REPS2
From Wikipedia, the free encyclopedia
RALBP1 associated Eps domain containing 2
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PDB rendering based on 1iq3. | |||||||||||
Available structures: 1iq3 | |||||||||||
Identifiers | |||||||||||
Symbol(s) | REPS2; POB1 | ||||||||||
External IDs | OMIM: 300317 MGI: 2663511 HomoloGene: 31255 | ||||||||||
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Orthologs | |||||||||||
Human | Mouse | ||||||||||
Entrez | 9185 | 194590 | |||||||||
Ensembl | ENSG00000169891 | ENSMUSG00000040855 | |||||||||
Uniprot | Q8NFH8 | Q3UHE9 | |||||||||
Refseq | XM_001134057 (mRNA) XP_001134057 (protein) |
XM_976063 (mRNA) XP_981157 (protein) |
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Location | Chr X: 16.87 - 17.08 Mb | Chr X: 157.76 - 157.99 Mb | |||||||||
Pubmed search | [1] | [2] |
RALBP1 associated Eps domain containing 2, also known as REPS2, is a human gene.[1]
The product of this gene is part of a protein complex that regulates the endocytosis of growth factor receptors. The encoded protein directly interacts with a GTPase activating protein that functions downstream of the small G protein Ral. Its expression can negatively affect receptor internalization and inhibit growth factor signaling. Multiple transcript variants encoding different isoforms have been found for this gene.[1]
[edit] References
[edit] Further reading
- Ikeda M, Ishida O, Hinoi T, et al. (1998). "Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral.". J. Biol. Chem. 273 (2): 814–21. PMID 9422736.
- Koshiba S, Kigawa T, Iwahara J, et al. (1999). "Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1).". FEBS Lett. 442 (2-3): 138–42. PMID 9928989.
- Nakashima S, Morinaka K, Koyama S, et al. (1999). "Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors.". EMBO J. 18 (13): 3629–42. doi: . PMID 10393179.
- Morinaka K, Koyama S, Nakashima S, et al. (1999). "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis.". Oncogene 18 (43): 5915–22. doi: . PMID 10557078.
- Matsuzaki T, Hanai S, Kishi H, et al. (2002). "Regulation of endocytosis of activin type II receptors by a novel PDZ protein through Ral/Ral-binding protein 1-dependent pathway.". J. Biol. Chem. 277 (21): 19008–18. doi: . PMID 11882656.
- Oshiro T, Koyama S, Sugiyama S, et al. (2002). "Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin-binding protein, is involved in cell migration.". J. Biol. Chem. 277 (41): 38618–26. doi: . PMID 12149250.
- Oosterhoff JK, Penninkhof F, Brinkmann AO, et al. (2003). "REPS2/POB1 is downregulated during human prostate cancer progression and inhibits growth factor signalling in prostate cancer cells.". Oncogene 22 (19): 2920–5. doi: . PMID 12771942.
- Rossé C, L'Hoste S, Offner N, et al. (2003). "RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis.". J. Biol. Chem. 278 (33): 30597–604. doi: . PMID 12775724.
- Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi: . PMID 14702039.
- Penninkhof F, Grootegoed JA, Blok LJ (2004). "Identification of REPS2 as a putative modulator of NF-kappaB activity in prostate cancer cells.". Oncogene 23 (33): 5607–15. doi: . PMID 15184881.
- Oosterhoff JK, Kühne LC, Grootegoed JA, Blok LJ (2005). "EGF signalling in prostate cancer cell lines is inhibited by a high expression level of the endocytosis protein REPS2.". Int. J. Cancer 113 (4): 561–7. doi: . PMID 15455380.
- Yadav S, Zajac E, Singhal SS, et al. (2005). "POB1 over-expression inhibits RLIP76-mediated transport of glutathione-conjugates, drugs and promotes apoptosis.". Biochem. Biophys. Res. Commun. 328 (4): 1003–9. doi: . PMID 15707977.