Q9Y3E7
uniprot
Q9Y3E7
canonical
amino_acid_sequence
MGLFGKTQEKPPKELVNEWSLKIRKEMRVVDRQIRDIQREEEKVKRSVKDAAKKGQKDVCIVLAKEMIRSRKAVSKLYASKAHMNSVLMGMKNQLAVLRVAGSLQKSTEVMKAMQSLVKIPEIQATMRELSKEMMKAGIIEEMLEDTFESMDDQEEMEEEAEMEIDRILFEITAGALGKAPSKVTDALPEPEPPGAMAASEDEEEEEEALEAMQSRLATLRS
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. Selectively binds to phosphatidylinositol 3,5-bisphosphate PtdIns(3,5)P2 and PtdIns(3,4)P2 in preference to other phosphoinositides tested. Involved in late stages of cytokinesis. Plays a role in endosomal sorting/trafficking of EGF receptor. Isoform 2 prevents stress-mediated cell death and accumulation of reactive oxygen species when expressed in yeast cells. {ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:15707591, ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:17331679, ECO:0000269|PubMed:18076377}.
uniprot
proteins
mass_dalton
25073
uniprot
proteins
mutagenesis
MUTAGEN 24..25; /note="RK->SA: Impairs HIV-1 release; when associated with S-28."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 28; /note="R->S: Impairs HIV-1 release; when associated with 24-S-A-25."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 48; /note="V->D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-64. Enhances inhibition of HIV-1 budding in vivo; when associated with D-168 and D-169."; /evidence="ECO:0000269|PubMed:19525971"; MUTAGEN 54; /note="K->S: Abolishes dimerization; when associated with N-56; E-59 and 62-D-E-63."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 56; /note="Q->N: Abolishes dimerization; when associated with S-54; E-59 and 62-D-E-63."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 59; /note="V->D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-62; D-168 and D-169."; /evidence="ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:19525971"; MUTAGEN 59; /note="V->E: Abolishes dimerization; when associated with S-54; N-56 and 62-D-E-63."; /evidence="ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:19525971"; MUTAGEN 62..63; /note="VL->DE: Abolishes dimerization; when associated with S-54; N-56 and E-59."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 62; /note="V->D: Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59; D-168 and D-169."; /evidence="ECO:0000269|PubMed:19525971"; MUTAGEN 64; /note="A->D: Induces assembly with CHMP2A into helical tubes in vitro; when associated with D-48."; /evidence="ECO:0000269|PubMed:19525971"; MUTAGEN 78..79; /note="YA->AE: Abolishes dimerization."; /evidence="ECO:0000269|PubMed:16740483"; MUTAGEN 168..169; /note="IL->DD: Induces assembly with CHMP2A into helical tubes in vitro and slightly enhances inhibition of HIV-1 budding in vivo. Abolishes interaction with CHMP2A and assembly into helical tubes in vitro; when associated with D-59 and D-62."; /evidence="ECO:0000269|PubMed:19525971"; MUTAGEN 179..222; /note="Missing: Membrane association; releases autoinhibition."; /evidence="ECO:0000269|PubMed:17547705"; MUTAGEN 216..217; /note="RL->AA: Abolishes interaction with VPS4A and STAMBP."; /evidence="ECO:0000269|PubMed:17146056"; MUTAGEN 221..222; /note="Missing: Abolishes interaction with VPS4A and STAMBP."; /evidence="ECO:0000269|PubMed:17146056"; MUTAGEN 222; /note="Missing: Impairs interaction with VPS4A and STAMBP."; /evidence="ECO:0000269|PubMed:17146056
uniprot
proteins
protein_family
SNF7 family
uniprot
proteins
pubmed
10810093
uniprot
proteins
pubmed
11549700
uniprot
proteins
pubmed
14505570
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15632132
uniprot
proteins
pubmed
15707591
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16533400
uniprot
proteins
pubmed
16730941
uniprot
proteins
pubmed
16740483
uniprot
proteins
pubmed
17146056
uniprot
proteins
pubmed
17261583
uniprot
proteins
pubmed
17331679
uniprot
proteins
pubmed
17547705
uniprot
proteins
pubmed
18076377
uniprot
proteins
pubmed
18395747
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18687924
uniprot
proteins
pubmed
19525971
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21543490
uniprot
proteins
pubmed
21827950
uniprot
proteins
pubmed
23186163
uniprot
proteins
sequence_length
222
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Lipid-anchor. Endosome. Late endosome membrane {ECO:0000305}. Note=Localizes to the midbody of dividing cells.
uniprot
proteins