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Charged multivesicular body protein 4b (Chromatin-modifying protein 4b) (CHMP4b) (SNF7 homolog associated with Alix 1) (SNF7-2) (hSnf7-2) (Vacuolar protein sorting-associated protein 32-2) (Vps32-2) (hVps32-2)

 CHM4B_HUMAN             Reviewed;         224 AA.
Q9H444; E1P5N4; Q53ZD6;
01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
22-NOV-2017, entry version 147.
RecName: Full=Charged multivesicular body protein 4b;
AltName: Full=Chromatin-modifying protein 4b;
Short=CHMP4b;
AltName: Full=SNF7 homolog associated with Alix 1;
AltName: Full=SNF7-2;
Short=hSnf7-2;
AltName: Full=Vacuolar protein sorting-associated protein 32-2;
Short=Vps32-2;
Short=hVps32-2;
Name=CHMP4B; Synonyms=C20orf178, SHAX1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH PDCD6IP.
PubMed=12860994; DOI=10.1074/jbc.M301604200;
Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
Yoshimori T., Maki M.;
"The ALG-2-interacting protein Alix associates with CHMP4b, a human
homologue of yeast Snf7 that is involved in multivesicular body
sorting.";
J. Biol. Chem. 278:39104-39113(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PDCD6IP.
PubMed=14583093; DOI=10.1042/BJ20031347;
Peck J.W., Bowden E.T., Burbelo P.D.;
"Structure and function of human Vps20 and Snf7 proteins.";
Biochem. J. 377:693-700(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Lung, and Testis;
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).
[6]
PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE,
ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lempens A., Norman J.C.;
Submitted (OCT-2009) to UniProtKB.
[7]
PROTEIN SEQUENCE OF 18-28 AND 78-107, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH PDCD6IP.
PubMed=14505569; DOI=10.1016/S0092-8674(03)00653-6;
Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
"AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning
in virus budding.";
Cell 114:689-699(2003).
[9]
FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHMP6; CHMP4C;
PDCD6IP; 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).
[10]
FUNCTION (MICROBIAL INFECTION), SELF-ASSOCIATION, AND INTERACTION WITH
CHMP2A; CHMP4A; CHMP4C; CHMP6; PDCD6IP 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).
[11]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[12]
TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP.
PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
Katoh K., Shibata H., Hatta K., Maki M.;
"CHMP4b is a major binding partner of the ALG-2-interacting protein
Alix among the three CHMP4 isoforms.";
Arch. Biochem. Biophys. 421:159-165(2004).
[13]
SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP6.
PubMed=15511219; DOI=10.1042/BJ20041227;
Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
Kobayashi T., Uchiyama Y., Maki M.;
"Human CHMP6, a myristoylated ESCRT-III protein, interacts directly
with an ESCRT-II component EAP20 and regulates endosomal cargo
sorting.";
Biochem. J. 387:17-26(2005).
[14]
INTERACTION WITH MISFOLDED CFTR.
PubMed=15007060; DOI=10.1083/jcb.200312018;
Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K.,
Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.;
"Misfolding diverts CFTR from recycling to degradation: quality
control at early endosomes.";
J. Cell Biol. 164:923-933(2004).
[15]
INTERACTION WITH CHMP7.
PubMed=16856878; DOI=10.1042/BJ20060897;
Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J.,
Maki M.;
"CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and
functions in the endosomal sorting pathway.";
Biochem. J. 400:23-32(2006).
[16]
AUTOINHIBITORY MECHANISM, AND INTRAMOLECULAR INTERACTION.
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).
[17]
INTERACTION WITH PDCD6IP.
PubMed=17428861; DOI=10.1128/JVI.00314-07;
Usami Y., Popov S., Goettlinger H.G.;
"Potent rescue of human immunodeficiency virus type 1 late domain
mutants by ALIX/AIP1 depends on its CHMP4 binding site.";
J. Virol. 81:6614-6622(2007).
[18]
INTERACTION WITH BROX.
