From Wikipedia, the free encyclopedia
RBL1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases RBL1, CP107, PRB1, p107, retinoblastoma-like 1, RB transcriptional corepressor like 1
External IDs OMIM: 116957; MGI: 103300; HomoloGene: 2172; GeneCards: RBL1; OMA: RBL1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 Mb Chr 2: 156.99 – 157.05 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000080839Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027641Ensembl, 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. ^ a b "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. S2CID  27478008.
  7. ^ a b 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. Bibcode: 2005Natur.437.1173R. doi: 10.1038/nature04209. PMID  16189514. S2CID  4427026.
  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. ^ a b 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. doi: 10.1128/JVI.67.12.7641-7647.1993. PMC  238233. PMID  8230483.
  11. ^ a b 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. S2CID  21761703.
  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. Bibcode: 1998PNAS...9510493F. 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. S2CID  8945574.
  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. S2CID  33828482.
  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

External links

From Wikipedia, the free encyclopedia
RBL1
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases RBL1, CP107, PRB1, p107, retinoblastoma-like 1, RB transcriptional corepressor like 1
External IDs OMIM: 116957; MGI: 103300; HomoloGene: 2172; GeneCards: RBL1; OMA: RBL1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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 Mb Chr 2: 156.99 – 157.05 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000080839Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000027641Ensembl, 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. ^ a b "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. S2CID  27478008.
  7. ^ a b 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. Bibcode: 2005Natur.437.1173R. doi: 10.1038/nature04209. PMID  16189514. S2CID  4427026.
  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. ^ a b 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. doi: 10.1128/JVI.67.12.7641-7647.1993. PMC  238233. PMID  8230483.
  11. ^ a b 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. S2CID  21761703.
  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. Bibcode: 1998PNAS...9510493F. 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. S2CID  8945574.
  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. S2CID  33828482.
  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

External links


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