme. |journal=J. Clin. Invest. |volume=80 |issue= 5 |pages= 1409-15 |year= 1987 |pmid= 3680503 |doi= }}
*{{cite journal | author=Hidaka Y, Tarlé SA, O'Toole TE, ''et al.'' |title=Nucleotide sequence of the human APRT gene. |journal=Nucleic Acids Res. |volume=15 |issue= 21 |pages= 9086 |year= 1988 |pmid= 3684585 |doi= }}
*{{cite journal | author=Chen J, Sahota A, Martin GF, ''et al.'' |title=Analysis of germline and in vivo somatic mutations in the human adenine phosphoribosyltransferase gene: mutational hot spots at the intron 4 splice donor site and at codon 87. |journal=Mutat. Res. |volume=287 |issue= 2 |pages= 217-25 |year= 1993 |pmid= 7685481 |doi= }}
*{{cite journal | author=Sahota A, Chen J, Boyadjiev SA, ''et al.'' |title=Missense mutation in the adenine phosphoribosyltransferase gene causing 2,8-dihydroxyadenine urolithiasis. |journal=Hum. Mol. Genet. |volume=3 |issue= 5 |pages= 817-8 |year= 1994 |pmid= 7915931 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CCR6... {November 18, 2007 9:37:07 PM PST}
- SEARCH REDIRECT: Control Box Found: C-C chemokine receptor type 6 {November 18, 2007 9:37:58 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:38:01 PM PST}
- SKIP SUMMARY: SKIPPING Summary, No Errors. {November 18, 2007 9:38:01 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:38:01 PM PST}
- UPDATED: Updated protein page: C-C chemokine receptor type 6 {November 18, 2007 9:38:08 PM PST}
- INFO: Beginning work on COL10A1... {November 18, 2007 9:38:08 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:38:34 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_COL10A1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gr3.
| PDB = {{PDB2|1gr3}}
| Name = Collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)
| HGNCid = 2185
| Symbol = COL10A1
| AltSymbols =;
| OMIM = 120110
| ECnumber =
| Homologene = 55466
| MGIid = 88445
| GeneAtlas_image1 = PBB_GE_COL10A1_217428_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_COL10A1_205941_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005198 |text = structural molecule activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}}
| Component = {{GNF_GO|id=GO:0005581 |text = collagen}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0001501 |text = skeletal development}} {{GNF_GO|id=GO:0006817 |text = phosphate transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1300
| Hs_Ensembl = ENSG00000123500
| Hs_RefseqProtein = NP_000484
| Hs_RefseqmRNA = NM_000493
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 116546791
| Hs_GenLoc_end = 116553989
| Hs_Uniprot = Q03692
| Mm_EntrezGene = 12813
| Mm_Ensembl = ENSMUSG00000039462
| Mm_RefseqmRNA = NM_009925
| Mm_RefseqProtein = NP_034055
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 34079251
| Mm_GenLoc_end = 34087720
| Mm_Uniprot = Q05306
}}
}}
'''Collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)''', also known as '''COL10A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: COL10A1 collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1300| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the alpha chain of type X collagen, a short chain collagen expressed by hypertrophic chondrocytes during endochondral ossification. Unlike type VIII collagen, the other short chain collagen, type X collagen is a homotrimer. Mutations in this gene are associated with Schmid type metaphyseal chondrodysplasia (SMCD) and Japanese type spondylometaphyseal dysplasia (SMD).<ref name="entrez">{{cite web | title = Entrez Gene: COL10A1 collagen, type X, alpha 1(Schmid metaphyseal chondrodysplasia)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1300| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Kuivaniemi H, Tromp G, Prockop DJ |title=Mutations in fibrillar collagens (types I, II, III, and XI), fibril-associated collagen (type IX), and network-forming collagen (type X) cause a spectrum of diseases of bone, cartilage, and blood vessels. |journal=Hum. Mutat. |volume=9 |issue= 4 |pages= 300-15 |year= 1997 |pmid= 9101290 |doi= 10.1002/(SICI)1098-1004(1997)9:4<300::AID-HUMU2>3.0.CO;2-9 }}
*{{cite journal | author=Kirsch T, Pfäffle M |title=Selective binding of anchorin CII (annexin V) to type II and X collagen and to chondrocalcin (C-propeptide of type II collagen). Implications for anchoring function between matrix vesicles and matrix proteins. |journal=FEBS Lett. |volume=310 |issue= 2 |pages= 143-7 |year= 1992 |pmid= 1397263 |doi= }}
*{{cite journal | author=Reichenberger E, Beier F, LuValle P, ''et al.'' |title=Genomic organization and full-length cDNA sequence of human collagen X. |journal=FEBS Lett. |volume=311 |issue= 3 |pages= 305-10 |year= 1992 |pmid= 1397333 |doi= }}
*{{cite journal | author=Apte SS, Seldin MF, Hayashi M, Olsen BR |title=Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gene to chromosome 10. |journal=Eur. J. Biochem. |volume=206 |issue= 1 |pages= 217-24 |year= 1992 |pmid= 1587271 |doi= }}
*{{cite journal | author=Reichenberger E, Aigner T, von der Mark K, ''et al.'' |title=In situ hybridization studies on the expression of type X collagen in fetal human cartilage. |journal=Dev. Biol. |volume=148 |issue= 2 |pages= 562-72 |year= 1992 |pmid= 1743401 |doi= }}
*{{cite journal | author=Thomas JT, Cresswell CJ, Rash B, ''et al.'' |title=The human collagen X gene. Complete primary translated sequence and chromosomal localization. |journal=Biochem. J. |volume=280 ( Pt 3) |issue= |pages= 617-23 |year= 1992 |pmid= 1764025 |doi= }}
*{{cite journal | author=Apte S, Mattei MG, Olsen BR |title=Cloning of human alpha 1(X) collagen DNA and localization of the COL10A1 gene to the q21-q22 region of human chromosome 6. |journal=FEBS Lett. |volume=282 |issue= 2 |pages= 393-6 |year= 1991 |pmid= 2037056 |doi= }}
*{{cite journal | author=Bonaventure J, Chaminade F, Maroteaux P |title=Mutations in three subdomains of the carboxy-terminal region of collagen type X account for most of the Schmid metaphyseal dysplasias. |journal=Hum. Genet. |volume=96 |issue= 1 |pages= 58-64 |year= 1995 |pmid= 7607655 |doi= }}
*{{cite journal | author=McIntosh I, Abbott MH, Francomano CA |title=Concentration of mutations causing Schmid metaphyseal chondrodysplasia in the C-terminal noncollagenous domain of type X collagen. |journal=Hum. Mutat. |volume=5 |issue= 2 |pages= 121-5 |year= 1995 |pmid= 7749409 |doi= 10.1002/humu.1380050204 }}
*{{cite journal | author=Chan D, Cole WG, Rogers JG, Bateman JF |title=Type X collagen multimer assembly in vitro is prevented by a Gly618 to Val mutation in the alpha 1(X) NC1 domain resulting in Schmid metaphyseal chondrodysplasia. |journal=J. Biol. Chem. |volume=270 |issue= 9 |pages= 4558-62 |year= 1995 |pmid= 7876225 |doi= }}
*{{cite journal | author=McIntosh I, Abbott MH, Warman ML, ''et al.'' |title=Additional mutations of type X collagen confirm COL10A1 as the Schmid metaphyseal chondrodysplasia locus. |journal=Hum. Mol. Genet. |volume=3 |issue= 2 |pages= 303-7 |year= 1994 |pmid= 8004099 |doi= }}
*{{cite journal | author=Dharmavaram RM, Elberson MA, Peng M, ''et al.'' |title=Identification of a mutation in type X collagen in a family with Schmid metaphyseal chondrodysplasia. |journal=Hum. Mol. Genet. |volume=3 |issue= 3 |pages= 507-9 |year= 1994 |pmid= 8012364 |doi= }}
*{{cite journal | author=Warman ML, Abbott M, Apte SS, ''et al.'' |title=A type X collagen mutation causes Schmid metaphyseal chondrodysplasia. |journal=Nat. Genet. |volume=5 |issue= 1 |pages= 79-82 |year= 1993 |pmid= 8220429 |doi= 10.1038/ng0993-79 }}
*{{cite journal | author=Wallis GA, Rash B, Sweetman WA, ''et al.'' |title=Amino acid substitutions of conserved residues in the carboxyl-terminal domain of the alpha 1(X) chain of type X collagen occur in two unrelated families with metaphyseal chondrodysplasia type Schmid. |journal=Am. J. Hum. Genet. |volume=54 |issue= 2 |pages= 169-78 |year= 1994 |pmid= 8304336 |doi= }}
*{{cite journal | author=Pokharel RK, Alimsardjono H, Uno K, ''et al.'' |title=A novel mutation substituting tryptophan with arginine in the carboxyl-terminal, non-collagenous domain of collagen X in a case of Schmid metaphyseal chondrodysplasia. |journal=Biochem. Biophys. Res. Commun. |volume=217 |issue= 3 |pages= 1157-62 |year= 1996 |pmid= 8554571 |doi= 10.1006/bbrc.1995.2890 }}
*{{cite journal | author=Wallis GA, Rash B, Sykes B, ''et al.'' |title=Mutations within the gene encoding the alpha 1 (X) chain of type X collagen (COL10A1) cause metaphyseal chondrodysplasia type Schmid but not several other forms of metaphyseal chondrodysplasia. |journal=J. Med. Genet. |volume=33 |issue= 6 |pages= 450-7 |year= 1996 |pmid= 8782043 |doi= }}
*{{cite journal | author=Stratakis CA, Orban Z, Burns AL, ''et al.'' |title=Dideoxyfingerprinting (ddF) analysis of the type X collagen gene (COL10A1) and identification of a novel mutation (S671P) in a kindred with Schmid metaphyseal chondrodysplasia. |journal=Biochem. Mol. Med. |volume=59 |issue= 2 |pages= 112-7 |year= 1997 |pmid= 8986632 |doi= }}
*{{cite journal | author=Beier F, Eerola I, Vuorio E, ''et al.'' |title=Variability in the upstream promoter and intron sequences of the human, mouse and chick type X collagen genes. |journal=Matrix Biol. |volume=15 |issue= 6 |pages= 415-22 |year= 1997 |pmid= 9049979 |doi= }}
*{{cite journal | author=Ikegawa S, Nakamura K, Nagano A, ''et al.'' |title=Mutations in the N-terminal globular domain of the type X collagen gene (COL10A1) in patients with Schmid metaphyseal chondrodysplasia. |journal=Hum. Mutat. |volume=9 |issue= 2 |pages= 131-5 |year= 1997 |pmid= 9067753 |doi= 10.1002/(SICI)1098-1004(1997)9:2<131::AID-HUMU5>3.0.CO;2-C }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CRYGD... {November 18, 2007 9:38:34 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:39:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_CRYGD_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1h4a.
| PDB = {{PDB2|1h4a}}, {{PDB2|1hk0}}, {{PDB2|2g98}}
| Name = Crystallin, gamma D
| HGNCid = 2411
| Symbol = CRYGD
| AltSymbols =; CACA; CCA3; CRYG4; cry-g-D
| OMIM = 123690
| ECnumber =
| Homologene = 36213
| MGIid = 88524
| GeneAtlas_image1 = PBB_GE_CRYGD_207532_at_tn.png
| Function = {{GNF_GO|id=GO:0005212 |text = structural constituent of eye lens}}
| Component =
| Process = {{GNF_GO|id=GO:0001654 |text = eye development}} {{GNF_GO|id=GO:0007601 |text = visual perception}} {{GNF_GO|id=GO:0050896 |text = response to stimulus}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1421
| Hs_Ensembl = ENSG00000118231
| Hs_RefseqProtein = NP_008822
| Hs_RefseqmRNA = NM_006891
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 208694577
| Hs_GenLoc_end = 208697458
| Hs_Uniprot = P07320
| Mm_EntrezGene = 12967
| Mm_Ensembl = ENSMUSG00000067299
| Mm_RefseqmRNA = NM_007776
| Mm_RefseqProtein = NP_031802
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 64996115
| Mm_GenLoc_end = 64997697
| Mm_Uniprot = Q6PGI0
}}
}}
'''Crystallin, gamma D''', also known as '''CRYGD''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CRYGD crystallin, gamma D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1421| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains the transparency and refractive index of the lens. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also considered as a superfamily. Alpha and beta families are further divided into acidic and basic groups. Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.<ref name="entrez">{{cite web | title = Entrez Gene: CRYGD crystallin, gamma D| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1421| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Graw J |title=The crystallins: genes, proteins and diseases. |journal=Biol. Chem. |volume=378 |issue= 11 |pages= 1331-48 |year= 1998 |pmid= 9426193 |doi= }}
*{{cite journal | author=Slingsby C, Clout NJ |title=Structure of the crystallins. |journal=Eye (London, England) |volume=13 ( Pt 3b) |issue= |pages= 395-402 |year= 2000 |pmid= 10627816 |doi= }}
*{{cite journal | author=Brakenhoff RH, Aarts HJ, Reek FH, ''et al.'' |title=Human gamma-crystallin genes. A gene family on its way to extinction. |journal=J. Mol. Biol. |volume=216 |issue= 3 |pages= 519-32 |year= 1991 |pmid= 2258929 |doi= }}
*{{cite journal | author=Shiloh Y, Donlon T, Bruns G, ''et al.'' |title=Assignment of the human gamma-crystallin gene cluster (CRYG) to the long arm of chromosome 2, region q33-36. |journal=Hum. Genet. |volume=73 |issue= 1 |pages= 17-9 |year= 1986 |pmid= 3011643 |doi= }}
*{{cite journal | author=Lubsen NH, Renwick JH, Tsui LC, ''et al.'' |title=A locus for a human hereditary cataract is closely linked to the gamma-crystallin gene family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 2 |pages= 489-92 |year= 1987 |pmid= 3025877 |doi= }}
*{{cite journal | author=Meakin SO, Du RP, Tsui LC, Breitman ML |title=Gamma-crystallins of the human eye lens: expression analysis of five members of the gene family. |journal=Mol. Cell. Biol. |volume=7 |issue= 8 |pages= 2671-9 |year= 1987 |pmid= 3670288 |doi= }}
*{{cite journal | author=Meakin SO, Breitman ML, Tsui LC |title=Structural and evolutionary relationships among five members of the human gamma-crystallin gene family. |journal=Mol. Cell. Biol. |volume=5 |issue= 6 |pages= 1408-14 |year= 1985 |pmid= 4033658 |doi= }}
*{{cite journal | author=Rogaev EI, Rogaeva EA, Korovaitseva GI, ''et al.'' |title=Linkage of polymorphic congenital cataract to the gamma-crystallin gene locus on human chromosome 2q33-35. |journal=Hum. Mol. Genet. |volume=5 |issue= 5 |pages= 699-703 |year= 1997 |pmid= 8733140 |doi= }}
*{{cite journal | author=Andley UP, Mathur S, Griest TA, Petrash JM |title=Cloning, expression, and chaperone-like activity of human alphaA-crystallin. |journal=J. Biol. Chem. |volume=271 |issue= 50 |pages= 31973-80 |year= 1997 |pmid= 8943244 |doi= }}
*{{cite journal | author=Lampi KJ, Ma Z, Shih M, ''et al.'' |title=Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens. |journal=J. Biol. Chem. |volume=272 |issue= 4 |pages= 2268-75 |year= 1997 |pmid= 8999933 |doi= }}
*{{cite journal | author=Stephan DA, Gillanders E, Vanderveen D, ''et al.'' |title=Progressive juvenile-onset punctate cataracts caused by mutation of the gammaD-crystallin gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 3 |pages= 1008-12 |year= 1999 |pmid= 9927684 |doi= }}
*{{cite journal | author=Héon E, Priston M, Schorderet DF, ''et al.'' |title=The gamma-crystallins and human cataracts: a puzzle made clearer. |journal=Am. J. Hum. Genet. |volume=65 |issue= 5 |pages= 1261-7 |year= 1999 |pmid= 10521291 |doi= }}
*{{cite journal | author=Pande A, Pande J, Asherie N, ''et al.'' |title=Molecular basis of a progressive juvenile-onset hereditary cataract. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 5 |pages= 1993-8 |year= 2000 |pmid= 10688888 |doi= 10.1073/pnas.040554397 }}
*{{cite journal | author=Kmoch S, Brynda J, Asfaw B, ''et al.'' |title=Link between a novel human gammaD-crystallin allele and a unique cataract phenotype explained by protein crystallography. |journal=Hum. Mol. Genet. |volume=9 |issue= 12 |pages= 1779-86 |year= 2000 |pmid= 10915766 |doi= }}
