REPS2

RalBP1-associated Eps domain-containing protein 2 is a protein that in humans is encoded by the REPS2 gene.[5][6][7]

REPS2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1IQ3
Identifiers
Aliases	REPS2, POB1, RALBP1 associated Eps domain containing 2
External IDs	OMIM: 300317 MGI: 2663511 HomoloGene: 31255 GeneCards: REPS2
Gene location (Human) Chr. X chromosome (human)[1] Band Xp22.2 Start 16,946,658 bp[1] End 17,153,272 bp[1]
Gene location (Mouse) Chr. X chromosome (mouse)[2] Band X|X F4 Start 162,411,954 bp[2] End 162,643,649 bp[2]
Gene ontology Molecular function • calcium ion binding • GO:0001948 protein binding • metal ion binding Cellular component • cytoplasm • cytosol Biological process • epidermal growth factor receptor signaling pathway • membrane organization • macromolecular complex assembly Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	9185	194590
Ensembl	ENSG00000169891	ENSMUSG00000040855
UniProt	Q8NFH8	Q80XA6
RefSeq (mRNA)	NM_001080975 NM_004726	NM_001290633 NM_178256 NM_001359102 NM_001359103 NM_001359104
RefSeq (protein)	NP_001074444 NP_004717	NP_001277562 NP_839987 NP_001346031 NP_001346032 NP_001346033
Location (UCSC)	Chr X: 16.95 – 17.15 Mb	Chr X: 162.41 – 162.64 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

Interactions

REPS2 has been shown to interact with EPN1,[8] EPS15[9] and RALBP1.[5]

References

1. GRCh38: Ensembl release 89: ENSG00000169891 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000040855 - Ensembl, 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. Ikeda M, Ishida O, Hinoi T, Kishida S, Kikuchi A (February 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. doi:10.1074/jbc.273.2.814. PMID 9422736.
6. Koshiba S, Kigawa T, Iwahara J, Kikuchi A, Yokoyama S (February 1999). "Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1)". FEBS Lett. 442 (2–3): 138–42. doi:10.1016/S0014-5793(98)01644-5. PMID 9928989.
7. "Entrez Gene: REPS2 RALBP1 associated Eps domain containing 2".
8. Morinaka K, Koyama S, Nakashima S, Hinoi T, Okawa K, Iwamatsu A, Kikuchi A (October 1999). "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis". Oncogene. 18 (43): 5915–22. doi:10.1038/sj.onc.1202974. PMID 10557078.
9. Nakashima S, Morinaka K, Koyama S, Ikeda M, Kishida M, Okawa K, Iwamatsu A, Kishida S, Kikuchi A (July 1999). "Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors". EMBO J. 18 (13): 3629–42. doi:10.1093/emboj/18.13.3629. PMC 1171441. PMID 10393179.

Further reading

• Nakashima S, Morinaka K, Koyama S, Ikeda M, Kishida M, Okawa K, Iwamatsu A, Kishida S, Kikuchi A (1999). "Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors". EMBO J. 18 (13): 3629–42. doi:10.1093/emboj/18.13.3629. PMC 1171441. PMID 10393179.
• Morinaka K, Koyama S, Nakashima S, Hinoi T, Okawa K, Iwamatsu A, Kikuchi A (1999). "Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis". Oncogene. 18 (43): 5915–22. doi:10.1038/sj.onc.1202974. PMID 10557078.
• Matsuzaki T, Hanai S, Kishi H, Liu Z, Bao Y, Kikuchi A, Tsuchida K, Sugino H (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:10.1074/jbc.M112472200. PMID 11882656.
• Oshiro T, Koyama S, Sugiyama S, Kondo A, Onodera Y, Asahara T, Sabe H, Kikuchi A (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:10.1074/jbc.M203453200. PMID 12149250.
• Oosterhoff JK, Penninkhof F, Brinkmann AO, Anton Grootegoed J, Blok LJ (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:10.1038/sj.onc.1206397. PMID 12771942.
• Rossé C, L'Hoste S, Offner N, Picard A, Camonis J (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:10.1074/jbc.M302191200. PMID 12775724.
• Penninkhof F, Grootegoed JA, Blok LJ (2004). "Identification of REPS2 as a putative modulator of NF-kappaB activity in prostate cancer cells" (PDF). Oncogene. 23 (33): 5607–15. doi:10.1038/sj.onc.1207750. 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:10.1002/ijc.20612. PMID 15455380.
• Yadav S, Zajac E, Singhal SS, Singhal J, Drake K, Awasthi YC, Awasthi S (2005). "POB1 over-expression inhibits RLIP76-mediated transport of glutathione-conjugates, drugs and promotes apoptosis". Biochem. Biophys. Res. Commun. 328 (4): 1003–9. doi:10.1016/j.bbrc.2005.01.055. PMID 15707977.