ID CHM4A_HUMAN Reviewed; 222 AA. AC Q9BY43; Q14D22; Q32Q79; Q86SZ8; Q96QJ9; Q9P026; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 07-FEB-2006, sequence version 3. DT 28-JAN-2026, entry version 198. DE RecName: Full=Charged multivesicular body protein 4a; DE AltName: Full=Chromatin-modifying protein 4a; DE Short=CHMP4a; DE AltName: Full=SNF7 homolog associated with Alix-2; DE AltName: Full=SNF7-1; DE Short=hSnf-1; DE AltName: Full=Vacuolar protein sorting-associated protein 32-1; DE Short=Vps32-1; DE Short=hVps32-1; GN Name=CHMP4A; Synonyms=C14orf123, SHAX2; ORFNames=CDA04, HSPC134; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP INTERACTION WITH PDCD6IP. RC TISSUE=Cervix; RX PubMed=12860994; DOI=10.1074/jbc.m301604200; RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E., RA Yoshimori T., Maki M.; RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human RT homologue of yeast Snf7 that is involved in multivesicular body sorting."; RL J. Biol. Chem. 278:39104-39113(2003). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-153, FUNCTION, RP SUBCELLULAR LOCATION, AND INTERACTION WITH PDCD6IP. RC TISSUE=Squamous cell carcinoma; RX PubMed=14583093; DOI=10.1042/bj20031347; RA Peck J.W., Bowden E.T., Burbelo P.D.; RT "Structure and function of human Vps20 and Snf7 proteins."; RL Biochem. J. 377:693-700(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Pheochromocytoma; RA Li Y., Huang Q., Peng Y., Song H., Yu Y., Xu S., Ren S., Chen Z., Han Z.; RT "A novel gene expressed in human pheochromocytoma."; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Umbilical cord blood; RX PubMed=11042152; DOI=10.1101/gr.140200; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for 300 RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor RT cells."; RL Genome Res. 10:1546-1560(2000). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=B-cell; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=12508121; DOI=10.1038/nature01348; RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., RA Waterston R., Hood L., Weissenbach J.; RT "The DNA sequence and analysis of human chromosome 14."; RL Nature 421:601-607(2003). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP ARG-153. RC TISSUE=Brain, and Prostate; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH PDCD6IP. RX PubMed=14505569; DOI=10.1016/s0092-8674(03)00653-6; RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.; RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in RT virus budding."; RL Cell 114:689-699(2003). RN [9] RP INTERACTION WITH CHMP4C; VPS4A AND PDCD6IP. RX PubMed=14505570; DOI=10.1016/s0092-8674(03)00714-1; RA von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y., RA Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A., RA Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.; RT "The protein network of HIV budding."; RL Cell 114:701-713(2003). RN [10] RP FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, AND INTERACTION WITH CHMP2A; RP CHMP4B; CHMP4C; CHMP6 AND PDCD6IP. RX PubMed=14519844; DOI=10.1073/pnas.2133846100; RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RT "Divergent retroviral late-budding domains recruit vacuolar protein sorting RT factors by using alternative adaptor proteins."; RL Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003). RN [11] RP ERRATUM OF PUBMED:14519844. RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.; RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003). RN [12] RP TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP. RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038; RA Katoh K., Shibata H., Hatta K., Maki M.; RT "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix RT among the three CHMP4 isoforms."; RL Arch. Biochem. Biophys. 421:159-165(2004). RN [13] RP SUBCELLULAR LOCATION, AND LIPID-BINDING. RX PubMed=15632132; DOI=10.1074/jbc.m413968200; RA Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.; RT "Interaction of the mammalian endosomal sorting complex required for RT transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the AAA+ RT ATPase SKD1."; RL J. Biol. Chem. 280:12799-12809(2005). RN [14] RP SUBCELLULAR LOCATION. RX PubMed=17853893; DOI=10.1038/sj.emboj.7601850; RA Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., RA Sundquist W.I.; RT "Human ESCRT and ALIX proteins interact with proteins of the midbody and RT function in cytokinesis."; RL EMBO J. 26:4215-4227(2007). RN [15] RP AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP3, AND MUTAGENESIS OF RP 182-ASP--SER-222. RX PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x; RA Shim S., Kimpler L.A., Hanson P.I.; RT "Structure/function analysis of four core ESCRT-III proteins reveals common RT regulatory role for extreme C-terminal domain."; RL Traffic 8:1068-1079(2007). RN [16] RP FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON MICROSCOPY. RX PubMed=18209100; DOI=10.1083/jcb.200707031; RA Hanson P.I., Roth R., Lin Y., Heuser J.E.; RT "Plasma membrane deformation by circular arrays of ESCRT-III protein RT filaments."; RL J. Cell Biol. 180:389-402(2008). RN [17] RP FUNCTION. RX PubMed=22660413; DOI=10.1038/ncb2502; RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A., RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P., RA David G.; RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes."; RL Nat. Cell Biol. 14:677-685(2012). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 210-222 IN COMPLEX WITH PDCD6IP, RP AND MUTAGENESIS OF GLU-209; LEU-214; LEU-217 AND TRP-220. RX PubMed=18511562; DOI=10.1073/pnas.0801567105; RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.; RT "ALIX-CHMP4 interactions in the human ESCRT pathway."; RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008). CC -!- FUNCTION: Probable core component of the endosomal sorting required for CC transport complex III (ESCRT-III) which is involved in multivesicular CC bodies (MVBs) formation and sorting of endosomal cargo proteins into CC MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by CC invagination and scission from the limiting membrane of the endosome CC and mostly are delivered to lysosomes enabling degradation of membrane CC proteins, such as stimulated growth factor receptors, lysosomal enzymes CC and lipids. The MVB pathway appears to require the sequential function CC of ESCRT-O, -I,-II and -III complexes. ESCRT-III proteins mostly CC dissociate from the invaginating membrane before the ILV is released. CC The ESCRT machinery also functions in topologically equivalent membrane CC fission events, such as the terminal stages of cytokinesis and the CC budding of enveloped viruses (HIV-1 and other lentiviruses). ESCRT-III CC proteins are believed to mediate the necessary vesicle extrusion and/or CC membrane fission activities, possibly in conjunction with the AAA CC ATPase VPS4. When overexpressed, membrane-assembled circular arrays of CC CHMP4A filaments can promote or stabilize negative curvature and CC outward budding. Via its interaction with PDCD6IP involved in HIV-1 CC p6- and p9-dependent virus release. CHMP4A/B/C are required for the CC exosomal release of SDCBP, CD63 and syndecan (PubMed:22660413). CC {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093, CC ECO:0000269|PubMed:18209100, ECO:0000269|PubMed:22660413}. CC -!- SUBUNIT: Probable core component of the endosomal sorting required for CC transport complex III (ESCRT-III). ESCRT-III components are thought to CC multimerize to form a flat lattice on the perimeter membrane of the CC endosome. Several assembly forms of ESCRT-III may exist that interact CC and act sequentially. Self-associates; overexpression leads to the CC assembly of filaments that curve and associate to create circular CC rings. Interacts with CHMP2A. Interacts with CHMP3; the interaction CC requires the release of CHMP4A autoinhibition. Interacts with CHMP4B. CC Interacts with CHMP4C. Interacts with CHMP6. Interacts with VPS4A. CC Interacts with PDCD6IP; the interaction is direct. CC {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569, CC ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, CC ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797, CC ECO:0000269|PubMed:17547705, ECO:0000269|PubMed:18511562}. CC -!- INTERACTION: CC Q9BY43; Q9H444: CHMP4B; NbExp=4; IntAct=EBI-747981, EBI-749627; CC Q9BY43; Q8WUM4: PDCD6IP; NbExp=3; IntAct=EBI-747981, EBI-310624; CC Q9BY43; Q9BSW7: SYT17; NbExp=6; IntAct=EBI-747981, EBI-745392; CC Q9BY43-2; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-12178895, EBI-749627; CC Q9BY43-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-12178895, EBI-741158; CC Q9BY43-2; P61970: NUTF2; NbExp=3; IntAct=EBI-12178895, EBI-591778; CC Q9BY43-2; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-12178895, EBI-745392; CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane. Late endosome CC membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. CC Note=Membrane-associated. Localizes to large vesicle-like structures. CC Localizes to the midbody of dividing cells. Localized in two distinct CC rings on either side of the Fleming body. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BY43-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BY43-2; Sequence=VSP_056264; CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in CC heart, kidney, liver and skeletal muscle. Also expressed in brain, CC placenta, lung and pancreas. {ECO:0000269|PubMed:14678797}. CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are thought to CC render the protein in a closed, soluble and inactive conformation CC through an autoinhibitory intramolecular interaction. The open and CC active conformation, which enables membrane binding and CC oligomerization, is achieved by interaction with other cellular binding CC partners, probably including other ESCRT components (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH10893.2; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=AAI07700.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC Sequence=CAD61949.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB100262; BAC79376.2; -; mRNA. DR EMBL; AY329084; AAQ91193.1; -; mRNA. DR EMBL; AF212243; AAK14928.1; -; mRNA. DR EMBL; AF161483; AAF29098.1; -; mRNA. DR EMBL; BX161512; CAD61949.1; ALT_INIT; mRNA. DR EMBL; AL096870; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL136295; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC010893; AAH10893.2; ALT_INIT; mRNA. DR EMBL; BC107699; AAI07700.1; ALT_INIT; mRNA. DR EMBL; BC113533; AAI13534.1; -; mRNA. DR EMBL; BC113535; AAI13536.1; -; mRNA. DR CCDS; CCDS9619.2; -. [Q9BY43-1] DR PDB; 3C3O; X-ray; 2.15 A; B=210-222. DR PDB; 5MK1; X-ray; 2.50 A; E/F/H/K=205-222. DR PDBsum; 3C3O; -. DR PDBsum; 5MK1; -. DR AlphaFoldDB; Q9BY43; -. DR SMR; Q9BY43; -. DR BioGRID; 118852; 79. DR ComplexPortal; CPX-329; ESCRT-III complex. DR CORUM; Q9BY43; -. DR DIP; DIP-39082N; -. DR FunCoup; Q9BY43; 1728. DR IntAct; Q9BY43; 56. DR MINT; Q9BY43; -. DR STRING; 9606.ENSP00000476412; -. DR GlyGen; Q9BY43; 1 site. DR iPTMnet; Q9BY43; -. DR PhosphoSitePlus; Q9BY43; -. DR BioMuta; CHMP4A; -. DR DMDM; 90152096; -. DR jPOST; Q9BY43; -. DR MassIVE; Q9BY43; -. DR PaxDb; 9606-ENSP00000324205; -. DR PeptideAtlas; Q9BY43; -. DR ProteomicsDB; 60344; -. DR ProteomicsDB; 79580; -. [Q9BY43-1] DR Pumba; Q9BY43; -. DR Antibodypedia; 56042; 38 antibodies from 14 providers. DR DNASU; 29082; -. DR Ensembl; ENST00000347519.12; ENSP00000324205.11; ENSG00000254505.12. [Q9BY43-1] DR Ensembl; ENST00000645308.4; ENSP00000495982.2; ENSG00000285302.5. [Q9BY43-1] DR GeneID; 29082; -. DR KEGG; hsa:29082; -. DR MANE-Select; ENST00000347519.12; ENSP00000324205.11; NM_014169.5; NP_054888.3. DR UCSC; uc001wni.4; human. [Q9BY43-1] DR AGR; HGNC:20274; -. DR ClinPGx; PA134888743; -. DR CTD; 29082; -. DR DisGeNET; 29082; -. DR GeneCards; CHMP4A; -. DR HGNC; HGNC:20274; CHMP4A. DR HPA; ENSG00000254505; Low tissue specificity. DR MIM; 610051; gene. DR OpenTargets; ENSG00000254505; -. DR VEuPathDB; HostDB:ENSG00000254505; -. DR eggNOG; KOG1656; Eukaryota. DR GeneTree; ENSGT00940000163323; -. DR HOGENOM; CLU_071097_0_1_1; -. DR InParanoid; Q9BY43; -. DR OMA; RCPKEGL; -. DR OrthoDB; 5592979at2759; -. DR PAN-GO; Q9BY43; 5 GO annotations based on evolutionary models. DR PhylomeDB; Q9BY43; -. DR PathwayCommons; Q9BY43; -. DR Reactome; R-HSA-162588; Budding and maturation of HIV virion. DR Reactome; R-HSA-1632852; Macroautophagy. DR Reactome; R-HSA-5620971; Pyroptosis. DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT). DR Reactome; R-HSA-9610379; HCMV Late Events. DR Reactome; R-HSA-9615710; Late endosomal microautophagy. DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III. DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex. DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex. DR SignaLink; Q9BY43; -. DR SIGNOR; Q9BY43; -. DR Agora; ENSG00000254505; -. DR BioGRID-ORCS; 29082; 11 hits in 1153 CRISPR screens. DR ChiTaRS; CHMP4A; human. DR EvolutionaryTrace; Q9BY43; -. DR GeneWiki; CHMP4A; -. DR GenomeRNAi; 29082; -. DR Pharos; Q9BY43; Tbio. DR PRO; PR:Q9BY43; -. DR Proteomes; UP000005640; Chromosome 14. DR RNAct; Q9BY43; protein. DR Bgee; ENSG00000254505; Expressed in popliteal artery and 100 other cell types or tissues. DR ExpressionAtlas; Q9BY43; baseline and differential. DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal. DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB. DR GO; GO:0000776; C:kinetochore; IDA:ComplexPortal. DR GO; GO:0005828; C:kinetochore microtubule; IDA:ComplexPortal. DR GO; GO:0005765; C:lysosomal membrane; IDA:ComplexPortal. DR GO; GO:0030117; C:membrane coat; IMP:UniProtKB. DR