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Vacuolar protein sorting-associated protein 4B (EC 3.6.4.6) (Cell migration-inducing gene 1 protein) (Suppressor of K( ) transport growth defect 1) (Protein SKD1)

 VPS4B_HUMAN             Reviewed;         444 AA.
O75351; Q69HW4; Q9GZS7;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
16-JAN-2004, sequence version 2.
25-OCT-2017, entry version 174.
RecName: Full=Vacuolar protein sorting-associated protein 4B;
EC=3.6.4.6;
AltName: Full=Cell migration-inducing gene 1 protein;
AltName: Full=Suppressor of K(+) transport growth defect 1;
Short=Protein SKD1;
Name=VPS4B; Synonyms=SKD1, VPS42; ORFNames=MIG1;
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, INTERACTION WITH VPS4A,
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLU-235.
PubMed=11563910; DOI=10.1006/jmbi.2001.4917;
Scheuring S., Roehricht R.A., Schoening-Burkhardt B., Beyer A.,
Mueller S., Abts H.F., Koehrer K.;
"Mammalian cells express two VPS4 proteins both of which are involved
in intracellular protein trafficking.";
J. Mol. Biol. 312:469-480(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Skin;
PubMed=12594041; DOI=10.1016/S0378-1119(02)01205-2;
Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P.,
Koehrer K.;
"Comparative sequence and expression analyses of four mammalian VPS4
genes.";
Gene 305:47-59(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Umbilical cord blood;
PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
Wang Y.-X., Chen S.-J., Chen Z.;
"Identification of genes expressed in human CD34(+) hematopoietic
stem/progenitor cells by expressed sequence tags and efficient full-
length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kim J.W.;
"Identification of a human cell migration gene 1.";
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=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).
[7]
INTERACTION WITH CHMP2A.
PubMed=11559748;
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.;
"CHMP1 functions as a member of a newly defined family of vesicle
trafficking proteins.";
J. Cell Sci. 114:2395-2404(2001).
[8]
FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP1A; CHMP1B CHMP2A;
CHMP4B AND CHMP6, AND SUBCELLULAR LOCATION.
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).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[11]
MUTAGENESIS OF ALA-15 AND LEU-66.
PubMed=18606141; DOI=10.1016/j.devcel.2008.05.014;
Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M.,
Kaplan J., Sundquist W.I.;
"Two distinct modes of ESCRT-III recognition are required for VPS4
functions in lysosomal protein targeting and HIV-1 budding.";
Dev. Cell 15:62-73(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[13]
INTERACTION WITH VTA1, AND MUTAGENESIS OF 390-GLY--TRP-396.
PubMed=18385515; DOI=10.1091/mbc.E07-12-1263;
Shim S., Merrill S.A., Hanson P.I.;
"Novel interactions of ESCRT-III with LIP5 and VPS4 and their
implications for ESCRT-III disassembly.";
Mol. Biol. Cell 19:2661-2672(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=18318008; DOI=10.1002/pmic.200700884;
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
Zou H., Gu J.;
"Large-scale phosphoproteome analysis of human liver tissue by
enrichment and fractionation of phosphopeptides with strong anion
exchange chromatography.";
Proteomics 8:1346-1361(2008).
[16]
FUNCTION, ASSOCIATION WITH THE CHMP2A-CHMP3 POLYMER, 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).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
INTERACTION WITH IST1.
PubMed=19129479; DOI=10.1091/mbc.E08-05-0475;
Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M.,
Sundquist W.I.;
"Biochemical analyses of human IST1 and its function in cytokinesis.";
Mol. Biol. Cell 20:1360-1373(2009).
[19]
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).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102 AND SER-108,
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).
[21]
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).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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).
[23]
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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, 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).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102; SER-108 AND
SER-410, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[26]
STRUCTURE BY NMR OF 1-77, DOMAIN, AND VARIANT MET-58.
PubMed=16018968; DOI=10.1016/j.bbrc.2005.06.110;
Takasu H., Jee J.G., Ohno A., Goda N., Fujiwara K., Tochio H.,
Shirakawa M., Hiroaki H.;
"Structural characterization of the MIT domain from human Vps4b.";
Biochem. Biophys. Res. Commun. 334:460-465(2005).
[27]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 123-444, SUBUNIT, INTERACTION
WITH VTA1, AND MUTAGENESIS OF 208-TRP-LEU-209 AND GLY-210.
