Vacuolar protein-sorting-associated protein 25 (VPS25)

The protein contains 176 amino acids for an estimated molecular weight of 20748 Da.

 

Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. The MVB pathway mediates delivery of transmembrane proteins into the lumen of the lysosome for degradation. The ESCRT-II complex is probably involved in the recruitment of the ESCRT-III complex. The ESCRT-II complex may also play a role in transcription regulation, possibly via its interaction with ELL. The ESCRT-II complex may be involved in facilitating the budding of certain RNA viruses. (updated: Feb. 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
  3. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  4. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  5. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  6. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete
TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.

Interpro domains
Total structural coverage: 100%
Model score: 100

(right-click above to access to more options from the contextual menu)

VariantDescription
dbSNP:rs34494804

The reference OMIM entry for this protein is 610907

Vacuolar protein sorting 25, s. cerevisiae, homolog of; vps25
Ell-associated protein, 20-kd; eap20

DESCRIPTION

VPS25, VPS36 (610903), and SNF8 (610904) form ESCRT-II (endosomal sorting complex required for transport II), a complex involved in endocytosis of ubiquitinated membrane proteins. VPS25, VPS36, and SNF8 are also associated in a multiprotein complex with RNA polymerase II elongation factor (ELL; 600284) (Slagsvold et al., 2005; Kamura et al., 2001).

CLONING

Kamura et al. (2001) purified the Ell-containing complex from rat liver extracts, and by peptide sequencing and database analysis, they identified mouse and human VPS25, which they called EAP20. The deduced mouse and human proteins contain 176 amino acids, have calculated molecular masses of 21 kD, and are identical.

GENE FUNCTION

Using mouse proteins expressed in mammalian and insect cells, Kamura et al. (2001) found that Eap30 (SNF8) and Eap20 could be coimmunoprecipitated in the absence of Eap45 (VPS36), and that Eap20 and Eap45 could be coimmunoprecipitated in the absence of Eap30. However, little Eap30 was coimmunoprecipitated with Eap45 in the absence of Eap20. Kamura et al. (2001) concluded that EAP20 bridges EAP30 and EAP45 and thereby nucleates assembly of the EAP complex. By coimmunoprecipitation of epitope-tagged proteins expressed in HEK293 cells, Yorikawa et al. (2005) showed that CHMP6 (610901) interacted with CHMP4B (610897) and EAP20. In vitro pull-down assays using recombinant proteins demonstrated direct physical interaction that was mediated by the N-terminal basic half of CHMP6. Epitope-tagged EAP20 localized diffusely in transfected HeLa cells, but it exhibited a punctate distribution when coexpressed with CHMP6.

MAPPING

Hartz (2007) mapped the VPS25 gene to chromosome 17q21.3 based on an alignment of the VPS25 sequence (GenBank GENBANK AB014763) with the genomic sequence (build 36.1). ... More on the omim web site

Subscribe to this protein entry history

May 13, 2019: Protein entry updated
Automatic update: model status changed

Nov. 17, 2018: Protein entry updated
Automatic update: model status changed

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

Oct. 27, 2017: Protein entry updated
Automatic update: model status changed

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610907 was added.

Feb. 24, 2016: Protein entry updated
Automatic update: model status changed