Retinoblastoma-like protein 1

RBL1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRBL1, CP107, PRB1, p107, retinoblastoma-like 1, RB transcriptional corepressor like 1
External IDsMGI: 103300 HomoloGene: 2172 GeneCards: RBL1
Gene location (Human)
Chr.Chromosome 20 (human)[1]
Band20q11.23Start36,996,349 bp[1]
End37,095,995 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

5933

19650

Ensembl

ENSG00000080839

ENSMUSG00000027641

UniProt

P28749

Q64701

RefSeq (mRNA)

NM_002895
NM_183404
NM_001323281
NM_001323282

NM_001139516
NM_011249

RefSeq (protein)

NP_001310210
NP_001310211
NP_002886
NP_899662

NP_001132988
NP_035379

Location (UCSC)Chr 20: 37 – 37.1 MbChr 2: 157.15 – 157.2 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Retinoblastoma-like 1 (p107), also known as RBL1, is a protein that in humans is encoded by the RBL1 gene.[5][6]

Function

The protein encoded by this gene is similar in sequence and possibly function to the product of the retinoblastoma 1 (RB1) gene. The RB1 gene product is a tumor suppressor protein that appears to be involved in cell cycle regulation, as it is phosphorylated in the S to M phase transition and is dephosphorylated in the G1 phase of the cell cycle. Both the RB1 protein and the product of this gene can form a complex with adenovirus E1A protein and SV40 Large T-antigen, with the SV40 large T-antigen binding only to the unphosphorylated form of each protein. In addition, both proteins can inhibit the transcription of cell cycle genes containing E2F binding sites in their promoters. Due to the sequence and biochemical similarities with the RB1 protein, it is thought that the protein encoded by this gene may also be a tumor suppressor. Two transcript variants encoding different isoforms have been found for this gene.[5]

Interactions

Retinoblastoma-like protein 1 has been shown to interact with:

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000080839 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027641 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: RBL1 retinoblastoma-like 1 (p107)".
  6. ↑ Ewen ME, Xing YG, Lawrence JB, Livingston DM (Sep 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell. 66 (6): 1155–64. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.
  7. 1 2 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 (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
  8. ↑ Fan S, Yuan R, Ma YX, Xiong J, Meng Q, Erdos M, Zhao JN, Goldberg ID, Pestell RG, Rosen EM (Aug 2001). "Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding". Oncogene. 20 (35): 4827–41. doi:10.1038/sj.onc.1204666. PMID 11521194.
  9. ↑ Sutcliffe JE, Cairns CA, McLees A, Allison SJ, Tosh K, White RJ (Jun 1999). "RNA polymerase III transcription factor IIIB is a target for repression by pocket proteins p107 and p130". Molecular and Cellular Biology. 19 (6): 4255–61. doi:10.1128/mcb.19.6.4255. PMC 104385. PMID 10330166.
  10. 1 2 Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (Dec 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". Journal of Virology. 67 (12): 7641–7. PMC 238233. PMID 8230483.
  11. 1 2 Joaquin M, Bessa M, Saville MK, Watson RJ (Nov 2002). "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene. 21 (52): 7923–32. doi:10.1038/sj.onc.1206001. PMID 12439743.
  12. ↑ Shanahan F, Seghezzi W, Parry D, Mahony D, Lees E (Feb 1999). "Cyclin E associates with BAF155 and BRG1, components of the mammalian SWI-SNF complex, and alters the ability of BRG1 to induce growth arrest". Molecular and Cellular Biology. 19 (2): 1460–9. doi:10.1128/mcb.19.2.1460. PMC 116074. PMID 9891079.
  13. ↑ Leng X, Noble M, Adams PD, Qin J, Harper JW (Apr 2002). "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Molecular and Cellular Biology. 22 (7): 2242–54. doi:10.1128/mcb.22.7.2242-2254.2002. PMC 133692. PMID 11884610.
  14. ↑ Lai A, Lee JM, Yang WM, DeCaprio JA, Kaelin WG, Seto E, Branton PE (Oct 1999). "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology. 19 (10): 6632–41. doi:10.1128/mcb.19.10.6632. PMC 84642. PMID 10490602.
  15. ↑ Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D (Sep 1998). "The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase". Proceedings of the National Academy of Sciences of the United States of America. 95 (18): 10493–8. doi:10.1073/pnas.95.18.10493. PMC 27922. PMID 9724731.
  16. ↑ Joaquin M, Watson RJ (Nov 2003). "The cell cycle-regulated B-Myb transcription factor overcomes cyclin-dependent kinase inhibitory activity of p57(KIP2) by interacting with its cyclin-binding domain". The Journal of Biological Chemistry. 278 (45): 44255–64. doi:10.1074/jbc.M308953200. PMID 12947099.
  17. ↑ Chen CR, Kang Y, Siegel PM, Massagué J (Jul 2002). "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell. 110 (1): 19–32. doi:10.1016/s0092-8674(02)00801-2. PMID 12150994.
  18. ↑ Wang S, Nath N, Adlam M, Chellappan S (Jun 1999). "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene. 18 (23): 3501–10. doi:10.1038/sj.onc.1202684. PMID 10376528.
  19. ↑ Fusco C, Reymond A, Zervos AS (Aug 1998). "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics. 51 (3): 351–8. doi:10.1006/geno.1998.5368. PMID 9721205.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Further reading

