Charged multivesicular body protein 5 (CHMP5)

The protein contains 219 amino acids for an estimated molecular weight of 24571 Da.

 

Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. The MVB pathway appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly dissociate from the invaginating membrane before the ILV is released. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and the budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. Involved in HIV-1 p6- and p9-dependent virus release. (updated: April 1, 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. 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.
  3. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  4. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  5. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

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.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

Interpro domains
Total structural coverage: 44%
Model score: 40
MODL_I-TASSER-3.0

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VariantDescription
dbSNP:rs11540558

The reference OMIM entry for this protein is 610900

Chmp family, member 5; chmp5
Chromatin-modifying protein 5
Charged multivesicular body protein 5
Hspc177

DESCRIPTION

CHMP5 belongs to the chromatin-modifying protein/charged multivesicular body protein (CHMP) family. These proteins are components of ESCRT-III (endosomal sorting complex required for transport III), a complex involved in degradation of surface receptor proteins and formation of endocytic multivesicular bodies (MVBs). Some CHMPs have both nuclear and cytoplasmic/vesicular distributions, and one such CHMP, CHMP1A (164010), is required for both MVB formation and regulation of cell cycle progression (Tsang et al., 2006).

CLONING

Ward et al. (2005) stated that CHMP5 is a small coiled-coil protein. Cell fractionation of COS-7 cells followed by Western blot analysis showed that endogenous Chmp5 was primarily a cytosolic protein. Fluorescence-tagged human CHMP5 localized to vesicles near the nucleus in transfected COS-7 cells.

GENE FUNCTION

Using affinity purification experiments, Ward et al. (2005) showed that LIP5 (610902) specifically interacted with CHMP5. Depletion of CHMP5 by small-interfering RNA did not alter the distribution of early or late endocytic markers in HeLa and 293T cells, but it altered EGFR (131550) trafficking and reduced EGFR degradation in lysosomes. Depletion of CHMP5 in 293T cells infected with human immunodeficiency virus (HIV)-1 increased release of infectious particles. Tsang et al. (2006) performed a systematic yeast 2-hybrid analysis of human ESCRT-III components, including CHMP5. CHMP5 interacted with SMARCA4 (603254), which may be involved in chromatin remodeling. In addition, CHMP5 interacted with the SUMO (see SUMO1; 601912)-conjugating enzyme UBE2I (601661) and appeared to be part of a network connecting CHMP1A, CHMP4B (610897), and CHMP5 with UBE2I, SUMO1, PIAS2 (603567), and HIPK2 (606868), all of which are involved in nuclear sumoylation processes.

MAPPING

Hartz (2007) mapped the CHMP5 gene to chromosome 9p13.3 based on an alignment of the CHMP5 sequence (GenBank GENBANK AF132968) with the genomic sequence (build 36.1). ... More on the omim web site

Subscribe to this protein entry history

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

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

Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 610900 was added.