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RBBP5

From Wikipedia, the free encyclopedia
RBBP5
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRBBP5, RBQ3, SWD1, retinoblastoma binding protein 5, RB binding protein 5, histone lysine methyltransferase complex subunit
External IDsOMIM: 600697; MGI: 1918367; HomoloGene: 3709; GeneCards: RBBP5; OMA:RBBP5 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001193272
NM_001193273
NM_005057

NM_172517
NM_001357486
NM_001357487

RefSeq (protein)

NP_001180201
NP_001180202
NP_005048

NP_766105
NP_001344415
NP_001344416

Location (UCSC)Chr 1: 205.09 – 205.12 MbChr 1: 132.41 – 132.43 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Retinoblastoma-binding protein 5 is a protein that in humans is encoded by the RBBP5 gene.[5][6]

Function

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The protein encoded by this gene is a ubiquitously expressed nuclear protein and belongs to a highly conserved subfamily of WD-repeat proteins. It is found among several proteins that bind directly to retinoblastoma protein, which regulates cell proliferation. The encoded protein interacts preferentially with the underphosphorylated retinoblastoma protein via the E1A-binding pocket B.[6]

Interactions

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RBBP5 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000117222Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026439Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Saijo M, Sakai Y, Kishino T, Niikawa N, Matsuura Y, Morino K, Tamai K, Taya Y (Jun 1995). "Molecular cloning of a human protein that binds to the retinoblastoma protein and chromosomal mapping". Genomics. 27 (3): 511–9. doi:10.1006/geno.1995.1084. PMID 7558034.
  6. ^ a b "Entrez Gene: RBBP5 retinoblastoma binding protein 5".
  7. ^ a b c Goo YH, Sohn YC, Kim DH, Kim SW, Kang MJ, Jung DJ, Kwak E, Barlev NA, Berger SL, Chow VT, Roeder RG, Azorsa DO, Meltzer PS, Suh PG, Song EJ, Lee KJ, Lee YC, Lee JW (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Molecular and Cellular Biology. 23 (1): 140–9. doi:10.1128/mcb.23.1.140-149.2003. PMC 140670. PMID 12482968.
  8. ^ Yokoyama A, Wang Z, Wysocka J, Sanyal M, Aufiero DJ, Kitabayashi I, Herr W, Cleary ML (Jul 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Molecular and Cellular Biology. 24 (13): 5639–49. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.

Further reading

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