CHMP2A
entrez
27243
canonical
uniprot
O43633
canonical
ensembl
ENSG00000130724
resolver
ensp
ENSP00000310440
resolver
ensp
ENSP00000469240
resolver
ensp
ENSP00000469453
resolver
ensp
ENSP00000471961
resolver
ensp
ENSP00000472097
resolver
ensp
ENSP00000472680
resolver
ensp
ENSP00000555003
resolver
ensp
ENSP00000555006
resolver
ensp
ENSP00000555007
resolver
ensp
ENSP00000555008
resolver
ensp
ENSP00000555009
resolver
ensp
ENSP00000555011
resolver
ensp
ENSP00000555013
resolver
ensp
ENSP00000555014
resolver
ensp
ENSP00000555015
resolver
ensp
ENSP00000555016
resolver
ensp
ENSP00000555017
resolver
ensp
ENSP00000555018
resolver
ensp
ENSP00000555019
resolver
ensp
ENSP00000587524
resolver
ensp
ENSP00000587526
resolver
ensp
ENSP00000587528
resolver
ensp
ENSP00000587529
resolver
ensp
ENSP00000587532
resolver
ensp
ENSP00000587533
resolver
ensp
ENSP00000587535
resolver
enst
ENST00000312547
resolver
enst
ENST00000596708
resolver
enst
ENST00000597848
resolver
enst
ENST00000600006
resolver
enst
ENST00000600118
resolver
enst
ENST00000601220
resolver
enst
ENST00000884944
resolver
enst
ENST00000884947
resolver
enst
ENST00000884948
resolver
enst
ENST00000884949
resolver
enst
ENST00000884950
resolver
enst
ENST00000884952
resolver
enst
ENST00000884954
resolver
enst
ENST00000884955
resolver
enst
ENST00000884956
resolver
enst
ENST00000884957
resolver
enst
ENST00000884958
resolver
enst
ENST00000884959
resolver
enst
ENST00000884960
resolver
enst
ENST00000917465
resolver
enst
ENST00000917467
resolver
enst
ENST00000917469
resolver
enst
ENST00000917470
resolver
enst
ENST00000917473
resolver
enst
ENST00000917474
resolver
enst
ENST00000917476
resolver
genesymbol
CHMP2A
resolver
genesymbol_syn
BC2
resolver
genesymbol_syn
CHMP2
resolver
hgnc
HGNC:30216
resolver
uniprot
B2R4W6
resolver
uniprot
M0R1T5
resolver
uniprot
Q3ZTT0
resolver
uniprot_entry
CHM2A_HUMAN
resolver
uniprot_entry
M0R1T5_HUMAN
resolver
uniprot_sec
B2R4W6
resolver
uniprot_sec
Q3ZTT0
resolver
amino_acid_sequence
MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD
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 (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes nuclear envelope sealing and mitotic spindle disassembly during late anaphase (PubMed:26040712). Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2 (PubMed:28242692). ESCRT-III proteins are believed to mediate the necessary vesicle extrusion and/or membrane fission activities, possibly in conjunction with the AAA ATPase VPS4. {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:26040712, ECO:0000269|PubMed:28242692, ECO:0000305}.; FUNCTION: (Microbial infection) The ESCRT machinery functions in topologically equivalent membrane fission events, such as the budding of enveloped viruses (HIV-1 and other lentiviruses). Involved in HIV-1 p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844}.
uniprot
proteins
mass_dalton
25104
uniprot
proteins
mutagenesis
MUTAGEN 169..170; /note="DE->AA: Diminishes interaction with VPS4B."; /evidence="ECO:0000269|PubMed:18385515"; MUTAGEN 181..222; /note="Missing: Membrane association; releases autoinhibition."; /evidence="ECO:0000269|PubMed:17547705"; MUTAGEN 216; /note="L->A: Diminishes interaction with VTA1."; /evidence="ECO:0000269|PubMed:18385515"; MUTAGEN 217..222; /note="Missing: Abolishes interaction with VTA1."; /evidence="ECO:0000269|PubMed:18385515
uniprot
proteins
post_translational_modification
PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and inhibits its interactions with VPS4A and VTA1 respectively. {ECO:0000269|PubMed:21543490}.
uniprot
proteins
protein_family
SNF7 family
uniprot
proteins
pubmed
11559748
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
14505570
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16533400
uniprot
proteins
pubmed
16730941
uniprot
proteins
pubmed
17547705
uniprot
proteins
pubmed
17853893
uniprot
proteins
pubmed
18385515
uniprot
proteins
pubmed
18687924
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21310966
uniprot
proteins
pubmed
21543490
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26040712
uniprot
proteins
pubmed
28242692
uniprot
proteins
sequence_length
222
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral membrane protein {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Cytoplasmic side {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Nucleus envelope {ECO:0000269|PubMed:28242692}. Note=Localizes to the midbody of dividing cells. Localized in two distinct rings on either side of the Fleming body. Localizes to the reforming nuclear envelope on chromatin disks during late anaphase (PubMed:28242692). {ECO:0000269|PubMed:28242692}.
uniprot
proteins