CHM4B_HUMAN
ID CHM4B_HUMAN Reviewed; 224 AA.
AC Q9H444; E1P5N4; Q53ZD6;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=Charged multivesicular body protein 4b;
DE AltName: Full=Chromatin-modifying protein 4b;
DE Short=CHMP4b;
DE AltName: Full=SNF7 homolog associated with Alix 1;
DE AltName: Full=SNF7-2;
DE Short=hSnf7-2;
DE AltName: Full=Vacuolar protein sorting-associated protein 32-2;
DE Short=Vps32-2;
DE Short=hVps32-2;
GN Name=CHMP4B; Synonyms=C20orf178, SHAX1;
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], FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH PDCD6IP.
RX PubMed=12860994; DOI=10.1074/jbc.m301604200;
RA Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E.,
RA Yoshimori T., Maki M.;
RT "The ALG-2-interacting protein Alix associates with CHMP4b, a human
RT homologue of yeast Snf7 that is involved in multivesicular body sorting.";
RL J. Biol. Chem. 278:39104-39113(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH PDCD6IP.
RX PubMed=14583093; DOI=10.1042/bj20031347;
RA Peck J.W., Bowden E.T., Burbelo P.D.;
RT "Structure and function of human Vps20 and Snf7 proteins.";
RL Biochem. J. 377:693-700(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, and Testis;
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 [6]
RP PROTEIN SEQUENCE OF 2-28, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP SER-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lempens A., Norman J.C.;
RL Submitted (OCT-2009) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 18-28 AND 78-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH PDCD6IP.
RX PubMed=14505569; DOI=10.1016/s0092-8674(03)00653-6;
RA Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.;
RT "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in
RT virus budding.";
RL Cell 114:689-699(2003).
RN [9]
RP FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH CHMP6; CHMP4C;
RP PDCD6IP; 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 [10]
RP FUNCTION (MICROBIAL INFECTION), SELF-ASSOCIATION, AND INTERACTION WITH
RP CHMP2A; CHMP4A; CHMP4C; CHMP6; PDCD6IP 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 [11]
RP ERRATUM OF PUBMED:14519844.
RA Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
RL Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
RN [12]
RP TISSUE SPECIFICITY, AND INTERACTION WITH PDCD6IP.
RX PubMed=14678797; DOI=10.1016/j.abb.2003.09.038;
RA Katoh K., Shibata H., Hatta K., Maki M.;
RT "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix
RT among the three CHMP4 isoforms.";
RL Arch. Biochem. Biophys. 421:159-165(2004).
RN [13]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH CHMP6.
RX PubMed=15511219; DOI=10.1042/bj20041227;
RA Yorikawa C., Shibata H., Waguri S., Hatta K., Horii M., Katoh K.,
RA Kobayashi T., Uchiyama Y., Maki M.;
RT "Human CHMP6, a myristoylated ESCRT-III protein, interacts directly with an
RT ESCRT-II component EAP20 and regulates endosomal cargo sorting.";
RL Biochem. J. 387:17-26(2005).
RN [14]
RP INTERACTION WITH MISFOLDED CFTR.
RX PubMed=15007060; DOI=10.1083/jcb.200312018;
RA Sharma M., Pampinella F., Nemes C., Benharouga M., So J., Du K.,
RA Bache K.G., Papsin B., Zerangue N., Stenmark H., Lukacs G.L.;
RT "Misfolding diverts CFTR from recycling to degradation: quality control at
RT early endosomes.";
RL J. Cell Biol. 164:923-933(2004).
RN [15]
RP INTERACTION WITH CHMP7.
RX PubMed=16856878; DOI=10.1042/bj20060897;
RA Horii M., Shibata H., Kobayashi R., Katoh K., Yorikawa C., Yasuda J.,
RA Maki M.;
RT "CHMP7, a novel ESCRT-III-related protein, associates with CHMP4b and
RT functions in the endosomal sorting pathway.";
RL Biochem. J. 400:23-32(2006).
RN [16]
RP AUTOINHIBITORY MECHANISM, AND INTRAMOLECULAR INTERACTION.
RX PubMed=17146056; DOI=10.1073/pnas.0603788103;
RA Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G.,
RA Goettlinger H.;
RT "Release of autoinhibition converts ESCRT-III components into potent
RT inhibitors of HIV-1 budding.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006).
