VPS25

Protein-coding gene in the species Homo sapiens
VPS25
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2ZME, 3CUQ, 3HTU

Identifiers
AliasesVPS25, DERP9, EAP20, FAP20, vacuolar protein sorting 25 homolog
External IDsOMIM: 610907; MGI: 106354; HomoloGene: 6303; GeneCards: VPS25; OMA:VPS25 - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for VPS25
Genomic location for VPS25
Band17q21.2Start42,773,449 bp[1]
End42,779,599 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for VPS25
Genomic location for VPS25
Band11 D|11 64.48 cMStart101,144,533 bp[2]
End101,150,375 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • mucosa of transverse colon

  • rectum

  • islet of Langerhans

  • skin of arm

  • right uterine tube

  • mucosa of ileum

  • body of stomach

  • smooth muscle tissue

  • stromal cell of endometrium

  • olfactory zone of nasal mucosa
Top expressed in
  • yolk sac

  • tail of embryo

  • genital tubercle

  • right kidney

  • lip

  • embryo

  • embryo

  • granulocyte

  • muscle of thigh

  • blastocyst
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • protein homodimerization activity
  • protein N-terminus binding
  • structural molecule activity
  • protein binding
Cellular component
  • cytoplasm
  • cytosol
  • endosome
  • membrane
  • nucleoplasm
  • endosome membrane
  • extracellular exosome
  • nucleus
  • ESCRT II complex
Biological process
  • regulation of transcription, DNA-templated
  • multivesicular body assembly
  • transcription, DNA-templated
  • endosomal transport
  • protein transport
  • protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway
  • macroautophagy
  • negative regulation of epidermal growth factor-activated receptor activity
  • transport
  • multivesicular body sorting pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

84313

28084

Ensembl

ENSG00000131475

ENSMUSG00000078656

UniProt

Q9BRG1

Q9CQ80

RefSeq (mRNA)

NM_032353

NM_001284411
NM_001284412
NM_001284414
NM_026776

RefSeq (protein)

NP_115729
NP_115729.1

NP_001271340
NP_001271341
NP_001271343
NP_081052

Location (UCSC)Chr 17: 42.77 – 42.78 MbChr 11: 101.14 – 101.15 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
ESCRT-II complex subunit
crystal structure of subunit vps25 of the endosomal trafficking complex escrt-ii
Identifiers
SymbolESCRT-II
PfamPF05871
InterProIPR008570
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

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 complex ESCRT-II (Endosomal Sorting Complexes Required for Transport protein II). ESCRT (ESCRT-I, -II, -III) complexes orchestrate efficient sorting of ubiquitinated transmembrane receptors to lysosomes via multivesicular bodies (MVBs).[7] ESCRT-II recruits the transport machinery for protein sorting at MVB.[8] In addition, the human ESCRT-II has been shown to form a complex with RNA polymerase II elongation factor ELL in order to exert transcriptional control activity. ESCRT-II transiently associates with the 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

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000131475 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000078656 – 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. ^ Yorikawa C, Shibata H, Waguri S, Hatta K, Horii M, Katoh K, Kobayashi T, Uchiyama Y, Maki M (Mar 2005). "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an ESCRT-II component EAP20 and regulates endosomal cargo sorting". Biochem J. 387 (Pt 1): 17–26. doi:10.1042/BJ20041227. PMC 1134928. PMID 15511219.
  6. ^ "Entrez Gene: VPS25 vacuolar protein sorting 25 homolog (S. cerevisiae)".
  7. ^ Gill DJ, Teo H, Sun J, Perisic O, Veprintsev DB, Emr SD, Williams RL (January 2007). "Structural insight into the ESCRT-I/-II link and its role in MVB trafficking". EMBO J. 26 (2): 600–12. doi:10.1038/sj.emboj.7601501. PMC 1783442. PMID 17215868.
  8. ^ Teo H, Perisic O, Gonzalez B, Williams RL (October 2004). "ESCRT-II, an endosome-associated complex required for protein sorting: crystal structure and interactions with ESCRT-III and membranes". Dev. Cell. 7 (4): 559–69. doi:10.1016/j.devcel.2004.09.003. PMID 15469844.
  9. ^ Babst M, Katzmann DJ, Snyder WB, Wendland B, Emr SD (August 2002). "Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body". Dev. Cell. 3 (2): 283–9. doi:10.1016/S1534-5807(02)00219-8. PMID 12194858.
  10. ^ Wernimont AK, Weissenhorn W (December 2004). "Crystal structure of subunit VPS25 of the endosomal trafficking complex ESCRT-II". BMC Struct. Biol. 4 (1): 10. doi:10.1186/1472-6807-4-10. PMC 539351. 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. doi:10.1074/jbc.M010142200. 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. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • von Schwedler UK, Stuchell M, Müller B, et al. (2003). "The protein network of HIV budding". Cell. 114 (6): 701–13. doi:10.1016/S0092-8674(03)00714-1. PMID 14505570. 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. Bibcode:2003PNAS..10012414M. doi:10.1073/pnas.2133846100. PMC 218772. 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. doi:10.1083/jcb.200312018. PMC 2172283. 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. doi:10.1101/gr.2596504. PMC 528928. 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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. 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. doi:10.1074/jbc.M508632200. PMID 16371348.
This article incorporates text from the public domain Pfam and InterPro: IPR008570


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