PubMed=18190528; DOI=10.1111/j.1742-4658.2007.06230.x;
Ichioka F., Kobayashi R., Katoh K., Shibata H., Maki M.;
"Brox, a novel farnesylated Bro1 domain-containing protein that
associates with charged multivesicular body protein 4 (CHMP4).";
FEBS J. 275:682-692(2008).
[19]
FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON CRYOMICROSCOPY.
PubMed=18209100; DOI=10.1083/jcb.200707031;
Hanson P.I., Roth R., Lin Y., Heuser J.E.;
"Plasma membrane deformation by circular arrays of ESCRT-III protein
filaments.";
J. Cell Biol. 180:389-402(2008).
[20]
INTERACTION WITH PTPN23.
PubMed=18434552; DOI=10.1073/pnas.0707601105;
Doyotte A., Mironov A., McKenzie E., Woodman P.;
"The Bro1-related protein HD-PTP/PTPN23 is required for endosomal
cargo sorting and multivesicular body morphogenesis.";
Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-114, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-223, 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).
[23]
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).
[24]
ISGYLATION, AND INTERACTION WITH 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, 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).
[26]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[27]
FUNCTION.
PubMed=22660413; DOI=10.1038/ncb2502;
Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G.,
Geeraerts A., Ivarsson Y., Depoortere F., Coomans C., Vermeiren E.,
Zimmermann P., David G.;
"Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
Nat. Cell Biol. 14:677-685(2012).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[29]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22422861; DOI=10.1126/science.1217180;
Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
"ESCRT-III governs the Aurora B-mediated abscission checkpoint through
CHMP4C.";
Science 336:220-225(2012).
[30]
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).
[31]
FUNCTION, AND SUBCELLULAR LOCATION.
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).
[32]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 207-224 IN COMPLEX WITH
PDCD6IP.
PubMed=18511562; DOI=10.1073/pnas.0801567105;
McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
"ALIX-CHMP4 interactions in the human ESCRT pathway.";
Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
[33]
VARIANTS CTRCT31 VAL-129 AND LYS-161.
PubMed=17701905; DOI=10.1086/519980;
Shiels A., Bennett T.M., Knopf H.L.S., Yamada K., Yoshiura K.,
Niikawa N., Shim S., Hanson P.I.;
"CHMP4B, a novel gene for autosomal dominant cataracts linked to
chromosome 20q.";
Am. J. Hum. Genet. 81:596-606(2007).
-!- 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 (PubMed:12860994, PubMed:18209100). 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). Plays a role in the
endosomal sorting pathway. ESCRT-III proteins are believed to
mediate the necessary vesicle extrusion and/or membrane fission
activities, possibly in conjunction with the AAA ATPase VPS4. When
overexpressed, membrane-assembled circular arrays of CHMP4B
filaments can promote or stabilize negative curvature and outward
budding. CHMP4A/B/C are required for the exosomal release of
SDCBP, CD63 and syndecan (PubMed:22660413).
{ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:18209100,
ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22660413,
ECO:0000269|PubMed:26040712}.
-!- FUNCTION: (Microbial infection) The ESCRT machinery also functions
in topologically equivalent membrane fission events, such as the
budding of enveloped viruses (HIV-1 and other lentiviruses). Via
its interaction with PDCD6IP involved in HIV-1 p6- and p9-
dependent virus release. {ECO:0000269|PubMed:14505569,
ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:22422861}.
-!- 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. Interacts with CHMP6 and
CHMP4C. Interacts with PDCD6IP; the interaction is direct.
Interacts with VPS4A; the interaction is direct. Interacts with
VPS4B; the interaction is direct. Interacts with CHMP7. Interacts
with CFTR; the interaction requires misfolded CFTR. Interacts with
PTPN23. {ECO:0000269|PubMed:12860994, ECO:0000269|PubMed:14505569,
ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:14583093, ECO:0000269|PubMed:14678797,
ECO:0000269|PubMed:15007060, ECO:0000269|PubMed:15511219,
ECO:0000269|PubMed:16856878, ECO:0000269|PubMed:17428861,
ECO:0000269|PubMed:18190528, ECO:0000269|PubMed:18434552,
ECO:0000269|PubMed:18511562, ECO:0000269|PubMed:21543490}.
