##gff-version 3 Q9Y3E7 UniProtKB Initiator methionine 1 1 . . . Note=Removed;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y3E7 UniProtKB Chain 2 222 . . . ID=PRO_0000211479;Note=Charged multivesicular body protein 3 Q9Y3E7 UniProtKB Region 2 113 . . . Note=Intramolecular interaction with C-terminus Q9Y3E7 UniProtKB Region 59 64 . . . Note=Important for autoinhibitory function Q9Y3E7 UniProtKB Region 151 222 . . . Note=Interaction with VPS4A Q9Y3E7 UniProtKB Region 151 220 . . . Note=Intramolecular interaction with N-terminus Q9Y3E7 UniProtKB Region 168 169 . . . Note=Important for autoinhibitory function Q9Y3E7 UniProtKB Region 180 222 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q9Y3E7 UniProtKB Region 203 207 . . . Note=Interaction with STAMBP Q9Y3E7 UniProtKB Region 221 222 . . . Note=Interaction with STAMBP Q9Y3E7 UniProtKB Coiled coil 22 54 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y3E7 UniProtKB Coiled coil 141 222 . . . Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y3E7 UniProtKB Motif 201 211 . . . Note=MIT-interacting motif Q9Y3E7 UniProtKB Site 48 48 . . . Note=Important for autoinhibitory function Q9Y3E7 UniProtKB Site 216 216 . . . Note=Interaction with STAMBP Q9Y3E7 UniProtKB Modified residue 200 200 . . . Note=Phosphoserine;Ontology_term=ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744,ECO:0007744;evidence=ECO:0007744|PubMed:18669648,ECO:0007744|PubMed:19690332,ECO:0007744|PubMed:20068231,ECO:0007744|PubMed:21406692,ECO:0007744|PubMed:23186163;Dbxref=PMID:18669648,PMID:19690332,PMID:20068231,PMID:21406692,PMID:23186163 Q9Y3E7 UniProtKB Lipidation 2 2 . . . Note=N-myristoyl glycine;Ontology_term=ECO:0000255;evidence=ECO:0000255 Q9Y3E7 UniProtKB Cross-link 179 179 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Q9Y3E7 UniProtKB Alternative sequence 1 66 . . . ID=VSP_041076;Note=In isoform 2. Missing;Ontology_term=ECO:0000303,ECO:0000303;evidence=ECO:0000303|PubMed:14702039,ECO:0000303|PubMed:17331679;Dbxref=PMID:14702039,PMID:17331679 Q9Y3E7 UniProtKB Alternative sequence 1 15 . . . ID=VSP_042124;Note=In isoform 3. MGLFGKTQEKPPKEL->MEGELYSALKEEEASESVSSTNFSGEMHFYELVEDTKDGIWLVQ;Ontology_term=ECO:0000303;evidence=ECO:0000303|PubMed:14702039;Dbxref=PMID:14702039 Q9Y3E7 UniProtKB Alternative sequence 74 113 . . . ID=VSP_042125;Note=In isoform 4. Missing;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y3E7 UniProtKB Mutagenesis 24 25 . . . Note=Impairs HIV-1 release%3B when associated with S-28. RK->SA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 28 28 . . . Note=Impairs HIV-1 release%3B when associated with 24-S-A-25. R->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 48 48 . . . Note=Induces assembly with CHMP2A into helical tubes in vitro%3B when associated with D-64. Enhances inhibition of HIV-1 budding in vivo%3B when associated with D-168 and D-169. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525971;Dbxref=PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 54 54 . . . Note=Abolishes dimerization%3B when associated with N-56%3B E-59 and 62-D-E-63. K->S;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 56 56 . . . Note=Abolishes dimerization%3B when associated with S-54%3B E-59 and 62-D-E-63. Q->N;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 59 59 . . . Note=Abolishes interaction with CHMP2A and assembly into helical tubes in vitro%3B when associated with D-62%3B D-168 and D-169. V->D;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16740483,ECO:0000269|PubMed:19525971;Dbxref=PMID:16740483,PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 59 59 . . . Note=Abolishes dimerization%3B when associated with S-54%3B N-56 and 62-D-E-63. V->E;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:16740483,ECO:0000269|PubMed:19525971;Dbxref=PMID:16740483,PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 62 63 . . . Note=Abolishes dimerization%3B when associated with S-54%3B N-56 and E-59. VL->DE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 62 62 . . . Note=Abolishes interaction with CHMP2A and assembly into helical tubes in vitro%3B when associated with D-59%3B D-168 and D-169. V->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525971;Dbxref=PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 64 64 . . . Note=Induces assembly with CHMP2A into helical tubes in vitro%3B when associated with D-48. A->D;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525971;Dbxref=PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 78 79 . . . Note=Abolishes dimerization. YA->AE;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:16740483;Dbxref=PMID:16740483 Q9Y3E7 UniProtKB Mutagenesis 168 169 . . . Note=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%3B when associated with D-59 and D-62. IL->DD;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19525971;Dbxref=PMID:19525971 Q9Y3E7 UniProtKB Mutagenesis 179 222 . . . Note=Membrane association%3B releases autoinhibition. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17547705;Dbxref=PMID:17547705 Q9Y3E7 UniProtKB Mutagenesis 216 217 . . . Note=Abolishes interaction with VPS4A and STAMBP. RL->AA;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17146056;Dbxref=PMID:17146056 Q9Y3E7 UniProtKB Mutagenesis 221 222 . . . Note=Abolishes interaction with VPS4A and STAMBP. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17146056;Dbxref=PMID:17146056 Q9Y3E7 UniProtKB Mutagenesis 222 222 . . . Note=Impairs interaction with VPS4A and STAMBP. Missing;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:17146056;Dbxref=PMID:17146056 Q9Y3E7 UniProtKB Sequence conflict 208 208 . . . Note=E->D;Ontology_term=ECO:0000305;evidence=ECO:0000305 Q9Y3E7 UniProtKB Helix 15 53 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Helix 57 100 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Helix 109 112 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Turn 113 115 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Beta strand 116 118 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7ZCG Q9Y3E7 UniProtKB Beta strand 120 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Helix 125 137 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Helix 164 167 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Beta strand 175 177 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2GD5 Q9Y3E7 UniProtKB Helix 201 220 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:2XZE