*{{cite journal | author=Pande A, Pande J, Asherie N, ''et al.'' |title=Crystal cataracts: human genetic cataract caused by protein crystallization. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 11 |pages= 6116-20 |year= 2001 |pmid= 11371638 |doi= 10.1073/pnas.101124798 }}
*{{cite journal | author=Santhiya ST, Shyam Manohar M, Rawlley D, ''et al.'' |title=Novel mutations in the gamma-crystallin genes cause autosomal dominant congenital cataracts. |journal=J. Med. Genet. |volume=39 |issue= 5 |pages= 352-8 |year= 2002 |pmid= 12011157 |doi= }}
*{{cite journal | author=MacCoss MJ, McDonald WH, Saraf A, ''et al.'' |title=Shotgun identification of protein modifications from protein complexes and lens tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 12 |pages= 7900-5 |year= 2002 |pmid= 12060738 |doi= 10.1073/pnas.122231399 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on CYP7A1... {November 18, 2007 9:39:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:39:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Cytochrome P450, family 7, subfamily A, polypeptide 1
| HGNCid = 2651
| Symbol = CYP7A1
| AltSymbols =; CP7A; CYP7; MGC126826; MGC138389
| OMIM = 118455
| ECnumber =
| Homologene = 30987
| MGIid = 106091
| GeneAtlas_image1 = PBB_GE_CYP7A1_207406_at_tn.png
| Function = {{GNF_GO|id=GO:0004497 |text = monooxygenase activity}} {{GNF_GO|id=GO:0005506 |text = iron ion binding}} {{GNF_GO|id=GO:0008123 |text = cholesterol 7-alpha-monooxygenase activity}} {{GNF_GO|id=GO:0020037 |text = heme binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0006118 |text = electron transport}} {{GNF_GO|id=GO:0006629 |text = lipid metabolic process}} {{GNF_GO|id=GO:0006699 |text = bile acid biosynthetic process}} {{GNF_GO|id=GO:0006707 |text = cholesterol catabolic process}} {{GNF_GO|id=GO:0008202 |text = steroid metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1581
| Hs_Ensembl = ENSG00000167910
| Hs_RefseqProtein = NP_000771
| Hs_RefseqmRNA = NM_000780
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 8
| Hs_GenLoc_start = 59565292
| Hs_GenLoc_end = 59575275
| Hs_Uniprot = P22680
| Mm_EntrezGene = 13122
| Mm_Ensembl = ENSMUSG00000028240
| Mm_RefseqmRNA = NM_007824
| Mm_RefseqProtein = NP_031850
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 6192759
| Mm_GenLoc_end = 6202778
| Mm_Uniprot = Q8BFR7
}}
}}
'''Cytochrome P450, family 7, subfamily A, polypeptide 1''', also known as '''CYP7A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: CYP7A1 cytochrome P450, family 7, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1581| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This endoplasmic reticulum membrane protein catalyzes the first reaction in the cholesterol catabolic pathway in the liver, which converts cholesterol to bile acids. This reaction is the rate limiting step and the major site of regulation of bile acid synthesis, which is the primary mechanism for the removal of cholesterol from the body.<ref name="entrez">{{cite web | title = Entrez Gene: CYP7A1 cytochrome P450, family 7, subfamily A, polypeptide 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1581| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schwarz M, Lund EG, Russell DW |title=Two 7 alpha-hydroxylase enzymes in bile acid biosynthesis. |journal=Curr. Opin. Lipidol. |volume=9 |issue= 2 |pages= 113-8 |year= 1998 |pmid= 9559267 |doi= }}
*{{cite journal | author=Davis RA, Miyake JH, Hui TY, Spann NJ |title=Regulation of cholesterol-7alpha-hydroxylase: BAREly missing a SHP. |journal=J. Lipid Res. |volume=43 |issue= 4 |pages= 533-43 |year= 2002 |pmid= 11907135 |doi= }}
*{{cite journal | author=Beigneux A, Hofmann AF, Young SG |title=Human CYP7A1 deficiency: progress and enigmas. |journal=J. Clin. Invest. |volume=110 |issue= 1 |pages= 29-31 |year= 2002 |pmid= 12093884 |doi= }}
*{{cite journal | author=Molowa DT, Chen WS, Cimis GM, Tan CP |title=Transcriptional regulation of the human cholesterol 7 alpha-hydroxylase gene. |journal=Biochemistry |volume=31 |issue= 9 |pages= 2539-44 |year= 1992 |pmid= 1312351 |doi= }}
*{{cite journal | author=Cohen JC, Cali JJ, Jelinek DF, ''et al.'' |title=Cloning of the human cholesterol 7 alpha-hydroxylase gene (CYP7) and localization to chromosome 8q11-q12. |journal=Genomics |volume=14 |issue= 1 |pages= 153-61 |year= 1992 |pmid= 1358792 |doi= }}
*{{cite journal | author=Karam WG, Chiang JY |title=Polymorphisms of human cholesterol 7 alpha-hydroxylase. |journal=Biochem. Biophys. Res. Commun. |volume=185 |issue= 2 |pages= 588-95 |year= 1992 |pmid= 1610352 |doi= }}
*{{cite journal | author=Noshiro M, Okuda K |title=Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase. |journal=FEBS Lett. |volume=268 |issue= 1 |pages= 137-40 |year= 1990 |pmid= 2384150 |doi= }}
*{{cite journal | author=Erickson SK, Bösterling B |title=Cholesterol 7 alpha-hydroxylase from human liver: partial purification and reconstruction into defined phospholipid-cholesterol vesicles. |journal=J. Lipid Res. |volume=22 |issue= 5 |pages= 872-6 |year= 1981 |pmid= 7288293 |doi= }}
*{{cite journal | author=Wang DP, Chiang JY |title=Structure and nucleotide sequences of the human cholesterol 7 alpha-hydroxylase gene (CYP7). |journal=Genomics |volume=20 |issue= 2 |pages= 320-3 |year= 1994 |pmid= 8020987 |doi= 10.1006/geno.1994.1177 }}
*{{cite journal | author=Nishimoto M, Noshiro M, Okuda K |title=Structure of the gene encoding human liver cholesterol 7 alpha-hydroxylase. |journal=Biochim. Biophys. Acta |volume=1172 |issue= 1-2 |pages= 147-50 |year= 1993 |pmid= 8439551 |doi= }}
*{{cite journal | author=Thompson JF, Lira ME, Lloyd DB, ''et al.'' |title=Cholesterol 7 alpha hydroxylase promoter separated from cyclophilin pseudogene by Alu sequence. |journal=Biochim. Biophys. Acta |volume=1168 |issue= 2 |pages= 239-42 |year= 1993 |pmid= 8504159 |doi= }}
*{{cite journal | author=Nitta M, Ku S, Brown C, ''et al.'' |title=CPF: an orphan nuclear receptor that regulates liver-specific expression of the human cholesterol 7alpha-hydroxylase gene. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 12 |pages= 6660-5 |year= 1999 |pmid= 10359768 |doi= }}
*{{cite journal | author=Norlin M, Andersson U, Björkhem I, Wikvall K |title=Oxysterol 7 alpha-hydroxylase activity by cholesterol 7 alpha-hydroxylase (CYP7A). |journal=J. Biol. Chem. |volume=275 |issue= 44 |pages= 34046-53 |year= 2000 |pmid= 10882719 |doi= 10.1074/jbc.M002663200 }}
*{{cite journal | author=Björkhem I, Araya Z, Rudling M, ''et al.'' |title=Differences in the regulation of the classical and the alternative pathway for bile acid synthesis in human liver. No coordinate regulation of CYP7A1 and CYP27A1. |journal=J. Biol. Chem. |volume=277 |issue= 30 |pages= 26804-7 |year= 2002 |pmid= 12011083 |doi= 10.1074/jbc.M202343200 }}
*{{cite journal | author=Pullinger CR, Eng C, Salen G, ''et al.'' |title=Human cholesterol 7alpha-hydroxylase (CYP7A1) deficiency has a hypercholesterolemic phenotype. |journal=J. Clin. Invest. |volume=110 |issue= 1 |pages= 109-17 |year= 2002 |pmid= 12093894 |doi= }}
*{{cite journal | author=Chen JY, Levy-Wilson B, Goodart S, Cooper AD |title=Mice expressing the human CYP7A1 gene in the mouse CYP7A1 knock-out background lack induction of CYP7A1 expression by cholesterol feeding and have increased hypercholesterolemia when fed a high fat diet. |journal=J. Biol. Chem. |volume=277 |issue= 45 |pages= 42588-95 |year= 2003 |pmid= 12202481 |doi= 10.1074/jbc.M205117200 }}
*{{cite journal | author=Rudling M, Angelin B, Ståhle L, ''et al.'' |title=Regulation of hepatic low-density lipoprotein receptor, 3-hydroxy-3-methylglutaryl coenzyme A reductase, and cholesterol 7alpha-hydroxylase mRNAs in human liver. |journal=J. Clin. Endocrinol. Metab. |volume=87 |issue= 9 |pages= 4307-13 |year= 2002 |pmid= 12213890 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DAZ1... {November 18, 2007 9:39:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:40:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Deleted in azoospermia 1
| HGNCid = 2682
| Symbol = DAZ1
| AltSymbols =; DAZ; SPGY; DAZ1; pDP1680; pDP1681
| OMIM = 400003
| ECnumber =
| Homologene = 88435
| MGIid =
| GeneAtlas_image1 = PBB_GE_DAZ1_207912_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DAZ1_208281_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_DAZ1_208282_x_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008494 |text = translation activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007283 |text = spermatogenesis}} {{GNF_GO|id=GO:0007338 |text = single fertilization}} {{GNF_GO|id=GO:0030154 |text = cell differentiation}} {{GNF_GO|id=GO:0045948 |text = positive regulation of translational initiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1617
| Hs_Ensembl = ENSG00000205916
| Hs_RefseqProtein = NP_004072
| Hs_RefseqmRNA = NM_004081
| Hs_GenLoc_db =
| Hs_GenLoc_chr = Y
| Hs_GenLoc_start = 25389368
| Hs_GenLoc_end = 25462575
| Hs_Uniprot =
| Mm_EntrezGene =
| Mm_Ensembl =
| Mm_RefseqmRNA =
| Mm_RefseqProtein =
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Deleted in azoospermia 1''', also known as '''DAZ1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DAZ1 deleted in azoospermia 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1617| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene is a member of the DAZ gene family and is a candidate for the human Y-chromosomal azoospermia factor (AZF). Its expression is restricted to premeiotic germ cells, particularly in spermatogonia. It encodes an RNA-binding protein that is important for spermatogenesis. Four copies of this gene are found on chromosome Y within palindromic duplications; one pair of genes is part of the P2 palindrome and the second pair is part of the P1 palindrome. Each gene contains a 2.4 kb repeat including a 72-bp exon, called the DAZ repeat; the number of DAZ repeats is variable and there are several variations in the sequence of the DAZ repeat. Each copy of the gene also contains a 10.8 kb region that may be amplified; this region includes five exons that encode an RNA recognition motif (RRM) domain. This gene contains three copies of the 10.8 kb repeat. However, no transcripts containing three copies of the RRM domain have been described; thus the RefSeq for this gene contains only two RRM domains.<ref name="entrez">{{cite web | title = Entrez Gene: DAZ1 deleted in azoospermia 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1617| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Foresta C, Ferlin A, Moro E, ''et al.'' |title=[Microdeletion of chromosome Y in male infertility: role of the DAZ gene] |journal=Ann. Ital. Med. Int. |volume=16 |issue= 2 |pages= 82-92 |year= 2002 |pmid= 11688365 |doi= }}
*{{cite journal | author=Fox MS, Reijo Pera RA |title=Male infertility, genetic analysis of the DAZ genes on the human Y chromosome and genetic analysis of DNA repair. |journal=Mol. Cell. Endocrinol. |volume=184 |issue= 1-2 |pages= 41-9 |year= 2002 |pmid= 11694340 |doi= }}
*{{cite journal | author=Vogt PH, Fernandes S |title=Polymorphic DAZ gene family in polymorphic structure of AZFc locus: Artwork or functional for human spermatogenesis? |journal=APMIS |volume=111 |issue= 1 |pages= 115-26; discussion 126-7 |year= 2003 |pmid= 12752250 |doi= }}
*{{cite journal | author=Reijo R, Lee TY, Salo P, ''et al.'' |title=Diverse spermatogenic defects in humans caused by Y chromosome deletions encompassing a novel RNA-binding protein gene. |journal=Nat. Genet. |volume=10 |issue= 4 |pages= 383-93 |year= 1995 |pmid= 7670487 |doi= 10.1038/ng0895-383 }}
*{{cite journal | author=Reijo R, Seligman J, Dinulos MB, ''et al.'' |title=Mouse autosomal homolog of DAZ, a candidate male sterility gene in humans, is expressed in male germ cells before and after puberty. |journal=Genomics |volume=35 |issue= 2 |pages= 346-52 |year= 1996 |pmid= 8661148 |doi= 10.1006/geno.1996.0366 }}
*{{cite journal | author=Cooke HJ, Lee M, Kerr S, Ruggiu M |title=A murine homologue of the human DAZ gene is autosomal and expressed only in male and female gonads. |journal=Hum. Mol. Genet. |volume=5 |issue= 4 |pages= 513-6 |year= 1996 |pmid= 8845845 |doi= }}
*{{cite journal | author=Saxena R, Brown LG, Hawkins T, ''et al.'' |title=The DAZ gene cluster on the human Y chromosome arose from an autosomal gene that was transposed, repeatedly amplified and pruned. |journal=Nat. Genet. |volume=14 |issue= 3 |pages= 292-9 |year= 1996 |pmid= 8896558 |doi= 10.1038/ng1196-292 }}
*{{cite journal | author=Yen PH, Chai NN, Salido EC |title=The human autosomal gene DAZLA: testis specificity and a candidate for male infertility. |journal=Hum. Mol. Genet. |volume=5 |issue= 12 |pages= 2013-7 |year= 1997 |pmid= 8968756 |doi= }}
*{{cite journal | author=Menke DB, Mutter GL, Page DC |title=Expression of DAZ, an azoospermia factor candidate, in human spermatogonia. |journal=Am. J. Hum. Genet. |volume=60 |issue= 1 |pages= 237-41 |year= 1997 |pmid= 8981970 |doi= }}
*{{cite journal | author=Yen PH, Chai NN, Salido EC |title=The human DAZ genes, a putative male infertility factor on the Y chromosome, are highly polymorphic in the DAZ repeat regions. |journal=Mamm. Genome |volume=8 |issue= 10 |pages= 756-9 |year= 1997 |pmid= 9321470 |doi= }}
*{{cite journal | author=Agulnik AI, Zharkikh A, Boettger-Tong H, ''et al.'' |title=Evolution of the DAZ gene family suggests that Y-linked DAZ plays little, or a limited, role in spermatogenesis but underlines a recent African origin for human populations. |journal=Hum. Mol. Genet. |volume=7 |issue= 9 |pages= 1371-7 |year= 1998 |pmid= 9700189 |doi= }}
*{{cite journal | author=Tsui S, Dai T, Roettger S, ''et al.'' |title=Identification of two novel proteins that interact with germ-cell-specific RNA-binding proteins DAZ and DAZL1. |journal=Genomics |volume=65 |issue= 3 |pages= 266-73 |year= 2000 |pmid= 10857750 |doi= 10.1006/geno.2000.6169 }}
*{{cite journal | author=Ruggiu M, Cooke HJ |title=In vivo and in vitro analysis of homodimerisation activity of the mouse Dazl1 protein. |journal=Gene |volume=252 |issue= 1-2 |pages= 119-26 |year= 2000 |pmid= 10903443 |doi= }}
*{{cite journal | author=Saxena R, de Vries JW, Repping S, ''et al.'' |title=Four DAZ genes in two clusters found in the AZFc region of the human Y chromosome. |journal=Genomics |volume=67 |issue= 3 |pages= 256-67 |year= 2000 |pmid= 10936047 |doi= 10.1006/geno.2000.6260 }}
*{{cite journal | author=Reijo RA, Dorfman DM, Slee R, ''et al.'' |title=DAZ family proteins exist throughout male germ cell development and transit from nucleus to cytoplasm at meiosis in humans and mice. |journal=Biol. Reprod. |volume=63 |issue= 5 |pages= 1490-6 |year= 2000 |pmid= 11058556 |doi= }}
*{{cite journal | author=Moro E, Ferlin A, Yen PH, ''et al.'' |title=Male infertility caused by a de novo partial deletion of the DAZ cluster on the Y chromosome. |journal=J. Clin. Endocrinol. Metab. |volume=85 |issue= 11 |pages= 4069-73 |year= 2000 |pmid= 11095434 |doi= }}
*{{cite journal | author=Xu EY, Moore FL, Pera RA |title=A gene family required for human germ cell development evolved from an ancient meiotic gene conserved in metazoans. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 13 |pages= 7414-9 |year= 2001 |pmid= 11390979 |doi= 10.1073/pnas.131090498 }}
