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Charged multivesicular body protein 2a (Chromatin-modifying protein 2a) (CHMP2a) (Putative breast adenocarcinoma marker BC-2) (Vacuolar protein sorting-associated protein 2-1) (Vps2-1) (hVps2-1)

 CHM2A_HUMAN             Reviewed;         222 AA.
O43633; B2R4W6; Q3ZTT0;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
30-AUG-2017, entry version 148.
RecName: Full=Charged multivesicular body protein 2a;
AltName: Full=Chromatin-modifying protein 2a;
Short=CHMP2a;
AltName: Full=Putative breast adenocarcinoma marker BC-2;
AltName: Full=Vacuolar protein sorting-associated protein 2-1;
Short=Vps2-1;
Short=hVps2-1;
Name=CHMP2A; Synonyms=BC2, CHMP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
Slater C., Thill G., Obar R.;
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Koczan D., Reimer T., Rump A., Merck-Rousseau M.F., Rosenthal A.,
Friese K., Thiesen H.J.;
"Role of the BC-2 gene in breast cancer.";
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=16533400; DOI=10.1186/1471-2164-7-48;
Kemmer D., Podowski R.M., Arenillas D., Lim J., Hodges E., Roth P.,
Sonnhammer E.L.L., Hoeoeg C., Wasserman W.W.;
"NovelFam3000 -- uncharacterized human protein domains conserved
across model organisms.";
BMC Genomics 7:48-48(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
PROTEIN SEQUENCE OF 1-7, AND ACETYLATION AT MET-1.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 72-222, AND PROTEIN SEQUENCE OF 75-89
AND 197-205.
Keesee S.K., Obar R., Wu Y.-J.;
"Materials and methods for detection of breast cancer.";
Patent number US5914238, 05-JUN-1996.
[11]
INTERACTION WITH VPS4B.
PubMed=11559748;
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
"CHMP1 functions as a member of a newly defined family of vesicle
trafficking proteins.";
J. Cell Sci. 114:2395-2404(2001).
[12]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH VPS4A AND VPS4B.
PubMed=14505570; DOI=10.1016/S0092-8674(03)00714-1;
von Schwedler U.K., Stuchell M., Mueller B., Ward D.M., Chung H.-Y.,
Morita E., Wang H.E., Davis T., He G.P., Cimbora D.M., Scott A.,
Kraeusslich H.-G., Kaplan J., Morham S.G., Sundquist W.I.;
"The protein network of HIV budding.";
Cell 114:701-713(2003).
[13]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHMP1B; CHMP2B;
CHMP3; CHMP4A; CHMP4B; CHMP4C; CHMP5 AND VPS4A.
PubMed=14519844; DOI=10.1073/pnas.2133846100;
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
"Divergent retroviral late-budding domains recruit vacuolar protein
sorting factors by using alternative adaptor proteins.";
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003).
[14]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[15]
SUBCELLULAR LOCATION, AND INTERACTION WITH MITD1.
PubMed=16730941; DOI=10.1016/j.ygeno.2006.04.003;
Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E.,
Sanderson C.M.;
"A systematic analysis of human CHMP protein interactions: additional
MIT domain-containing proteins bind to multiple components of the
human ESCRT III complex.";
Genomics 88:333-346(2006).
[16]
SUBCELLULAR LOCATION.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[17]
AUTOINHIBITORY MECHANISM, INTERACTION WITH VPS4B, AND MUTAGENESIS OF
181-ASN--ASP-222.
PubMed=17547705; DOI=10.1111/j.1600-0854.2007.00584.x;
Shim S., Kimpler L.A., Hanson P.I.;
"Structure/function analysis of four core ESCRT-III proteins reveals
common regulatory role for extreme C-terminal domain.";
Traffic 8:1068-1079(2007).
[18]
INTERACTION WITH VTA1, AND MUTAGENESIS OF 169-ASP-GLU-170; LEU-216 AND
217-LYS--ASP-222.
