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Charged multivesicular body protein 3 (Chromatin-modifying protein 3) (Neuroendocrine differentiation factor) (Vacuolar protein sorting-associated protein 24) (hVps24)

 CHMP3_HUMAN             Reviewed;         222 AA.
Q9Y3E7; A8K3W0; B4DG34; B8ZZM0; B8ZZX5; Q3ZTS9; Q53S71; Q53SU5;
Q9NZ51;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 147.
RecName: Full=Charged multivesicular body protein 3;
AltName: Full=Chromatin-modifying protein 3;
AltName: Full=Neuroendocrine differentiation factor;
AltName: Full=Vacuolar protein sorting-associated protein 24;
Short=hVps24;
Name=CHMP3; Synonyms=CGI149, NEDF, VPS24; ORFNames=CGI-149;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND POSSIBLE INTERACTION WITH
IGFBP7.
PubMed=11549700; DOI=10.1210/jcem.86.9.7845;
Wilson E.M., Oh Y., Hwa V., Rosenfeld R.G.;
"Interaction of IGF-binding protein-related protein 1 with a novel
protein, neuroendocrine differentiation factor, results in
neuroendocrine differentiation of prostate cancer cells.";
J. Clin. Endocrinol. Metab. 86:4504-4511(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND SUBCELLULAR
LOCATION.
TISSUE=Heart;
PubMed=15707591; DOI=10.1016/j.yexcr.2004.11.003;
Yan Q., Hunt P.R., Frelin L., Vida T.A., Pevsner J., Bean A.J.;
"mVps24p functions in EGF receptor sorting/trafficking from the early
endosome.";
Exp. Cell Res. 304:265-273(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [MRNA] (ISOFORM 2), AND FUNCTION.
TISSUE=Heart;
PubMed=17331679; DOI=10.1016/j.gene.2006.12.039;
Khoury C.M., Yang Z., Ismail S., Greenwood M.T.;
"Characterization of a novel alternatively spliced human transcript
encoding an N-terminally truncated Vps24 protein that suppresses the
effects of Bax in an ESCRT independent manner in yeast.";
Gene 391:233-241(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Amygdala, Pericardium, and Synovial cell;
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].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[8]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
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).
[10]
FUNCTION IN HIV-1 BUDDING, AND INTERACTION WITH CHMP4A.
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).
[11]
INTERACTION WITH CHMP2A 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).
[12]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[13]
TISSUE SPECIFICITY.
PubMed=15632132; DOI=10.1074/jbc.M413968200;
Lin Y., Kimpler L.A., Naismith T.V., Lauer J.M., Hanson P.I.;
"Interaction of the mammalian endosomal sorting complex required for
transport (ESCRT) III protein hSnf7-1 with itself, membranes, and the
AAA+ ATPase SKD1.";
J. Biol. Chem. 280:12799-12809(2005).
[14]
SUBCELLULAR LOCATION, AND INTERACTION WITH STAMBP.
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).
[15]
AUTOINHIBITORY MECHANISM, INTRAMOLECULAR INTERACTION, INTERACTION WITH
STAMBP AND VPS4A, AND MUTAGENESIS OF 216-ARG-LEU-217; 221-ARG-SER-222
AND SER-222.
PubMed=17146056; DOI=10.1073/pnas.0603788103;
Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G.,
Goettlinger H.;
"Release of autoinhibition converts ESCRT-III components into potent
inhibitors of HIV-1 budding.";
Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006).
[16]
INTERACTION WITH STAMBP, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=17261583; DOI=10.1074/jbc.M611635200;
Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P.,
Goettlinger H.G., Kirchhausen T.;
"Targeting of AMSH to endosomes is required for epidermal growth
factor receptor degradation.";
J. Biol. Chem. 282:9805-9812(2007).
[17]
AUTOINHIBITORY MECHANISM, INTERACTION WITH CHMP4A, AND MUTAGENESIS OF
179-LYS--SER-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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
POLYMERIZATION WITH CHMP2A, 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]
FUNCTION IN CYTOKINESIS, AND SUBCELLULAR LOCATION.
