RBBP5
Retinoblastoma-binding protein 5 is a protein that in humans is encoded by the RBBP5 gene.[1][2]
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.[2]
Interactions
RBBP5 has been shown to interact with NCOA6,[3] MLL3,[3] ASCL2[3] and MLL.[4]
References
- ↑ Saijo M, Sakai Y, Kishino T, Niikawa N, Matsuura Y, Morino K, Tamai K, Taya Y (Nov 1995). "Molecular cloning of a human protein that binds to the retinoblastoma protein and chromosomal mapping". Genomics 27 (3): 511–519. doi:10.1006/geno.1995.1084. PMID 7558034.
- ↑ 2.0 2.1 "Entrez Gene: RBBP5 retinoblastoma binding protein 5".
- ↑ 3.0 3.1 3.2 Goo, Young-Hwa; Sohn Young Chang, Kim Dae-Hwan, Kim Seung-Whan, Kang Min-Jung, Jung Dong-Ju, Kwak Eunyee, Barlev Nickolai A, Berger Shelley L, Chow Vincent T, Roeder Robert G, Azorsa David O, Meltzer Paul S, Suh Pan-Gil, Song Eun Joo, Lee Kong-Joo, Lee Young Chul, Lee Jae Woon (Jan 2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. (United States) 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. ISSN 0270-7306. PMC 140670. PMID 12482968.
- ↑ Yokoyama, Akihiko; Wang Zhong; Wysocka Joanna; Sanyal Mrinmoy; Aufiero Deborah J; Kitabayashi Issay; Herr Winship; Cleary Michael L (Jul 2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. (United States) 24 (13): 5639–5649. doi:10.1128/MCB.24.13.5639-5649.2004. ISSN 0270-7306. PMC 480881. PMID 15199122.
Further reading
- Hillier LD; Lennon G; Becker M et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–828. doi:10.1101/gr.6.9.807. PMID 8889549.
- Suzuki Y; Tsunoda T; Sese J et al. (2001). "Identification and characterization of the potential promoter regions of 1031 kinds of human genes". Genome Res. 11 (5): 677–84. doi:10.1101/gr.164001. PMC 311086. PMID 11337467.
- Strausberg RL; Feingold EA; Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Goo YH; Sohn YC; Kim DH et al. (2003). "Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins". Mol. Cell. Biol. 23 (1): 140–149. doi:10.1128/MCB.23.1.140-149.2003. PMC 140670. PMID 12482968.
- Hughes CM; Rozenblatt-Rosen O; Milne TA et al. (2004). "Menin associates with a trithorax family histone methyltransferase complex and with the hoxc8 locus". Mol. Cell 13 (4): 587–597. doi:10.1016/S1097-2765(04)00081-4. PMID 14992727.
- Yokoyama A; Wang Z; Wysocka J et al. (2004). "Leukemia proto-oncoprotein MLL forms a SET1-like histone methyltransferase complex with menin to regulate Hox gene expression". Mol. Cell. Biol. 24 (13): 5639–5649. doi:10.1128/MCB.24.13.5639-5649.2004. PMC 480881. PMID 15199122.
- Dou Y; Milne TA; Tackett AJ et al. (2005). "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF". Cell 121 (6): 873–885. doi:10.1016/j.cell.2005.04.031. PMID 15960975.
- Scacheri PC; Davis S; Odom DT et al. (2006). "Genome-wide analysis of menin binding provides insights into MEN1 tumorigenesis". PLoS Genet. 2 (4): e51. doi:10.1371/journal.pgen.0020051. PMC 1428788. PMID 16604156.
- Higa LA; Wu M; Ye T et al. (2006). "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation". Nat. Cell Biol. 8 (11): 1277–1283. doi:10.1038/ncb1490. PMID 17041588.
- Olsen JV; Blagoev B; Gnad F et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID 17081983.