RN [17]
RP INTERACTION WITH PDCD6IP.
RX PubMed=17428861; DOI=10.1128/jvi.00314-07;
RA Usami Y., Popov S., Goettlinger H.G.;
RT "Potent rescue of human immunodeficiency virus type 1 late domain mutants
RT by ALIX/AIP1 depends on its CHMP4 binding site.";
RL J. Virol. 81:6614-6622(2007).
RN [18]
RP INTERACTION WITH BROX.
RX PubMed=18190528; DOI=10.1111/j.1742-4658.2007.06230.x;
RA Ichioka F., Kobayashi R., Katoh K., Shibata H., Maki M.;
RT "Brox, a novel farnesylated Bro1 domain-containing protein that associates
RT with charged multivesicular body protein 4 (CHMP4).";
RL FEBS J. 275:682-692(2008).
RN [19]
RP FUNCTION, SELF-ASSOCIATION, AND STRUCTURE BY ELECTRON MICROSCOPY.
RX PubMed=18209100; DOI=10.1083/jcb.200707031;
RA Hanson P.I., Roth R., Lin Y., Heuser J.E.;
RT "Plasma membrane deformation by circular arrays of ESCRT-III protein
RT filaments.";
RL J. Cell Biol. 180:389-402(2008).
RN [20]
RP INTERACTION WITH PTPN23.
RX PubMed=18434552; DOI=10.1073/pnas.0707601105;
RA Doyotte A., Mironov A., McKenzie E., Woodman P.;
RT "The Bro1-related protein HD-PTP/PTPN23 is required for endosomal cargo
RT sorting and multivesicular body morphogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:6308-6313(2008).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-6 AND LYS-114, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184 AND SER-223, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP ISGYLATION, AND INTERACTION WITH 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-223, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [27]
RP FUNCTION.
RX PubMed=22660413; DOI=10.1038/ncb2502;
RA Baietti M.F., Zhang Z., Mortier E., Melchior A., Degeest G., Geeraerts A.,
RA Ivarsson Y., Depoortere F., Coomans C., Vermeiren E., Zimmermann P.,
RA David G.;
RT "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes.";
RL Nat. Cell Biol. 14:677-685(2012).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22422861; DOI=10.1126/science.1217180;
RA Carlton J.G., Caballe A., Agromayor M., Kloc M., Martin-Serrano J.;
RT "ESCRT-III governs the Aurora B-mediated abscission checkpoint through
RT CHMP4C.";
RL Science 336:220-225(2012).
RN [30]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [32]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 207-224 IN COMPLEX WITH PDCD6IP.
RX PubMed=18511562; DOI=10.1073/pnas.0801567105;
RA McCullough J., Fisher R.D., Whitby F.G., Sundquist W.I., Hill C.P.;
RT "ALIX-CHMP4 interactions in the human ESCRT pathway.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:7687-7691(2008).
RN [33]
RP VARIANTS CTRCT31 VAL-129 AND LYS-161.
RX PubMed=17701905; DOI=10.1086/519980;
RA Shiels A., Bennett T.M., Knopf H.L.S., Yamada K., Yoshiura K., Niikawa N.,
RA Shim S., Hanson P.I.;
RT "CHMP4B, a novel gene for autosomal dominant cataracts linked to chromosome
RT 20q.";
RL Am. J. Hum. Genet. 81:596-606(2007).
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 (PubMed:12860994, PubMed:18209100). The ESCRT machinery also functions
CC in topologically equivalent membrane fission events, such as the
CC terminal stages of cytokinesis (PubMed:21310966). Together with SPAST,
CC the ESCRT-III complex promotes nuclear envelope sealing and mitotic
CC spindle disassembly during late anaphase (PubMed:26040712). Plays a
CC role in the endosomal sorting pathway. ESCRT-III proteins are believed
CC to mediate the necessary vesicle extrusion and/or membrane fission
CC activities, possibly in conjunction with the AAA ATPase VPS4. When
CC overexpressed, membrane-assembled circular arrays of CHMP4B filaments
CC can promote or stabilize negative curvature and outward budding.
