Biology:Retinoblastoma-like protein 1
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Short description: Mammalian protein found in Homo sapiens
 Generic protein structure example |
Retinoblastoma-like 1 (p107), also known as RBL1, is a protein that in humans is encoded by the RBL1 gene.[1][2]
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.[1]
Interactions
Retinoblastoma-like protein 1 has been shown to interact with:
- BEGAIN,[3]
- BRCA1,[4]
- BRF1,[5]
- Cyclin A2,[6][7]
- Cyclin-dependent kinase 2,[8][9]
- E2F1,[6]
- HDAC1,[10][11]
- MYBL2[7][12]
- Mothers against decapentaplegic homolog 3,[13]
- Prohibitin,[14] and
- RBBP8.[15][3]
See also
References
- ↑ 1.0 1.1 "Entrez Gene: RBL1 retinoblastoma-like 1 (p107)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5933.
- ↑ "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell 66 (6): 1155–64. Sep 1991. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.
- ↑ 3.0 3.1 "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. Oct 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "Disruption of BRCA1 LXCXE motif alters BRCA1 functional activity and regulation of RB family but not RB protein binding". Oncogene 20 (35): 4827–41. Aug 2001. doi:10.1038/sj.onc.1204666. PMID 11521194.
- ↑ "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. Jun 1999. doi:10.1128/mcb.19.6.4255. PMID 10330166.
- ↑ 6.0 6.1 "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. Dec 1993. doi:10.1128/JVI.67.12.7641-7647.1993. PMID 8230483.
- ↑ 7.0 7.1 "B-Myb overcomes a p107-mediated cell proliferation block by interacting with an N-terminal domain of p107". Oncogene 21 (52): 7923–32. Nov 2002. doi:10.1038/sj.onc.1206001. PMID 12439743.
- ↑ "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. Feb 1999. doi:10.1128/mcb.19.2.1460. PMID 9891079.
- ↑ "Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4". Molecular and Cellular Biology 22 (7): 2242–54. Apr 2002. doi:10.1128/mcb.22.7.2242-2254.2002. PMID 11884610.
- ↑ "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins". Molecular and Cellular Biology 19 (10): 6632–41. Oct 1999. doi:10.1128/mcb.19.10.6632. PMID 10490602.
- ↑ "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. Sep 1998. doi:10.1073/pnas.95.18.10493. PMID 9724731. Bibcode: 1998PNAS...9510493F.
- ↑ "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. Nov 2003. doi:10.1074/jbc.M308953200. PMID 12947099.
- ↑ "E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression". Cell 110 (1): 19–32. Jul 2002. doi:10.1016/s0092-8674(02)00801-2. PMID 12150994.
- ↑ "Prohibitin, a potential tumor suppressor, interacts with RB and regulates E2F function". Oncogene 18 (23): 3501–10. Jun 1999. doi:10.1038/sj.onc.1202684. PMID 10376528.
- ↑ "Molecular cloning and characterization of a novel retinoblastoma-binding protein". Genomics 51 (3): 351–8. Aug 1998. 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
- "Interaction between human cyclin A and adenovirus E1A-associated p107 protein". Science 255 (5040): 87–90. Jan 1992. doi:10.1126/science.1532458. PMID 1532458. Bibcode: 1992Sci...255...87F.
- "Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein". Cell 66 (6): 1155–64. Sep 1991. doi:10.1016/0092-8674(91)90038-Z. PMID 1833063.
- "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. Oct 1995. doi:10.1128/mcb.15.10.5444. PMID 7565695.
- "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. Jul 1995. doi:10.1128/mcb.15.7.3552. PMID 7791762.
- "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. Mar 1995. doi:10.1073/pnas.92.6.2403. PMID 7892279. Bibcode: 1995PNAS...92.2403S.
- "Differential specificity for binding of retinoblastoma binding protein 2 to RB, p107, and TATA-binding protein". Molecular and Cellular Biology 14 (11): 7256–64. Nov 1994. doi:10.1128/mcb.14.11.7256. PMID 7935440.
- "E2F-4, a new member of the E2F transcription factor family, interacts with p107". Genes & Development 8 (22): 2665–79. Nov 1994. doi:10.1101/gad.8.22.2665. PMID 7958924.
- "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. Nov 1994. doi:10.1101/gad.8.22.2680. PMID 7958925.
- "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. Sep 1994. doi:10.1002/j.1460-2075.1994.tb06725.x. PMID 8076603.
- "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. Dec 1993. doi:10.1128/JVI.67.12.7641-7647.1993. PMID 8230483.
- "Inhibition of cell proliferation by p107, a relative of the retinoblastoma protein". Genes & Development 7 (7A): 1111–25. Jul 1993. doi:10.1101/gad.7.7a.1111. PMID 8319904.
- "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. Apr 1996. doi:10.1073/pnas.93.8.3215. PMID 8622916. Bibcode: 1996PNAS...93.3215I.
- "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. May 1996. doi:10.1073/pnas.93.10.4633. PMID 8643455. Bibcode: 1996PNAS...93.4633X.
- "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. Sep 1996. doi:10.1073/pnas.93.19.10315. PMID 8816797. Bibcode: 1996PNAS...9310315V.
- "Rb interacts with TAF(II)250/TFIID through multiple domains". Oncogene 15 (4): 385–92. Jul 1997. doi:10.1038/sj.onc.1201204. PMID 9242374.
- "E2F activity is regulated by cell cycle-dependent changes in subcellular localization". Molecular and Cellular Biology 17 (12): 7268–82. Dec 1997. doi:10.1128/mcb.17.12.7268. PMID 9372959.
- "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. Mar 1998. doi:10.1073/pnas.95.6.2850. PMID 9501179. Bibcode: 1998PNAS...95.2850T.
- "Negative regulation of DNA replication by the retinoblastoma protein is mediated by its association with MCM7". Molecular and Cellular Biology 18 (5): 2748–57. May 1998. doi:10.1128/mcb.18.5.2748. PMID 9566894.
- "A retinoblastoma-binding protein that affects cell-cycle control and confers transforming ability". Nature Genetics 19 (4): 371–4. Aug 1998. doi:10.1038/1258. PMID 9697699.
- "A cellular repressor of E1A-stimulated genes that inhibits activation by E2F". Molecular and Cellular Biology 18 (9): 5032–41. Sep 1998. doi:10.1128/mcb.18.9.5032. PMID 9710587.
External links
- RBL1+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)
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