*{{cite journal | author=Friel A, Houghton JA, Glennon M, ''et al.'' |title=A preliminary report on the implication of RT-PCR detection of DAZ, RBMY1, USP9Y and Protamine-2 mRNA in testicular biopsy samples from azoospermic men. |journal=Int. J. Androl. |volume=25 |issue= 1 |pages= 59-64 |year= 2002 |pmid= 11869379 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DCT... {November 18, 2007 9:40:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:41:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dopachrome tautomerase (dopachrome delta-isomerase, tyrosine-related protein 2)
| HGNCid = 2709
| Symbol = DCT
| AltSymbols =; TYRP2
| OMIM = 191275
| ECnumber =
| Homologene = 1447
| MGIid = 102563
| GeneAtlas_image1 = PBB_GE_DCT_205338_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DCT_205337_at_tn.png
| GeneAtlas_image3 = PBB_GE_DCT_216512_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004167 |text = dopachrome isomerase activity}} {{GNF_GO|id=GO:0005507 |text = copper ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016491 |text = oxidoreductase activity}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042470 |text = melanosome}}
| Process = {{GNF_GO|id=GO:0006583 |text = melanin biosynthetic process from tyrosine}} {{GNF_GO|id=GO:0008152 |text = metabolic process}} {{GNF_GO|id=GO:0008544 |text = epidermis development}} {{GNF_GO|id=GO:0048066 |text = pigmentation during development}} {{GNF_GO|id=GO:0048468 |text = cell development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1638
| Hs_Ensembl = ENSG00000080166
| Hs_RefseqProtein = NP_001913
| Hs_RefseqmRNA = NM_001922
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 93887559
| Hs_GenLoc_end = 93929924
| Hs_Uniprot = P40126
| Mm_EntrezGene = 13190
| Mm_Ensembl = ENSMUSG00000022129
| Mm_RefseqmRNA = XM_979031
| Mm_RefseqProtein = XP_984125
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 14
| Mm_GenLoc_start = 116895153
| Mm_GenLoc_end = 116934531
| Mm_Uniprot = Q6NXI2
}}
}}
'''Dopachrome tautomerase (dopachrome delta-isomerase, tyrosine-related protein 2)''', also known as '''DCT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DCT dopachrome tautomerase (dopachrome delta-isomerase, tyrosine-related protein 2)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1638| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jackson IJ, Chambers DM, Tsukamoto K, ''et al.'' |title=A second tyrosinase-related protein, TRP-2, maps to and is mutated at the mouse slaty locus. |journal=EMBO J. |volume=11 |issue= 2 |pages= 527-35 |year= 1992 |pmid= 1537334 |doi= }}
*{{cite journal | author=Tobin D, Quinn AG, Ito S, Thody AJ |title=The presence of tyrosinase and related proteins in human epidermis and their relationship to melanin type. |journal=Pigment Cell Res. |volume=7 |issue= 4 |pages= 204-9 |year= 1995 |pmid= 7855064 |doi= }}
*{{cite journal | author=Bernd A, Ramirez-Bosca A, Kippenberger S, ''et al.'' |title=Levels of dopachrome tautomerase in human melanocytes cultured in vitro. |journal=Melanoma Res. |volume=4 |issue= 5 |pages= 287-91 |year= 1995 |pmid= 7858411 |doi= }}
*{{cite journal | author=Yokoyama K, Yasumoto K, Suzuki H, Shibahara S |title=Cloning of the human DOPAchrome tautomerase/tyrosinase-related protein 2 gene and identification of two regulatory regions required for its pigment cell-specific expression. |journal=J. Biol. Chem. |volume=269 |issue= 43 |pages= 27080-7 |year= 1994 |pmid= 7929451 |doi= }}
*{{cite journal | author=Orlow SJ, Zhou BK, Chakraborty AK, ''et al.'' |title=High-molecular-weight forms of tyrosinase and the tyrosinase-related proteins: evidence for a melanogenic complex. |journal=J. Invest. Dermatol. |volume=103 |issue= 2 |pages= 196-201 |year= 1994 |pmid= 8040609 |doi= }}
*{{cite journal | author=Sturm RA, Baker E, Sutherland GR |title=Assignment of the tyrosinase-related protein-2 gene (TYRP2) to human chromosome 13q31-q32 by fluorescence in situ hybridization: extended synteny with mouse chromosome 14. |journal=Genomics |volume=21 |issue= 1 |pages= 293-6 |year= 1994 |pmid= 8088811 |doi= 10.1006/geno.1994.1266 }}
*{{cite journal | author=Abdel-Malek Z, Swope V, Collins C, ''et al.'' |title=Contribution of melanogenic proteins to the heterogeneous pigmentation of human melanocytes. |journal=J. Cell. Sci. |volume=106 ( Pt 4) |issue= |pages= 1323-31 |year= 1994 |pmid= 8126111 |doi= }}
*{{cite journal | author=Yokoyama K, Suzuki H, Yasumoto K, ''et al.'' |title=Molecular cloning and functional analysis of a cDNA coding for human DOPAchrome tautomerase/tyrosinase-related protein-2. |journal=Biochim. Biophys. Acta |volume=1217 |issue= 3 |pages= 317-21 |year= 1994 |pmid= 8148378 |doi= }}
*{{cite journal | author=Cassady JL, Sturm RA |title=Sequence of the human dopachrome tautomerase-encoding TRP-2 cDNA. |journal=Gene |volume=143 |issue= 2 |pages= 295-8 |year= 1994 |pmid= 8206391 |doi= }}
*{{cite journal | author=Odh G, Hindemith A, Rosengren AM, ''et al.'' |title=Isolation of a new tautomerase monitored by the conversion of D-dopachrome to 5,6-dihydroxyindole. |journal=Biochem. Biophys. Res. Commun. |volume=197 |issue= 2 |pages= 619-24 |year= 1994 |pmid= 8267597 |doi= 10.1006/bbrc.1993.2524 }}
*{{cite journal | author=Bouchard B, Del Marmol V, Jackson IJ, ''et al.'' |title=Molecular characterization of a human tyrosinase-related-protein-2 cDNA. Patterns of expression in melanocytic cells. |journal=Eur. J. Biochem. |volume=219 |issue= 1-2 |pages= 127-34 |year= 1994 |pmid= 8306979 |doi= }}
*{{cite journal | author=Sturm RA, O'Sullivan BJ, Box NF, ''et al.'' |title=Chromosomal structure of the human TYRP1 and TYRP2 loci and comparison of the tyrosinase-related protein gene family. |journal=Genomics |volume=29 |issue= 1 |pages= 24-34 |year= 1996 |pmid= 8530077 |doi= 10.1006/geno.1995.1211 }}
*{{cite journal | author=Björk P, Aman P, Hindemith A, ''et al.'' |title=A new enzyme activity in human blood cells and isolation of the responsible protein (D-dopachrome tautomerase) from erythrocytes. |journal=Eur. J. Haematol. |volume=57 |issue= 3 |pages= 254-6 |year= 1996 |pmid= 8898931 |doi= }}
*{{cite journal | author=Smith-Thomas L, Richardson P, Thody AJ, ''et al.'' |title=Human ocular melanocytes and retinal pigment epithelial cells differ in their melanogenic properties in vivo and in vitro. |journal=Curr. Eye Res. |volume=15 |issue= 11 |pages= 1079-91 |year= 1997 |pmid= 8950502 |doi= }}
*{{cite journal | author=Wang RF, Appella E, Kawakami Y, ''et al.'' |title=Identification of TRP-2 as a human tumor antigen recognized by cytotoxic T lymphocytes. |journal=J. Exp. Med. |volume=184 |issue= 6 |pages= 2207-16 |year= 1997 |pmid= 8976176 |doi= }}
*{{cite journal | author=Chi DD, Merchant RE, Rand R, ''et al.'' |title=Molecular detection of tumor-associated antigens shared by human cutaneous melanomas and gliomas. |journal=Am. J. Pathol. |volume=150 |issue= 6 |pages= 2143-52 |year= 1997 |pmid= 9176405 |doi= }}
*{{cite journal | author=Sugimoto H, Taniguchi M, Nakagawa A, ''et al.'' |title=Crystallization and preliminary X-ray analysis of human D-dopachrome tautomerase. |journal=J. Struct. Biol. |volume=120 |issue= 1 |pages= 105-8 |year= 1997 |pmid= 9356298 |doi= 10.1006/jsbi.1997.3904 }}
*{{cite journal | author=Nishihira J, Fujinaga M, Kuriyama T, ''et al.'' |title=Molecular cloning of human D-dopachrome tautomerase cDNA: N-terminal proline is essential for enzyme activation. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 2 |pages= 538-44 |year= 1998 |pmid= 9480844 |doi= 10.1006/bbrc.1998.8123 }}
*{{cite journal | author=Kippenberger S, Loitsch S, Solano F, ''et al.'' |title=Quantification of tyrosinase, TRP-1, and Trp-2 transcripts in human melanocytes by reverse transcriptase-competitive multiplex PCR--regulation by steroid hormones. |journal=J. Invest. Dermatol. |volume=110 |issue= 4 |pages= 364-7 |year= 1998 |pmid= 9540976 |doi= 10.1046/j.1523-1747.1998.00144.x }}
*{{cite journal | author=Lupetti R, Pisarra P, Verrecchia A, ''et al.'' |title=Translation of a retained intron in tyrosinase-related protein (TRP) 2 mRNA generates a new cytotoxic T lymphocyte (CTL)-defined and shared human melanoma antigen not expressed in normal cells of the melanocytic lineage. |journal=J. Exp. Med. |volume=188 |issue= 6 |pages= 1005-16 |year= 1998 |pmid= 9743519 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DDX5... {November 18, 2007 9:41:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:42:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = DEAD (Asp-Glu-Ala-Asp) box polypeptide 5
| HGNCid = 2746
| Symbol = DDX5
| AltSymbols =; DKFZp686J01190; G17P1; HLR1; HUMP68; p68
| OMIM = 180630
| ECnumber =
| Homologene = 74312
| MGIid = 105037
| GeneAtlas_image1 = PBB_GE_DDX5_200033_at_tn.png
| GeneAtlas_image2 = PBB_GE_DDX5_200034_s_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0003724 |text = RNA helicase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0008026 |text = ATP-dependent helicase activity}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}}
| Process = {{GNF_GO|id=GO:0006397 |text = mRNA processing}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}} {{GNF_GO|id=GO:0016049 |text = cell growth}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1655
| Hs_Ensembl = ENSG00000108654
| Hs_RefseqProtein = NP_004387
| Hs_RefseqmRNA = NM_004396
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 17
| Hs_GenLoc_start = 59926202
| Hs_GenLoc_end = 59932872
| Hs_Uniprot = P17844
| Mm_EntrezGene = 13207
| Mm_Ensembl = ENSMUSG00000020719
| Mm_RefseqmRNA = NM_007840
| Mm_RefseqProtein = NP_031866
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 11
| Mm_GenLoc_start = 106596446
| Mm_GenLoc_end = 106604584
| Mm_Uniprot = O35662
}}
}}
'''DEAD (Asp-Glu-Ala-Asp) box polypeptide 5''', also known as '''DDX5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DDX5 DEAD (Asp-Glu-Ala-Asp) box polypeptide 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1655| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure, such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein, which is a RNA-dependent ATPase, and also a proliferation-associated nuclear antigen, specifically reacting with the simian virus 40 tumor antigen. This gene consists of 13 exons, and alternatively spliced transcripts containing several intron sequences have been detected, but no isoforms encoded by these transcripts have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: DDX5 DEAD (Asp-Glu-Ala-Asp) box polypeptide 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1655| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Iggo RD, Jamieson DJ, MacNeill SA, ''et al.'' |title=p68 RNA helicase: identification of a nucleolar form and cloning of related genes containing a conserved intron in yeasts. |journal=Mol. Cell. Biol. |volume=11 |issue= 3 |pages= 1326-33 |year= 1991 |pmid= 1996094 |doi= }}
*{{cite journal | author=Hloch P, Schiedner G, Stahl H |title=Complete cDNA sequence of the human p68 protein. |journal=Nucleic Acids Res. |volume=18 |issue= 10 |pages= 3045 |year= 1990 |pmid= 2349099 |doi= }}
*{{cite journal | author=Ford MJ, Anton IA, Lane DP |title=Nuclear protein with sequence homology to translation initiation factor eIF-4A. |journal=Nature |volume=332 |issue= 6166 |pages= 736-8 |year= 1988 |pmid= 2451786 |doi= 10.1038/332736a0 }}
*{{cite journal | author=Iggo R, Gough A, Xu W, ''et al.'' |title=Chromosome mapping of the human gene encoding the 68-kDa nuclear antigen (p68) by using the polymerase chain reaction. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 16 |pages= 6211-4 |year= 1989 |pmid= 2762324 |doi= }}
*{{cite journal | author=Buelt MK, Glidden BJ, Storm DR |title=Regulation of p68 RNA helicase by calmodulin and protein kinase C. |journal=J. Biol. Chem. |volume=269 |issue= 47 |pages= 29367-70 |year= 1994 |pmid= 7525583 |doi= }}
*{{cite journal | author=Brody LC, Abel KJ, Castilla LH, ''et al.'' |title=Construction of a transcription map surrounding the BRCA1 locus of human chromosome 17. |journal=Genomics |volume=25 |issue= 1 |pages= 238-47 |year= 1995 |pmid= 7774924 |doi= }}
*{{cite journal | author=Endoh H, Maruyama K, Masuhiro Y, ''et al.'' |title=Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor alpha. |journal=Mol. Cell. Biol. |volume=19 |issue= 8 |pages= 5363-72 |year= 1999 |pmid= 10409727 |doi= }}
*{{cite journal | author=Rössler OG, Hloch P, Schütz N, ''et al.'' |title=Structure and expression of the human p68 RNA helicase gene. |journal=Nucleic Acids Res. |volume=28 |issue= 4 |pages= 932-9 |year= 2000 |pmid= 10648785 |doi= }}
*{{cite journal | author=Nicol SM, Causevic M, Prescott AR, Fuller-Pace FV |title=The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase. |journal=Exp. Cell Res. |volume=257 |issue= 2 |pages= 272-80 |year= 2000 |pmid= 10837141 |doi= 10.1006/excr.2000.4886 }}
*{{cite journal | author=Watanabe M, Yanagisawa J, Kitagawa H, ''et al.'' |title=A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA. |journal=EMBO J. |volume=20 |issue= 6 |pages= 1341-52 |year= 2001 |pmid= 11250900 |doi= 10.1093/emboj/20.6.1341 }}
*{{cite journal | author=Akileswaran L, Taraska JW, Sayer JA, ''et al.'' |title=A-kinase-anchoring protein AKAP95 is targeted to the nuclear matrix and associates with p68 RNA helicase. |journal=J. Biol. Chem. |volume=276 |issue= 20 |pages= 17448-54 |year= 2001 |pmid= 11279182 |doi= 10.1074/jbc.M101171200 }}
*{{cite journal | author=Andersen JS, Lyon CE, Fox AH, ''et al.'' |title=Directed proteomic analysis of the human nucleolus. |journal=Curr. Biol. |volume=12 |issue= 1 |pages= 1-11 |year= 2002 |pmid= 11790298 |doi= }}
*{{cite journal | author=Jurica MS, Licklider LJ, Gygi SR, ''et al.'' |title=Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis. |journal=RNA |volume=8 |issue= 4 |pages= 426-39 |year= 2002 |pmid= 11991638 |doi= }}
*{{cite journal | author=Liu ZR |title=p68 RNA helicase is an essential human splicing factor that acts at the U1 snRNA-5' splice site duplex. |journal=Mol. Cell. Biol. |volume=22 |issue= 15 |pages= 5443-50 |year= 2002 |pmid= 12101238 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Rossow KL, Janknecht R |title=Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300. |journal=Oncogene |volume=22 |issue= 1 |pages= 151-6 |year= 2003 |pmid= 12527917 |doi= 10.1038/sj.onc.1206067 }}
*{{cite journal | author=Ogilvie VC, Wilson BJ, Nicol SM, ''et al.'' |title=The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells. |journal=Nucleic Acids Res. |volume=31 |issue= 5 |pages= 1470-80 |year= 2003 |pmid= 12595555 |doi= }}
*{{cite journal | author=Guil S, Gattoni R, Carrascal M, ''et al.'' |title=Roles of hnRNP A1, SR proteins, and p68 helicase in c-H-ras alternative splicing regulation. |journal=Mol. Cell. Biol. |volume=23 |issue= 8 |pages= 2927-41 |year= 2003 |pmid= 12665590 |doi= }}