PubMed=18076377; DOI=10.1042/BJ20071296;
Dukes J.D., Richardson J.D., Simmons R., Whitley P.;
"A dominant-negative ESCRT-III protein perturbs cytokinesis and
trafficking to lysosomes.";
Biochem. J. 411:233-239(2008).
[21]
AUTOINHIBITORY MECHANISM, AND INTERACTION WITH STAMBP.
PubMed=18395747; DOI=10.1016/j.jmb.2008.03.030;
Lata S., Roessle M., Solomons J., Jamin M., Goettlinger H.G.,
Svergun D.I., Weissenhorn W.;
"Structural basis for autoinhibition of ESCRT-III CHMP3.";
J. Mol. Biol. 378:818-827(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
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).
[25]
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).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-200, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[28]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 5-183, SUBUNIT, FUNCTION IN
HIV-1 BUDDING, AND MUTAGENESIS OF 24-ARG-LYS-25; ARG-28; LYS-54;
GLN-56; VAL-59; 62-VAL-LEU-63 AND 78-TYR-ALA-79.
PubMed=16740483; DOI=10.1016/j.devcel.2006.03.013;
Muziol T., Pineda-Molina E., Ravelli R.B., Zamborlini A., Usami Y.,
Goettlinger H., Weissenhorn W.;
"Structural basis for budding by the ESCRT-III factor CHMP3.";
Dev. Cell 10:821-830(2006).
[29]
X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS) OF 1-222, INTERACTION WITH
CHMP2A, AND MUTAGENESIS OF VAL-48; VAL-59; VAL-62; ALA-64 AND
168-ILE-LEU-169.
PubMed=19525971; DOI=10.1038/nsmb.1621;
Bajorek M., Schubert H.L., McCullough J., Langelier C., Eckert D.M.,
Stubblefield W.M., Uter N.T., Myszka D.G., Hill C.P., Sundquist W.I.;
"Structural basis for ESCRT-III protein autoinhibition.";
Nat. Struct. Mol. Biol. 16:754-762(2009).
[30]
X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 183-222 IN COMPLEX WITH
STAMBP FRAGMENT.
PubMed=21827950; DOI=10.1016/j.str.2011.05.011;
Solomons J., Sabin C., Poudevigne E., Usami Y., Hulsik D.L.,
Macheboeuf P., Hartlieb B., Gottlinger H., Weissenhorn W.;
"Structural basis for Escrt-III Chmp3 recruitment of Amsh.";
Structure 19:1149-1159(2011).
-!- 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}.
-!- 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. Forms a metastable
monomer in solution; its core structure (without part of the
putative autoinhibitory C-terminal acidic region) oligomerizes
into a flat lattice via two different dimerization interfaces. In
vitro, heteromerizes with CHMP2A (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.
May interact with IGFBP7; the relevance of such interaction
however remains unclear. Interacts with CHMP2A. Interacts with
CHMP4A; the interaction requires the release of CHMP4A
autoinhibition. Interacts with VPS4A. Interacts with STAMBP; the
interaction appears to relieve the autoinhibition of CHMP3.
Interacts with VTA1. {ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:16730941,
ECO:0000269|PubMed:16740483, ECO:0000269|PubMed:17146056,
ECO:0000269|PubMed:17261583, ECO:0000269|PubMed:17547705,
ECO:0000269|PubMed:18395747, ECO:0000269|PubMed:19525971,
ECO:0000269|PubMed:21543490, ECO:0000269|PubMed:21827950}.
-!- INTERACTION:
O43633:CHMP2A; NbExp=3; IntAct=EBI-2118119, EBI-2692789;
Q9UQN3:CHMP2B; NbExp=2; IntAct=EBI-2118119, EBI-718324;
Q9H444:CHMP4B; NbExp=5; IntAct=EBI-2118119, EBI-749627;
O95630:STAMBP; NbExp=19; IntAct=EBI-2118119, EBI-396676;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Membrane; Lipid-anchor.