GO; GO:0030496; C:midbody; IDA:FlyBase. DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central. DR GO; GO:0032585; C:multivesicular body membrane; IDA:ComplexPortal. DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal. DR GO; GO:0051117; F:ATPase binding; IPI:UniProtKB. DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal. DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal. DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal. DR GO; GO:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central. DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL. DR GO; GO:0090148; P:membrane fission; NAS:ComplexPortal. DR GO; GO:0010324; P:membrane invagination; IMP:UniProtKB. DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB. DR GO; GO:0007080; P:mitotic metaphase chromosome alignment; IMP:UniProtKB. DR GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL. DR GO; GO:0071985; P:multivesicular body sorting pathway; IDA:ComplexPortal. DR GO; GO:0061763; P:multivesicular body-lysosome fusion; NAS:ComplexPortal. DR GO; GO:0050877; P:nervous system process; IMP:UniProtKB. DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:ComplexPortal. DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB. DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal. DR GO; GO:0097320; P:plasma membrane tubulation; IMP:UniProtKB. DR GO; GO:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:UniProtKB. DR GO; GO:0051258; P:protein polymerization; IMP:UniProtKB. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW. DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:ComplexPortal. DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal. DR GO; GO:0006900; P:vesicle budding from membrane; IMP:UniProtKB. DR GO; GO:0051469; P:vesicle fusion with vacuole; NAS:ComplexPortal. DR GO; GO:0046761; P:viral budding from plasma membrane; IDA:ComplexPortal. DR GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB. DR FunFam; 1.10.287.1060:FF:000001; Charged multivesicular body protein 4b; 1. DR Gene3D; 6.10.250.1710; -; 1. DR Gene3D; 1.10.287.1060; ESAT-6-like; 1. DR InterPro; IPR005024; Snf7_fam. DR PANTHER; PTHR22761; CHARGED MULTIVESICULAR BODY PROTEIN; 1. DR PANTHER; PTHR22761:SF14; CHARGED MULTIVESICULAR BODY PROTEIN 4A; 1. DR Pfam; PF03357; Snf7; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasmic vesicle; KW Endosome; Lipid-binding; Membrane; Phosphoprotein; Protein transport; KW Proteomics identification; Reference proteome; Transport. FT CHAIN 1..222 FT /note="Charged multivesicular body protein 4a" FT /id="PRO_0000211488" FT REGION 1..150 FT /note="Intramolecular interaction with C-terminus" FT /evidence="ECO:0000250" FT REGION 1..116 FT /note="Interaction with phosphoinosides" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 151..222 FT /note="Intramolecular interaction with N-terminus" FT /evidence="ECO:0000250" FT REGION 180..211 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 20..105 FT /evidence="ECO:0000255" FT COILED 155..180 FT /evidence="ECO:0000255" FT MOD_RES 196 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VAR_SEQ 1 FT /note="M -> MSRRRPEDGLGKAGPCVMRHHPPRSKAEVWRTLRGGGGRGELAM FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_056264" FT VARIANT 153 FT /note="G -> R (in dbSNP:rs2295322)" FT /evidence="ECO:0000269|PubMed:14583093, FT ECO:0000269|PubMed:15489334" FT /id="VAR_023384" FT MUTAGEN 182..222 FT /note="Missing: Membrane association; releases FT autoinhibition." FT /evidence="ECO:0000269|PubMed:17547705" FT MUTAGEN 209 FT /note="E->A: Reduces interaction with PDCD6IP." FT /evidence="ECO:0000269|PubMed:18511562" FT MUTAGEN 214 FT /note="L->A: Abolishes interaction with PDCD6IP." FT /evidence="ECO:0000269|PubMed:18511562" FT MUTAGEN 217 FT /note="L->A: Abolishes interaction with PDCD6IP." FT /evidence="ECO:0000269|PubMed:18511562" FT MUTAGEN 220 FT /note="W->A: Abolishes interaction with PDCD6IP." FT /evidence="ECO:0000269|PubMed:18511562" FT CONFLICT 16 FT /note="G -> R (in Ref. 4; AAF29098)" FT /evidence="ECO:0000305" FT CONFLICT 66 FT /note="L -> S (in Ref. 4; AAF29098)" FT /evidence="ECO:0000305" FT CONFLICT 152..153 FT /note="FG -> LLE (in Ref. 4; AAF29098)" FT /evidence="ECO:0000305" FT HELIX 212..218 FT /evidence="ECO:0007829|PDB:3C3O" SQ SEQUENCE 222 AA; 25098 MW; 6712BA6AAA1D7CB7 CRC64; MSGLGRLFGK GKKEKGPTPE EAIQKLKETE KILIKKQEFL EQKIQQELQT AKKYGTKNKR AALQALRRKK RFEQQLAQTD GTLSTLEFQR EAIENATTNA EVLRTMELAA QSMKKAYQDM DIDKVDELMT DITEQQEVAQ QISDAISRPM GFGDDVDEDE LLEELEELEQ EELAQELLNV GDKEEEPSVK LPSVPSTHLP AGPAPKVDED EEALKQLAEW VS //