Retinoblastoma-like protein 2

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VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Retinoblastoma-like protein 2 is a protein that in humans is encoded by the RBL2 gene.[1][2]

Interactions

Retinoblastoma-like protein 2 has been shown to interact with:

See also

References

  1. Mayol X, Graña X, Baldi A, Sang N, Hu Q, Giordano A (Sep 1993). "Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain". Oncogene. 8 (9): 2561–6. PMID 8361765.
  2. Baldi A, Boccia V, Claudio PP, De Luca A, Giordano A (May 1996). "Genomic structure of the human retinoblastoma-related Rb2/p130 gene". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 4629–32. doi:10.1073/pnas.93.10.4629. PMC 39329. PMID 8643454.
  3. 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.
  4. 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.
  5. Wang S, Ghosh RN, Chellappan SP (Dec 1998). "Raf-1 physically interacts with Rb and regulates its function: a link between mitogenic signaling and cell cycle regulation". Molecular and Cellular Biology. 18 (12): 7487–98. doi:10.1128/mcb.18.12.7487. PMC 109329. PMID 9819434.
  6. 6.0 6.1 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.
  7. Li Y, Graham C, Lacy S, Duncan AM, Whyte P (Dec 1993). "The adenovirus E1A-associated 130-kD protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E". Genes & Development. 7 (12A): 2366–77. doi:10.1101/gad.7.12a.2366. PMID 8253383.
  8. Lacy S, Whyte P (May 1997). "Identification of a p130 domain mediating interactions with cyclin A/cdk 2 and cyclin E/cdk 2 complexes". Oncogene. 14 (20): 2395–406. doi:10.1038/sj.onc.1201085. PMID 9188854.
  9. 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.
  10. Bouzahzah B, Fu M, Iavarone A, Factor VM, Thorgeirsson SS, Pestell RG (Aug 2000). "Transforming growth factor-beta1 recruits histone deacetylase 1 to a p130 repressor complex in transgenic mice in vivo". Cancer Research. 60 (16): 4531–7. PMID 10969803.
  11. 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.
  12. Meloni AR, Smith EJ, Nevins JR (Aug 1999). "A mechanism for Rb/p130-mediated transcription repression involving recruitment of the CtBP corepressor". Proceedings of the National Academy of Sciences of the United States of America. 96 (17): 9574–9. doi:10.1073/pnas.96.17.9574. PMC 22250. PMID 10449734.
  13. 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.

Further reading

External links

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