CHM2A_HUMAN
ID CHM2A_HUMAN Reviewed; 222 AA.
AC O43633; B2R4W6; Q3ZTT0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Charged multivesicular body protein 2a;
DE AltName: Full=Chromatin-modifying protein 2a;
DE Short=CHMP2a;
DE AltName: Full=Putative breast adenocarcinoma marker BC-2;
DE AltName: Full=Vacuolar protein sorting-associated protein 2-1;
DE Short=Vps2-1;
DE Short=hVps2-1;
GN Name=CHMP2A; Synonyms=BC2, CHMP2;
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].
RA Slater C., Thill G., Obar R.;
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Koczan D., Reimer T., Rump A., Merck-Rousseau M.F., Rosenthal A.,
RA Friese K., Thiesen H.J.;
RT "Role of the BC-2 gene in breast cancer.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=16533400; DOI=10.1186/1471-2164-7-48;
RA Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
RA Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
RT "NovelFam3000 -- uncharacterized human protein domains conserved across
RT model organisms.";
RL BMC Genomics 7:48-48(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [9]
RP PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 72-222, AND PROTEIN SEQUENCE OF 75-89 AND
RP 197-205.
RA Keesee S.K., Obar R., Wu Y.-J.;
RT "Materials and methods for detection of breast cancer.";
RL Patent number US5914238, 05-JUN-1996.
RN [11]
RP INTERACTION WITH VPS4B.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [12]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VPS4A AND VPS4B.
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 [13]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHMP1B; CHMP2B; CHMP3;
RP CHMP4A; CHMP4B; CHMP4C; CHMP5 AND VPS4A.
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 [14]
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 [15]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH MITD1.
RX PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
RA Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
RA Sanderson C.M.;
RT "A systematic analysis of human CHMP protein interactions: additional MIT
RT domain-containing proteins bind to multiple components of the human ESCRT
RT III complex.";
RL Genomics 88:333-346(2006).
RN [16]
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 [17]
RP AUTOINHIBITORY MECHANISM, INTERACTION WITH VPS4B, AND MUTAGENESIS OF
RP 181-ASN--ASP-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 [18]
RP INTERACTION WITH VTA1, AND MUTAGENESIS OF 169-ASP-GLU-170; LEU-216 AND
RP 217-LYS--ASP-222.
RX PubMed=18385515; DOI=10.1091/mbc.e07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications
RT for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [19]
RP POLYMERIZATION WITH CHMP3, AND ELECTRON MICROSCOPY.
RX PubMed=18687924; DOI=10.1126/science.1161070;
RA Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G.,
RA Weissenhorn W.;
RT "Helical structures of ESCRT-III are disassembled by VPS4.";
RL Science 321:1354-1357(2008).
RN [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [21]
RP ISGYLATION, AND INTERACTION WITH VTA1 AND VPS4A.
RX PubMed=21543490; DOI=10.1128/jvi.02610-10;
RA Kuang Z., Seo E.J., Leis J.;
RT "Mechanism of inhibition of retrovirus release from cells by interferon-
RT induced gene ISG15.";
RL J. Virol. 85:7153-7161(2011).
RN [22]
RP FUNCTION.
RX PubMed=21310966; DOI=10.1126/science.1201847;
RA Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H.,
RA Mueller-Reichert T., Gerlich D.W.;
RT "Cortical constriction during abscission involves helices of ESCRT-III-
RT dependent filaments.";
RL Science 331:1616-1620(2011).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; THR-185; SER-188;
RP SER-190 AND SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [25]
RP FUNCTION.
RX PubMed=26040712; DOI=10.1038/nature14408;
RA Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W.,
RA Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.;
RT "Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear
RT envelope sealing.";
RL Nature 522:231-235(2015).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=28242692; DOI=10.1073/pnas.1613916114;
RA Gu M., LaJoie D., Chen O.S., von Appen A., Ladinsky M.S., Redd M.J.,
RA Nikolova L., Bjorkman P.J., Sundquist W.I., Ullman K.S., Frost A.;
RT "LEM2 recruits CHMP7 for ESCRT-mediated nuclear envelope closure in fission
RT yeast and human cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:E2166-E2175(2017).
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
CC (PubMed:21310966). Together with SPAST, the ESCRT-III complex promotes
CC nuclear envelope sealing and mitotic spindle disassembly during late
CC anaphase (PubMed:26040712). Recruited to the reforming nuclear envelope
CC (NE) during anaphase by LEMD2 (PubMed:28242692). ESCRT-III proteins are
CC believed to mediate the necessary vesicle extrusion and/or membrane
CC fission activities, possibly in conjunction with the AAA ATPase VPS4.