Endosome. Late endosome membrane {ECO:0000305}. Note=Localizes to
the midbody of dividing cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=Vps24alpha;
IsoId=Q9Y3E7-1; Sequence=Displayed;
Name=2; Synonyms=Vps24beta;
IsoId=Q9Y3E7-2; Sequence=VSP_041076;
Name=3;
IsoId=Q9Y3E7-3; Sequence=VSP_042124;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9Y3E7-4; Sequence=VSP_042125;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in heart, brain,
placenta, lung, liver, skeletal muscle, kidney and pancreas.
{ECO:0000269|PubMed:15632132}.
-!- 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.
-!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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EMBL; AF219226; AAF26737.1; -; mRNA.
EMBL; AY364249; AAQ76808.1; -; mRNA.
EMBL; AF151907; AAD34144.1; -; mRNA.
EMBL; AK290725; BAF83414.1; -; mRNA.
EMBL; AK294389; BAG57645.1; -; mRNA.
EMBL; AK312353; BAG35273.1; -; mRNA.
EMBL; AK315835; BAF98726.1; -; mRNA.
EMBL; AC015971; AAX93078.1; -; Genomic_DNA.
EMBL; AC064848; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC068288; AAY24211.1; -; Genomic_DNA.
EMBL; CH471053; EAW99448.1; -; Genomic_DNA.
EMBL; CH471053; EAW99449.1; -; Genomic_DNA.
EMBL; CH471053; EAW99450.1; -; Genomic_DNA.
EMBL; CH471053; EAW99451.1; -; Genomic_DNA.
EMBL; BC004419; AAH04419.1; -; mRNA.
CCDS; CCDS33236.1; -. [Q9Y3E7-1]
CCDS; CCDS42707.1; -. [Q9Y3E7-2]
CCDS; CCDS54375.1; -. [Q9Y3E7-4]
RefSeq; NP_001005753.1; NM_001005753.2. [Q9Y3E7-2]
RefSeq; NP_001180446.1; NM_001193517.1. [Q9Y3E7-4]
RefSeq; NP_001185883.1; NM_001198954.1. [Q9Y3E7-3]
RefSeq; NP_057163.1; NM_016079.3. [Q9Y3E7-1]
UniGene; Hs.591582; -.
PDB; 2GD5; X-ray; 2.80 A; A/B/C/D=9-183.
PDB; 2XZE; X-ray; 1.75 A; Q/R=183-222.
PDB; 3FRT; X-ray; 4.00 A; A/B=8-222.
PDB; 3FRV; X-ray; 3.70 A; A=1-150.
PDBsum; 2GD5; -.
PDBsum; 2XZE; -.
PDBsum; 3FRT; -.
PDBsum; 3FRV; -.
ProteinModelPortal; Q9Y3E7; -.
SMR; Q9Y3E7; -.
BioGrid; 119660; 31.
BioGrid; 1529307; 2.
CORUM; Q9Y3E7; -.
DIP; DIP-48532N; -.
IntAct; Q9Y3E7; 25.
MINT; MINT-1185988; -.
STRING; 9606.ENSP00000405575; -.
iPTMnet; Q9Y3E7; -.
PhosphoSitePlus; Q9Y3E7; -.
BioMuta; CHMP3; -.
DMDM; 73917763; -.
EPD; Q9Y3E7; -.
PaxDb; Q9Y3E7; -.
PeptideAtlas; Q9Y3E7; -.
PRIDE; Q9Y3E7; -.
DNASU; 51652; -.
Ensembl; ENST00000263856; ENSP00000263856; ENSG00000115561. [Q9Y3E7-1]
Ensembl; ENST00000409225; ENSP00000386590; ENSG00000115561. [Q9Y3E7-2]
Ensembl; ENST00000409727; ENSP00000387045; ENSG00000115561. [Q9Y3E7-4]
GeneID; 100526767; -.