-!- INTERACTION:
Self; NbExp=7; IntAct=EBI-749627, EBI-749627;
Q5VW32:BROX; NbExp=5; IntAct=EBI-749627, EBI-6286053;
Q6P1N0:CC2D1A; NbExp=3; IntAct=EBI-749627, EBI-7112364;
O43633:CHMP2A; NbExp=3; IntAct=EBI-749627, EBI-2692789;
Q9UQN3:CHMP2B; NbExp=2; IntAct=EBI-749627, EBI-718324;
Q9Y3E7:CHMP3; NbExp=5; IntAct=EBI-749627, EBI-2118119;
Q9BY43:CHMP4A; NbExp=4; IntAct=EBI-749627, EBI-747981;
Q9NZZ3:CHMP5; NbExp=4; IntAct=EBI-749627, EBI-751303;
Q8WUX9:CHMP7; NbExp=3; IntAct=EBI-749627, EBI-749253;
Q8WUM4:PDCD6IP; NbExp=6; IntAct=EBI-749627, EBI-310624;
Q9WU78-1:Pdcd6ip (xeno); NbExp=2; IntAct=EBI-749627, EBI-15788421;
Q9H3S7:PTPN23; NbExp=4; IntAct=EBI-749627, EBI-724478;
O95630:STAMBP; NbExp=3; IntAct=EBI-749627, EBI-396676;
P63279:UBE2I; NbExp=3; IntAct=EBI-749627, EBI-80168;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:15511219}. Late endosome membrane
{ECO:0000269|PubMed:15511219, ECO:0000305|PubMed:12860994};
Peripheral membrane protein {ECO:0000305}. Midbody
{ECO:0000269|PubMed:21310966, ECO:0000269|PubMed:22422861}.
Nucleus envelope {ECO:0000269|PubMed:26040712}. Note=Recruited to
the nuclear envelope by CHMP7 during late anaphase
(PubMed:26040712). Localizes transiently to the midbody arms
immediately before abscission (PubMed:22422861).
{ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:26040712}.
-!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
heart and skeletal muscle. Also expressed in brain, colon, thymus,
spleen, kidney, liver, small intestine, placenta, lung and
peripheral blood lymphocytes. {ECO:0000269|PubMed:14678797}.
-!- 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. Isgylation weakens its interaction with VPS4A.
{ECO:0000269|PubMed:21543490}.
-!- DISEASE: Cataract 31, multiple types (CTRCT31) [MIM:605387]: An
opacification of the crystalline lens of the eye that frequently
results in visual impairment or blindness. Opacities vary in
morphology, are often confined to a portion of the lens, and may
be static or progressive. In general, the more posteriorly located
and dense an opacity, the greater the impact on visual function.
CTRCT31 includes posterior polar, progressive posterior
subcapsular, nuclear, and anterior subcapsular cataracts.
{ECO:0000269|PubMed:17701905}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
-!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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EMBL; AB100261; BAC79375.1; -; mRNA.
EMBL; AY329085; AAQ91194.1; -; mRNA.
EMBL; AL050349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW76293.1; -; Genomic_DNA.
EMBL; CH471077; EAW76294.1; -; Genomic_DNA.
EMBL; BC033859; AAH33859.1; -; mRNA.
CCDS; CCDS13228.1; -.
RefSeq; NP_789782.1; NM_176812.4.
UniGene; Hs.472471; -.
PDB; 3C3Q; X-ray; 2.10 A; B=207-224.
PDB; 3UM3; X-ray; 3.80 A; B=121-224.
PDB; 4ABM; X-ray; 1.80 A; A/B/C/D=23-97.
PDB; 5MK2; X-ray; 1.70 A; C=205-224.
PDBsum; 3C3Q; -.
PDBsum; 3UM3; -.
PDBsum; 4ABM; -.
PDBsum; 5MK2; -.
ProteinModelPortal; Q9H444; -.
SMR; Q9H444; -.
BioGrid; 126170; 118.
CORUM; Q9H444; -.
DIP; DIP-29924N; -.
IntAct; Q9H444; 113.
MINT; MINT-5000054; -.
STRING; 9606.ENSP00000217402; -.
iPTMnet; Q9H444; -.
