CHMP4A
entrez
29082
canonical
uniprot
Q9BY43
canonical
ensembl
ENSG00000254505
resolver
ensembl
ENSG00000285302
resolver
ensp
ENSP00000324205
resolver
genesymbol
CHMP4A
resolver
genesymbol_syn
C14orf123
resolver
genesymbol_syn
SHAX2
resolver
hgnc
HGNC:20274
resolver
uniprot
Q14D22
resolver
uniprot
Q32Q79
resolver
uniprot
Q86SZ8
resolver
uniprot
Q96QJ9
resolver
uniprot
Q9P026
resolver
uniprot_entry
CHM4A_HUMAN
resolver
uniprot_sec
Q14D22
resolver
uniprot_sec
Q32Q79
resolver
uniprot_sec
Q86SZ8
resolver
uniprot_sec
Q96QJ9
resolver
uniprot_sec
Q9P026
resolver
amino_acid_sequence
MSGLGRLFGKGKKEKGPTPEEAIQKLKETEKILIKKQEFLEQKIQQELQTAKKYGTKNKRAALQALRRKKRFEQQLAQTDGTLSTLEFQREAIENATTNAEVLRTMELAAQSMKKAYQDMDIDKVDELMTDITEQQEVAQQISDAISRPMGFGDDVDEDELLEELEELEQEELAQELLNVGDKEEEPSVKLPSVPSTHLPAGPAPKVDEDEEALKQLAEWVS
uniprot
proteins
function
FUNCTION: Probable core 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. When overexpressed, membrane-assembled circular arrays of CHMP4A filaments can promote or stabilize negative curvature and outward budding. Via its interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus release. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:18209100, ECO:0000269|PubMed:22660413}.
uniprot
proteins
mass_dalton
25098
uniprot
proteins
mutagenesis
MUTAGEN 182..222; /note="Missing: Membrane association; releases autoinhibition."; /evidence="ECO:0000269|PubMed:17547705"; MUTAGEN 209; /note="E->A: Reduces interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:18511562"; MUTAGEN 214; /note="L->A: Abolishes interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:18511562"; MUTAGEN 217; /note="L->A: Abolishes interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:18511562"; MUTAGEN 220; /note="W->A: Abolishes interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:18511562
uniprot
proteins
protein_family
SNF7 family
uniprot
proteins
pubmed
11042152
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
12860994
uniprot
proteins
pubmed
14505569
uniprot
proteins
pubmed
14505570
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14583093
uniprot
proteins
pubmed
14678797
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15632132
uniprot
proteins
pubmed
17547705
uniprot
proteins
pubmed
17853893
uniprot
proteins
pubmed
18209100
uniprot
proteins
pubmed
18511562
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
222
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Note=Membrane-associated. Localizes to large vesicle-like structures. Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body.
uniprot
proteins