CHMP5
entrez
51510
canonical
uniprot
Q9NZZ3
canonical
ensembl
ENSG00000086065
resolver
ensp
ENSP00000223500
resolver
ensp
ENSP00000442725
resolver
genesymbol
CHMP5
resolver
genesymbol_syn
C9orf83
resolver
genesymbol_syn
SNF7DC2
resolver
hgnc
HGNC:26942
resolver
uniprot
B2RD95
resolver
uniprot
B4DIR6
resolver
uniprot
Q5VXW2
resolver
uniprot
Q96AV2
resolver
uniprot
Q9HB68
resolver
uniprot
Q9NYS4
resolver
uniprot
Q9Y323
resolver
uniprot_entry
CHMP5_HUMAN
resolver
uniprot_sec
B2RD95
resolver
uniprot_sec
B4DIR6
resolver
uniprot_sec
Q5VXW2
resolver
uniprot_sec
Q96AV2
resolver
uniprot_sec
Q9HB68
resolver
uniprot_sec
Q9NYS4
resolver
uniprot_sec
Q9Y323
resolver
amino_acid_sequence
MNRLFGKAKPKAPPPSLTDCIGTVDSRAESIDKKISRLDAELVKYKDQIKKMREGPAKNMVKQKALRVLKQKRMYEQQRDNLAQQSFNMEQANYTIQSLKDTKTTVDAMKLGVKEMKKAYKQVKIDQIEDLQDQLEDMMEDANEIQEALSRSYGTPELDEDDLEAELDALGDELLADEDSSYLDEAASAPAIPEGVPTDTKNKDGVLVDEFGLPQIPAS
uniprot
proteins
function
FUNCTION: 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) (PubMed:14519844). 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 (PubMed:14519844). {ECO:0000269|PubMed:14519844}.
uniprot
proteins
mass_dalton
24571
uniprot
proteins
mutagenesis
MUTAGEN 7..11; /note="KAKPK->RARPR: Decreased stearoylation in response to S.flexneri infection."; /evidence="ECO:0000269|PubMed:30061757"; MUTAGEN 7; /note="K->R: Decreased stearoylation in response to S.flexneri infection."; /evidence="ECO:0000269|PubMed:30061757
uniprot
proteins
post_translational_modification
PTM: (Microbial infection) Stearoylated By S.flexneri N-epsilon-fatty acyltransferase IcsB, promoting S.flexneri evasion of autophagy. {ECO:0000269|PubMed:30061757}.; PTM: ISGylated. Isgylation inhibits its interaction with VTA1. {ECO:0000269|PubMed:21543490}.
uniprot
proteins
protein_family
SNF7 family
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15644320
uniprot
proteins
pubmed
17261583
uniprot
proteins
pubmed
17853893
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21543490
uniprot
proteins
pubmed
22484091
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27812135
uniprot
proteins
pubmed
30061757
uniprot
proteins
sequence_length
219
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15644320}. Endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Midbody {ECO:0000269|PubMed:17853893}. Note=Localizes to the midbody of dividing cells (PubMed:17853893). Localized in two distinct rings on either side of the Flemming body (PubMed:17853893). {ECO:0000269|PubMed:17853893}.
uniprot
proteins