GeneID; 51652; -.
KEGG; hsa:100526767; -.
KEGG; hsa:51652; -.
UCSC; uc002srj.4; human. [Q9Y3E7-1]
CTD; 100526767; -.
CTD; 51652; -.
DisGeNET; 100526767; -.
DisGeNET; 51652; -.
EuPathDB; HostDB:ENSG00000115561.15; -.
GeneCards; CHMP3; -.
HGNC; HGNC:29865; CHMP3.
HPA; HPA015673; -.
MIM; 610052; gene.
neXtProt; NX_Q9Y3E7; -.
OpenTargets; ENSG00000115561; -.
OpenTargets; ENSG00000249884; -.
PharmGKB; PA134920495; -.
eggNOG; KOG0800; Eukaryota.
eggNOG; KOG3229; Eukaryota.
eggNOG; COG5491; LUCA.
GeneTree; ENSGT00550000074896; -.
HOGENOM; HOG000177219; -.
HOVERGEN; HBG107031; -.
InParanoid; Q9Y3E7; -.
KO; K12193; -.
OMA; QMKNQLA; -.
OrthoDB; EOG091G0EZD; -.
PhylomeDB; Q9Y3E7; -.
TreeFam; TF105848; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-1632852; Macroautophagy.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
SignaLink; Q9Y3E7; -.
ChiTaRS; CHMP3; human.
EvolutionaryTrace; Q9Y3E7; -.
GeneWiki; VPS24; -.
PRO; PR:Q9Y3E7; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000115561; -.
CleanEx; HS_VPS24; -.
Genevisible; Q9Y3E7; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:UniProtKB.
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:0005622; C:intracellular; IMP:ParkinsonsUK-UCL.
GO; GO:0005770; C:late endosome; IDA:ParkinsonsUK-UCL.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0031210; F:phosphatidylcholine binding; IMP:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IMP:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:UniProtKB.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0097352; P:autophagosome maturation; TAS:ParkinsonsUK-UCL.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:0071985; P:multivesicular body sorting pathway; TAS:ParkinsonsUK-UCL.
GO; GO:0061763; P:multivesicular body-lysosome fusion; IMP:ParkinsonsUK-UCL.
GO; GO:1902187; P:negative regulation of viral release from host cell; 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:0051258; P:protein polymerization; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:2000641; P:regulation of early endosome to late endosome transport; IMP:ParkinsonsUK-UCL.
GO; GO:0050792; P:regulation of viral process; IMP:UniProtKB.
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;
3D-structure; Alternative splicing; Apoptosis; Cell cycle;
Cell division; Coiled coil; Complete proteome; Cytoplasm; Endosome;
Isopeptide bond; Lipoprotein; Membrane; Myristate; Phosphoprotein;
Protein transport; Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000255}.
CHAIN 2 222 Charged multivesicular body protein 3.
/FTId=PRO_0000211479.
REGION 2 113 Intramolecular interaction with C-
terminus.
REGION 59 64 Important for autoinhibitory function.
REGION 151 222 Interaction with VPS4A.
REGION 151 220 Intramolecular interaction with N-
terminus.
REGION 168 169 Important for autoinhibitory function.
REGION 203 207 Interaction with STAMBP.
REGION 221 222 Interaction with STAMBP.
COILED 22 54 {ECO:0000255}.
COILED 141 222 {ECO:0000255}.
MOTIF 201 211 MIT-interacting motif.
BINDING 216 216 STAMBP.
SITE 48 48 Important for autoinhibitory function.
MOD_RES 200 200 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
LIPID 2 2 N-myristoyl glycine. {ECO:0000255}.
CROSSLNK 179 179 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
VAR_SEQ 1 66 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:17331679}.
/FTId=VSP_041076.