PubMed=18385515; DOI=10.1091/mbc.E07-12-1263;
Shim S., Merrill S.A., Hanson P.I.;
"Novel interactions of ESCRT-III with LIP5 and VPS4 and their
implications for ESCRT-III disassembly.";
Mol. Biol. Cell 19:2661-2672(2008).
[19]
POLYMERIZATION WITH CHMP3, AND ELECTRON MICROSCOPY.
PubMed=18687924; DOI=10.1126/science.1161070;
Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G.,
Weissenhorn W.;
"Helical structures of ESCRT-III are disassembled by VPS4.";
Science 321:1354-1357(2008).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[21]
ISGYLATION, AND INTERACTION WITH VTA1 AND VPS4A.
PubMed=21543490; DOI=10.1128/JVI.02610-10;
Kuang Z., Seo E.J., Leis J.;
"Mechanism of inhibition of retrovirus release from cells by
interferon-induced gene ISG15.";
J. Virol. 85:7153-7161(2011).
[22]
FUNCTION.
PubMed=21310966; DOI=10.1126/science.1201847;
Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I.,
Leonhardt H., Mueller-Reichert T., Gerlich D.W.;
"Cortical constriction during abscission involves helices of ESCRT-
III-dependent filaments.";
Science 331:1616-1620(2011).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-203, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; THR-185; SER-188;
SER-190 AND SER-203, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
FUNCTION.
PubMed=26040712; DOI=10.1038/nature14408;
Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W.,
Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.;
"Spastin and ESCRT-III coordinate mitotic spindle disassembly and
nuclear envelope sealing.";
Nature 522:231-235(2015).
-!- 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). 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: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}.
-!- SUBUNIT: Probable core component of the endosomal sorting required
for transport complex III (ESCRT-III). ESCRT-III components are
thought to multimerize to form a flat lattice on the perimeter
membrane of the endosome. Several assembly forms of ESCRT-III may
exist that interact and act sequentally. In vitro, heteromerizes
with CHMP3 (but not CHMP4) to form helical tubular structures that
expose membrane-interacting sites on the outside whereas VPS4B can
associate on the inside of the tubule. Interacts with CHMP1B,
CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP5. Interacts with
VPS4A; the interaction is direct. Interacts with VPS4B; the
interaction is direct. Interacts with MITD1. Interacts with VTA1;
the interaction probably involves the open conformation of CHMP2A.
{ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:16730941,
ECO:0000269|PubMed:17547705, ECO:0000269|PubMed:18385515,
ECO:0000269|PubMed:21543490}.
-!- INTERACTION:
Q9Y3E7:CHMP3; NbExp=3; IntAct=EBI-2692789, EBI-2118119;
Q9H444:CHMP4B; NbExp=3; IntAct=EBI-2692789, EBI-749627;
Q8NF50-2:DOCK8; NbExp=3; IntAct=EBI-2692789, EBI-10174653;
Q8WV92:MITD1; NbExp=7; IntAct=EBI-2692789, EBI-2691489;
Q9UN37:VPS4A; NbExp=3; IntAct=EBI-2692789, EBI-1171942;
-!- 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}.
Note=Localizes to the midbody of dividing cells. Localized in two
distinct rings on either side of the Fleming body.
-!- DOMAIN: The acidic C-terminus and the basic N-termminus are
thought to render the protein in a closed, soluble and inactive
conformation through an autoinhibitory intramolecular interaction.
The open and active conformation, which enables membrane binding
and oligomerization, is achieved by interaction with other
cellular binding partners, probably including other ESCRT
components.
-!- PTM: ISGylated in a CHMP5-dependent manner. Isgylation weakens and
inhibits its interactions with VPS4A and VTA1 respectively.
{ECO:0000269|PubMed:21543490}.
-!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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EMBL; AF042384; AAC00005.1; -; mRNA.
EMBL; AJ277113; CAC14310.1; -; Genomic_DNA.
EMBL; AY364248; AAQ76807.1; -; mRNA.
EMBL; BT007298; AAP35962.1; -; mRNA.
EMBL; CR457002; CAG33283.1; -; mRNA.
EMBL; AK311974; BAG34913.1; -; mRNA.
EMBL; CH471135; EAW72609.1; -; Genomic_DNA.
