RBBP5

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 IDsMGI: 1918367 HomoloGene: 3709 GeneCards: RBBP5
Gene location (Human)
Chr.Chromosome 1 (human)[1]
Band1q32.1Start205,086,142 bp[1]
End205,122,015 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
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 MbChr 1: 132.48 – 132.51 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

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

RBBP5 has been shown to interact with:

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000117222 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000026439 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  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. 1 2 "Entrez Gene: RBBP5 retinoblastoma binding protein 5".
  7. 1 2 3 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

  • 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.
  • 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.
  • 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.


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