CC CHMP4A/B/C are required for the exosomal release of SDCBP, CD63 and
CC syndecan (PubMed:22660413). {ECO:0000269|PubMed:12860994,
CC ECO:0000269|PubMed:18209100, ECO:0000269|PubMed:21310966,
CC ECO:0000269|PubMed:22660413, ECO:0000269|PubMed:26040712}.
CC -!- FUNCTION: (Microbial infection) The ESCRT machinery also functions in
CC topologically equivalent membrane fission events, such as the budding
CC of enveloped viruses (HIV-1 and other lentiviruses). Via its
CC interaction with PDCD6IP involved in HIV-1 p6- and p9-dependent virus
CC release. {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:22422861}.
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. Interacts with CHMP6 and CHMP4C. Interacts with
CC PDCD6IP; the interaction is direct. Interacts with VPS4A; the
CC interaction is direct. Interacts with VPS4B; the interaction is direct.
CC Interacts with CHMP7. Interacts with CFTR; the interaction requires
CC misfolded CFTR. Interacts with PTPN23. {ECO:0000269|PubMed:12860994,
CC ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:14583093,
CC ECO:0000269|PubMed:14678797, ECO:0000269|PubMed:15007060,
CC ECO:0000269|PubMed:15511219, ECO:0000269|PubMed:16856878,
CC ECO:0000269|PubMed:17428861, ECO:0000269|PubMed:18190528,
CC ECO:0000269|PubMed:18434552, ECO:0000269|PubMed:18511562,
CC ECO:0000269|PubMed:21543490}.
CC -!- INTERACTION:
CC Q9H444; Q5VW32: BROX; NbExp=5; IntAct=EBI-749627, EBI-6286053;
CC Q9H444; Q6P1N0: CC2D1A; NbExp=3; IntAct=EBI-749627, EBI-7112364;
CC Q9H444; O43633: CHMP2A; NbExp=3; IntAct=EBI-749627, EBI-2692789;
CC Q9H444; Q9UQN3: CHMP2B; NbExp=2; IntAct=EBI-749627, EBI-718324;
CC Q9H444; Q9Y3E7: CHMP3; NbExp=5; IntAct=EBI-749627, EBI-2118119;
CC Q9H444; Q9BY43: CHMP4A; NbExp=4; IntAct=EBI-749627, EBI-747981;
CC Q9H444; Q9BY43-2: CHMP4A; NbExp=3; IntAct=EBI-749627, EBI-12178895;
CC Q9H444; Q9H444: CHMP4B; NbExp=7; IntAct=EBI-749627, EBI-749627;
CC Q9H444; Q9NZZ3: CHMP5; NbExp=4; IntAct=EBI-749627, EBI-751303;
CC Q9H444; Q8WUX9: CHMP7; NbExp=3; IntAct=EBI-749627, EBI-749253;
CC Q9H444; P42858: HTT; NbExp=7; IntAct=EBI-749627, EBI-466029;
CC Q9H444; Q8WUM4: PDCD6IP; NbExp=6; IntAct=EBI-749627, EBI-310624;
CC Q9H444; O60664: PLIN3; NbExp=3; IntAct=EBI-749627, EBI-725795;
CC Q9H444; Q9H3S7: PTPN23; NbExp=4; IntAct=EBI-749627, EBI-724478;
CC Q9H444; O95630: STAMBP; NbExp=3; IntAct=EBI-749627, EBI-396676;
CC Q9H444; P63279: UBE2I; NbExp=3; IntAct=EBI-749627, EBI-80168;
CC Q9H444; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-749627, EBI-10180829;
CC Q9H444; Q9WU78-1: Pdcd6ip; Xeno; NbExp=2; IntAct=EBI-749627, EBI-15788421;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:15511219}.
CC Late endosome membrane {ECO:0000269|PubMed:15511219,
CC ECO:0000305|PubMed:12860994}; Peripheral membrane protein
CC {ECO:0000305}. Midbody {ECO:0000269|PubMed:21310966,
CC ECO:0000269|PubMed:22422861}. Nucleus envelope
CC {ECO:0000269|PubMed:26040712}. Note=Recruited to the nuclear envelope
CC by CHMP7 during late anaphase (PubMed:26040712). Localizes transiently
CC to the midbody arms immediately before abscission (PubMed:22422861).
CC {ECO:0000269|PubMed:22422861, ECO:0000269|PubMed:26040712}.