PubMed=16193069; DOI=10.1038/sj.emboj.7600818;
Scott A., Chung H.Y., Gonciarz-Swiatek M., Hill G.C., Whitby F.G.,
Gaspar J., Holton J.M., Viswanathan R., Ghaffarian S., Hill C.P.,
Sundquist W.I.;
"Structural and mechanistic studies of VPS4 proteins.";
EMBO J. 24:3658-3669(2005).
[28]
STRUCTURE BY NMR OF 1-108.
RIKEN structural genomics initiative (RSGI);
"Solution structure of MIT domain from human SKD1.";
Submitted (NOV-2005) to the PDB data bank.
[29]
STRUCTURE BY NMR OF 1-86 IN COMPLEX WITH CHMP2B, AND INTERACTION WITH
CHMP1B.
PubMed=17928862; DOI=10.1038/nature06172;
Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A.,
Ghaffarian S., Sundquist W.I.;
"ESCRT-III recognition by VPS4 ATPases.";
Nature 449:740-744(2007).
-!- FUNCTION: Involved in late steps of the endosomal multivesicular
bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III
assemblies and catalyzes their disassembly, possibly in
combination with membrane fission. Redistributes the ESCRT-III
components to the cytoplasm for further rounds of MVB sorting.
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. In conjunction with the
ESCRT machinery also appears to function in topologically
equivalent membrane fission events, such as the terminal stages of
cytokinesis and enveloped virus budding (HIV-1 and other
lentiviruses). VPS4A/B are required for the exosomal release of
SDCBP, CD63 and syndecan (PubMed:22660413).
{ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:18687924, ECO:0000269|PubMed:22660413}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Proposed to be monomeric or homodimeric in nucleotide-
free form and to oligomerize upon binding to ATP to form two
stacked hexameric or heptameric rings with a central pore through
which ESCRT-III substrates are translocated in an ATP-dependent
manner. In vitro, associates on the inside of a helical tubular
structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A,
CHMP1B, CHMP2A, CHMP4B and CHMP6. Interacts with VPS4A; the
interaction suggests a heteromeric assembly with VPS4A. Interacts
with VTA1. {ECO:0000269|PubMed:11559748,
ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:14505570,
ECO:0000269|PubMed:16193069, ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18385515, ECO:0000269|PubMed:19129479}.
-!- INTERACTION:
Q9UQN3-1:CHMP2B; NbExp=2; IntAct=EBI-2514459, EBI-15663586;
Q9NZZ3:CHMP5; NbExp=5; IntAct=EBI-2514459, EBI-751303;
Q96K21:ZFYVE19; NbExp=5; IntAct=EBI-2514459, EBI-6448240;
Q96K21-3:ZFYVE19; NbExp=3; IntAct=EBI-2514459, EBI-10187928;
-!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane; Peripheral
membrane protein. Late endosome membrane {ECO:0000305}; Peripheral
membrane protein {ECO:0000305}. Note=Membrane-associated in the
prevacuolar endosomal compartment. Localized in HIV-1 particles
purified from acutely infected cells.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:11563910}.
-!- DOMAIN: The MIT domain serves as an adapter for ESCRT-III
proteins. It forms an asymmetric three-helix bundle that binds
amphipathic MIM (MIT interacting motif) helices along the groove
between MIT helices 2 and 3 present in a subset of ESCRT-III
proteins thus establishing the canonical MIM-MIT interaction. In
an extended conformation along the groove between helices 1 and 3,
also binds to a type-2 MIT interacting motif (MIM2).
{ECO:0000269|PubMed:16018968}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}.
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EMBL; AF195514; AAG33022.1; -; mRNA.
EMBL; AF282904; AAG01471.1; -; Genomic_DNA.
EMBL; AF038960; AAC39874.1; -; mRNA.
EMBL; AY232629; AAP59551.1; -; mRNA.
EMBL; CH471096; EAW63143.1; -; Genomic_DNA.
EMBL; BC039574; AAH39574.1; -; mRNA.
CCDS; CCDS11983.1; -.
RefSeq; NP_004860.2; NM_004869.3.
UniGene; Hs.126550; -.
PDB; 1WR0; NMR; -; A=1-77.
PDB; 1XWI; X-ray; 2.80 A; A=123-444.
PDB; 2CPT; NMR; -; A=1-104.
PDB; 2JQH; NMR; -; A=1-86.
PDB; 2JQK; NMR; -; A=1-86.
PDB; 4U7Y; X-ray; 2.50 A; A=1-89.
PDBsum; 1WR0; -.
PDBsum; 1XWI; -.
PDBsum; 2CPT; -.
PDBsum; 2JQH; -.