CC {ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:26040712,
CC ECO:0000269|PubMed:28242692, ECO:0000305}.
CC -!- FUNCTION: (Microbial infection) The ESCRT machinery functions in
CC topologically equivalent membrane fission events, such as the budding
CC of enveloped viruses (HIV-1 and other lentiviruses). Involved in HIV-1
CC p6- and p9-dependent virus release. {ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844}.
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. In vitro, heteromerizes with CHMP3 (but not
CC CHMP4) to form helical tubular structures that expose membrane-
CC interacting sites on the outside whereas VPS4B can associate on the
CC inside of the tubule. Interacts with CHMP1B, CHMP2B, CHMP3, CHMP4A,
CC CHMP4B, CHMP4C and CHMP5. Interacts with VPS4A; the interaction is
CC direct. Interacts with VPS4B; the interaction is direct. Interacts with
CC MITD1. Interacts with VTA1; the interaction probably involves the open
CC conformation of CHMP2A. {ECO:0000269|PubMed:11559748,
CC ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
CC ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17547705,
CC ECO:0000269|PubMed:18385515, ECO:0000269|PubMed:21543490}.
CC -!- INTERACTION:
CC O43633; Q9Y3E7: CHMP3; NbExp=3; IntAct=EBI-2692789, EBI-2118119;
CC O43633; Q9Y3E7-1: CHMP3; NbExp=2; IntAct=EBI-2692789, EBI-15613847;
CC O43633; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-2692789, EBI-749627;
CC O43633; Q8NF50-2: DOCK8; NbExp=3; IntAct=EBI-2692789, EBI-10174653;
CC O43633; P42858: HTT; NbExp=3; IntAct=EBI-2692789, EBI-466029;
CC O43633; Q8WV92: MITD1; NbExp=8; IntAct=EBI-2692789, EBI-2691489;
CC O43633; Q9UN37: VPS4A; NbExp=3; IntAct=EBI-2692789, EBI-1171942;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}; Peripheral
CC membrane protein {ECO:0000269|PubMed:16730941,
CC ECO:0000269|PubMed:17853893}; Cytoplasmic side
CC {ECO:0000269|PubMed:16730941, ECO:0000269|PubMed:17853893}. Nucleus
CC envelope {ECO:0000269|PubMed:28242692}. Note=Localizes to the midbody
CC of dividing cells. Localized in two distinct rings on either side of
CC the Fleming body. Localizes to the reforming nuclear envelope on
CC chromatin disks during late anaphase (PubMed:28242692).
CC {ECO:0000269|PubMed:28242692}.
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.
CC -!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and
CC inhibits its interactions with VPS4A and VTA1 respectively.
CC {ECO:0000269|PubMed:21543490}.
CC -!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AF042384; AAC00005.1; -; mRNA.
DR EMBL; AJ277113; CAC14310.1; -; Genomic_DNA.
DR EMBL; AY364248; AAQ76807.1; -; mRNA.
DR EMBL; BT007298; AAP35962.1; -; mRNA.
DR EMBL; CR457002; CAG33283.1; -; mRNA.
DR EMBL; AK311974; BAG34913.1; -; mRNA.
DR EMBL; CH471135; EAW72609.1; -; Genomic_DNA.
DR EMBL; BC002502; AAH02502.1; -; mRNA.
DR CCDS; CCDS12986.1; -.
DR RefSeq; NP_055268.1; NM_014453.3.
DR RefSeq; NP_940818.1; NM_198426.2.
DR AlphaFoldDB; O43633; -.
DR SMR; O43633; -.
DR BioGRID; 118091; 108.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; O43633; -.
DR DIP; DIP-48533N; -.
DR IntAct; O43633; 48.
DR MINT; O43633; -.
DR STRING; 9606.ENSP00000469240; -.
DR iPTMnet; O43633; -.
DR MetOSite; O43633; -.
DR PhosphoSitePlus; O43633; -.
DR BioMuta; CHMP2A; -.
DR OGP; O43633; -.
DR EPD; O43633; -.
DR jPOST; O43633; -.
DR MassIVE; O43633; -.
DR MaxQB; O43633; -.
DR PaxDb; O43633; -.
DR PeptideAtlas; O43633; -.
DR PRIDE; O43633; -.
DR ProteomicsDB; 49086; -.
DR Antibodypedia; 33353; 173 antibodies from 24 providers.
DR DNASU; 27243; -.
DR Ensembl; ENST00000312547.7; ENSP00000310440.1; ENSG00000130724.10.
DR Ensembl; ENST00000596708.2; ENSP00000471961.2; ENSG00000130724.10.
