fbpx
Wikipedia

RBBP5

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

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

Function edit

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 edit

RBBP5 has been shown to interact with:

References edit

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000117222 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000026439 – Ensembl, 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 edit

  • 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.


rbbp5, retinoblastoma, binding, protein, protein, that, humans, encoded, gene, available, structurespdbortholog, search, pdbe, rcsblist, codes3p4f, 4x8n, 4x8p, 5f6k, 5f6lidentifiersaliases, rbq3, swd1, retinoblastoma, binding, protein, binding, protein, histon. Retinoblastoma binding protein 5 is a protein that in humans is encoded by the RBBP5 gene 5 6 RBBP5Available structuresPDBOrtholog search PDBe RCSBList of PDB id codes3P4F 4X8N 4X8P 5F6K 5F6LIdentifiersAliasesRBBP5 RBQ3 SWD1 retinoblastoma binding protein 5 RB binding protein 5 histone lysine methyltransferase complex subunitExternal IDsOMIM 600697 MGI 1918367 HomoloGene 3709 GeneCards RBBP5 OMA RBBP5 orthologsGene location Human Chr Chromosome 1 human 1 Band1q32 1Start205 086 142 bp 1 End205 122 015 bp 1 Gene location Mouse Chr Chromosome 1 mouse 2 Band1 1 E4Start132 405 103 bp 2 End132 433 397 bp 2 RNA expression patternBgeeHumanMouse ortholog Top expressed insecondary oocyteAchilles tendonislet of Langerhansganglionic eminencestromal cell of endometriummonocytegastrocnemius musclebloodlymph noderectumTop expressed inhandcondylefossatrigeminal ganglionotolith organutriclerenal corpusclesecondary oocytesubstantia nigrafacial motor nucleusMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionmethylated histone binding protein binding histone methyltransferase activity H3 K4 specific histone lysine N methyltransferase activityCellular componentMLL1 complex nucleolus MLL3 4 complex nucleus nucleoplasm histone methyltransferase complex Set1C COMPASS complexBiological processresponse 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 organizationSources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez5929213464EnsemblENSG00000117222ENSMUSG00000026439UniProtQ15291Q8BX09RefSeq mRNA NM 001193272NM 001193273NM 005057NM 172517NM 001357486NM 001357487RefSeq protein NP 001180201NP 001180202NP 005048NP 766105NP 001344415NP 001344416Location UCSC Chr 1 205 09 205 12 MbChr 1 132 41 132 43 MbPubMed search 3 4 WikidataView Edit HumanView Edit Mouse Contents 1 Function 2 Interactions 3 References 4 Further readingFunction editThe 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 editRBBP5 has been shown to interact with ASCL2 7 MLL 8 MLL3 7 and NCOA6 7 References edit a b c GRCh38 Ensembl release 89 ENSG00000117222 Ensembl May 2017 a b c GRCm38 Ensembl release 89 ENSMUSG00000026439 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine 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 a b Entrez Gene RBBP5 retinoblastoma binding protein 5 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 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 editHillier 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 nbsp This article on a gene on human chromosome 1 is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title RBBP5 amp oldid 1216464856, wikipedia, wiki, book, books, library,

article

, read, download, free, free download, mp3, video, mp4, 3gp, jpg, jpeg, gif, png, picture, music, song, movie, book, game, games.