VPS4B_HUMAN
ID VPS4B_HUMAN Reviewed; 444 AA.
AC O75351; Q69HW4; Q9GZS7;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-JAN-2004, sequence version 2.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Vacuolar protein sorting-associated protein 4B {ECO:0000305};
DE EC=3.6.4.6 {ECO:0000269|PubMed:18687924};
DE AltName: Full=Cell migration-inducing gene 1 protein;
DE AltName: Full=Suppressor of K(+) transport growth defect 1;
DE Short=Protein SKD1;
GN Name=VPS4B {ECO:0000312|HGNC:HGNC:10895}; Synonyms=SKD1, VPS42;
GN ORFNames=MIG1;
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, INTERACTION WITH VPS4A, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-235.
RX PubMed=11563910; DOI=10.1006/jmbi.2001.4917;
RA Scheuring S., Roehricht R.A., Schoening-Burkhardt B., Beyer A., Mueller S.,
RA Abts H.F., Koehrer K.;
RT "Mammalian cells express two VPS4 proteins both of which are involved in
RT intracellular protein trafficking.";
RL J. Mol. Biol. 312:469-480(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Skin;
RX PubMed=12594041; DOI=10.1016/s0378-1119(02)01205-2;
RA Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K.;
RT "Comparative sequence and expression analyses of four mammalian VPS4
RT genes.";
RL Gene 305:47-59(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kim J.W.;
RT "Identification of a human cell migration gene 1.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=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 [7]
RP INTERACTION WITH CHMP2A.
RX PubMed=11559748; DOI=10.1242/jcs.114.13.2395;
RA Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
RT "CHMP1 functions as a member of a newly defined family of vesicle
RT trafficking proteins.";
RL J. Cell Sci. 114:2395-2404(2001).
RN [8]
RP FUNCTION IN HIV-1 BUDDING (MICROBIAL INFECTION), INTERACTION WITH CHMP1A;
RP CHMP1B CHMP2A; CHMP4B AND CHMP6, AND SUBCELLULAR LOCATION.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [11]
RP MUTAGENESIS OF ALA-15 AND LEU-66, AND FUNCTION (MICROBIAL INFECTION).
RX PubMed=18606141; DOI=10.1016/j.devcel.2008.05.014;
RA Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J.,
RA Sundquist W.I.;
RT "Two distinct modes of ESCRT-III recognition are required for VPS4
RT functions in lysosomal protein targeting and HIV-1 budding.";
RL Dev. Cell 15:62-73(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [13]
RP INTERACTION WITH VTA1, AND MUTAGENESIS OF 390-GLY--TRP-396.
RX PubMed=18385515; DOI=10.1091/mbc.e07-12-1263;
RA Shim S., Merrill S.A., Hanson P.I.;
RT "Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications
RT for ESCRT-III disassembly.";
RL Mol. Biol. Cell 19:2661-2672(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [16]
RP FUNCTION, ASSOCIATION WITH THE CHMP2A-CHMP3 POLYMER, ELECTRON MICROSCOPY,
RP AND CATALYTIC ACTIVITY.
RX PubMed=18687924; DOI=10.1126/science.1161070;
RA Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G.,
RA Weissenhorn W.;
RT "Helical structures of ESCRT-III are disassembled by VPS4.";
RL Science 321:1354-1357(2008).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP INTERACTION WITH IST1.
RX PubMed=19129479; DOI=10.1091/mbc.e08-05-0475;
RA Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
RA Sundquist W.I.;
RT "Biochemical analyses of human IST1 and its function in cytokinesis.";
RL Mol. Biol. Cell 20:1360-1373(2009).
RN [19]
RP IDENTIFICATION 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102 AND SER-108, 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 [21]
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102; SER-108 AND
RP SER-410, AND 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 [26]
RP STRUCTURE BY NMR OF 1-77, DOMAIN, AND VARIANT MET-58.
RX PubMed=16018968; DOI=10.1016/j.bbrc.2005.06.110;
RA Takasu H., Jee J.G., Ohno A., Goda N., Fujiwara K., Tochio H.,
RA Shirakawa M., Hiroaki H.;
RT "Structural characterization of the MIT domain from human Vps4b.";
RL Biochem. Biophys. Res. Commun. 334:460-465(2005).
RN [27]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 123-444, SUBUNIT, INTERACTION WITH
RP VTA1, MUTAGENESIS OF 208-TRP-LEU-209 AND GLY-210, AND FUNCTION (MICROBIAL
RP INFECTION).
RX PubMed=16193069; DOI=10.1038/sj.emboj.7600818;
RA Scott A., Chung H.Y., Gonciarz-Swiatek M., Hill G.C., Whitby F.G.,
RA Gaspar J., Holton J.M., Viswanathan R., Ghaffarian S., Hill C.P.,
RA Sundquist W.I.;
RT "Structural and mechanistic studies of VPS4 proteins.";
RL EMBO J. 24:3658-3669(2005).
