CHMP4C
entrez
92421
canonical
uniprot
Q96CF2
canonical
ensembl
ENSG00000164695
resolver
ensp
ENSP00000297265
resolver
enst
ENST00000297265
resolver
genesymbol
CHMP4C
resolver
genesymbol_syn
SHAX3
resolver
hgnc
HGNC:30599
resolver
uniprot
B2RBZ1
resolver
uniprot_entry
CHM4C_HUMAN
resolver
uniprot_sec
B2RBZ1
resolver
amino_acid_sequence
MSKLGKFFKGGGSSKSRAAPSPQEALVRLRETEEMLGKKQEYLENRIQREIALAKKHGTQNKRAALQALKRKKRFEKQLTQIDGTLSTIEFQREALENSHTNTEVLRNMGFAAKAMKSVHENMDLNKIDDLMQEITEQQDIAQEISEAFSQRVGFGDDFDEDELMAELEELEQEELNKKMTNIRLPNVPSSSLPAQPNRKPGMSSTARRSRAASSQRAEEEDDDIKQLAAWAT
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). Key component of the cytokinesis checkpoint, a process required to delay abscission to prevent both premature resolution of intercellular chromosome bridges and accumulation of DNA damage: upon phosphorylation by AURKB, together with ZFYVE19/ANCHR, retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. Deactivation of AURKB results in dephosphorylation of CHMP4C followed by its dissociation from ANCHR and VPS4 and subsequent abscission (PubMed:22422861, PubMed:24814515). 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. CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:24814515}.
uniprot
proteins
mass_dalton
26411
uniprot
proteins
mutagenesis
MUTAGEN 210; /note="S->A: Abolishes localization to the Flemming body and ability to delay abscission."; /evidence="ECO:0000269|PubMed:22422861
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-210 by AURKB during cytokinesis: together with ZFYVE19/ANCHR, phosphorylated CHMP4C retains abscission-competent VPS4 (VPS4A and/or VPS4B) at the midbody ring until abscission checkpoint signaling is terminated at late cytokinesis. {ECO:0000269|PubMed:22422861}.
uniprot
proteins
protein_family
SNF7 family
uniprot
proteins
pubmed
14505569
uniprot
proteins
pubmed
14505570
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14583093
uniprot
proteins
pubmed
14678797
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18511562
uniprot
proteins
pubmed
22422861
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
24814515
uniprot
proteins
sequence_length
233
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Late endosome membrane {ECO:0000305|PubMed:14583093}; Peripheral membrane protein {ECO:0000305}. Midbody, Midbody ring {ECO:0000269|PubMed:22422861}. Note=Localizes to the midbody during late cytokinesis. During its recruitment, localizes initially to the midbody arms, before being directed to the central region, the midbody ring, also called Flemming body. Phosphorylation at Ser-210 by AURKB triggers localization to midbody ring. {ECO:0000269|PubMed:22422861}.
uniprot
proteins