*{{cite journal | author=Fujita T, Kobayashi Y, Wada O, ''et al.'' |title=Full activation of estrogen receptor alpha activation function-1 induces proliferation of breast cancer cells. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26704-14 |year= 2003 |pmid= 12738788 |doi= 10.1074/jbc.M301031200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DSG1... {November 18, 2007 9:42:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:43:02 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Desmoglein 1
| HGNCid = 3048
| Symbol = DSG1
| AltSymbols =; CDHF4; DG1; DSG
| OMIM = 125670
| ECnumber =
| Homologene = 1463
| MGIid = 94930
| GeneAtlas_image1 = PBB_GE_DSG1_206642_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015643 |text = toxin binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0030057 |text = desmosome}}
| Process = {{GNF_GO|id=GO:0007043 |text = intercellular junction assembly}} {{GNF_GO|id=GO:0007156 |text = homophilic cell adhesion}} {{GNF_GO|id=GO:0016339 |text = calcium-dependent cell-cell adhesion}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1828
| Hs_Ensembl = ENSG00000134760
| Hs_RefseqProtein = NP_001933
| Hs_RefseqmRNA = NM_001942
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 27152050
| Hs_GenLoc_end = 27190457
| Hs_Uniprot = Q02413
| Mm_EntrezGene = 13510
| Mm_Ensembl = ENSMUSG00000069441
| Mm_RefseqmRNA = XM_484705
| Mm_RefseqProtein = XP_484705
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 20454028
| Mm_GenLoc_end = 20484290
| Mm_Uniprot = Q61495
}}
}}
'''Desmoglein 1''', also known as '''DSG1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DSG1 desmoglein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1828| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Desmosomes are cell-cell junctions between epithelial, myocardial and certain other cell types. Desmoglein 1 is a calcium-binding transmembrane glycoprotein component of desmosomes in vertebrate epithelial cells. Currently, three desmoglein subfamily members have been identified and all are members of the cadherin cell adhesion molecule superfamily. These desmoglein gene family members are located in a cluster on chromosome 18. The protein encoded by this gene has been identified as the autoantigen of the autoimmune skin blistering disease pemphigus foliaceus.<ref name="entrez">{{cite web | title = Entrez Gene: DSG1 desmoglein 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1828| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Amagai M |title=Desmoglein as a target in autoimmunity and infection. |journal=J. Am. Acad. Dermatol. |volume=48 |issue= 2 |pages= 244-52 |year= 2003 |pmid= 12582396 |doi= 10.1067/mjd.2003.7 }}
*{{cite journal | author=Wheeler GN, Parker AE, Thomas CL, ''et al.'' |title=Desmosomal glycoprotein DGI, a component of intercellular desmosome junctions, is related to the cadherin family of cell adhesion molecules. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 11 |pages= 4796-800 |year= 1991 |pmid= 1711210 |doi= }}
*{{cite journal | author=Amagai M, Klaus-Kovtun V, Stanley JR |title=Autoantibodies against a novel epithelial cadherin in pemphigus vulgaris, a disease of cell adhesion. |journal=Cell |volume=67 |issue= 5 |pages= 869-77 |year= 1992 |pmid= 1720352 |doi= }}
*{{cite journal | author=Martínez RD |title=[Characterization of the desmoglein in renal cells in culture] |journal=Revista alergia México |volume=38 |issue= 2 |pages= 59-64 |year= 1992 |pmid= 1754823 |doi= }}
*{{cite journal | author=Nilles LA, Parry DA, Powers EE, ''et al.'' |title=Structural analysis and expression of human desmoglein: a cadherin-like component of the desmosome. |journal=J. Cell. Sci. |volume=99 ( Pt 4) |issue= |pages= 809-21 |year= 1992 |pmid= 1770008 |doi= }}
*{{cite journal | author=Arnemann J, Spurr NK, Wheeler GN, ''et al.'' |title=Chromosomal assignment of the human genes coding for the major proteins of the desmosome junction, desmoglein DGI (DSG), desmocollins DGII/III (DSC), desmoplakins DPI/II (DSP), and plakoglobin DPIII (JUP). |journal=Genomics |volume=10 |issue= 3 |pages= 640-5 |year= 1991 |pmid= 1889810 |doi= }}
*{{cite journal | author=Roh JY, Stanley JR |title=Plakoglobin binding by human Dsg3 (pemphigus vulgaris antigen) in keratinocytes requires the cadherin-like intracytoplasmic segment. |journal=J. Invest. Dermatol. |volume=104 |issue= 5 |pages= 720-4 |year= 1995 |pmid= 7738346 |doi= }}
*{{cite journal | author=Simrak D, Cowley CM, Buxton RS, Arnemann J |title=Tandem arrangement of the closely linked desmoglein genes on human chromosome 18. |journal=Genomics |volume=25 |issue= 2 |pages= 591-4 |year= 1995 |pmid= 7790000 |doi= }}
*{{cite journal | author=Wang Y, Amagai M, Minoshima S, ''et al.'' |title=The human genes for desmogleins (DSG1 and DSG3) are located in a small region on chromosome 18q12. |journal=Genomics |volume=20 |issue= 3 |pages= 492-5 |year= 1994 |pmid= 8034325 |doi= 10.1006/geno.1994.1207 }}
*{{cite journal | author=Schäfer S, Koch PJ, Franke WW |title=Identification of the ubiquitous human desmoglein, Dsg2, and the expression catalogue of the desmoglein subfamily of desmosomal cadherins. |journal=Exp. Cell Res. |volume=211 |issue= 2 |pages= 391-9 |year= 1994 |pmid= 8143788 |doi= 10.1006/excr.1994.1103 }}
*{{cite journal | author=Adams MJ, Reichel MB, King IA, ''et al.'' |title=Characterization of the regulatory regions in the human desmoglein genes encoding the pemphigus foliaceous and pemphigus vulgaris antigens. |journal=Biochem. J. |volume=329 ( Pt 1) |issue= |pages= 165-74 |year= 1998 |pmid= 9405290 |doi= }}
*{{cite journal | author=Marcozzi C, Burdett ID, Buxton RS, Magee AI |title=Coexpression of both types of desmosomal cadherin and plakoglobin confers strong intercellular adhesion. |journal=J. Cell. Sci. |volume=111 ( Pt 4) |issue= |pages= 495-509 |year= 1998 |pmid= 9443898 |doi= }}
*{{cite journal | author=Smith EA, Fuchs E |title=Defining the interactions between intermediate filaments and desmosomes. |journal=J. Cell Biol. |volume=141 |issue= 5 |pages= 1229-41 |year= 1998 |pmid= 9606214 |doi= }}
*{{cite journal | author=Rickman L, Simrak D, Stevens HP, ''et al.'' |title=N-terminal deletion in a desmosomal cadherin causes the autosomal dominant skin disease striate palmoplantar keratoderma. |journal=Hum. Mol. Genet. |volume=8 |issue= 6 |pages= 971-6 |year= 1999 |pmid= 10332028 |doi= }}
*{{cite journal | author=Li G, Schaider H, Satyamoorthy K, ''et al.'' |title=Downregulation of E-cadherin and Desmoglein 1 by autocrine hepatocyte growth factor during melanoma development. |journal=Oncogene |volume=20 |issue= 56 |pages= 8125-35 |year= 2002 |pmid= 11781826 |doi= 10.1038/sj.onc.1205034 }}
*{{cite journal | author=Chen X, Bonne S, Hatzfeld M, ''et al.'' |title=Protein binding and functional characterization of plakophilin 2. Evidence for its diverse roles in desmosomes and beta -catenin signaling. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10512-22 |year= 2002 |pmid= 11790773 |doi= 10.1074/jbc.M108765200 }}
*{{cite journal | author=Martel P, Gilbert D, Busson M, ''et al.'' |title=Epistasis between DSG1 and HLA class II genes in pemphigus foliaceus. |journal=Genes Immun. |volume=3 |issue= 4 |pages= 205-10 |year= 2003 |pmid= 12058255 |doi= 10.1038/sj.gene.6363839 }}
*{{cite journal | author=Hanakawa Y, Schechter NM, Lin C, ''et al.'' |title=Molecular mechanisms of blister formation in bullous impetigo and staphylococcal scalded skin syndrome. |journal=J. Clin. Invest. |volume=110 |issue= 1 |pages= 53-60 |year= 2002 |pmid= 12093888 |doi= }}
*{{cite journal | author=Hanakawa Y, Amagai M, Shirakata Y, ''et al.'' |title=Differential effects of desmoglein 1 and desmoglein 3 on desmosome formation. |journal=J. Invest. Dermatol. |volume=119 |issue= 6 |pages= 1231-6 |year= 2003 |pmid= 12485422 |doi= 10.1046/j.1523-1747.2002.19648.x }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DTNA... {November 18, 2007 9:43:02 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:44:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dystrobrevin, alpha
| HGNCid = 3057
| Symbol = DTNA
| AltSymbols =; DRP3; D18S892E; DTN; LVNC1
| OMIM = 601239
| ECnumber =
| Homologene = 20362
| MGIid = 106039
| GeneAtlas_image1 = PBB_GE_DTNA_208430_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_DTNA_210736_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_DTNA_211493_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005792 |text = microsome}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006941 |text = striated muscle contraction}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007274 |text = neuromuscular synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1837
| Hs_Ensembl = ENSG00000134769
| Hs_RefseqProtein = NP_001381
| Hs_RefseqmRNA = NM_001390
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 18
| Hs_GenLoc_start = 30327279
| Hs_GenLoc_end = 30725341
| Hs_Uniprot = Q9Y4J8
| Mm_EntrezGene = 13527
| Mm_Ensembl = ENSMUSG00000024302
| Mm_RefseqmRNA = NM_010087
| Mm_RefseqProtein = NP_034217
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 18
| Mm_GenLoc_start = 23558452
| Mm_GenLoc_end = 23794673
| Mm_Uniprot = Q9D2N4
}}
}}
'''Dystrobrevin, alpha''', also known as '''DTNA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DTNA dystrobrevin, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1837| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the dystrobrevin subfamily and the dystrophin family. This protein is a component of the dystrophin-associated protein complex (DPC). The DPC consists of dystrophin and several integral and peripheral membrane proteins, including dystroglycans, sarcoglycans, syntrophins and alpha- and beta-dystrobrevin. The DPC localizes to the sarcolemma and its disruption is associated with various forms of muscular dystrophy. This protein may be involved in the formation and stability of synapses as well as the clustering of nicotinic acetylcholine receptors. Multiple alternatively spliced transcript variants encoding different isoforms have been identified.<ref name="entrez">{{cite web | title = Entrez Gene: DTNA dystrobrevin, alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1837| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Straub V, Campbell KP |title=Muscular dystrophies and the dystrophin-glycoprotein complex. |journal=Curr. Opin. Neurol. |volume=10 |issue= 2 |pages= 168-75 |year= 1997 |pmid= 9146999 |doi= }}
*{{cite journal | author=Ozawa E, Noguchi S, Mizuno Y, ''et al.'' |title=From dystrophinopathy to sarcoglycanopathy: evolution of a concept of muscular dystrophy. |journal=Muscle Nerve |volume=21 |issue= 4 |pages= 421-38 |year= 1998 |pmid= 9533777 |doi= }}
*{{cite journal | author=Blake DJ |title=Dystrobrevin dynamics in muscle-cell signalling: a possible target for therapeutic intervention in Duchenne muscular dystrophy? |journal=Neuromuscul. Disord. |volume=12 Suppl 1 |issue= |pages= S110-7 |year= 2002 |pmid= 12206805 |doi= }}
*{{cite journal | author=Ahn AH, Kunkel LM |title=Syntrophin binds to an alternatively spliced exon of dystrophin. |journal=J. Cell Biol. |volume=128 |issue= 3 |pages= 363-71 |year= 1995 |pmid= 7844150 |doi= }}
*{{cite journal | author=Khurana TS, Engle EC, Bennett RR, ''et al.'' |title=(CA) repeat polymorphism in the chromosome 18 encoded dystrophin-like protein. |journal=Hum. Mol. Genet. |volume=3 |issue= 5 |pages= 841 |year= 1994 |pmid= 8081380 |doi= }}
*{{cite journal | author=Ahn AH, Freener CA, Gussoni E, ''et al.'' |title=The three human syntrophin genes are expressed in diverse tissues, have distinct chromosomal locations, and each bind to dystrophin and its relatives. |journal=J. Biol. Chem. |volume=271 |issue= 5 |pages= 2724-30 |year= 1996 |pmid= 8576247 |doi= }}
*{{cite journal | author=Blake DJ, Nawrotzki R, Peters MF, ''et al.'' |title=Isoform diversity of dystrobrevin, the murine 87-kDa postsynaptic protein. |journal=J. Biol. Chem. |volume=271 |issue= 13 |pages= 7802-10 |year= 1996 |pmid= 8631824 |doi= }}
*{{cite journal | author=Sadoulet-Puccio HM, Khurana TS, Cohen JB, Kunkel LM |title=Cloning and characterization of the human homologue of a dystrophin related phosphoprotein found at the Torpedo electric organ post-synaptic membrane. |journal=Hum. Mol. Genet. |volume=5 |issue= 4 |pages= 489-96 |year= 1996 |pmid= 8845841 |doi= }}
*{{cite journal | author=Ambrose HJ, Blake DJ, Nawrotzki RA, Davies KE |title=Genomic organization of the mouse dystrobrevin gene: comparative analysis with the dystrophin gene. |journal=Genomics |volume=39 |issue= 3 |pages= 359-69 |year= 1997 |pmid= 9119373 |doi= 10.1006/geno.1996.4515 }}
*{{cite journal | author=Metzinger L, Blake DJ, Squier MV, ''et al.'' |title=Dystrobrevin deficiency at the sarcolemma of patients with muscular dystrophy. |journal=Hum. Mol. Genet. |volume=6 |issue= 7 |pages= 1185-91 |year= 1997 |pmid= 9215691 |doi= }}
*{{cite journal | author=Sadoulet-Puccio HM, Rajala M, Kunkel LM |title=Dystrobrevin and dystrophin: an interaction through coiled-coil motifs. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 23 |pages= 12413-8 |year= 1997 |pmid= 9356463 |doi= }}
*{{cite journal | author=Blake DJ, Nawrotzki R, Loh NY, ''et al.'' |title=beta-dystrobrevin, a member of the dystrophin-related protein family. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=95 |issue= 1 |pages= 241-6 |year= 1998 |pmid= 9419360 |doi= }}
*{{cite journal | author=Nawrotzki R, Loh NY, Ruegg MA, ''et al.'' |title=Characterisation of alpha-dystrobrevin in muscle. |journal=J. Cell. Sci. |volume=111 ( Pt 17) |issue= |pages= 2595-605 |year= 1999 |pmid= 9701558 |doi= }}
*{{cite journal | author=Blake DJ, Hawkes R, Benson MA, Beesley PW |title=Different dystrophin-like complexes are expressed in neurons and glia. |journal=J. Cell Biol. |volume=147 |issue= 3 |pages= 645-58 |year= 1999 |pmid= 10545507 |doi= }}
*{{cite journal | author=Sadoulet-Puccio HM, Feener CA, Schaid DJ, ''et al.'' |title=The genomic organization of human dystrobrevin. |journal=Neurogenetics |volume=1 |issue= 1 |pages= 37-42 |year= 2000 |pmid= 10735273 |doi= }}
*{{cite journal | author=Piluso G, Mirabella M, Ricci E, ''et al.'' |title=Gamma1- and gamma2-syntrophins, two novel dystrophin-binding proteins localized in neuronal cells. |journal=J. Biol. Chem. |volume=275 |issue= 21 |pages= 15851-60 |year= 2000 |pmid= 10747910 |doi= 10.1074/jbc.M000439200 }}
*{{cite journal | author=Yoshida M, Hama H, Ishikawa-Sakurai M, ''et al.'' |title=Biochemical evidence for association of dystrobrevin with the sarcoglycan-sarcospan complex as a basis for understanding sarcoglycanopathy. |journal=Hum. Mol. Genet. |volume=9 |issue= 7 |pages= 1033-40 |year= 2000 |pmid= 10767327 |doi= }}
*{{cite journal | author=Tommasi di Vignano A, Di Zenzo G, Sudol M, ''et al.'' |title=Contribution of the different modules in the utrophin carboxy-terminal region to the formation and regulation of the DAP complex. |journal=FEBS Lett. |volume=471 |issue= 2-3 |pages= 229-34 |year= 2000 |pmid= 10767429 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on DVL1... {November 18, 2007 9:44:09 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:44:32 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_DVL1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1fsh.