RN [28]
RP STRUCTURE BY NMR OF 1-108.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of MIT domain from human SKD1.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [29]
RP STRUCTURE BY NMR OF 1-86 IN COMPLEX WITH CHMP2B, AND INTERACTION WITH
RP CHMP1B.
RX PubMed=17928862; DOI=10.1038/nature06172;
RA Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A.,
RA Ghaffarian S., Sundquist W.I.;
RT "ESCRT-III recognition by VPS4 ATPases.";
RL Nature 449:740-744(2007).
CC -!- FUNCTION: Involved in late steps of the endosomal multivesicular bodies
CC (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and
CC catalyzes their ATP-dependent disassembly, possibly in combination with
CC membrane fission (PubMed:18687924). Redistributes the ESCRT-III
CC components to the cytoplasm for further rounds of MVB sorting. MVBs
CC contain intraluminal vesicles (ILVs) that are generated by invagination
CC and scission from the limiting membrane of the endosome and mostly are
CC delivered to lysosomes enabling degradation of membrane proteins, such
CC as stimulated growth factor receptors, lysosomal enzymes and lipids.
CC VPS4A/B are required for the exosomal release of SDCBP, CD63 and
CC syndecan (PubMed:22660413). {ECO:0000269|PubMed:11563910,
CC ECO:0000269|PubMed:18687924, ECO:0000269|PubMed:22660413}.
CC -!- FUNCTION: (Microbial infection) In conjunction with the ESCRT machinery
CC also appears to function in topologically equivalent membrane fission
CC events, such as the terminal stages of cytokinesis and enveloped virus
CC budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:16193069, ECO:0000269|PubMed:18606141}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.6;
CC Evidence={ECO:0000269|PubMed:18687924};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:18687924};
CC -!- SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-free
CC form and to oligomerize upon binding to ATP to form two stacked
CC hexameric or heptameric rings with a central pore through which ESCRT-
CC III substrates are translocated in an ATP-dependent manner. In vitro,
CC associates on the inside of a helical tubular structure formed by a
CC CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and
CC CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric
CC assembly with VPS4A. Interacts with VTA1. {ECO:0000269|PubMed:11559748,
CC ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:14505570,
CC ECO:0000269|PubMed:16193069, ECO:0000269|PubMed:17928862,
CC ECO:0000269|PubMed:18385515, ECO:0000269|PubMed:19129479}.
CC -!- INTERACTION:
CC O75351; P54253: ATXN1; NbExp=3; IntAct=EBI-2514459, EBI-930964;
CC O75351; Q9HD42: CHMP1A; NbExp=3; IntAct=EBI-2514459, EBI-1057156;
CC O75351; Q9UQN3-1: CHMP2B; NbExp=2; IntAct=EBI-2514459, EBI-15663586;
CC O75351; Q9NZZ3: CHMP5; NbExp=6; IntAct=EBI-2514459, EBI-751303;
CC O75351; P42858: HTT; NbExp=3; IntAct=EBI-2514459, EBI-466029;
CC O75351; Q9BW62: KATNAL1; NbExp=3; IntAct=EBI-2514459, EBI-743591;
CC O75351; Q96K21: ZFYVE19; NbExp=7; IntAct=EBI-2514459, EBI-6448240;
CC O75351; Q96K21-3: ZFYVE19; NbExp=3; IntAct=EBI-2514459, EBI-10187928;
CC -!- SUBCELLULAR LOCATION: Late endosome membrane
CC {ECO:0000250|UniProtKB:P46467}; Peripheral membrane protein
CC {ECO:0000305}. Note=Membrane-associated in the prevacuolar endosomal
CC compartment. Localized in HIV-1 particles purified from acutely
CC infected cells. {ECO:0000269|PubMed:14505570}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:11563910}.
CC -!- DOMAIN: The MIT domain serves as an adapter for ESCRT-III proteins. It
CC forms an asymmetric three-helix bundle that binds amphipathic MIM (MIT
CC interacting motif) helices along the groove between MIT helices 2 and 3
CC present in a subset of ESCRT-III proteins thus establishing the
CC canonical MIM-MIT interaction. In an extended conformation along the
CC groove between helices 1 and 3, also binds to a type-2 MIT interacting
CC motif (MIM2). {ECO:0000269|PubMed:16018968}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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DR EMBL; AF195514; AAG33022.1; -; mRNA.
DR EMBL; AF282904; AAG01471.1; -; Genomic_DNA.
DR EMBL; AF038960; AAC39874.1; -; mRNA.
DR EMBL; AY232629; AAP59551.1; -; mRNA.
DR EMBL; CH471096; EAW63143.1; -; Genomic_DNA.
DR EMBL; BC039574; AAH39574.1; -; mRNA.
