RBBP5

RBBP5
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3P4F, 4X8N, 4X8P, 5F6K, 5F6L
Identifiers
Aliases	RBBP5, RBQ3, SWD1, retinoblastoma binding protein 5, RB binding protein 5, histone lysine methyltransferase complex subunit
External IDs	OMIM: 600697 MGI: 1918367 HomoloGene: 3709 GeneCards: RBBP5
Gene location (Human) Chr. Chromosome 1 (human) Band 1q32.1 Start 205,086,142 bp End 205,122,015 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1|1 E4 Start 132,405,103 bp End 132,433,397 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte Achilles tendon islet of Langerhans ganglionic eminence stromal cell of endometrium monocyte gastrocnemius muscle blood lymph node rectum Top expressed in hand condyle fossa trigeminal ganglion otolith organ utricle renal corpuscle secondary oocyte substantia nigra facial motor nucleus More reference expression data BioGPS More reference expression data
Gene ontology Molecular function methylated histone binding protein binding histone methyltransferase activity (H3-K4 specific) histone-lysine N-methyltransferase activity Cellular component MLL1 complex nucleolus MLL3/4 complex nucleus nucleoplasm histone methyltransferase complex Set1C/COMPASS complex Biological process response to estrogen histone H3-K4 methylation regulation of transcription, DNA-templated transcription, DNA-templated cellular response to DNA damage stimulus beta-catenin-TCF complex assembly post-translational protein modification regulation of megakaryocyte differentiation chromatin organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5929 213464 Ensembl ENSG00000117222 ENSMUSG00000026439 UniProt Q15291 Q8BX09 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 Mb Chr 1: 132.41 – 132.43 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

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

Function

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.

Interactions

RBBP5 has been shown to interact with:

• ASCL2,
• MLL,
• MLL3, and
• NCOA6.

Further reading

• Hillier LD, Lennon G, Becker M, Bonaldo MF, Chiapelli B, Chissoe S, Dietrich N, DuBuque T, Favello A, Gish W, Hawkins M, Hultman M, Kucaba T, Lacy M, Le M, Le N, Mardis E, Moore B, Morris M, Parsons J, Prange C, Rifkin L, Rohlfing T, Schellenberg K, Bento Soares M, Tan F, Thierry-Meg J, Trevaskis E, Underwood K, Wohldman P, Waterston R, Wilson R, Marra M (Sep 1996). "Generation and analysis of 280,000 human expressed sequence tags". Genome Research. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID 8889549.
• Suzuki Y, Tsunoda T, Sese J, Taira H, Mizushima-Sugano J, Hata H, Ota T, Isogai T, Tanaka T, Nakamura Y, Suyama A, Sakaki Y, Morishita S, Okubo K, Sugano S (May 2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Research. 11 (5): 677–84. doi:10.1101/gr.gr-1640r. PMC 311086. PMID 11337467.
• 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.
• Hughes CM, Rozenblatt-Rosen O, Milne TA, Copeland TD, Levine SS, Lee JC, Hayes DN, Shanmugam KS, Bhattacharjee A, Biondi CA, Kay GF, Hayward NK, Hess JL, Meyerson M (Feb 2004). "Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus". Molecular Cell. 13 (4): 587–97. doi:10.1016/S1097-2765(04)00081-4. PMID 14992727.
• 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.
• Dou Y, Milne TA, Tackett AJ, Smith ER, Fukuda A, Wysocka J, Allis CD, Chait BT, Hess JL, Roeder RG (Jun 2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell. 121 (6): 873–85. doi:10.1016/j.cell.2005.04.031. PMID 15960975. S2CID 14717470.
• Scacheri PC, Davis S, Odom DT, Crawford GE, Perkins S, Halawi MJ, Agarwal SK, Marx SJ, Spiegel AM, Meltzer PS, Collins FS (Apr 2006). "Genome-wide analysis of menin binding provides insights into MEN1 tumorigenesis". PLOS Genetics. 2 (4): e51. doi:10.1371/journal.pgen.0020051. PMC 1428788. PMID 16604156.
• Higa LA, Wu M, Ye T, Kobayashi R, Sun H, Zhang H (Nov 2006). "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation". Nature Cell Biology. 8 (11): 1277–83. doi:10.1038/ncb1490. PMID 17041588. S2CID 22180568.
• Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M (Nov 2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. S2CID 7827573.