| PDB = {{PDB2|1fsh}}, {{PDB2|1mc7}}
| Name = Dishevelled, dsh homolog 1 (Drosophila)
| HGNCid = 3084
| Symbol = DVL1
| AltSymbols =; DVL; MGC54245
| OMIM = 601365
| ECnumber =
| Homologene = 20926
| MGIid = 94941
| Function = {{GNF_GO|id=GO:0004871 |text = signal transducer activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0007222 |text = Wnt receptor signaling pathway}} {{GNF_GO|id=GO:0007242 |text = intracellular signaling cascade}} {{GNF_GO|id=GO:0007275 |text = multicellular organismal development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0009653 |text = anatomical structure morphogenesis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 1855
| Hs_Ensembl =
| Hs_RefseqProtein = NP_004412
| Hs_RefseqmRNA = NM_004421
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 13542
| Mm_Ensembl = ENSMUSG00000029071
| Mm_RefseqmRNA = NM_010091
| Mm_RefseqProtein = NP_034221
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 4
| Mm_GenLoc_start = 154691212
| Mm_GenLoc_end = 154703103
| Mm_Uniprot = Q3TRW4
}}
}}
'''Dishevelled, dsh homolog 1 (Drosophila)''', also known as '''DVL1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1855| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = DVL1, the human homolog of the Drosophila dishevelled gene (dsh) encodes a cytoplasmic phosphoprotein that regulates cell proliferation, acting as a transducer molecule for developmental processes, including segmentation and neuroblast specification. DVL1 is a candidate gene for neuroblastomatous transformation. The Schwartz-Jampel syndrome and Charcot-Marie-Tooth disease type 2A have been mapped to the same region as DVL1. The phenotypes of these diseases may be consistent with defects which might be expected from aberrant expression of a DVL gene during development. Three transcript variants encoding three different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: DVL1 dishevelled, dsh homolog 1 (Drosophila)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1855| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wharton KA |title=Runnin' with the Dvl: proteins that associate with Dsh/Dvl and their significance to Wnt signal transduction. |journal=Dev. Biol. |volume=253 |issue= 1 |pages= 1-17 |year= 2003 |pmid= 12490194 |doi= }}
*{{cite journal | author=Klingensmith J, Nusse R, Perrimon N |title=The Drosophila segment polarity gene dishevelled encodes a novel protein required for response to the wingless signal. |journal=Genes Dev. |volume=8 |issue= 1 |pages= 118-30 |year= 1994 |pmid= 8288125 |doi= }}
*{{cite journal | author=Pizzuti A, Novelli G, Mari A, ''et al.'' |title=Human homologue sequences to the Drosophila dishevelled segment-polarity gene are deleted in the DiGeorge syndrome. |journal=Am. J. Hum. Genet. |volume=58 |issue= 4 |pages= 722-9 |year= 1996 |pmid= 8644734 |doi= }}
*{{cite journal | author=Pizzuti A, Amati F, Calabrese G, ''et al.'' |title=cDNA characterization and chromosomal mapping of two human homologues of the Drosophila dishevelled polarity gene. |journal=Hum. Mol. Genet. |volume=5 |issue= 7 |pages= 953-8 |year= 1997 |pmid= 8817329 |doi= }}
*{{cite journal | author=Steitz SA, Tsang M, Sussman DJ |title=Wnt-mediated relocalization of dishevelled proteins. |journal=In Vitro Cell. Dev. Biol. Anim. |volume=32 |issue= 7 |pages= 441-5 |year= 1997 |pmid= 8856345 |doi= }}
*{{cite journal | author=Semënov MV, Snyder M |title=Human dishevelled genes constitute a DHR-containing multigene family. |journal=Genomics |volume=42 |issue= 2 |pages= 302-10 |year= 1997 |pmid= 9192851 |doi= 10.1006/geno.1997.4713 }}
*{{cite journal | author=Bui TD, Beier DR, Jonssen M, ''et al.'' |title=cDNA cloning of a human dishevelled DVL-3 gene, mapping to 3q27, and expression in human breast and colon carcinomas. |journal=Biochem. Biophys. Res. Commun. |volume=239 |issue= 2 |pages= 510-6 |year= 1997 |pmid= 9344861 |doi= 10.1006/bbrc.1997.7500 }}
*{{cite journal | author=Ikeda S, Kishida S, Yamamoto H, ''et al.'' |title=Axin, a negative regulator of the Wnt signaling pathway, forms a complex with GSK-3beta and beta-catenin and promotes GSK-3beta-dependent phosphorylation of beta-catenin. |journal=EMBO J. |volume=17 |issue= 5 |pages= 1371-84 |year= 1998 |pmid= 9482734 |doi= 10.1093/emboj/17.5.1371 }}
*{{cite journal | author=Kishida S, Yamamoto H, Hino S, ''et al.'' |title=DIX domains of Dvl and axin are necessary for protein interactions and their ability to regulate beta-catenin stability. |journal=Mol. Cell. Biol. |volume=19 |issue= 6 |pages= 4414-22 |year= 1999 |pmid= 10330181 |doi= }}
*{{cite journal | author=Fagotto F, Jho E, Zeng L, ''et al.'' |title=Domains of axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization. |journal=J. Cell Biol. |volume=145 |issue= 4 |pages= 741-56 |year= 1999 |pmid= 10330403 |doi= }}
*{{cite journal | author=Li L, Yuan H, Weaver CD, ''et al.'' |title=Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1. |journal=EMBO J. |volume=18 |issue= 15 |pages= 4233-40 |year= 1999 |pmid= 10428961 |doi= 10.1093/emboj/18.15.4233 }}
*{{cite journal | author=Inobe M, Katsube K, Miyagoe Y, ''et al.'' |title=Identification of EPS8 as a Dvl1-associated molecule. |journal=Biochem. Biophys. Res. Commun. |volume=266 |issue= 1 |pages= 216-21 |year= 2000 |pmid= 10581192 |doi= 10.1006/bbrc.1999.1782 }}
*{{cite journal | author=Strovel ET, Wu D, Sussman DJ |title=Protein phosphatase 2Calpha dephosphorylates axin and activates LEF-1-dependent transcription. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2399-403 |year= 2000 |pmid= 10644691 |doi= }}
*{{cite journal | author=Song DH, Sussman DJ, Seldin DC |title=Endogenous protein kinase CK2 participates in Wnt signaling in mammary epithelial cells. |journal=J. Biol. Chem. |volume=275 |issue= 31 |pages= 23790-7 |year= 2000 |pmid= 10806215 |doi= 10.1074/jbc.M909107199 }}
*{{cite journal | author=Hino S, Kishida S, Michiue T, ''et al.'' |title=Inhibition of the Wnt signaling pathway by Idax, a novel Dvl-binding protein. |journal=Mol. Cell. Biol. |volume=21 |issue= 1 |pages= 330-42 |year= 2001 |pmid= 11113207 |doi= 10.1128/MCB.21.1.330-342.2001 }}
*{{cite journal | author=Rubinfeld B, Tice DA, Polakis P |title=Axin-dependent phosphorylation of the adenomatous polyposis coli protein mediated by casein kinase 1epsilon. |journal=J. Biol. Chem. |volume=276 |issue= 42 |pages= 39037-45 |year= 2001 |pmid= 11487578 |doi= 10.1074/jbc.M105148200 }}
*{{cite journal | author=Chen W, Hu LA, Semenov MV, ''et al.'' |title=beta-Arrestin1 modulates lymphoid enhancer factor transcriptional activity through interaction with phosphorylated dishevelled proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 14889-94 |year= 2002 |pmid= 11742073 |doi= 10.1073/pnas.211572798 }}
*{{cite journal | author=Habas R, Kato Y, He X |title=Wnt/Frizzled activation of Rho regulates vertebrate gastrulation and requires a novel Formin homology protein Daam1. |journal=Cell |volume=107 |issue= 7 |pages= 843-54 |year= 2002 |pmid= 11779461 |doi= }}
*{{cite journal | author=Russ C, Lovestone S, Powell JF |title=Identification of genomic organisation, sequence variants and analysis of the role of the human dishevelled 1 gene in late onset Alzheimer's disease. |journal=Mol. Psychiatry |volume=7 |issue= 1 |pages= 104-9 |year= 2002 |pmid= 11803455 |doi= 10.1038/sj/mp/4000941 }}
*{{cite journal | author=Gao ZH, Seeling JM, Hill V, ''et al.'' |title=Casein kinase I phosphorylates and destabilizes the beta-catenin degradation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 3 |pages= 1182-7 |year= 2002 |pmid= 11818547 |doi= 10.1073/pnas.032468199 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ESRRA... {November 18, 2007 9:44:32 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:45:05 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ESRRA_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lo1.
| PDB = {{PDB2|1lo1}}, {{PDB2|1xb7}}
| Name = Estrogen-related receptor alpha
| HGNCid = 3471
| Symbol = ESRRA
| AltSymbols =; ERR1; ERRa; ERRalpha; ESRL1; NR3B1
| OMIM = 601998
| ECnumber =
| Homologene = 20941
| MGIid = 1346831
| GeneAtlas_image1 = PBB_GE_ESRRA_1487_at_tn.png
| GeneAtlas_image2 = PBB_GE_ESRRA_203193_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005496 |text = steroid binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016439 |text = tRNA-pseudouridine synthase activity}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2101
| Hs_Ensembl = ENSG00000173153
| Hs_RefseqProtein = NP_004442
| Hs_RefseqmRNA = NM_004451
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 63829616
| Hs_GenLoc_end = 63840786
| Hs_Uniprot = P11474
| Mm_EntrezGene = 26379
| Mm_Ensembl = ENSMUSG00000024955
| Mm_RefseqmRNA = NM_007953
| Mm_RefseqProtein = NP_031979
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 6978022
| Mm_GenLoc_end = 6988862
| Mm_Uniprot = Q3U110
}}
}}
'''Estrogen-related receptor alpha''', also known as '''ESRRA''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ESRRA estrogen-related receptor alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2101| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a nuclear receptor that is closely related to the estrogen receptor. This protein acts as a site-specific transcription regulator and has been also shown to interact with estrogen and the transcripton factor TFIIB by direct protein-protein contact. The binding and regulatory activities of this protein have been demonstrated in the regulation of a variety of genes including lactoferrin, osteopontin, medium-chain acyl coenzyme A dehydrogenase (MCAD) and thyroid hormone receptor genes. A processed pseudogene of ESRRA is located on chromosome 13q12.1.<ref name="entrez">{{cite web | title = Entrez Gene: ESRRA estrogen-related receptor alpha| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2101| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Giguère V, Yang N, Segui P, Evans RM |title=Identification of a new class of steroid hormone receptors. |journal=Nature |volume=331 |issue= 6151 |pages= 91-4 |year= 1988 |pmid= 3267207 |doi= 10.1038/331091a0 }}
*{{cite journal | author=Wiley SR, Kraus RJ, Zuo F, ''et al.'' |title=SV40 early-to-late switch involves titration of cellular transcriptional repressors. |journal=Genes Dev. |volume=7 |issue= 11 |pages= 2206-19 |year= 1993 |pmid= 8224847 |doi= }}
*{{cite journal | author=Yang N, Shigeta H, Shi H, Teng CT |title=Estrogen-related receptor, hERR1, modulates estrogen receptor-mediated response of human lactoferrin gene promoter. |journal=J. Biol. Chem. |volume=271 |issue= 10 |pages= 5795-804 |year= 1996 |pmid= 8621448 |doi= }}
*{{cite journal | author=Johnston SD, Liu X, Zuo F, ''et al.'' |title=Estrogen-related receptor alpha 1 functionally binds as a monomer to extended half-site sequences including ones contained within estrogen-response elements. |journal=Mol. Endocrinol. |volume=11 |issue= 3 |pages= 342-52 |year= 1997 |pmid= 9058380 |doi= }}
*{{cite journal | author=Sladek R, Bader JA, Giguère V |title=The orphan nuclear receptor estrogen-related receptor alpha is a transcriptional regulator of the human medium-chain acyl coenzyme A dehydrogenase gene. |journal=Mol. Cell. Biol. |volume=17 |issue= 9 |pages= 5400-9 |year= 1997 |pmid= 9271417 |doi= }}
*{{cite journal | author=Shi H, Shigeta H, Yang N, ''et al.'' |title=Human estrogen receptor-like 1 (ESRL1) gene: genomic organization, chromosomal localization, and promoter characterization. |journal=Genomics |volume=44 |issue= 1 |pages= 52-60 |year= 1997 |pmid= 9286700 |doi= 10.1006/geno.1997.4850 }}
*{{cite journal | author=Sladek R, Beatty B, Squire J, ''et al.'' |title=Chromosomal mapping of the human and murine orphan receptors ERRalpha (ESRRA) and ERRbeta (ESRRB) and identification of a novel human ERRalpha-related pseudogene. |journal=Genomics |volume=45 |issue= 2 |pages= 320-6 |year= 1998 |pmid= 9344655 |doi= 10.1006/geno.1997.4939 }}
*{{cite journal | author=Vanacker JM, Bonnelye E, Delmarre C, Laudet V |title=Activation of the thyroid hormone receptor alpha gene promoter by the orphan nuclear receptor ERR alpha. |journal=Oncogene |volume=17 |issue= 19 |pages= 2429-35 |year= 1998 |pmid= 9824153 |doi= 10.1038/sj.onc.1202167 }}
*{{cite journal | author=Zhang Z, Teng CT |title=Estrogen receptor alpha and estrogen receptor-related receptor alpha1 compete for binding and coactivator. |journal=Mol. Cell. Endocrinol. |volume=172 |issue= 1-2 |pages= 223-33 |year= 2001 |pmid= 11165056 |doi= }}
*{{cite journal | author=Eiler S, Gangloff M, Duclaud S, ''et al.'' |title=Overexpression, purification, and crystal structure of native ER alpha LBD. |journal=Protein Expr. Purif. |volume=22 |issue= 2 |pages= 165-73 |year= 2001 |pmid= 11437591 |doi= 10.1006/prep.2001.1409 }}
*{{cite journal | author=Zhou D, Chen S |title=PNRC2 is a 16 kDa coactivator that interacts with nuclear receptors through an SH3-binding motif. |journal=Nucleic Acids Res. |volume=29 |issue= 19 |pages= 3939-48 |year= 2001 |pmid= 11574675 |doi= }}
*{{cite journal | author=Tchernev VT, Mansfield TA, Giot L, ''et al.'' |title=The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins. |journal=Mol. Med. |volume=8 |issue= 1 |pages= 56-64 |year= 2002 |pmid= 11984006 |doi= }}
*{{cite journal | author=Kraus RJ, Ariazi EA, Farrell ML, Mertz JE |title=Estrogen-related receptor alpha 1 actively antagonizes estrogen receptor-regulated transcription in MCF-7 mammary cells. |journal=J. Biol. Chem. |volume=277 |issue= 27 |pages= 24826-34 |year= 2002 |pmid= 11986328 |doi= 10.1074/jbc.M202952200 }}
*{{cite journal | author=Ichida M, Nemoto S, Finkel T |title=Identification of a specific molecular repressor of the peroxisome proliferator-activated receptor gamma Coactivator-1 alpha (PGC-1alpha). |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50991-5 |year= 2003 |pmid= 12397057 |doi= 10.1074/jbc.M210262200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Schreiber SN, Knutti D, Brogli K, ''et al.'' |title=The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha). |journal=J. Biol. Chem. |volume=278 |issue= 11 |pages= 9013-8 |year= 2003 |pmid= 12522104 |doi= 10.1074/jbc.M212923200 }}
*{{cite journal | author=Igarashi M, Kawaguchi Y, Hirai K, Mizuno F |title=Physical interaction of Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) with human oestrogen-related receptor 1 (hERR1): hERR1 interacts with a conserved domain of EBNA-LP that is critical for EBV-induced B-cell immortalization. |journal=J. Gen. Virol. |volume=84 |issue= Pt 2 |pages= 319-27 |year= 2003 |pmid= 12560563 |doi= }}
*{{cite journal | author=Sengupta K, Banerjee S, Saxena N, Banerjee SK |title=Estradiol-induced vascular endothelial growth factor-A expression in breast tumor cells is biphasic and regulated by estrogen receptor-alpha dependent pathway. |journal=Int. J. Oncol. |volume=22 |issue= 3 |pages= 609-14 |year= 2003 |pmid= 12579315 |doi= }}
*{{cite journal | author=Sumi D, Ignarro LJ |title=Estrogen-related receptor alpha 1 up-regulates endothelial nitric oxide synthase expression. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=100 |issue= 24 |pages= 14451-6 |year= 2004 |pmid= 14610283 |doi= 10.1073/pnas.2235590100 }}
*{{cite journal | author=Laganière J, Tremblay GB, Dufour CR, ''et al.'' |title=A polymorphic autoregulatory hormone response element in the human estrogen-related receptor alpha (ERRalpha) promoter dictates peroxisome proliferator-activated receptor gamma coactivator-1alpha control of ERRalpha expression. |journal=J. Biol. Chem. |volume=279 |issue= 18 |pages= 18504-10 |year= 2004 |pmid= 14978033 |doi= 10.1074/jbc.M313543200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FKBP4... {November 18, 2007 9:45:05 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:45:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_FKBP4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1n1a.