DR CCDS; CCDS11983.1; -.
DR RefSeq; NP_004860.2; NM_004869.3.
DR PDB; 1WR0; NMR; -; A=1-77.
DR PDB; 1XWI; X-ray; 2.80 A; A=123-444.
DR PDB; 2CPT; NMR; -; A=1-104.
DR PDB; 2JQH; NMR; -; A=1-86.
DR PDB; 2JQK; NMR; -; A=1-86.
DR PDB; 4U7Y; X-ray; 2.50 A; A=1-89.
DR PDB; 7L9X; X-ray; 2.81 A; A=1-444.
DR PDBsum; 1WR0; -.
DR PDBsum; 1XWI; -.
DR PDBsum; 2CPT; -.
DR PDBsum; 2JQH; -.
DR PDBsum; 2JQK; -.
DR PDBsum; 4U7Y; -.
DR PDBsum; 7L9X; -.
DR AlphaFoldDB; O75351; -.
DR SMR; O75351; -.
DR BioGRID; 114901; 74.
DR ComplexPortal; CPX-338; VPS4A/B complex.
DR DIP; DIP-53790N; -.
DR IntAct; O75351; 21.
DR STRING; 9606.ENSP00000238497; -.
DR BindingDB; O75351; -.
DR ChEMBL; CHEMBL2311229; -.
DR GlyGen; O75351; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O75351; -.
DR MetOSite; O75351; -.
DR PhosphoSitePlus; O75351; -.
DR BioMuta; VPS4B; -.
DR EPD; O75351; -.
DR jPOST; O75351; -.
DR MassIVE; O75351; -.
DR MaxQB; O75351; -.
DR PaxDb; O75351; -.
DR PeptideAtlas; O75351; -.
DR PRIDE; O75351; -.
DR ProteomicsDB; 49918; -.
DR Antibodypedia; 23094; 195 antibodies from 30 providers.
DR DNASU; 9525; -.
DR Ensembl; ENST00000238497.10; ENSP00000238497.4; ENSG00000119541.10.
DR GeneID; 9525; -.
DR KEGG; hsa:9525; -.
DR MANE-Select; ENST00000238497.10; ENSP00000238497.4; NM_004869.4; NP_004860.2.
DR UCSC; uc002lix.4; human.
DR CTD; 9525; -.
DR DisGeNET; 9525; -.
DR GeneCards; VPS4B; -.
DR HGNC; HGNC:10895; VPS4B.
DR HPA; ENSG00000119541; Low tissue specificity.
DR MalaCards; VPS4B; -.
DR MIM; 609983; gene.
DR neXtProt; NX_O75351; -.
DR OpenTargets; ENSG00000119541; -.
DR Orphanet; 99789; Dentin dysplasia type I.
DR PharmGKB; PA35795; -.
DR VEuPathDB; HostDB:ENSG00000119541; -.
DR eggNOG; KOG0739; Eukaryota.
DR GeneTree; ENSGT00940000154973; -.
DR HOGENOM; CLU_000688_21_2_1; -.
DR InParanoid; O75351; -.
DR OMA; AVQYFIH; -.
DR OrthoDB; 787710at2759; -.
DR PhylomeDB; O75351; -.
DR TreeFam; TF105012; -.
DR PathwayCommons; O75351; -.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR SignaLink; O75351; -.
DR BioGRID-ORCS; 9525; 68 hits in 1083 CRISPR screens.
DR ChiTaRS; VPS4B; human.
DR EvolutionaryTrace; O75351; -.
DR GeneWiki; VPS4B; -.
DR GenomeRNAi; 9525; -.
DR Pharos; O75351; Tchem.
DR PRO; PR:O75351; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; O75351; protein.
DR Bgee; ENSG00000119541; Expressed in esophagus squamous epithelium and 200 other tissues.
DR ExpressionAtlas; O75351; baseline and differential.
DR Genevisible; O75351; HS.
DR GO; GO:1904949; C:ATPase complex; IC:ComplexPortal.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005768; C:endosome; IDA:MGI.
DR GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030496; C:midbody; IC:ComplexPortal.
DR GO; GO:0005643; C:nuclear pore; IC:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IC:ComplexPortal.
DR GO; GO:0006914; P:autophagy; IC:ComplexPortal.
DR GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
DR GO; GO:0016197; P:endosomal transport; IDA:MGI.
DR GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:1904903; P:ESCRT III complex disassembly; IDA:UniProtKB.
DR GO; GO:0061738; P:late endosomal microautophagy; IEA:Ensembl.
DR GO; GO:0061764; P:late endosome to lysosome transport via multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0016236; P:macroautophagy; NAS:ParkinsonsUK-UCL.
DR GO; GO:0090148; P:membrane fission; IC:ComplexPortal.