VAR_SEQ 1 15 MGLFGKTQEKPPKEL -> MEGELYSALKEEEASESVSSTN
FSGEMHFYELVEDTKDGIWLVQ (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042124.
VAR_SEQ 74 113 Missing (in isoform 4). {ECO:0000305}.
/FTId=VSP_042125.
MUTAGEN 24 25 RK->SA: Impairs HIV-1 release; when
associated with S-28.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 28 28 R->S: Impairs HIV-1 release; when
associated with 24-S-A-25.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 48 48 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.
{ECO:0000269|PubMed:19525971}.
MUTAGEN 54 54 K->S: Abolishes dimerization; when
associated with N-56; E-59 and 62-D-E-63.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 56 56 Q->N: Abolishes dimerization; when
associated with S-54; E-59 and 62-D-E-63.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 59 59 V->D: Abolishes interaction with CHMP2A
and assembly into helical tubes in vitro;
when associated with D-62; D-168 and D-
169. {ECO:0000269|PubMed:16740483,
ECO:0000269|PubMed:19525971}.
MUTAGEN 59 59 V->E: Abolishes dimerization; when
associated with S-54; N-56 and 62-D-E-63.
{ECO:0000269|PubMed:16740483,
ECO:0000269|PubMed:19525971}.
MUTAGEN 62 63 VL->DE: Abolishes dimerization; when
associated with S-54; N-56 and E-59.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 62 62 V->D: Abolishes interaction with CHMP2A
and assembly into helical tubes in vitro;
when associated with D-59; D-168 and D-
169. {ECO:0000269|PubMed:19525971}.
MUTAGEN 64 64 A->D: Induces assembly with CHMP2A into
helical tubes in vitro; when associated
with D-48. {ECO:0000269|PubMed:19525971}.
MUTAGEN 78 79 YA->AE: Abolishes dimerization.
{ECO:0000269|PubMed:16740483}.
MUTAGEN 168 169 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.
{ECO:0000269|PubMed:19525971}.
MUTAGEN 179 222 Missing: Membrane association; releases
autoinhibition.
{ECO:0000269|PubMed:17547705}.
MUTAGEN 216 217 RL->AA: Abolishes interaction with VPS4A
and STAMBP.
{ECO:0000269|PubMed:17146056}.
MUTAGEN 221 222 Missing: Abolishes interaction with VPS4A
and STAMBP.
{ECO:0000269|PubMed:17146056}.
MUTAGEN 222 222 Missing: Impairs interaction with VPS4A
and STAMBP.
{ECO:0000269|PubMed:17146056}.
CONFLICT 208 208 E -> D (in Ref. 1; AAF26737).
{ECO:0000305}.
HELIX 15 53 {ECO:0000244|PDB:2GD5}.
HELIX 57 100 {ECO:0000244|PDB:2GD5}.
HELIX 109 112 {ECO:0000244|PDB:2GD5}.
TURN 113 115 {ECO:0000244|PDB:2GD5}.
STRAND 120 122 {ECO:0000244|PDB:2GD5}.
HELIX 125 137 {ECO:0000244|PDB:2GD5}.
HELIX 164 167 {ECO:0000244|PDB:2GD5}.
STRAND 175 177 {ECO:0000244|PDB:2GD5}.
HELIX 201 220 {ECO:0000244|PDB:2XZE}.
SEQUENCE 222 AA; 25073 MW; 7B1ACE5EA453E8C0 CRC64;
MGLFGKTQEK PPKELVNEWS LKIRKEMRVV DRQIRDIQRE EEKVKRSVKD AAKKGQKDVC
IVLAKEMIRS RKAVSKLYAS KAHMNSVLMG MKNQLAVLRV AGSLQKSTEV MKAMQSLVKI
PEIQATMREL SKEMMKAGII EEMLEDTFES MDDQEEMEEE AEMEIDRILF EITAGALGKA
PSKVTDALPE PEPPGAMAAS EDEEEEEEAL EAMQSRLATL RS


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