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC heart and skeletal muscle. Also expressed in brain, colon, thymus,
CC spleen, kidney, liver, small intestine, placenta, lung and peripheral
CC blood lymphocytes. {ECO:0000269|PubMed:14678797}.
CC -!- DOMAIN: The acidic C-terminus and the basic N-termminus are thought to
CC render the protein in a closed, soluble and inactive conformation
CC through an autoinhibitory intramolecular interaction. The open and
CC active conformation, which enables membrane binding and
CC oligomerization, is achieved by interaction with other cellular binding
CC partners, probably including other ESCRT components.
CC -!- PTM: ISGylated. Isgylation weakens its interaction with VPS4A.
CC {ECO:0000269|PubMed:21543490}.
CC -!- DISEASE: Cataract 31, multiple types (CTRCT31) [MIM:605387]: An
CC opacification of the crystalline lens of the eye that frequently
CC results in visual impairment or blindness. Opacities vary in
CC morphology, are often confined to a portion of the lens, and may be
CC static or progressive. In general, the more posteriorly located and
CC dense an opacity, the greater the impact on visual function. CTRCT31
CC includes posterior polar, progressive posterior subcapsular, nuclear,
CC and anterior subcapsular cataracts. {ECO:0000269|PubMed:17701905}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- MISCELLANEOUS: Its overexpression strongly inhibits HIV-1 release.
CC -!- SIMILARITY: Belongs to the SNF7 family. {ECO:0000305}.
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DR EMBL; AB100261; BAC79375.1; -; mRNA.
DR EMBL; AY329085; AAQ91194.1; -; mRNA.
DR EMBL; AL050349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW76293.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW76294.1; -; Genomic_DNA.
DR EMBL; BC033859; AAH33859.1; -; mRNA.
DR CCDS; CCDS13228.1; -.
DR RefSeq; NP_789782.1; NM_176812.4.
DR PDB; 3C3Q; X-ray; 2.10 A; B=207-224.
DR PDB; 3UM3; X-ray; 3.80 A; B=121-224.
DR PDB; 4ABM; X-ray; 1.80 A; A/B/C/D=23-97.
DR PDB; 5MK2; X-ray; 1.70 A; C=205-224.
DR PDBsum; 3C3Q; -.
DR PDBsum; 3UM3; -.
DR PDBsum; 4ABM; -.
DR PDBsum; 5MK2; -.
DR AlphaFoldDB; Q9H444; -.
DR SMR; Q9H444; -.
DR BioGRID; 126170; 695.
DR ComplexPortal; CPX-329; ESCRT-III complex.
DR CORUM; Q9H444; -.
DR DIP; DIP-29924N; -.
DR IntAct; Q9H444; 131.
DR MINT; Q9H444; -.
DR STRING; 9606.ENSP00000217402; -.
DR iPTMnet; Q9H444; -.
DR MetOSite; Q9H444; -.
DR PhosphoSitePlus; Q9H444; -.
DR BioMuta; CHMP4B; -.
DR DMDM; 24636296; -.
DR EPD; Q9H444; -.
DR jPOST; Q9H444; -.
DR MassIVE; Q9H444; -.
DR MaxQB; Q9H444; -.
DR PaxDb; Q9H444; -.
DR PeptideAtlas; Q9H444; -.
DR PRIDE; Q9H444; -.
DR ProteomicsDB; 80785; -.
DR Antibodypedia; 25737; 182 antibodies from 25 providers.
DR DNASU; 128866; -.
DR Ensembl; ENST00000217402.3; ENSP00000217402.2; ENSG00000101421.4.
DR GeneID; 128866; -.
DR KEGG; hsa:128866; -.
DR MANE-Select; ENST00000217402.3; ENSP00000217402.2; NM_176812.5; NP_789782.1.
DR UCSC; uc002xaa.4; human.
DR CTD; 128866; -.
DR DisGeNET; 128866; -.
DR GeneCards; CHMP4B; -.
DR HGNC; HGNC:16171; CHMP4B.
DR HPA; ENSG00000101421; Low tissue specificity.
DR MalaCards; CHMP4B; -.
DR MIM; 605387; phenotype.
DR MIM; 610897; gene.
DR neXtProt; NX_Q9H444; -.
DR OpenTargets; ENSG00000101421; -.
