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Gene Review

REPS2  -  RALBP1 associated Eps domain containing 2

Homo sapiens

Synonyms: POB1, Partner of RalBP1, RalBP1-associated Eps domain-containing protein 2, RalBP1-interacting protein 2
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Disease relevance of REPS2


High impact information on REPS2

  • POB1 is a binding protein of RalBP1 and has the Eps15 homology (EH) domain [2].
  • The EH domain of POB1 bound directly to Epsin and Eps15 [2].
  • Deletion mutants of POB1 inhibited internalization of EGF and insulin [2].
  • POB1 formed a complex with PAG2 in intact cells [3].
  • The carboxyl-terminal region containing the proline-rich motifs of POB1 directly bound to the carboxyl-terminal region including the SH3 domain of PAG2 [3].

Chemical compound and disease context of REPS2


Biological context of REPS2


Anatomical context of REPS2


Associations of REPS2 with chemical compounds

  • Both doxorubicin and a model GSH-conjugate, dinitrophenyl-S-glutathione (DNP-SG), transport were inhibited by POB1 in a concentration-dependent manner but not by POB1(1-512), lacking RLIP76-binding site [6].
  • These results suggest that RalBP1 makes a complex with POB1 and that this complex may provide a link between tyrosine kinase, Src homology 3 (SH3)-containing protein, and Ral [5].

Physical interactions of REPS2

  • Furthermore, POB1 bound to Grb2 but not to Nck or Crk [5].

Regulatory relationships of REPS2


Other interactions of REPS2

  • Internalisation and signalling of EGF receptors was examined in different prostate cancer cell lines, in relation to the expression level of the endocytosis-related REPS2 gene [7].
  • From these experiments, it is concluded that increased REPS2 expression negatively affects EGF receptor internalisation and subsequent signalling [7].
  • Substitutions of Pro(423) and Pro(426) with Ala (POB1(PA)) impaired the binding of POB1 to PAG2 [3].
  • These results suggest that phosphorylation of Epsin in mitotic phase inhibits receptor-mediated endocytosis by disassembly of its complex with POB1 and alpha-adaptin [8].
  • In the calcium-bound state, the orientation of the fourth alpha-helix relative to the other helices of the POB1 EH domain is slightly different from that of calbindin, and much more different from those of calmodulin and troponin C, on the basis of their atomic coordinates [9].


  1. Identification of REPS2 as a putative modulator of NF-kappaB activity in prostate cancer cells. Penninkhof, F., Grootegoed, J.A., Blok, L.J. Oncogene (2004) [Pubmed]
  2. Small G protein Ral and its downstream molecules regulate endocytosis of EGF and insulin receptors. Nakashima, S., Morinaka, K., Koyama, S., Ikeda, M., Kishida, M., Okawa, K., Iwamatsu, A., Kishida, S., Kikuchi, A. EMBO J. (1999) [Pubmed]
  3. Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin-binding protein, is involved in cell migration. Oshiro, T., Koyama, S., Sugiyama, S., Kondo, A., Onodera, Y., Asahara, T., Sabe, H., Kikuchi, A. J. Biol. Chem. (2002) [Pubmed]
  4. REPS2/POB1 is downregulated during human prostate cancer progression and inhibits growth factor signalling in prostate cancer cells. Oosterhoff, J.K., Penninkhof, F., Brinkmann, A.O., Anton Grootegoed, J., Blok, L.J. Oncogene (2003) [Pubmed]
  5. Identification and characterization of a novel protein interacting with Ral-binding protein 1, a putative effector protein of Ral. Ikeda, M., Ishida, O., Hinoi, T., Kishida, S., Kikuchi, A. J. Biol. Chem. (1998) [Pubmed]
  6. POB1 over-expression inhibits RLIP76-mediated transport of glutathione-conjugates, drugs and promotes apoptosis. Yadav, S., Zajac, E., Singhal, S.S., Singhal, J., Drake, K., Awasthi, Y.C., Awasthi, S. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
  7. EGF signalling in prostate cancer cell lines is inhibited by a high expression level of the endocytosis protein REPS2. Oosterhoff, J.K., Kühne, L.C., Grootegoed, J.A., Blok, L.J. Int. J. Cancer (2005) [Pubmed]
  8. Regulation of complex formation of POB1/epsin/adaptor protein complex 2 by mitotic phosphorylation. Kariya, K., Koyama, S., Nakashima, S., Oshiro, T., Morinaka, K., Kikuchi, A. J. Biol. Chem. (2000) [Pubmed]
  9. Solution structure of the Eps15 homology domain of a human POB1 (partner of RalBP1). Koshiba, S., Kigawa, T., Iwahara, J., Kikuchi, A., Yokoyama, S. FEBS Lett. (1999) [Pubmed]
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