VPS25
Ensembl | |||||||||
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| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 17: 42.77 – 42.78 Mb | Chr 11: 101.14 – 101.15 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
| ESCRT-II complex subunit | |||||||||
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 crystal structure of subunit vps25 of the endosomal trafficking complex escrt-ii | |||||||||
| Identifiers | |||||||||
| Symbol | ESCRT-II | ||||||||
| Pfam | PF05871 | ||||||||
| InterPro | IPR008570 | ||||||||
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Vacuolar protein-sorting-associated protein 25 is a protein that in humans is encoded by the VPS25 gene.[5][6]
It is a component of the endosome-associated
endosomal membrane and thereby initiates the formation of ESCRT-III, a membrane-associated protein complex that functions immediately downstream of ESCRT-II during sorting of MVB cargo. ESCRT-II in turn functions downstream of ESCRT-I, a protein complex that binds to ubiquitinated endosomal cargo.[9]
ESCRT-II is a trilobal complex composed of two copies of vps25, one copy of vps22 and the C-terminal region of vps36. The crystal structure of vps25 revealed two winged-helix domains, the N-terminal domain of vps25 interacting with vps22 and vps36.[10]
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000131475 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078656 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- PMID 15511219.
- ^ "Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)".
- PMID 17215868.
- PMID 15469844.
- PMID 12194858.
- PMID 15579210.
Further reading
- Kamura T, Burian D, Khalili H, et al. (2001). "Cloning and characterization of ELL-associated proteins EAP45 and EAP20. a role for yeast EAP-like proteins in regulation of gene expression by glucose". J. Biol. Chem. 276 (19): 16528–33. PMID 11278625.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932.
- von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. S2CID 16894972.
- Martin-Serrano J, Yarovoy A, Perez-Caballero D, et al. (2003). "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins". Proc. Natl. Acad. Sci. U.S.A. 100 (21): 12414–9. PMID 14519844.
- Sharma M, Pampinella F, Nemes C, et al. (2004). "Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes". J. Cell Biol. 164 (6): 923–33. PMID 15007060.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. PMID 15489334.
- Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. S2CID 4427026.
- Bowers K, Piper SC, Edeling MA, et al. (2006). "Degradation of endocytosed epidermal growth factor and virally ubiquitinated major histocompatibility complex class I is independent of mammalian ESCRTII". J. Biol. Chem. 281 (8): 5094–105. PMID 16371348.
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