EMBL; BC002502; AAH02502.1; -; mRNA.
CCDS; CCDS12986.1; -.
RefSeq; NP_055268.1; NM_014453.3.
RefSeq; NP_940818.1; NM_198426.2.
UniGene; Hs.12107; -.
ProteinModelPortal; O43633; -.
SMR; O43633; -.
BioGrid; 118091; 52.
DIP; DIP-48533N; -.
IntAct; O43633; 34.
MINT; MINT-5005843; -.
STRING; 9606.ENSP00000310440; -.
iPTMnet; O43633; -.
PhosphoSitePlus; O43633; -.
OGP; O43633; -.
EPD; O43633; -.
MaxQB; O43633; -.
PaxDb; O43633; -.
PeptideAtlas; O43633; -.
PRIDE; O43633; -.
DNASU; 27243; -.
Ensembl; ENST00000312547; ENSP00000310440; ENSG00000130724.
Ensembl; ENST00000600118; ENSP00000469240; ENSG00000130724.
Ensembl; ENST00000601220; ENSP00000472680; ENSG00000130724.
GeneID; 27243; -.
KEGG; hsa:27243; -.
UCSC; uc002qti.3; human.
CTD; 27243; -.
GeneCards; CHMP2A; -.
HGNC; HGNC:30216; CHMP2A.
HPA; HPA041153; -.
HPA; HPA042031; -.
MIM; 610893; gene.
neXtProt; NX_O43633; -.
OpenTargets; ENSG00000130724; -.
PharmGKB; PA142672111; -.
eggNOG; KOG3230; Eukaryota.
eggNOG; COG5491; LUCA.
GeneTree; ENSGT00550000074737; -.
HOGENOM; HOG000177218; -.
HOVERGEN; HBG107298; -.
InParanoid; O43633; -.
KO; K12191; -.
OMA; NMNRQLN; -.
PhylomeDB; O43633; -.
TreeFam; TF300118; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; CHMP2A; human.
GeneWiki; CHMP2A; -.
GenomeRNAi; 27243; -.
PRO; PR:O43633; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000130724; -.
CleanEx; HS_CHMP2A; -.
ExpressionAtlas; O43633; baseline and differential.
Genevisible; O43633; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000815; C:ESCRT III complex; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0030117; C:membrane coat; IMP:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0031210; F:phosphatidylcholine binding; IMP:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
GO; GO:0045184; P:establishment of protein localization; IMP:UniProtKB.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0010324; P:membrane invagination; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:1903723; P:negative regulation of centriole elongation; IMP:UniProtKB.
GO; GO:0031468; P:nuclear envelope reassembly; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IMP:UniProtKB.
GO; GO:0051258; P:protein polymerization; IMP:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0050792; P:regulation of viral process; IMP:UniProtKB.
GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
GO; GO:0039702; P:viral budding via host ESCRT complex; IDA:UniProtKB.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
InterPro; IPR005024; Snf7_fam.
Pfam; PF03357; Snf7; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome;
Direct protein sequencing; Endosome; Membrane; Phosphoprotein;
Protein transport; Reference proteome; Transport; Ubl conjugation.
CHAIN 1 222 Charged multivesicular body protein 2a.
/FTId=PRO_0000211462.
REGION 56 222 Interaction with VPS4B.
REGION 217 222 Interaction with VTA1.
COILED 12 53 {ECO:0000255}.
COILED 195 222 {ECO:0000255}.
MOTIF 210 220 MIT-interacting motif.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000269|PubMed:12665801}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 185 185 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 190 190 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 203 203 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MUTAGEN 169 170 DE->AA: Diminishes interaction with
VPS4B. {ECO:0000269|PubMed:18385515}.
MUTAGEN 181 222 Missing: Membrane association; releases
autoinhibition.
{ECO:0000269|PubMed:17547705}.
MUTAGEN 216 216 L->A: Diminishes interaction with VTA1.
{ECO:0000269|PubMed:18385515}.
MUTAGEN 217 222 Missing: Abolishes interaction with VTA1.
{ECO:0000269|PubMed:18385515}.
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


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