RBBP8

RBBP8
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases RBBP8, COM1, CTIP, JWDS, RIM, SAE2, SCKL2, retinoblastoma binding protein 8, RB binding protein 8, endonuclease
External IDs MGI: 2442995 HomoloGene: 28546 GeneCards: RBBP8
RNA expression pattern
More reference expression data
Orthologs
Species Human Mouse
Entrez

5932

225182

Ensembl

ENSG00000101773

ENSMUSG00000041238

UniProt

Q99708

Q80YR6

RefSeq (mRNA)

NM_002894
NM_203291
NM_203292

NM_001081223
NM_001252495
NM_175458

RefSeq (protein)

NP_002885.1
NP_976036.1
NP_976037.1
NP_002885.1
NP_976036.1

NP_001074692.1
NP_001239424.1

Location (UCSC) Chr 18: 22.8 – 23.03 Mb Chr 18: 11.63 – 11.74 Mb
PubMed search [1] [2]
Wikidata
View/Edit HumanView/Edit Mouse

Retinoblastoma-binding protein 8 is a protein that in humans is encoded by the RBBP8 gene.[3][4][5]

Function

The protein encoded by this gene is a ubiquitously expressed nuclear protein. It is found among several proteins that bind directly to retinoblastoma protein, which regulates cell proliferation. This protein complexes with transcriptional co-repressor CTBP. It is also associated with BRCA1 and is thought to modulate the functions of BRCA1 in transcriptional regulation, DNA repair, and/or cell cycle checkpoint control. It is suggested that this gene may itself be a tumor suppressor acting in the same pathway as BRCA1. Three transcript variants encoding two different isoforms have been found for this gene. More transcript variants exist, but their full-length natures have not been determined.[5]

Interactions

RBBP8 has been shown to interact with:

References

  1. ↑ "Human PubMed Reference:".
  2. ↑ "Mouse PubMed Reference:".
  3. 1 2 3 4 Fusco C, Reymond A, Zervos AS (October 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics. 51 (3): 351–8. doi:10.1006/geno.1998.5368. PMID 9721205.
  4. ↑ Sartori AA, Lukas C, Coates J, Mistrik M, Fu S, Bartek J, Baer R, Lukas J, Jackson SP (November 2007). "Human CtIP promotes DNA end resection". Nature. 450 (7169): 509–14. doi:10.1038/nature06337. PMC 2409435Freely accessible. PMID 17965729.
  5. 1 2 "Entrez Gene: RBBP8 retinoblastoma binding protein 8".
  6. 1 2 Li S, Ting NS, Zheng L, Chen PL, Ziv Y, Shiloh Y, Lee EY, Lee WH (July 2000). "Functional link of BRCA1 and ataxia telangiectasia gene product in DNA damage response". Nature. 406 (6792): 210–5. doi:10.1038/35018134. PMID 10910365.
  7. ↑ Kim ST, Lim DS, Canman CE, Kastan MB (Dec 1999). "Substrate specificities and identification of putative substrates of ATM kinase family members". J. Biol. Chem. 274 (53): 37538–43. doi:10.1074/jbc.274.53.37538. PMID 10608806.
  8. 1 2 Li S, Chen PL, Subramanian T, Chinnadurai G, Tomlinson G, Osborne CK, Sharp ZD, Lee WH (April 1999). "Binding of CtIP to the BRCT repeats of BRCA1 involved in the transcription regulation of p21 is disrupted upon DNA damage". J. Biol. Chem. 274 (16): 11334–8. doi:10.1074/jbc.274.16.11334. PMID 10196224.
  9. ↑ Rodriguez M, Yu X, Chen J, Songyang Z (Dec 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. doi:10.1074/jbc.C300407200. PMID 14578343.
  10. ↑ Wong AK, Ormonde PA, Pero R, Chen Y, Lian L, Salada G, Berry S, Lawrence Q, Dayananth P, Ha P, Tavtigian SV, Teng DH, Bartel PL (November 1998). "Characterization of a carboxy-terminal BRCA1 interacting protein". Oncogene. 17 (18): 2279–85. doi:10.1038/sj.onc.1202150. PMID 9811458.
  11. ↑ Wu-Baer F, Baer R (November 2001). "Effect of DNA damage on a BRCA1 complex". Nature. 414 (6859): 36. doi:10.1038/35102118. PMID 11689934.
  12. ↑ Yu X, Wu LC, Bowcock AM, Aronheim A, Baer R (September 1998). "The C-terminal (BRCT) domains of BRCA1 interact in vivo with CtIP, a protein implicated in the CtBP pathway of transcriptional repression". J. Biol. Chem. 273 (39): 25388–92. doi:10.1074/jbc.273.39.25388. PMID 9738006.
  13. ↑ Yu X, Baer R (June 2000). "Nuclear localization and cell cycle-specific expression of CtIP, a protein that associates with the BRCA1 tumor suppressor". J. Biol. Chem. 275 (24): 18541–9. doi:10.1074/jbc.M909494199. PMID 10764811.
  14. ↑ Schaeper U, Subramanian T, Lim L, Boyd JM, Chinnadurai G (April 1998). "Interaction between a cellular protein that binds to the C-terminal region of adenovirus E1A (CtBP) and a novel cellular protein is disrupted by E1A through a conserved PLDLS motif". J. Biol. Chem. 273 (15): 8549–52. doi:10.1074/jbc.273.15.8549. PMID 9535825.
  15. ↑ Sum EY, Peng B, Yu X, Chen J, Byrne J, Lindeman GJ, Visvader JE (March 2002). "The LIM domain protein LMO4 interacts with the cofactor CtIP and the tumor suppressor BRCA1 and inhibits BRCA1 activity". J. Biol. Chem. 277 (10): 7849–56. doi:10.1074/jbc.M110603200. PMID 11751867.
  16. ↑ Sutherland KD, Visvader JE, Choong DY, Sum EY, Lindeman GJ, Campbell IG (October 2003). "Mutational analysis of the LMO4 gene, encoding a BRCA1-interacting protein, in breast carcinomas". Int. J. Cancer. 107 (1): 155–8. doi:10.1002/ijc.11343. PMID 12925972.
  17. ↑ Dick FA, Sailhamer E, Dyson NJ (May 2000). "Mutagenesis of the pRB pocket reveals that cell cycle arrest functions are separable from binding to viral oncoproteins". Mol. Cell. Biol. 20 (10): 3715–27. doi:10.1128/mcb.20.10.3715-3727.2000. PMC 85672Freely accessible. PMID 10779361.
  18. ↑ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  19. ↑ Meloni AR, Smith EJ, Nevins JR (August 1999). "A mechanism for Rb/p130-mediated transcription repression involving recruitment of the CtBP corepressor". Proc. Natl. Acad. Sci. U.S.A. 96 (17): 9574–9. doi:10.1073/pnas.96.17.9574. PMC 22250Freely accessible. PMID 10449734.
  20. ↑ Germani A, Prabel A, Mourah S, Podgorniak MP, Di Carlo A, Ehrlich R, Gisselbrecht S, Varin-Blank N, Calvo F, Bruzzoni-Giovanelli H (Dec 2003). "SIAH-1 interacts with CtIP and promotes its degradation by the proteasome pathway". Oncogene. 22 (55): 8845–51. doi:10.1038/sj.onc.1206994. PMID 14654780.

Further reading

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