DR Orphanet; 98993; Early-onset posterior polar cataract.
DR Orphanet; 441447; Early-onset posterior subcapsular cataract.
DR PharmGKB; PA25721; -.
DR VEuPathDB; HostDB:ENSG00000101421; -.
DR eggNOG; KOG1656; Eukaryota.
DR GeneTree; ENSGT00940000154663; -.
DR HOGENOM; CLU_071097_0_0_1; -.
DR InParanoid; Q9H444; -.
DR OMA; WSWFGGA; -.
DR OrthoDB; 1490465at2759; -.
DR PhylomeDB; Q9H444; -.
DR TreeFam; TF314269; -.
DR PathwayCommons; Q9H444; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-1632852; Macroautophagy.
DR Reactome; R-HSA-5620971; Pyroptosis.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9668328; Sealing of the nuclear envelope (NE) by ESCRT-III.
DR Reactome; R-HSA-9679504; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR Reactome; R-HSA-9694676; Translation of Replicase and Assembly of the Replication Transcription Complex.
DR SignaLink; Q9H444; -.
DR SIGNOR; Q9H444; -.
DR BioGRID-ORCS; 128866; 599 hits in 1087 CRISPR screens.
DR ChiTaRS; CHMP4B; human.
DR EvolutionaryTrace; Q9H444; -.
DR GeneWiki; CHMP4B; -.
DR GenomeRNAi; 128866; -.
DR Pharos; Q9H444; Tbio.
DR PRO; PR:Q9H444; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H444; protein.
DR Bgee; ENSG00000101421; Expressed in ileal mucosa and 182 other tissues.
DR Genevisible; Q9H444; HS.
DR GO; GO:1904930; C:amphisome membrane; IDA:ComplexPortal.
DR GO; GO:0000421; C:autophagosome membrane; IDA:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0009898; C:cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:UniProtKB.
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:0030117; C:membrane coat; IDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
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:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:ComplexPortal.
DR GO; GO:0031982; C:vesicle; IDA:BHF-UCL.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0042802; F:identical protein binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IMP:ParkinsonsUK-UCL.
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:0032511; P:late endosome to vacuole transport via multivesicular body sorting pathway; IBA:GO_Central.
DR GO; GO:0016236; P:macroautophagy; TAS:ParkinsonsUK-UCL.
DR GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB.
DR GO; GO:0090148; P:membrane fission; IMP:UniProtKB.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; 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:1902902; P:negative regulation of autophagosome assembly; IMP:UniProtKB.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:1901215; P:negative regulation of neuron death; 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:0006620; P:post-translational protein targeting to endoplasmic reticulum membrane; IMP:UniProtKB.
DR GO; GO:0051258; P:protein polymerization; IDA:UniProtKB.
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:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0006900; P:vesicle budding from membrane; IBA:GO_Central.
DR GO; GO:0051469; P:vesicle fusion with vacuole; IC:ComplexPortal.
DR GO; GO:0046755; P:viral budding; IMP:UniProtKB.
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 InterPro; IPR005024; Snf7_fam.
DR PANTHER; PTHR22761; PTHR22761; 1.
DR Pfam; PF03357; Snf7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cataract; Coiled coil; Cytoplasm;
KW Direct protein sequencing; Disease variant; Endosome;
KW Host-virus interaction; Membrane; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Transport; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT CHAIN 2..224
FT /note="Charged multivesicular body protein 4b"
FT /id="PRO_0000211489"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 185..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 23..183
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.6, ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 114
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT VARIANT 129
FT /note="D -> V (in CTRCT31; dbSNP:rs118203965)"
FT /evidence="ECO:0000269|PubMed:17701905"
FT /id="VAR_037579"
FT VARIANT 161
FT /note="E -> K (in CTRCT31; dbSNP:rs118203966)"
FT /evidence="ECO:0000269|PubMed:17701905"
FT /id="VAR_037580"
FT HELIX 23..57
FT /evidence="ECO:0007829|PDB:4ABM"
FT HELIX 62..96
FT /evidence="ECO:0007829|PDB:4ABM"
FT HELIX 209..212
FT /evidence="ECO:0007829|PDB:3C3Q"
FT HELIX 213..221
FT /evidence="ECO:0007829|PDB:5MK2"
SQ 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