| PDB = {{PDB2|1n1a}}, {{PDB2|1p5q}}, {{PDB2|1q1c}}, {{PDB2|1qz2}}, {{PDB2|1rot}}, {{PDB2|1rou}}
| Name = FK506 binding protein 4, 59kDa
| HGNCid = 3720
| Symbol = FKBP4
| AltSymbols =; PPIase; FKBP52; FKBP59; HBI; Hsp56; p52
| OMIM = 600611
| ECnumber =
| Homologene = 36085
| MGIid = 95543
| GeneAtlas_image1 = PBB_GE_FKBP4_200895_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_FKBP4_200894_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003755 |text = peptidyl-prolyl cis-trans isomerase activity}} {{GNF_GO|id=GO:0005524 |text = ATP binding}} {{GNF_GO|id=GO:0005525 |text = GTP binding}} {{GNF_GO|id=GO:0005528 |text = FK506 binding}} {{GNF_GO|id=GO:0016853 |text = isomerase activity}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}} {{GNF_GO|id=GO:0031072 |text = heat shock protein binding}} {{GNF_GO|id=GO:0035259 |text = glucocorticoid receptor binding}} {{GNF_GO|id=GO:0051219 |text = phosphoprotein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006457 |text = protein folding}} {{GNF_GO|id=GO:0006463 |text = steroid hormone receptor complex assembly}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0031503 |text = protein complex localization}} {{GNF_GO|id=GO:0046661 |text = male sex differentiation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2288
| Hs_Ensembl = ENSG00000004478
| Hs_RefseqProtein = NP_002005
| Hs_RefseqmRNA = NM_002014
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 12
| Hs_GenLoc_start = 2774414
| Hs_GenLoc_end = 2783381
| Hs_Uniprot = Q02790
| Mm_EntrezGene = 14228
| Mm_Ensembl = ENSMUSG00000030357
| Mm_RefseqmRNA = NM_010219
| Mm_RefseqProtein = NP_034349
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 128395157
| Mm_GenLoc_end = 128404275
| Mm_Uniprot = Q8CBS1
}}
}}
'''FK506 binding protein 4, 59kDa''', also known as '''FKBP4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: FKBP4 FK506 binding protein 4, 59kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2288| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is a member of the immunophilin protein family, which play a role in immunoregulation and basic cellular processes involving protein folding and trafficking. This encoded protein is a cis-trans prolyl isomerase that binds to the immunosuppressants FK506 and rapamycin. It has high structural and functional similarity to FK506-binding protein 1A (FKBP1A), but unlike FKBP1A, this protein does not have immunosuppressant activity when complexed with FK506. It interacts with interferon regulatory factor-4 and plays an important role in immunoregulatory gene expression in B and T lymphocytes. This encoded protein is known to associate with phytanoyl-CoA alpha-hydroxylase. It can also associate with two heat shock proteins (hsp90 and hsp70) and thus may play a role in the intracellular trafficking of hetero-oligomeric forms of the steroid hormone receptors. This protein correlates strongly with adeno-associated virus type 2 vectors (AAV) resulting in a significant increase in AAV-mediated transgene expression in human cell lines. Thus this encoded protein is thought to have important implications for the optimal use of AAV vectors in human gene therapy. This gene has been found to have multiple polyadenylation sites.<ref name="entrez">{{cite web | title = Entrez Gene: FKBP4 FK506 binding protein 4, 59kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2288| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schiene-Fischer C, Yu C |title=Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. |journal=FEBS Lett. |volume=495 |issue= 1-2 |pages= 1-6 |year= 2001 |pmid= 11322937 |doi= }}
*{{cite journal | author=Peattie DA, Harding MW, Fleming MA, ''et al.'' |title=Expression and characterization of human FKBP52, an immunophilin that associates with the 90-kDa heat shock protein and is a component of steroid receptor complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 22 |pages= 10974-8 |year= 1992 |pmid= 1279700 |doi= }}
*{{cite journal | author=Yem AW, Tomasselli AG, Heinrikson RL, ''et al.'' |title=The Hsp56 component of steroid receptor complexes binds to immobilized FK506 and shows homology to FKBP-12 and FKBP-13. |journal=J. Biol. Chem. |volume=267 |issue= 5 |pages= 2868-71 |year= 1992 |pmid= 1371107 |doi= }}
*{{cite journal | author=Tai PK, Albers MW, Chang H, ''et al.'' |title=Association of a 59-kilodalton immunophilin with the glucocorticoid receptor complex. |journal=Science |volume=256 |issue= 5061 |pages= 1315-8 |year= 1992 |pmid= 1376003 |doi= }}
*{{cite journal | author=Wiederrecht G, Hung S, Chan HK, ''et al.'' |title=Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506-binding protein as well as a protein complex. |journal=J. Biol. Chem. |volume=267 |issue= 30 |pages= 21753-60 |year= 1992 |pmid= 1383226 |doi= }}
*{{cite journal | author=Sanchez ER, Faber LE, Henzel WJ, Pratt WB |title=The 56-59-kilodalton protein identified in untransformed steroid receptor complexes is a unique protein that exists in cytosol in a complex with both the 70- and 90-kilodalton heat shock proteins. |journal=Biochemistry |volume=29 |issue= 21 |pages= 5145-52 |year= 1990 |pmid= 2378870 |doi= }}
*{{cite journal | author=Alnemri ES, Fernandes-Alnemri T, Nelki DS, ''et al.'' |title=Overexpression, characterization, and purification of a recombinant mouse immunophilin FKBP-52 and identification of an associated phosphoprotein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 14 |pages= 6839-43 |year= 1993 |pmid= 8341706 |doi= }}
*{{cite journal | author=Chambraud B, Radanyi C, Camonis JH, ''et al.'' |title=FAP48, a new protein that forms specific complexes with both immunophilins FKBP59 and FKBP12. Prevention by the immunosuppressant drugs FK506 and rapamycin. |journal=J. Biol. Chem. |volume=271 |issue= 51 |pages= 32923-9 |year= 1997 |pmid= 8955134 |doi= }}
*{{cite journal | author=Bruner KL, Derfoul A, Robertson NM, ''et al.'' |title=The unliganded mineralocorticoid receptor is associated with heat shock proteins 70 and 90 and the immunophilin FKBP-52. |journal=Receptors & signal transduction |volume=7 |issue= 2 |pages= 85-98 |year= 1998 |pmid= 9392437 |doi= }}
*{{cite journal | author=Miyata Y, Chambraud B, Radanyi C, ''et al.'' |title=Phosphorylation of the immunosuppressant FK506-binding protein FKBP52 by casein kinase II: regulation of HSP90-binding activity of FKBP52. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 26 |pages= 14500-5 |year= 1998 |pmid= 9405642 |doi= }}
*{{cite journal | author=Bermingham NA, Rauf S, Katsanis N, ''et al.'' |title=The immunophilin FKBP4 (FKBP52/FKBP59) maps to the distal short arm of human chromosome 12. |journal=Mamm. Genome |volume=9 |issue= 3 |pages= 268 |year= 1998 |pmid= 9501323 |doi= }}
*{{cite journal | author=Chambraud B, Radanyi C, Camonis JH, ''et al.'' |title=Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 5 |pages= 2104-9 |year= 1999 |pmid= 10051602 |doi= }}
*{{cite journal | author=Mamane Y, Sharma S, Petropoulos L, ''et al.'' |title=Posttranslational regulation of IRF-4 activity by the immunophilin FKBP52. |journal=Immunity |volume=12 |issue= 2 |pages= 129-40 |year= 2000 |pmid= 10714679 |doi= }}
*{{cite journal | author=Neye H |title=Mutation of FKBP associated protein 48 (FAP48) at proline 219 disrupts the interaction with FKBP12 and FKBP52. |journal=Regul. Pept. |volume=97 |issue= 2-3 |pages= 147-52 |year= 2001 |pmid= 11164950 |doi= }}
*{{cite journal | author=Galigniana MD, Radanyi C, Renoir JM, ''et al.'' |title=Evidence that the peptidylprolyl isomerase domain of the hsp90-binding immunophilin FKBP52 is involved in both dynein interaction and glucocorticoid receptor movement to the nucleus. |journal=J. Biol. Chem. |volume=276 |issue= 18 |pages= 14884-9 |year= 2001 |pmid= 11278753 |doi= 10.1074/jbc.M010809200 }}
*{{cite journal | author=Qing K, Hansen J, Weigel-Kelley KA, ''et al.'' |title=Adeno-associated virus type 2-mediated gene transfer: role of cellular FKBP52 protein in transgene expression. |journal=J. Virol. |volume=75 |issue= 19 |pages= 8968-76 |year= 2001 |pmid= 11533160 |doi= 10.1128/JVI.75.19.8968-8976.2001 }}
*{{cite journal | author=Guo Y, Guettouche T, Fenna M, ''et al.'' |title=Evidence for a mechanism of repression of heat shock factor 1 transcriptional activity by a multichaperone complex. |journal=J. Biol. Chem. |volume=276 |issue= 49 |pages= 45791-9 |year= 2002 |pmid= 11583998 |doi= 10.1074/jbc.M105931200 }}
*{{cite journal | author=Davies TH, Ning YM, Sánchez ER |title=A new first step in activation of steroid receptors: hormone-induced switching of FKBP51 and FKBP52 immunophilins. |journal=J. Biol. Chem. |volume=277 |issue= 7 |pages= 4597-600 |year= 2002 |pmid= 11751894 |doi= 10.1074/jbc.C100531200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on FPRL1... {November 18, 2007 9:45:56 PM PST}
- SEARCH REDIRECT: Control Box Found: FPRL1 {November 18, 2007 9:46:40 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:46:43 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:46:43 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:46:43 PM PST}
- UPDATED: Updated protein page: FPRL1 {November 18, 2007 9:46:53 PM PST}
- INFO: Beginning work on GABRB3... {November 18, 2007 9:46:53 PM PST}
- SEARCH REDIRECT: Control Box Found: GABRB3 {November 18, 2007 9:47:36 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:47:39 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:47:39 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:47:39 PM PST}
- UPDATED: Updated protein page: GABRB3 {November 18, 2007 9:47:56 PM PST}
- INFO: Beginning work on GRIK2... {November 18, 2007 9:47:56 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:48:48 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_GRIK2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s50.
| PDB = {{PDB2|1s50}}, {{PDB2|1s7y}}, {{PDB2|1s9t}}, {{PDB2|1sd3}}, {{PDB2|1tt1}}, {{PDB2|1yae}}, {{PDB2|2i0b}}, {{PDB2|2i0c}}
| Name = Glutamate receptor, ionotropic, kainate 2
| HGNCid = 4580
| Symbol = GRIK2
| AltSymbols =; EAA4; GLR6; GLUR6; MGC74427
| OMIM = 138244
| ECnumber =
| Homologene = 40717
| MGIid = 95815
| GeneAtlas_image1 = PBB_GE_GRIK2_213845_at_tn.png
| GeneAtlas_image2 = PBB_GE_GRIK2_215655_at_tn.png
| Function = {{GNF_GO|id=GO:0004872 |text = receptor activity}} {{GNF_GO|id=GO:0005216 |text = ion channel activity}} {{GNF_GO|id=GO:0005234 |text = extracellular-glutamate-gated ion channel activity}} {{GNF_GO|id=GO:0015277 |text = kainate selective glutamate receptor activity}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0045211 |text = postsynaptic membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0007215 |text = glutamate signaling pathway}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}} {{GNF_GO|id=GO:0031557 |text = induction of programmed cell death in response to chemical stimulus}} {{GNF_GO|id=GO:0048172 |text = regulation of short-term neuronal synaptic plasticity}} {{GNF_GO|id=GO:0050806 |text = positive regulation of synaptic transmission}} {{GNF_GO|id=GO:0051402 |text = neuron apoptosis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2898
| Hs_Ensembl = ENSG00000164418
| Hs_RefseqProtein = NP_068775
| Hs_RefseqmRNA = NM_021956
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 101953385
| Hs_GenLoc_end = 102624651
| Hs_Uniprot = Q13002
| Mm_EntrezGene = 14806
| Mm_Ensembl = ENSMUSG00000056073
| Mm_RefseqmRNA = NM_010349
| Mm_RefseqProtein = NP_034479
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 10
| Mm_GenLoc_start = 48789583
| Mm_GenLoc_end = 49471674
| Mm_Uniprot = P39087
}}
}}
'''Glutamate receptor, ionotropic, kainate 2''', also known as '''GRIK2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GRIK2 glutamate receptor, ionotropic, kainate 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2898| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a subunit of a kainate glutamate receptor. Glutamate receptors mediate the majority of excitatory neurotransmission in the brain. This receptor may have a role in synaptic plasticity and may be important for learning and memory. It also may be involved in the transmission of light information from the retina to the hypothalamus. The structure and function of the encoded protein is changed by RNA editing. Alternatively spliced transcript variants encoding distinct isoforms have been described for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: GRIK2 glutamate receptor, ionotropic, kainate 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2898| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Seeburg PH, Higuchi M, Sprengel R |title=RNA editing of brain glutamate receptor channels: mechanism and physiology. |journal=Brain Res. Brain Res. Rev. |volume=26 |issue= 2-3 |pages= 217-29 |year= 1998 |pmid= 9651532 |doi= }}
*{{cite journal | author=Paschen W, Hedreen JC, Ross CA |title=RNA editing of the glutamate receptor subunits GluR2 and GluR6 in human brain tissue. |journal=J. Neurochem. |volume=63 |issue= 5 |pages= 1596-602 |year= 1994 |pmid= 7523595 |doi= }}
*{{cite journal | author=Hoo KH, Nutt SL, Fletcher EJ, ''et al.'' |title=Functional expression and pharmacological characterization of the human EAA4 (GluR6) glutamate receptor: a kainate selective channel subunit. |journal=Recept. Channels |volume=2 |issue= 4 |pages= 327-37 |year= 1995 |pmid= 7536611 |doi= }}
*{{cite journal | author=Sander T, Janz D, Ramel C, ''et al.'' |title=Refinement of map position of the human GluR6 kainate receptor gene (GRIK2) and lack of association and linkage with idiopathic generalized epilepsies. |journal=Neurology |volume=45 |issue= 9 |pages= 1713-20 |year= 1995 |pmid= 7675232 |doi= }}
*{{cite journal | author=Nutt SL, Kamboj RK |title=RNA editing of human kainate receptor subunits. |journal=Neuroreport |volume=5 |issue= 18 |pages= 2625-9 |year= 1995 |pmid= 7696618 |doi= }}
*{{cite journal | author=Paschen W, Blackstone CD, Huganir RL, Ross CA |title=Human GluR6 kainate receptor (GRIK2): molecular cloning, expression, polymorphism, and chromosomal assignment. |journal=Genomics |volume=20 |issue= 3 |pages= 435-40 |year= 1994 |pmid= 8034316 |doi= 10.1006/geno.1994.1198 }}
*{{cite journal | author=Raymond LA, Blackstone CD, Huganir RL |title=Phosphorylation and modulation of recombinant GluR6 glutamate receptors by cAMP-dependent protein kinase. |journal=Nature |volume=361 |issue= 6413 |pages= 637-41 |year= 1993 |pmid= 8094892 |doi= 10.1038/361637a0 }}
*{{cite journal | author=Roche KW, Raymond LA, Blackstone C, Huganir RL |title=Transmembrane topology of the glutamate receptor subunit GluR6. |journal=J. Biol. Chem. |volume=269 |issue= 16 |pages= 11679-82 |year= 1994 |pmid= 8163463 |doi= }}
*{{cite journal | author=Taverna FA, Wang LY, MacDonald JF, Hampson DR |title=A transmembrane model for an ionotropic glutamate receptor predicted on the basis of the location of asparagine-linked oligosaccharides. |journal=J. Biol. Chem. |volume=269 |issue= 19 |pages= 14159-64 |year= 1994 |pmid= 8188697 |doi= }}
*{{cite journal | author=Wenthold RJ, Trumpy VA, Zhu WS, Petralia RS |title=Biochemical and assembly properties of GluR6 and KA2, two members of the kainate receptor family, determined with subunit-specific antibodies. |journal=J. Biol. Chem. |volume=269 |issue= 2 |pages= 1332-9 |year= 1994 |pmid= 8288598 |doi= }}
*{{cite journal | author=Pickering DS, Taverna FA, Salter MW, Hampson DR |title=Palmitoylation of the GluR6 kainate receptor. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 26 |pages= 12090-4 |year= 1996 |pmid= 8618850 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Porter RH, Eastwood SL, Harrison PJ |title=Distribution of kainate receptor subunit mRNAs in human hippocampus, neocortex and cerebellum, and bilateral reduction of hippocampal GluR6 and KA2 transcripts in schizophrenia. |journal=Brain Res. |volume=751 |issue= 2 |pages= 217-31 |year= 1997 |pmid= 9099808 |doi= }}
*{{cite journal | author=Rubinsztein DC, Leggo J, Chiano M, ''et al.'' |title=Genotypes at the GluR6 kainate receptor locus are associated with variation in the age of onset of Huntington disease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 8 |pages= 3872-6 |year= 1997 |pmid= 9108071 |doi= }}
*{{cite journal | author=Ripellino JA, Neve RL, Howe JR |title=Expression and heteromeric interactions of non-N-methyl-D-aspartate glutamate receptor subunits in the developing and adult cerebellum. |journal=Neuroscience |volume=82 |issue= 2 |pages= 485-97 |year= 1998 |pmid= 9466455 |doi= }}
*{{cite journal | author=Garcia EP, Mehta S, Blair LA, ''et al.'' |title=SAP90 binds and clusters kainate receptors causing incomplete desensitization. |journal=Neuron |volume=21 |issue= 4 |pages= 727-39 |year= 1998 |pmid= 9808460 |doi= }}
*{{cite journal | author=Leuschner WD, Hoch W |title=Subtype-specific assembly of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptor subunits is mediated by their n-terminal domains. |journal=J. Biol. Chem. |volume=274 |issue= 24 |pages= 16907-16 |year= 1999 |pmid= 10358037 |doi= }}
*{{cite journal | author=Smith HJ |title=The introduction of MR in the Nordic countries with special reference to Norway: central control versus local initiatives. |journal=Journal of magnetic resonance imaging : JMRI |volume=13 |issue= 4 |pages= 639-44 |year= 2001 |pmid= 11276111 |doi= }}
*{{cite journal | author=Mehta S, Wu H, Garner CC, Marshall J |title=Molecular mechanisms regulating the differential association of kainate receptor subunits with SAP90/PSD-95 and SAP97. |journal=J. Biol. Chem. |volume=276 |issue= 19 |pages= 16092-9 |year= 2001 |pmid= 11279111 |doi= 10.1074/jbc.M100643200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on GTF2H4... {November 18, 2007 9:48:48 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:49:21 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = General transcription factor IIH, polypeptide 4, 52kDa
| HGNCid = 4658
| Symbol = GTF2H4
| AltSymbols =; TFIIH
| OMIM = 601760
| ECnumber =
| Homologene = 7090
| MGIid = 1338799
| GeneAtlas_image1 = PBB_GE_GTF2H4_203577_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003702 |text = RNA polymerase II transcription factor activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005675 |text = holo TFIIH complex}}
| Process = {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 2968
| Hs_Ensembl = ENSG00000137411
| Hs_RefseqProtein = NP_001508
| Hs_RefseqmRNA = NM_001517
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 6
| Hs_GenLoc_start = 30983997
| Hs_GenLoc_end = 31002215
| Hs_Uniprot = Q92759
| Mm_EntrezGene = 14885
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_010364
| Mm_RefseqProtein = NP_034494
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''General transcription factor IIH, polypeptide 4, 52kDa''', also known as '''GTF2H4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GTF2H4 general transcription factor IIH, polypeptide 4, 52kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2968| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24-7 |year= 1998 |pmid= 9570510 |doi= }}
*{{cite journal | author=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447-9 |year= 1998 |pmid= 9651670 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Blau J, Xiao H, McCracken S, ''et al.'' |title=Three functional classes of transcriptional activation domain. |journal=Mol. Cell. Biol. |volume=16 |issue= 5 |pages= 2044-55 |year= 1996 |pmid= 8628270 |doi= }}
*{{cite journal | author=Drapkin R, Le Roy G, Cho H, ''et al.'' |title=Human cyclin-dependent kinase-activating kinase exists in three distinct complexes. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 13 |pages= 6488-93 |year= 1996 |pmid= 8692842 |doi= }}
*{{cite journal | author=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605-10 |year= 1996 |pmid= 8849451 |doi= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi= }}
*{{cite journal | author=Marinoni JC, Roy R, Vermeulen W, ''et al.'' |title=Cloning and characterization of p52, the fifth subunit of the core of the transcription/DNA repair factor TFIIH. |journal=EMBO J. |volume=16 |issue= 5 |pages= 1093-102 |year= 1997 |pmid= 9118947 |doi= 10.1093/emboj/16.5.1093 }}
*{{cite journal | author=Cujec TP, Cho H, Maldonado E, ''et al.'' |title=The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme. |journal=Mol. Cell. Biol. |volume=17 |issue= 4 |pages= 1817-23 |year= 1997 |pmid= 9121429 |doi= }}
*{{cite journal | author=Rossignol M, Kolb-Cheynel I, Egly JM |title=Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. |journal=EMBO J. |volume=16 |issue= 7 |pages= 1628-37 |year= 1997 |pmid= 9130708 |doi= 10.1093/emboj/16.7.1628 }}
*{{cite journal | author=Scully R, Anderson SF, Chao DM, ''et al.'' |title=BRCA1 is a component of the RNA polymerase II holoenzyme. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 11 |pages= 5605-10 |year= 1997 |pmid= 9159119 |doi= }}
*{{cite journal | author=García-Martínez LF, Mavankal G, Neveu JM, ''et al.'' |title=Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription. |journal=EMBO J. |volume=16 |issue= 10 |pages= 2836-50 |year= 1997 |pmid= 9184228 |doi= 10.1093/emboj/16.10.2836 }}
*{{cite journal | author=Nekhai S, Shukla RR, Kumar A |title=A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity. |journal=J. Virol. |volume=71 |issue= 10 |pages= 7436-41 |year= 1997 |pmid= 9311822 |doi= }}
*{{cite journal | author=Cujec TP, Okamoto H, Fujinaga K, ''et al.'' |title=The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II. |journal=Genes Dev. |volume=11 |issue= 20 |pages= 2645-57 |year= 1997 |pmid= 9334327 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Li XY, Green MR |title=The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor. |journal=Genes Dev. |volume=12 |issue= 19 |pages= 2992-6 |year= 1998 |pmid= 9765201 |doi= }}
*{{cite journal | author=Ping YH, Rana TM |title=Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes. |journal=J. Biol. Chem. |volume=274 |issue= 11 |pages= 7399-404 |year= 1999 |pmid= 10066804 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HSPB8... {November 18, 2007 9:50:43 PM PST}
- SEARCH REDIRECT: Control Box Found: HSPB8 {November 18, 2007 9:51:26 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:51:28 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:51:28 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:51:28 PM PST}
- UPDATED: Updated protein page: HSPB8 {November 18, 2007 9:51:37 PM PST}
- INFO: Beginning work on HTRA2... {November 18, 2007 9:52:06 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:52:37 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_HTRA2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1lcy.