PhosphoSitePlus; Q9H444; -.
BioMuta; CHMP4B; -.
DMDM; 24636296; -.
EPD; Q9H444; -.
MaxQB; Q9H444; -.
PaxDb; Q9H444; -.
PeptideAtlas; Q9H444; -.
PRIDE; Q9H444; -.
Ensembl; ENST00000217402; ENSP00000217402; ENSG00000101421.
GeneID; 128866; -.
KEGG; hsa:128866; -.
UCSC; uc002xaa.4; human.
CTD; 128866; -.
DisGeNET; 128866; -.
EuPathDB; HostDB:ENSG00000101421.3; -.
GeneCards; CHMP4B; -.
HGNC; HGNC:16171; CHMP4B.
HPA; HPA041401; -.
HPA; HPA051751; -.
MalaCards; CHMP4B; -.
MIM; 605387; phenotype.
MIM; 610897; gene.
neXtProt; NX_Q9H444; -.
OpenTargets; ENSG00000101421; -.
Orphanet; 98993; Posterior polar cataract.
PharmGKB; PA25721; -.
eggNOG; KOG1656; Eukaryota.
eggNOG; ENOG410YE9I; LUCA.
GeneTree; ENSGT00390000005006; -.
HOGENOM; HOG000209960; -.
HOVERGEN; HBG050928; -.
InParanoid; Q9H444; -.
KO; K12194; -.
OMA; MQVNTLE; -.
OrthoDB; EOG091G0V7X; -.
PhylomeDB; Q9H444; -.
TreeFam; TF314269; -.
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).
ChiTaRS; CHMP4B; human.
EvolutionaryTrace; Q9H444; -.
GeneWiki; CHMP4B; -.
GenomeRNAi; 128866; -.
PRO; PR:Q9H444; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101421; -.
CleanEx; HS_CHMP4B; -.
Genevisible; Q9H444; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
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:0030117; C:membrane coat; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0006914; P:autophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB.
GO; GO:0090148; P:membrane fission; IMP:UniProtKB.
GO; GO:0000281; P:mitotic cytokinesis; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; TAS:ParkinsonsUK-UCL.
GO; GO:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:1901215; P:negative regulation of neuron death; IMP:UniProtKB.
GO; GO:0031468; P:nuclear envelope reassembly; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0006620; P:posttranslational protein targeting to endoplasmic reticulum membrane; IMP:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
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:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0007034; P:vacuolar transport; IEA:InterPro.
GO; GO:0046755; P:viral budding; 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; Acetylation; Cataract; Coiled coil; Complete proteome;
Cytoplasm; Direct protein sequencing; Disease mutation; Endosome;
Membrane; Nucleus; Phosphoprotein; Protein transport;
Reference proteome; Transport; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
CHAIN 2 224 Charged multivesicular body protein 4b.
/FTId=PRO_0000211489.
COILED 23 183 {ECO:0000255}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:22814378,
ECO:0000269|Ref.6}.
MOD_RES 6 6 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 114 114 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 223 223 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
VARIANT 129 129 D -> V (in CTRCT31; dbSNP:rs118203965).
{ECO:0000269|PubMed:17701905}.
/FTId=VAR_037579.
VARIANT 161 161 E -> K (in CTRCT31; dbSNP:rs118203966).
{ECO:0000269|PubMed:17701905}.
/FTId=VAR_037580.
HELIX 23 57 {ECO:0000244|PDB:4ABM}.
HELIX 62 96 {ECO:0000244|PDB:4ABM}.
HELIX 209 212 {ECO:0000244|PDB:3C3Q}.
HELIX 213 221 {ECO:0000244|PDB:5MK2}.
SEQUENCE 224 AA; 24950 MW; DB1D79DD3803CB2F CRC64;
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE LTAAKKHGTK
NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN TNTEVLKNMG YAAKAMKAAH
DNMDIDKVDE LMQDIADQQE LAEEISTAIS KPVGFGEEFD EDELMAELEE LEQEELDKNL
LEISGPETVP LPNVPSIALP SKPAKKKEEE DDDMKELENW AGSM


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