  • Faha B, Ewen ME, Tsai LH, Livingston DM, Harlow E (Jan 1992). "Interaction between human cyclin A and adenovirus E1A-associated p107 protein". Science. 255 (5040): 87–90. doi:10.1126/science.1532458. PMID 1532458.
  • Ewen ME, Xing YG, Lawrence JB, Livingston DM (Sep 1991). "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell. 66 (6): 1155–64. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.
  • Datta PK, Raychaudhuri P, Bagchi S (Oct 1995). "Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription". Molecular and Cellular Biology. 15 (10): 5444–52. doi:10.1128/mcb.15.10.5444. PMC 230794. PMID 7565695.
  • Zhu L, Zhu L, Xie E, Chang LS (Jul 1995). "Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins". Molecular and Cellular Biology. 15 (7): 3552–62. doi:10.1128/mcb.15.7.3552. PMC 230592. PMID 7791762.
  • Sardet C, Vidal M, Cobrinik D, Geng Y, Onufryk C, Chen A, Weinberg RA (Mar 1995). "E2F-4 and E2F-5, two members of the E2F family, are expressed in the early phases of the cell cycle". Proceedings of the National Academy of Sciences of the United States of America. 92 (6): 2403–7. doi:10.1073/pnas.92.6.2403. PMC 42492. PMID 7892279.
  • Kim YW, Otterson GA, Kratzke RA, Coxon AB, Kaye FJ (Nov 1994). "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein". Molecular and Cellular Biology. 14 (11): 7256–64. doi:10.1128/mcb.14.11.7256. PMC 359260. PMID 7935440.
  • Ginsberg D, Vairo G, Chittenden T, Xiao ZX, Xu G, Wydner KL, DeCaprio JA, Lawrence JB, Livingston DM (Nov 1994). "E2F-4, a new member of the E2F transcription factor family, interacts with p107". Genes & Development. 8 (22): 2665–79. doi:10.1101/gad.8.22.2665. PMID 7958924.
  • Beijersbergen RL, Kerkhoven RM, Zhu L, Carlée L, Voorhoeve PM, Bernards R (Nov 1994). "E2F-4, a new member of the E2F gene family, has oncogenic activity and associates with p107 in vivo". Genes & Development. 8 (22): 2680–90. doi:10.1101/gad.8.22.2680. PMID 7958925.
  • Beijersbergen RL, Hijmans EM, Zhu L, Bernards R (Sep 1994). "Interaction of c-Myc with the pRb-related protein p107 results in inhibition of c-Myc-mediated transactivation". The EMBO Journal. 13 (17): 4080–6. PMC 395329. PMID 8076603.
  • Dyson N, Dembski M, Fattaey A, Ngwu C, Ewen M, Helin K (Dec 1993). "Analysis of p107-associated proteins: p107 associates with a form of E2F that differs from pRB-associated E2F-1". Journal of Virology. 67 (12): 7641–7. PMC 238233. PMID 8230483.
  • Zhu L, van den Heuvel S, Helin K, Fattaey A, Ewen M, Livingston D, Dyson N, Harlow E (Jul 1993). "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein". Genes & Development. 7 (7A): 1111–25. doi:10.1101/gad.7.7a.1111. PMID 8319904.
  • Ikeda MA, Jakoi L, Nevins JR (Apr 1996). "A unique role for the Rb protein in controlling E2F accumulation during cell growth and differentiation". Proceedings of the National Academy of Sciences of the United States of America. 93 (8): 3215–20. doi:10.1073/pnas.93.8.3215. PMC 39585. PMID 8622916.
  • Xiao ZX, Ginsberg D, Ewen M, Livingston DM (May 1996). "Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 4633–7. doi:10.1073/pnas.93.10.4633. PMC 39330. PMID 8643455.
  • Vidal M, Brachmann RK, Fattaey A, Harlow E, Boeke JD (Sep 1996). "Reverse two-hybrid and one-hybrid systems to detect dissociation of protein-protein and DNA-protein interactions". Proceedings of the National Academy of Sciences of the United States of America. 93 (19): 10315–20. doi:10.1073/pnas.93.19.10315. PMC 38381. PMID 8816797.
  • Shao Z, Siegert JL, Ruppert S, Robbins PD (Jul 1997). "Rb interacts with TAF(II)250/TFIID through multiple domains". Oncogene. 15 (4): 385–92. doi:10.1038/sj.onc.1201204. PMID 9242374.
  • Verona R, Moberg K, Estes S, Starz M, Vernon JP, Lees JA (Dec 1997). "E2F activity is regulated by cell cycle-dependent changes in subcellular localization". Molecular and Cellular Biology. 17 (12): 7268–82. doi:10.1128/mcb.17.12.7268. PMC 232584. PMID 9372959.
  • Trimarchi JM, Fairchild B, Verona R, Moberg K, Andon N, Lees JA (Mar 1998). "E2F-6, a member of the E2F family that can behave as a transcriptional repressor". Proceedings of the National Academy of Sciences of the United States of America. 95 (6): 2850–5. doi:10.1073/pnas.95.6.2850. PMC 19658. PMID 9501179.
  • Sterner JM, Dew-Knight S, Musahl C, Kornbluth S, Horowitz JM (May 1998). "Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7". Molecular and Cellular Biology. 18 (5): 2748–57. doi:10.1128/mcb.18.5.2748. PMC 110654. PMID 9566894.
  • Woitach JT, Zhang M, Niu CH, Thorgeirsson SS (Aug 1998). "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability". Nature Genetics. 19 (4): 371–4. doi:10.1038/1258. PMID 9697699.
  • Veal E, Eisenstein M, Tseng ZH, Gill G (Sep 1998). "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F". Molecular and Cellular Biology. 18 (9): 5032–41. doi:10.1128/mcb.18.9.5032. PMC 109088. PMID 9710587.
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