From Wikipedia, the free encyclopedia
RBL2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases RBL2, P130, Rb2, retinoblastoma-like 2, RB transcriptional corepressor like 2, BRUWAG
External IDs OMIM: 180203; MGI: 105085; HomoloGene: 4098; GeneCards: RBL2; OMA: RBL2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005611
NM_001323608
NM_001323609
NM_001323610
NM_001323611

NM_001282000
NM_001282001
NM_011250

RefSeq (protein)

NP_001310537
NP_001310538
NP_001310539
NP_001310540
NP_005602

NP_001268929
NP_001268930
NP_035380

Location (UCSC) Chr 16: 53.43 – 53.49 Mb Chr 8: 91.8 – 91.85 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Retinoblastoma-like protein 2 is a protein that in humans is encoded by the RBL2 gene. [5] [6]

Interactions

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

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103479Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031666Ensembl, 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. ^ 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.
  6. ^ 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. Bibcode: 1996PNAS...93.4629B. doi: 10.1073/pnas.93.10.4629. PMC  39329. PMID  8643454.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ a b 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.
  11. ^ 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.
  12. ^ 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. S2CID  26359262.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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. Bibcode: 1999PNAS...96.9574M. doi: 10.1073/pnas.96.17.9574. PMC  22250. PMID  10449734.
  17. ^ 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.

From Wikipedia, the free encyclopedia
RBL2
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
Aliases RBL2, P130, Rb2, retinoblastoma-like 2, RB transcriptional corepressor like 2, BRUWAG
External IDs OMIM: 180203; MGI: 105085; HomoloGene: 4098; GeneCards: RBL2; OMA: RBL2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_005611
NM_001323608
NM_001323609
NM_001323610
NM_001323611

NM_001282000
NM_001282001
NM_011250

RefSeq (protein)

NP_001310537
NP_001310538
NP_001310539
NP_001310540
NP_005602

NP_001268929
NP_001268930
NP_035380

Location (UCSC) Chr 16: 53.43 – 53.49 Mb Chr 8: 91.8 – 91.85 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Retinoblastoma-like protein 2 is a protein that in humans is encoded by the RBL2 gene. [5] [6]

Interactions

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

See also

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000103479Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031666Ensembl, 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. ^ 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.
  6. ^ 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. Bibcode: 1996PNAS...93.4629B. doi: 10.1073/pnas.93.10.4629. PMC  39329. PMID  8643454.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ a b 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.
  11. ^ 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.
  12. ^ 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. S2CID  26359262.
  13. ^ 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.
  14. ^ 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.
  15. ^ 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.
  16. ^ 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. Bibcode: 1999PNAS...96.9574M. doi: 10.1073/pnas.96.17.9574. PMC  22250. PMID  10449734.
  17. ^ 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.


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