| PDB = {{PDB2|1lcy}}
| Name = HtrA serine peptidase 2
| HGNCid = 14348
| Symbol = HTRA2
| AltSymbols =; OMI; PARK13; PRSS25
| OMIM = 606441
| ECnumber =
| Homologene = 8300
| MGIid = 1928676
| GeneAtlas_image1 = PBB_GE_HTRA2_211152_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_HTRA2_203089_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}} {{GNF_GO|id=GO:0051082 |text = unfolded protein binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005758 |text = mitochondrial intermembrane space}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005789 |text = endoplasmic reticulum membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006950 |text = response to stress}} {{GNF_GO|id=GO:0007005 |text = mitochondrion organization and biogenesis}} {{GNF_GO|id=GO:0007628 |text = adult walking behavior}} {{GNF_GO|id=GO:0008629 |text = induction of apoptosis by intracellular signals}} {{GNF_GO|id=GO:0030900 |text = forebrain development}} {{GNF_GO|id=GO:0040014 |text = regulation of body size}} {{GNF_GO|id=GO:0048666 |text = neuron development}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 27429
| Hs_Ensembl = ENSG00000115317
| Hs_RefseqProtein = NP_037379
| Hs_RefseqmRNA = NM_013247
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 74610040
| Hs_GenLoc_end = 74614191
| Hs_Uniprot = O43464
| Mm_EntrezGene = 64704
| Mm_Ensembl = ENSMUSG00000068329
| Mm_RefseqmRNA = NM_019752
| Mm_RefseqProtein = NP_062726
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 83016938
| Mm_GenLoc_end = 83020229
| Mm_Uniprot = Q3TXN0
}}
}}
'''HtrA serine peptidase 2''', also known as '''HTRA2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: HTRA2 HtrA serine peptidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27429| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a serine protease. The protein has been localized in the endoplasmic reticulum and interacts with an alternatively spliced form of mitogen-activated protein kinase 14. The protein has also been localized to the mitochondria with release to the cytosol following apoptotic stimulus. The protein is thought to induce apoptosis by binding the apoptosis inhibitory protein baculoviral IAP repeat-containing 4. Nuclear localization of this protein has also been observed. Alternate splicing of this gene results in two transcript variants encoding different isoforms. Additional transcript variants have been described, but their full-length sequences have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: HTRA2 HtrA serine peptidase 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27429| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Zurawa-Janicka D, Narkiewicz J, Lipińska B |title=[Characterization of the HtrA family of proteins] |journal=Postepy Biochem. |volume=53 |issue= 1 |pages= 27-36 |year= 2007 |pmid= 17718385 |doi= }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Faccio L, Fusco C, Chen A, ''et al.'' |title=Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia. |journal=J. Biol. Chem. |volume=275 |issue= 4 |pages= 2581-8 |year= 2000 |pmid= 10644717 |doi= }}
*{{cite journal | author=Savopoulos JW, Carter PS, Turconi S, ''et al.'' |title=Expression, purification, and functional analysis of the human serine protease HtrA2. |journal=Protein Expr. Purif. |volume=19 |issue= 2 |pages= 227-34 |year= 2000 |pmid= 10873535 |doi= 10.1006/prep.2000.1240 }}
*{{cite journal | author=Gray CW, Ward RV, Karran E, ''et al.'' |title=Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. |journal=Eur. J. Biochem. |volume=267 |issue= 18 |pages= 5699-710 |year= 2000 |pmid= 10971580 |doi= }}
*{{cite journal | author=Faccio L, Fusco C, Viel A, Zervos AS |title=Tissue-specific splicing of Omi stress-regulated endoprotease leads to an inactive protease with a modified PDZ motif. |journal=Genomics |volume=68 |issue= 3 |pages= 343-7 |year= 2000 |pmid= 10995577 |doi= 10.1006/geno.2000.6263 }}
*{{cite journal | author=Suzuki Y, Imai Y, Nakayama H, ''et al.'' |title=A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. |journal=Mol. Cell |volume=8 |issue= 3 |pages= 613-21 |year= 2001 |pmid= 11583623 |doi= }}
*{{cite journal | author=Verhagen AM, Silke J, Ekert PG, ''et al.'' |title=HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 445-54 |year= 2002 |pmid= 11604410 |doi= 10.1074/jbc.M109891200 }}
*{{cite journal | author=Hegde R, Srinivasula SM, Zhang Z, ''et al.'' |title=Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. |journal=J. Biol. Chem. |volume=277 |issue= 1 |pages= 432-8 |year= 2002 |pmid= 11606597 |doi= 10.1074/jbc.M109721200 }}
*{{cite journal | author=Vucic D, Deshayes K, Ackerly H, ''et al.'' |title=SMAC negatively regulates the anti-apoptotic activity of melanoma inhibitor of apoptosis (ML-IAP). |journal=J. Biol. Chem. |volume=277 |issue= 14 |pages= 12275-9 |year= 2002 |pmid= 11801603 |doi= 10.1074/jbc.M112045200 }}
*{{cite journal | author=van Loo G, van Gurp M, Depuydt B, ''et al.'' |title=The serine protease Omi/HtrA2 is released from mitochondria during apoptosis. Omi interacts with caspase-inhibitor XIAP and induces enhanced caspase activity. |journal=Cell Death Differ. |volume=9 |issue= 1 |pages= 20-6 |year= 2002 |pmid= 11803371 |doi= 10.1038/sj/cdd/4400970 }}
*{{cite journal | author=Li W, Srinivasula SM, Chai J, ''et al.'' |title=Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi. |journal=Nat. Struct. Biol. |volume=9 |issue= 6 |pages= 436-41 |year= 2002 |pmid= 11967569 |doi= 10.1038/nsb795 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Yang QH, Church-Hajduk R, Ren J, ''et al.'' |title=Omi/HtrA2 catalytic cleavage of inhibitor of apoptosis (IAP) irreversibly inactivates IAPs and facilitates caspase activity in apoptosis. |journal=Genes Dev. |volume=17 |issue= 12 |pages= 1487-96 |year= 2003 |pmid= 12815069 |doi= 10.1101/gad.1097903 }}
*{{cite journal | author=Srinivasula SM, Gupta S, Datta P, ''et al.'' |title=Inhibitor of apoptosis proteins are substrates for the mitochondrial serine protease Omi/HtrA2. |journal=J. Biol. Chem. |volume=278 |issue= 34 |pages= 31469-72 |year= 2003 |pmid= 12835328 |doi= 10.1074/jbc.C300240200 }}
*{{cite journal | author=Suzuki Y, Takahashi-Niki K, Akagi T, ''et al.'' |title=Mitochondrial protease Omi/HtrA2 enhances caspase activation through multiple pathways. |journal=Cell Death Differ. |volume=11 |issue= 2 |pages= 208-16 |year= 2004 |pmid= 14605674 |doi= 10.1038/sj.cdd.4401343 }}
*{{cite journal | author=Okada M, Adachi S, Imai T, ''et al.'' |title=A novel mechanism for imatinib mesylate-induced cell death of BCR-ABL-positive human leukemic cells: caspase-independent, necrosis-like programmed cell death mediated by serine protease activity. |journal=Blood |volume=103 |issue= 6 |pages= 2299-307 |year= 2004 |pmid= 14645012 |doi= 10.1182/blood-2003-05-1605 }}
*{{cite journal | author=Park HJ, Seong YM, Choi JY, ''et al.'' |title=Alzheimer's disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi. |journal=Neurosci. Lett. |volume=357 |issue= 1 |pages= 63-7 |year= 2004 |pmid= 15036614 |doi= 10.1016/j.neulet.2003.11.068 }}
*{{cite journal | author=Guo Y, Cheong N, Zhang Z, ''et al.'' |title=Tim50, a component of the mitochondrial translocator, regulates mitochondrial integrity and cell death. |journal=J. Biol. Chem. |volume=279 |issue= 23 |pages= 24813-25 |year= 2004 |pmid= 15044455 |doi= 10.1074/jbc.M402049200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LAMB1... {November 18, 2007 9:49:22 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:49:45 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Laminin, beta 1
| HGNCid = 6486
| Symbol = LAMB1
| AltSymbols =; CLM; MGC142015
| OMIM = 150240
| ECnumber =
| Homologene = 1722
| MGIid = 96743
| GeneAtlas_image1 = PBB_GE_LAMB1_201505_at_tn.png
| GeneAtlas_image2 = PBB_GE_LAMB1_211651_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005201 |text = extracellular matrix structural constituent}} {{GNF_GO|id=GO:0019899 |text = enzyme binding}}
| Component = {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005606 |text = laminin-1 complex}} {{GNF_GO|id=GO:0005607 |text = laminin-2 complex}} {{GNF_GO|id=GO:0043257 |text = laminin-8 complex}} {{GNF_GO|id=GO:0043259 |text = laminin-10 complex}} {{GNF_GO|id=GO:0048471 |text = perinuclear region of cytoplasm}}
| Process = {{GNF_GO|id=GO:0007155 |text = cell adhesion}} {{GNF_GO|id=GO:0007566 |text = embryo implantation}} {{GNF_GO|id=GO:0030335 |text = positive regulation of cell migration}} {{GNF_GO|id=GO:0031175 |text = neurite development}} {{GNF_GO|id=GO:0042476 |text = odontogenesis}} {{GNF_GO|id=GO:0050679 |text = positive regulation of epithelial cell proliferation}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3912
| Hs_Ensembl = ENSG00000091136
| Hs_RefseqProtein = NP_002282
| Hs_RefseqmRNA = NM_002291
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 107351499
| Hs_GenLoc_end = 107431040
| Hs_Uniprot = P07942
| Mm_EntrezGene = 16777
| Mm_Ensembl = ENSMUSG00000002900
| Mm_RefseqmRNA = NM_008482
| Mm_RefseqProtein = NP_032508
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 12
| Mm_GenLoc_start = 31851443
| Mm_GenLoc_end = 31915700
| Mm_Uniprot = Q0V927
}}
}}
'''Laminin, beta 1''', also known as '''LAMB1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LAMB1 laminin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3912| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: LAMB1 laminin, beta 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3912| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ljubimova JY, Fujita M, Khazenzon NM, ''et al.'' |title=Changes in laminin isoforms associated with brain tumor invasion and angiogenesis. |journal=Front. Biosci. |volume=11 |issue= |pages= 81-8 |year= 2006 |pmid= 16146715 |doi= }}
*{{cite journal | author=Bonneau D, Huret JL, Godeau G, ''et al.'' |title=Recurrent ctb(7)(q31.3) and possible laminin involvement in a neonatal cutis laxa with a Marfan phenotype. |journal=Hum. Genet. |volume=87 |issue= 3 |pages= 317-9 |year= 1991 |pmid= 1864606 |doi= }}
*{{cite journal | author=Vuolteenaho R, Chow LT, Tryggvason K |title=Structure of the human laminin B1 chain gene. |journal=J. Biol. Chem. |volume=265 |issue= 26 |pages= 15611-6 |year= 1990 |pmid= 1975589 |doi= }}
*{{cite journal | author=Ikonen J, Pikkarainen T, Savolainen ER, Tryggvason K |title=A Hpa I polymorphism in the human laminin B1 chain gene on 7q22. |journal=Nucleic Acids Res. |volume=17 |issue= 1 |pages= 473 |year= 1989 |pmid= 2563160 |doi= }}
*{{cite journal | author=Roche KB, Moore JW, Surana RB, Wilson BE |title=Aortic root dilatation associated with partial trisomy 7(q31.2----qter). |journal=Pediatric cardiology |volume=10 |issue= 1 |pages= 53-5 |year= 1989 |pmid= 2704655 |doi= }}
*{{cite journal | author=Sasaki M, Kato S, Kohno K, ''et al.'' |title=Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 4 |pages= 935-9 |year= 1987 |pmid= 3493487 |doi= }}
*{{cite journal | author=Pikkarainen T, Eddy R, Fukushima Y, ''et al.'' |title=Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7. |journal=J. Biol. Chem. |volume=262 |issue= 22 |pages= 10454-62 |year= 1987 |pmid= 3611077 |doi= }}
*{{cite journal | author=Jaye M, Modi WS, Ricca GA, ''et al.'' |title=Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization. |journal=Am. J. Hum. Genet. |volume=41 |issue= 4 |pages= 605-15 |year= 1987 |pmid= 3661559 |doi= }}
*{{cite journal | author=Burgeson RE, Chiquet M, Deutzmann R, ''et al.'' |title=A new nomenclature for the laminins. |journal=Matrix Biol. |volume=14 |issue= 3 |pages= 209-11 |year= 1994 |pmid= 7921537 |doi= }}
*{{cite journal | author=Lohi J, Leivo I, Franssila K, Virtanen I |title=Changes in the distribution of integrins and their basement membrane ligands during development of human thyroid follicular epithelium. |journal=Histochem. J. |volume=29 |issue= 4 |pages= 337-45 |year= 1997 |pmid= 9184849 |doi= }}
*{{cite journal | author=Taylor J, Muntoni F, Robb S, ''et al.'' |title=Early onset autosomal dominant myopathy with rigidity of the spine: a possible role for laminin beta 1? |journal=Neuromuscul. Disord. |volume=7 |issue= 4 |pages= 211-6 |year= 1997 |pmid= 9196901 |doi= }}
*{{cite journal | author=Sewry CA, D'Alessandro M, Wilson LA, ''et al.'' |title=Expression of laminin chains in skin in merosin-deficient congenital muscular dystrophy. |journal=Neuropediatrics |volume=28 |issue= 4 |pages= 217-22 |year= 1997 |pmid= 9309712 |doi= }}
*{{cite journal | author=Mahida YR, Beltinger J, Makh S, ''et al.'' |title=Adult human colonic subepithelial myofibroblasts express extracellular matrix proteins and cyclooxygenase-1 and -2. |journal=Am. J. Physiol. |volume=273 |issue= 6 Pt 1 |pages= G1341-8 |year= 1998 |pmid= 9435560 |doi= }}
*{{cite journal | author=O'Grady P, Thai TC, Saito H |title=The laminin-nidogen complex is a ligand for a specific splice isoform of the transmembrane protein tyrosine phosphatase LAR. |journal=J. Cell Biol. |volume=141 |issue= 7 |pages= 1675-84 |year= 1998 |pmid= 9647658 |doi= }}
*{{cite journal | author=Koch M, Olson PF, Albus A, ''et al.'' |title=Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain. |journal=J. Cell Biol. |volume=145 |issue= 3 |pages= 605-18 |year= 1999 |pmid= 10225960 |doi= }}
*{{cite journal | author=Merlini L, Villanova M, Sabatelli P, ''et al.'' |title=Decreased expression of laminin beta 1 in chromosome 21-linked Bethlem myopathy. |journal=Neuromuscul. Disord. |volume=9 |issue= 5 |pages= 326-9 |year= 1999 |pmid= 10407855 |doi= }}
*{{cite journal | author=Kikkawa Y, Sanzen N, Fujiwara H, ''et al.'' |title=Integrin binding specificity of laminin-10/11: laminin-10/11 are recognized by alpha 3 beta 1, alpha 6 beta 1 and alpha 6 beta 4 integrins. |journal=J. Cell. Sci. |volume=113 ( Pt 5) |issue= |pages= 869-76 |year= 2000 |pmid= 10671376 |doi= }}
*{{cite journal | author=Hirosaki T, Mizushima H, Tsubota Y, ''et al.'' |title=Structural requirement of carboxyl-terminal globular domains of laminin alpha 3 chain for promotion of rapid cell adhesion and migration by laminin-5. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22495-502 |year= 2000 |pmid= 10801807 |doi= 10.1074/jbc.M001326200 }}
*{{cite journal | author=Champliaud MF, Virtanen I, Tiger CF, ''et al.'' |title=Posttranslational modifications and beta/gamma chain associations of human laminin alpha1 and laminin alpha5 chains: purification of laminin-3 from placenta. |journal=Exp. Cell Res. |volume=259 |issue= 2 |pages= 326-35 |year= 2000 |pmid= 10964500 |doi= 10.1006/excr.2000.4980 }}