PDBsum; 2JQK; -.
PDBsum; 4U7Y; -.
ProteinModelPortal; O75351; -.
SMR; O75351; -.
BioGrid; 114901; 49.
DIP; DIP-53790N; -.
IntAct; O75351; 10.
STRING; 9606.ENSP00000238497; -.
ChEMBL; CHEMBL2311229; -.
iPTMnet; O75351; -.
PhosphoSitePlus; O75351; -.
BioMuta; VPS4B; -.
EPD; O75351; -.
MaxQB; O75351; -.
PaxDb; O75351; -.
PeptideAtlas; O75351; -.
PRIDE; O75351; -.
DNASU; 9525; -.
Ensembl; ENST00000238497; ENSP00000238497; ENSG00000119541.
GeneID; 9525; -.
KEGG; hsa:9525; -.
UCSC; uc002lix.4; human.
CTD; 9525; -.
DisGeNET; 9525; -.
EuPathDB; HostDB:ENSG00000119541.9; -.
GeneCards; VPS4B; -.
HGNC; HGNC:10895; VPS4B.
HPA; CAB046445; -.
HPA; HPA040393; -.
HPA; HPA057649; -.
MalaCards; VPS4B; -.
MIM; 609983; gene.
neXtProt; NX_O75351; -.
OpenTargets; ENSG00000119541; -.
PharmGKB; PA35795; -.
eggNOG; KOG0739; Eukaryota.
eggNOG; ENOG410XRHN; LUCA.
GeneTree; ENSGT00550000074466; -.
HOGENOM; HOG000225146; -.
HOVERGEN; HBG057074; -.
InParanoid; O75351; -.
KO; K12196; -.
OMA; THFKKVK; -.
OrthoDB; EOG091G0Q8J; -.
PhylomeDB; O75351; -.
TreeFam; TF105012; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; VPS4B; human.
EvolutionaryTrace; O75351; -.
GeneWiki; VPS4B; -.
GenomeRNAi; 9525; -.
PRO; PR:O75351; -.
Proteomes; UP000005640; Chromosome 18.
Bgee; ENSG00000119541; -.
CleanEx; HS_VPS4B; -.
ExpressionAtlas; O75351; baseline and differential.
Genevisible; O75351; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005768; C:endosome; IDA:MGI.
GO; GO:0010008; C:endosome membrane; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IDA:MGI.
GO; GO:0042623; F:ATPase activity, coupled; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0030301; P:cholesterol transport; IEA:Ensembl.
GO; GO:0016197; P:endosomal transport; IDA:MGI.
GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
GO; GO:0061738; P:late endosomal microautophagy; IEA:Ensembl.
GO; GO:0016236; P:macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; NAS:ParkinsonsUK-UCL.
GO; GO:0060548; P:negative regulation of cell death; IMP:UniProtKB.
GO; GO:1903542; P:negative regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:1903724; P:positive regulation of centriole elongation; IMP:UniProtKB.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:UniProtKB.
GO; GO:1903902; P:positive regulation of viral life cycle; IMP:UniProtKB.
GO; GO:0048524; P:positive regulation of viral process; IMP:UniProtKB.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0006813; P:potassium ion transport; IEA:Ensembl.
GO; GO:0051261; P:protein depolymerization; IDA:UniProtKB.
GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
GO; GO:0010824; P:regulation of centrosome duplication; IMP:UniProtKB.
GO; GO:1901673; P:regulation of mitotic spindle assembly; IMP:UniProtKB.
GO; GO:0050792; P:regulation of viral process; IMP:UniProtKB.
GO; GO:0033993; P:response to lipid; IDA:UniProtKB.
GO; GO:0043162; P:ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0090611; P:ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway; IMP:UniProtKB.
GO; GO:0039702; P:viral budding via host ESCRT complex; IGI:UniProtKB.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019076; P:viral release from host cell; IMP:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR003959; ATPase_AAA_core.
InterPro; IPR003960; ATPase_AAA_CS.
InterPro; IPR007330; MIT.
InterPro; IPR036181; MIT_dom_sf.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR015415; Vps4_C.
Pfam; PF00004; AAA; 1.
Pfam; PF04212; MIT; 1.
Pfam; PF09336; Vps4_C; 1.
SMART; SM00382; AAA; 1.
SMART; SM00745; MIT; 1.
SUPFAM; SSF116846; SSF116846; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS00674; AAA; 1.
1: Evidence at protein level;
3D-structure; Acetylation; ATP-binding; Cell cycle; Cell division;
Coiled coil; Complete proteome; Endosome; Hydrolase; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Protein transport;
Reference proteome; Transport.