DR Ensembl; ENST00000597848.2; ENSP00000469453.2; ENSG00000130724.10.
DR Ensembl; ENST00000600118.6; ENSP00000469240.1; ENSG00000130724.10.
DR Ensembl; ENST00000601220.5; ENSP00000472680.1; ENSG00000130724.10.
DR GeneID; 27243; -.
DR KEGG; hsa:27243; -.
DR MANE-Select; ENST00000312547.7; ENSP00000310440.1; NM_014453.4; NP_055268.1.
DR UCSC; uc002qti.3; human.
DR CTD; 27243; -.
DR DisGeNET; 27243; -.
DR GeneCards; CHMP2A; -.
DR HGNC; HGNC:30216; CHMP2A.
DR HPA; ENSG00000130724; Low tissue specificity.
DR MIM; 610893; gene.
DR neXtProt; NX_O43633; -.
DR OpenTargets; ENSG00000130724; -.
DR PharmGKB; PA142672111; -.
DR VEuPathDB; HostDB:ENSG00000130724; -.
DR eggNOG; KOG3230; Eukaryota.
DR GeneTree; ENSGT00950000182832; -.
DR HOGENOM; CLU_069208_1_0_1; -.
DR InParanoid; O43633; -.
DR OMA; RYAKKFM; -.
DR OrthoDB; 1254120at2759; -.
DR PhylomeDB; O43633; -.
DR TreeFam; TF300118; -.
DR PathwayCommons; O43633; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
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; O43633; -.
DR SIGNOR; O43633; -.
DR BioGRID-ORCS; 27243; 793 hits in 1088 CRISPR screens.
DR ChiTaRS; CHMP2A; human.
DR GeneWiki; CHMP2A; -.
DR GenomeRNAi; 27243; -.
DR Pharos; O43633; Tbio.
DR PRO; PR:O43633; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O43633; protein.
DR Bgee; ENSG00000130724; Expressed in mucosa of transverse colon and 211 other tissues.
DR ExpressionAtlas; O43633; baseline and differential.
DR Genevisible; O43633; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA: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:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030117; C:membrane coat; IMP:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:ComplexPortal.
DR GO; GO:0005771; C:multivesicular body; IBA:GO_Central.
DR GO; GO:0032585; C:multivesicular body membrane; IDA:ComplexPortal.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005643; C:nuclear pore; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0031210; F:phosphatidylcholine binding; IMP:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ComplexPortal.
DR GO; GO:0032509; P:endosome transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
DR GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:ComplexPortal.
DR GO; GO:0045324; P:late endosome to vacuole transport; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC: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 plate congression; 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; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:1903723; P:negative regulation of centriole elongation; IMP:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IMP:UniProtKB.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IDA:ComplexPortal.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
DR GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IDA:ComplexPortal.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC: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 GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
DR InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR10476; PTHR10476; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Direct protein sequencing; Endosome;
KW Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT CHAIN 1..222
FT /note="Charged multivesicular body protein 2a"
FT /id="PRO_0000211462"
FT REGION 56..222
FT /note="Interaction with VPS4B"
FT REGION 217..222
FT /note="Interaction with VTA1"
FT COILED 12..53
FT /evidence="ECO:0000255"
FT COILED 195..222
FT /evidence="ECO:0000255"
FT MOTIF 210..220
FT /note="MIT-interacting motif"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|PubMed:12665801"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 185
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 203
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MUTAGEN 169..170
FT /note="DE->AA: Diminishes interaction with VPS4B."
FT /evidence="ECO:0000269|PubMed:18385515"
FT MUTAGEN 181..222
FT /note="Missing: Membrane association; releases
FT autoinhibition."
FT /evidence="ECO:0000269|PubMed:17547705"
FT MUTAGEN 216
FT /note="L->A: Diminishes interaction with VTA1."
FT /evidence="ECO:0000269|PubMed:18385515"
FT MUTAGEN 217..222
FT /note="Missing: Abolishes interaction with VTA1."
FT /evidence="ECO:0000269|PubMed:18385515"
SQ SEQUENCE 222 AA; 25104 MW; F2B86C623829E32E CRC64;
MDLLFGRRKT PEELLRQNQR ALNRAMRELD RERQKLETQE KKIIADIKKM AKQGQMDAVR
IMAKDLVRTR RYVRKFVLMR ANIQAVSLKI QTLKSNNSMA QAMKGVTKAM GTMNRQLKLP
QIQKIMMEFE RQAEIMDMKE EMMNDAIDDA MGDEEDEEES DAVVSQVLDE LGLSLTDELS
NLPSTGGSLS VAAGGKKAEA AASALADADA DLEERLKNLR RD