*{{cite journal | author=Pedraza C, Geberhiwot T, Ingerpuu S, ''et al.'' |title=Monocytic cells synthesize, adhere to, and migrate on laminin-8 (alpha 4 beta 1 gamma 1). |journal=J. Immunol. |volume=165 |issue= 10 |pages= 5831-8 |year= 2000 |pmid= 11067943 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LBP... {November 18, 2007 9:49:45 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:50:09 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Lipopolysaccharide binding protein
| HGNCid = 6517
| Symbol = LBP
| AltSymbols =; MGC22233
| OMIM = 151990
| ECnumber =
| Homologene = 3055
| MGIid = 1098776
| GeneAtlas_image1 = PBB_GE_LBP_214461_at_tn.png
| GeneAtlas_image2 = PBB_GE_LBP_211652_s_at_tn.png
| Function = {{GNF_GO|id=GO:0001530 |text = lipopolysaccharide binding}} {{GNF_GO|id=GO:0008289 |text = lipid binding}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006869 |text = lipid transport}} {{GNF_GO|id=GO:0006953 |text = acute-phase response}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 3929
| Hs_Ensembl = ENSG00000129988
| Hs_RefseqProtein = NP_004130
| Hs_RefseqmRNA = NM_004139
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 20
| Hs_GenLoc_start = 36408299
| Hs_GenLoc_end = 36439067
| Hs_Uniprot = P18428
| Mm_EntrezGene = 16803
| Mm_Ensembl = ENSMUSG00000016024
| Mm_RefseqmRNA = NM_008489
| Mm_RefseqProtein = NP_032515
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 157997986
| Mm_GenLoc_end = 158023737
| Mm_Uniprot = Q61805
}}
}}
'''Lipopolysaccharide binding protein''', also known as '''LBP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: LBP lipopolysaccharide binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3929| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is involved in the acute-phase immunologic response to gram-negative bacterial infections. Gram-negative bacteria contain a glycolipid, lipopolysaccharide (LPS), on their outer cell wall. Together with bactericidal permeability-increasing protein (BPI), the encoded protein binds LPS and interacts with the CD14 receptor, probably playing a role in regulating LPS-dependent monocyte responses. Studies in mice suggest that the encoded protein is necessary for the rapid acute-phase response to LPS but not for the clearance of LPS from circulation. This protein is part of a family of structurally and functionally related proteins, including BPI, plasma cholesteryl ester transfer protein (CETP), and phospholipid transfer protein (PLTP). Finally, this gene is found on chromosome 20, immediately downstream of the BPI gene.<ref name="entrez">{{cite web | title = Entrez Gene: LBP lipopolysaccharide binding protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3929| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Schumann RR, Leong SR, Flaggs GW, ''et al.'' |title=Structure and function of lipopolysaccharide binding protein. |journal=Science |volume=249 |issue= 4975 |pages= 1429-31 |year= 1990 |pmid= 2402637 |doi= }}
*{{cite journal | author=Wilde CG, Seilhamer JJ, McGrogan M, ''et al.'' |title=Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation. |journal=J. Biol. Chem. |volume=269 |issue= 26 |pages= 17411-6 |year= 1994 |pmid= 7517398 |doi= }}
*{{cite journal | author=Gray PW, Corcorran AE, Eddy RL, ''et al.'' |title=The genes for the lipopolysaccharide binding protein (LBP) and the bactericidal permeability increasing protein (BPI) are encoded in the same region of human chromosome 20. |journal=Genomics |volume=15 |issue= 1 |pages= 188-90 |year= 1993 |pmid= 8432532 |doi= 10.1006/geno.1993.1030 }}
*{{cite journal | author=Park CT, Wright SD |title=Plasma lipopolysaccharide-binding protein is found associated with a particle containing apolipoprotein A-I, phospholipid, and factor H-related proteins. |journal=J. Biol. Chem. |volume=271 |issue= 30 |pages= 18054-60 |year= 1996 |pmid= 8663389 |doi= }}
*{{cite journal | author=Nanbo A, Nishimura H, Nagasawa S |title=Lipopolysaccharide binding protein from normal human plasma purified with high efficiency. |journal=Protein Expr. Purif. |volume=10 |issue= 1 |pages= 55-60 |year= 1997 |pmid= 9179291 |doi= 10.1006/prep.1996.0712 }}
*{{cite journal | author=Hubacek JA, Büchler C, Aslanidis C, Schmitz G |title=The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved. |journal=Biochem. Biophys. Res. Commun. |volume=236 |issue= 2 |pages= 427-30 |year= 1997 |pmid= 9240454 |doi= 10.1006/bbrc.1997.6970 }}
*{{cite journal | author=Jack RS, Fan X, Bernheiden M, ''et al.'' |title=Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection. |journal=Nature |volume=389 |issue= 6652 |pages= 742-5 |year= 1997 |pmid= 9338787 |doi= 10.1038/39622 }}
*{{cite journal | author=Kirschning CJ, Au-Young J, Lamping N, ''et al.'' |title=Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins. |journal=Genomics |volume=46 |issue= 3 |pages= 416-25 |year= 1998 |pmid= 9441745 |doi= 10.1006/geno.1997.5030 }}
*{{cite journal | author=Beamer LJ, Carroll SF, Eisenberg D |title=The BPI/LBP family of proteins: a structural analysis of conserved regions. |journal=Protein Sci. |volume=7 |issue= 4 |pages= 906-14 |year= 1998 |pmid= 9568897 |doi= }}
*{{cite journal | author=Sato M, Saeki Y, Tanaka K, Kaneda Y |title=Ribosome-associated protein LBP/p40 binds to S21 protein of 40S ribosome: analysis using a yeast two-hybrid system. |journal=Biochem. Biophys. Res. Commun. |volume=256 |issue= 2 |pages= 385-90 |year= 1999 |pmid= 10079194 |doi= 10.1006/bbrc.1999.0343 }}
*{{cite journal | author=Vreugdenhil AC, Dentener MA, Snoek AM, ''et al.'' |title=Lipopolysaccharide binding protein and serum amyloid A secretion by human intestinal epithelial cells during the acute phase response. |journal=J. Immunol. |volume=163 |issue= 5 |pages= 2792-8 |year= 1999 |pmid= 10453023 |doi= }}
*{{cite journal | author=Vesy CJ, Kitchens RL, Wolfbauer G, ''et al.'' |title=Lipopolysaccharide-binding protein and phospholipid transfer protein release lipopolysaccharides from gram-negative bacterial membranes. |journal=Infect. Immun. |volume=68 |issue= 5 |pages= 2410-7 |year= 2000 |pmid= 10768924 |doi= }}
*{{cite journal | author=Labéta MO, Vidal K, Nores JE, ''et al.'' |title=Innate recognition of bacteria in human milk is mediated by a milk-derived highly expressed pattern recognition receptor, soluble CD14. |journal=J. Exp. Med. |volume=191 |issue= 10 |pages= 1807-12 |year= 2000 |pmid= 10811873 |doi= }}
*{{cite journal | author=Dentener MA, Vreugdenhil AC, Hoet PH, ''et al.'' |title=Production of the acute-phase protein lipopolysaccharide-binding protein by respiratory type II epithelial cells: implications for local defense to bacterial endotoxins. |journal=Am. J. Respir. Cell Mol. Biol. |volume=23 |issue= 2 |pages= 146-53 |year= 2000 |pmid= 10919979 |doi= }}
*{{cite journal | author=Nagaoka I, Hirota S, Niyonsaba F, ''et al.'' |title=Cathelicidin family of antibacterial peptides CAP18 and CAP11 inhibit the expression of TNF-alpha by blocking the binding of LPS to CD14(+) cells. |journal=J. Immunol. |volume=167 |issue= 6 |pages= 3329-38 |year= 2001 |pmid= 11544322 |doi= }}
*{{cite journal | author=Gutsmann T, Müller M, Carroll SF, ''et al.'' |title=Dual role of lipopolysaccharide (LPS)-binding protein in neutralization of LPS and enhancement of LPS-induced activation of mononuclear cells. |journal=Infect. Immun. |volume=69 |issue= 11 |pages= 6942-50 |year= 2001 |pmid= 11598069 |doi= 10.1128/IAI.69.11.6942-6950.2001 }}
*{{cite journal | author=Iovine N, Eastvold J, Elsbach P, ''et al.'' |title=The carboxyl-terminal domain of closely related endotoxin-binding proteins determines the target of protein-lipopolysaccharide complexes. |journal=J. Biol. Chem. |volume=277 |issue= 10 |pages= 7970-8 |year= 2002 |pmid= 11773072 |doi= 10.1074/jbc.M109622200 }}
*{{cite journal | author=Deloukas P, Matthews LH, Ashurst J, ''et al.'' |title=The DNA sequence and comparative analysis of human chromosome 20. |journal=Nature |volume=414 |issue= 6866 |pages= 865-71 |year= 2002 |pmid= 11780052 |doi= 10.1038/414865a }}
*{{cite journal | author=Kaden J, Zwerenz P, Lambrecht HG, Dostatni R |title=Lipopolysaccharide-binding protein as a new and reliable infection marker after kidney transplantation. |journal=Transpl. Int. |volume=15 |issue= 4 |pages= 163-72 |year= 2002 |pmid= 11976738 |doi= 10.1007/s00147-002-0392-2 }}
*{{cite journal | author=Reyes O, Vallespi MG, Garay HE, ''et al.'' |title=Identification of single amino acid residues essential for the binding of lipopolysaccharide (LPS) to LPS binding protein (LBP) residues 86-99 by using an Ala-scanning library. |journal=J. Pept. Sci. |volume=8 |issue= 4 |pages= 144-50 |year= 2002 |pmid= 11991204 |doi= 10.1002/psc.375 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on LDHA... {November 18, 2007 9:50:10 PM PST}
- SEARCH REDIRECT: Control Box Found: LDHA {November 18, 2007 9:50:35 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:50:37 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:50:37 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:50:37 PM PST}
- UPDATED: Updated protein page: LDHA {November 18, 2007 9:50:43 PM PST}
- INFO: Beginning work on PCSK9... {November 18, 2007 9:52:37 PM PST}
- SEARCH REDIRECT: Control Box Found: PCSK9 {November 18, 2007 9:53:14 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:53:15 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:53:15 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:53:15 PM PST}
- UPDATED: Updated protein page: PCSK9 {November 18, 2007 9:53:22 PM PST}
- INFO: Beginning work on POLL... {November 18, 2007 9:51:37 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:52:06 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_POLL_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nzp.
| PDB = {{PDB2|1nzp}}, {{PDB2|1rzt}}, {{PDB2|1xsl}}, {{PDB2|1xsn}}, {{PDB2|1xsp}}, {{PDB2|2bcq}}, {{PDB2|2bcr}}, {{PDB2|2bcs}}, {{PDB2|2bcu}}, {{PDB2|2bcv}}, {{PDB2|2gws}}, {{PDB2|2pfn}}, {{PDB2|2pfo}}, {{PDB2|2pfp}}, {{PDB2|2pfq}}
| Name = Polymerase (DNA directed), lambda
| HGNCid = 9184
| Symbol = POLL
| AltSymbols =; BETA-N; FLJ46002; POL-KAPPA
| OMIM = 606343
| ECnumber =
| Homologene = 40863
| MGIid = 1889000
| GeneAtlas_image1 = PBB_GE_POLL_221049_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003890 |text = beta DNA polymerase activity}} {{GNF_GO|id=GO:0016449 |text = lambda DNA polymerase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0016829 |text = lyase activity}} {{GNF_GO|id=GO:0030145 |text = manganese ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005634 |text = nucleus}}
| Process = {{GNF_GO|id=GO:0006260 |text = DNA replication}} {{GNF_GO|id=GO:0006281 |text = DNA repair}} {{GNF_GO|id=GO:0006289 |text = nucleotide-excision repair}} {{GNF_GO|id=GO:0016446 |text = somatic hypermutation of immunoglobulin genes}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 27343
| Hs_Ensembl = ENSG00000166169
| Hs_RefseqProtein = NP_037406
| Hs_RefseqmRNA = NM_013274
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 10
| Hs_GenLoc_start = 103328629
| Hs_GenLoc_end = 103338004
| Hs_Uniprot = Q9UGP5
| Mm_EntrezGene = 56626
| Mm_Ensembl = ENSMUSG00000025218
| Mm_RefseqmRNA = NM_020032
| Mm_RefseqProtein = NP_064416
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 19
| Mm_GenLoc_start = 45605586
| Mm_GenLoc_end = 45613854
| Mm_Uniprot = Q9QXE2
}}
}}
'''Polymerase (DNA directed), lambda''', also known as '''POLL''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: POLL polymerase (DNA directed), lambda| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=27343| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Niida H, Nakanishi M |title=[A novel mammalian DNA polymerase: DNA polymerase lambda (pol lambda)] |journal=Seikagaku |volume=74 |issue= 3 |pages= 224-6 |year= 2002 |pmid= 11974915 |doi= }}
*{{cite journal | author=Nagasawa K, Kitamura K, Yasui A, ''et al.'' |title=Identification and characterization of human DNA polymerase beta 2, a DNA polymerase beta -related enzyme. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 31233-8 |year= 2000 |pmid= 10887191 |doi= 10.1074/jbc.M004263200 }}
*{{cite journal | author=García-Díaz M, Domínguez O, López-Fernández LA, ''et al.'' |title=DNA polymerase lambda (Pol lambda), a novel eukaryotic DNA polymerase with a potential role in meiosis. |journal=J. Mol. Biol. |volume=301 |issue= 4 |pages= 851-67 |year= 2000 |pmid= 10966791 |doi= 10.1006/jmbi.2000.4005 }}
*{{cite journal | author=Aoufouchi S, Flatter E, Dahan A, ''et al.'' |title=Two novel human and mouse DNA polymerases of the polX family. |journal=Nucleic Acids Res. |volume=28 |issue= 18 |pages= 3684-93 |year= 2000 |pmid= 10982892 |doi= }}
*{{cite journal | author=García-Díaz M, Bebenek K, Kunkel TA, Blanco L |title=Identification of an intrinsic 5'-deoxyribose-5-phosphate lyase activity in human DNA polymerase lambda: a possible role in base excision repair. |journal=J. Biol. Chem. |volume=276 |issue= 37 |pages= 34659-63 |year= 2001 |pmid= 11457865 |doi= 10.1074/jbc.M106336200 }}
*{{cite journal | author=Haracska L, Unk I, Johnson RE, ''et al.'' |title=Stimulation of DNA synthesis activity of human DNA polymerase kappa by PCNA. |journal=Mol. Cell. Biol. |volume=22 |issue= 3 |pages= 784-91 |year= 2002 |pmid= 11784855 |doi= }}
*{{cite journal | author=García-Díaz M, Bebenek K, Sabariegos R, ''et al.'' |title=DNA polymerase lambda, a novel DNA repair enzyme in human cells. |journal=J. Biol. Chem. |volume=277 |issue= 15 |pages= 13184-91 |year= 2002 |pmid= 11821417 |doi= 10.1074/jbc.M111601200 }}
*{{cite journal | author=Shimazaki N, Yoshida K, Kobayashi T, ''et al.'' |title=Over-expression of human DNA polymerase lambda in E. coli and characterization of the recombinant enzyme. |journal=Genes Cells |volume=7 |issue= 7 |pages= 639-51 |year= 2003 |pmid= 12081642 |doi= }}
*{{cite journal | author=Maga G, Villani G, Ramadan K, ''et al.'' |title=Human DNA polymerase lambda functionally and physically interacts with proliferating cell nuclear antigen in normal and translesion DNA synthesis. |journal=J. Biol. Chem. |volume=277 |issue= 50 |pages= 48434-40 |year= 2003 |pmid= 12368291 |doi= 10.1074/jbc.M206889200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
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}}
{{refend}}
{{protein-stub}}
end log.