CHAIN 1 444 Vacuolar protein sorting-associated
protein 4B.
/FTId=PRO_0000084767.
DOMAIN 4 82 MIT.
NP_BIND 174 181 ATP. {ECO:0000255}.
COILED 19 82 {ECO:0000255}.
MOD_RES 10 10 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9UN37}.
MOD_RES 93 93 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18318008,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 108 108 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:24275569}.
MOD_RES 410 410 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VARIANT 58 58 I -> M (common polymorphism; induces
thermal instability; dbSNP:rs17688948).
{ECO:0000269|PubMed:16018968}.
/FTId=VAR_023385.
MUTAGEN 15 15 A->D: Reduces HIV-1 release 10-fold; when
associated with D-66.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 15 15 A->D: Reduces HIV-1 release 2-fold.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 66 66 L->D: Reduces HIV-1 release 10-fold; when
associated with D-15.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 66 66 L->D: Reduces HIV-1 release 3-fold.
{ECO:0000269|PubMed:18606141}.
MUTAGEN 208 209 WL->AA: Strongly impairs HIV-1 release.
{ECO:0000269|PubMed:16193069}.
MUTAGEN 210 210 G->A: Impairs HIV-1 release.
{ECO:0000269|PubMed:16193069}.
MUTAGEN 235 235 E->Q: Defective in vacuolar protein
sorting. {ECO:0000269|PubMed:11563910}.
MUTAGEN 390 396 Missing: Abolishes interaction with VTA1.
{ECO:0000269|PubMed:18385515}.
CONFLICT 114 114 K -> R (in Ref. 3; AAC39874).
{ECO:0000305}.
CONFLICT 127 127 E -> D (in Ref. 3; AAC39874).
{ECO:0000305}.
CONFLICT 342 342 S -> G (in Ref. 3; AAC39874).
{ECO:0000305}.
TURN 1 3 {ECO:0000244|PDB:1WR0}.
HELIX 6 24 {ECO:0000244|PDB:4U7Y}.
HELIX 27 47 {ECO:0000244|PDB:4U7Y}.
HELIX 52 81 {ECO:0000244|PDB:4U7Y}.
STRAND 87 89 {ECO:0000244|PDB:2CPT}.
STRAND 125 127 {ECO:0000244|PDB:1XWI}.
HELIX 133 135 {ECO:0000244|PDB:1XWI}.
HELIX 140 155 {ECO:0000244|PDB:1XWI}.
HELIX 157 159 {ECO:0000244|PDB:1XWI}.
STRAND 168 178 {ECO:0000244|PDB:1XWI}.
HELIX 180 190 {ECO:0000244|PDB:1XWI}.
STRAND 195 200 {ECO:0000244|PDB:1XWI}.
HELIX 213 225 {ECO:0000244|PDB:1XWI}.
STRAND 227 234 {ECO:0000244|PDB:1XWI}.
TURN 235 237 {ECO:0000244|PDB:1XWI}.
HELIX 238 240 {ECO:0000244|PDB:1XWI}.
STRAND 243 245 {ECO:0000244|PDB:1XWI}.
HELIX 250 263 {ECO:0000244|PDB:1XWI}.
STRAND 265 267 {ECO:0000244|PDB:1XWI}.
STRAND 272 279 {ECO:0000244|PDB:1XWI}.
TURN 281 283 {ECO:0000244|PDB:1XWI}.
HELIX 286 290 {ECO:0000244|PDB:1XWI}.
STRAND 294 297 {ECO:0000244|PDB:1XWI}.
HELIX 303 314 {ECO:0000244|PDB:1XWI}.
HELIX 323 331 {ECO:0000244|PDB:1XWI}.
HELIX 338 349 {ECO:0000244|PDB:1XWI}.
HELIX 351 358 {ECO:0000244|PDB:1XWI}.
STRAND 360 368 {ECO:0000244|PDB:1XWI}.
STRAND 375 383 {ECO:0000244|PDB:1XWI}.
STRAND 386 388 {ECO:0000244|PDB:1XWI}.
STRAND 391 393 {ECO:0000244|PDB:1XWI}.
HELIX 396 398 {ECO:0000244|PDB:1XWI}.
HELIX 401 403 {ECO:0000244|PDB:1XWI}.
HELIX 411 419 {ECO:0000244|PDB:1XWI}.
HELIX 427 438 {ECO:0000244|PDB:1XWI}.
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


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