DR GO; GO:0061952; P:midbody abscission; IMP:UniProtKB.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
DR GO; GO:0071985; P:multivesicular body sorting pathway; IC:ComplexPortal.
DR GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
DR GO; GO:1903542; P:negative regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:0031468; P:nuclear membrane reassembly; IC:ComplexPortal.
DR GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
DR GO; GO:0001778; P:plasma membrane repair; IC:ComplexPortal.
DR GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
DR GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
DR GO; GO:0051261; P:protein depolymerization; IDA:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
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:0033993; P:response to lipid; IDA:UniProtKB.
DR GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
DR GO; GO:0046761; P:viral budding from plasma membrane; IMP:UniProtKB.
DR GO; GO:0039702; P:viral budding via host ESCRT complex; IGI:UniProtKB.
DR CDD; cd02678; MIT_VPS4; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR031255; VPS4.
DR InterPro; IPR015415; Vps4_C.
DR InterPro; IPR045253; VPS4_MIT.
DR PANTHER; PTHR23074:SF72; PTHR23074:SF72; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF04212; MIT; 1.
DR Pfam; PF09336; Vps4_C; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00745; MIT; 1.
DR SUPFAM; SSF116846; SSF116846; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00674; AAA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell cycle; Cell division; Coiled coil;
KW Endosome; Hydrolase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT CHAIN 1..444
FT /note="Vacuolar protein sorting-associated protein 4B"
FT /id="PRO_0000084767"
FT DOMAIN 4..82
FT /note="MIT"
FT REGION 77..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 19..82
FT /evidence="ECO:0000255"
FT COMPBIAS 77..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 174..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VARIANT 58
FT /note="I -> M (induces thermal instability;
FT dbSNP:rs17688948)"
FT /evidence="ECO:0000269|PubMed:16018968"
FT /id="VAR_023385"
FT MUTAGEN 15
FT /note="A->D: Reduces HIV-1 release 10-fold; when associated
FT with D-66."
FT /evidence="ECO:0000269|PubMed:18606141"
FT MUTAGEN 15
FT /note="A->D: Reduces HIV-1 release 2-fold."
FT /evidence="ECO:0000269|PubMed:18606141"
FT MUTAGEN 66
FT /note="L->D: Reduces HIV-1 release 10-fold; when associated
FT with D-15."
FT /evidence="ECO:0000269|PubMed:18606141"
FT MUTAGEN 66
FT /note="L->D: Reduces HIV-1 release 3-fold."
FT /evidence="ECO:0000269|PubMed:18606141"
FT MUTAGEN 208..209
FT /note="WL->AA: Strongly impairs HIV-1 release."
FT /evidence="ECO:0000269|PubMed:16193069"
FT MUTAGEN 210
FT /note="G->A: Impairs HIV-1 release."
FT /evidence="ECO:0000269|PubMed:16193069"
FT MUTAGEN 235
FT /note="E->Q: Defective in vacuolar protein sorting."
FT /evidence="ECO:0000269|PubMed:11563910"
FT MUTAGEN 390..396
FT /note="Missing: Abolishes interaction with VTA1."
FT /evidence="ECO:0000269|PubMed:18385515"
FT CONFLICT 114
FT /note="K -> R (in Ref. 3; AAC39874)"
FT /evidence="ECO:0000305"
FT CONFLICT 127
FT /note="E -> D (in Ref. 3; AAC39874)"
FT /evidence="ECO:0000305"
FT CONFLICT 342
FT /note="S -> G (in Ref. 3; AAC39874)"
FT /evidence="ECO:0000305"
FT TURN 1..3
FT /evidence="ECO:0007829|PDB:1WR0"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:4U7Y"
FT HELIX 27..47
FT /evidence="ECO:0007829|PDB:4U7Y"
FT HELIX 52..81
FT /evidence="ECO:0007829|PDB:4U7Y"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2CPT"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 140..155
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 157..159
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 168..178
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 213..225
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 227..234
FT /evidence="ECO:0007829|PDB:1XWI"
FT TURN 235..237
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 238..240
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 265..267
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 272..279
FT /evidence="ECO:0007829|PDB:1XWI"
FT TURN 281..283
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 286..290
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 303..314
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 323..331
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 351..358
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 360..368
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 375..383
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1XWI"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 401..403
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 411..419
FT /evidence="ECO:0007829|PDB:1XWI"
FT HELIX 427..438
FT /evidence="ECO:0007829|PDB:1XWI"
FT TURN 440..443
FT /evidence="ECO:0007829|PDB:7L9X"
SQ SEQUENCE 444 AA; 49302 MW; 9D565E4B20AF73FB CRC64;
MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA
KCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN DSDGEGESDD PEKKKLQNQL
QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK
SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC
GSRSENESEA ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL
PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT
HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MSDMLRSLSN
TKPTVNEHDL LKLKKFTEDF GQEG
