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Vacuolar protein sorting-associated protein 4A (EC 3.6.4.6) (Protein SKD2) (VPS4-1) (hVPS4)

 VPS4A_HUMAN             Reviewed;         437 AA.
Q9UN37; B2RCB7; Q8TF07; Q9UI03; Q9Y582;
12-APR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-2000, sequence version 1.
18-JUL-2018, entry version 169.
RecName: Full=Vacuolar protein sorting-associated protein 4A;
EC=3.6.4.6;
AltName: Full=Protein SKD2;
AltName: Full=VPS4-1;
Short=hVPS4;
Name=VPS4A {ECO:0000312|EMBL:AAG01470.1};
Synonyms=VPS4 {ECO:0000312|EMBL:AAD42971.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAK52408.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, INTERACTION WITH VPS4B, AND MUTAGENESIS OF GLU-228.
TISSUE=Keratinocyte;
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] {ECO:0000312|EMBL:AAG01470.1}
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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] {ECO:0000312|EMBL:AAL75948.1}
NUCLEOTIDE SEQUENCE [MRNA].
Ding J.B., Yu L., Zhao S.Y.;
"Cloning of a new human cDNA homologous to Homo sapiens SKD1
protein.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000312|EMBL:AAL75948.1}
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
Patejunas G.;
"Isolation of a homolog of SKD1.";
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000312|EMBL:AAF17203.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Hypothalamus {ECO:0000312|EMBL:AAF17203.1};
PubMed=10931946; DOI=10.1073/pnas.160270997;
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
"Gene expression profiling in the human hypothalamus-pituitary-adrenal
axis and full-length cDNA cloning.";
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[7] {ECO:0000312|EMBL:AAL75948.1}
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.
[8] {ECO:0000312|EMBL:AAH47932.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[9] {ECO:0000305, ECO:0000312|EMBL:AAD42971.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 6-437, SUBCELLULAR LOCATION, TISSUE
SPECIFICITY, AND MUTAGENESIS OF LYS-173 AND GLU-228.
TISSUE=Brain {ECO:0000312|EMBL:AAD42971.1};
PubMed=10637304; DOI=10.1091/mbc.11.1.227;
Bishop N., Woodman P.;
"ATPase-defective mammalian VPS4 localizes to aberrant endosomes and
impairs cholesterol trafficking.";
Mol. Biol. Cell 11:227-239(2000).
[10]
FUNCTION IN VIRUS RELEASE, AND MUTAGENESIS OF LYS-173 AND GLU-228.
PubMed=11595185; DOI=10.1016/S0092-8674(01)00506-2;
Garrus J.E., von Schwedler U.K., Pornillos O.W., Morham S.G.,
Zavitz K.H., Wang H.E., Wettstein D.A., Stray K.M., Cote M.,
Rich R.L., Myszka D.G., Sundquist W.I.;
"Tsg101 and the vacuolar protein sorting pathway are essential for
HIV-1 budding.";
Cell 107:55-65(2001).
[11] {ECO:0000305}
INTERACTION WITH CHMP1A, AND MUTAGENESIS OF GLU-228.
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).
[12] {ECO:0000305}
INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP4A; CHMP4B; CHMP4C AND
CHMP6.
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).
[13]
INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP2B AND CHMP3.
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).
[14]
ERRATUM.
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.;
Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003).
[15] {ECO:0000305}
FUNCTION, AND MUTAGENESIS OF GLU-228.
PubMed=15075231; DOI=10.1242/jcs.00998;
Sachse M., Strous G.J., Klumperman J.;
"ATPase-deficient hVPS4 impairs formation of internal endosomal
vesicles and stabilizes bilayered clathrin coats on endosomal
vacuoles.";
J. Cell Sci. 117:1699-1708(2004).
[16]
MUTAGENESIS OF 201-TRP-LEU-202 AND GLY-203.
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).
[17]
SUBCELLULAR LOCATION.
PubMed=17853893; DOI=10.1038/sj.emboj.7601850;
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P.,
Rodesch C.K., Sundquist W.I.;
"Human ESCRT and ALIX proteins interact with proteins of the midbody
and function in cytokinesis.";
EMBO J. 26:4215-4227(2007).
[18]
INTERACTION WITH SPAST.
PubMed=18997780; DOI=10.1038/nsmb.1512;
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J.,
Blackstone C., Hurley J.H.;
"Structural basis for midbody targeting of spastin by the ESCRT-III
protein CHMP1B.";
Nat. Struct. Mol. Biol. 15:1278-1286(2008).
[19]
INTERACTION WITH IST1, AND MUTAGENESIS OF LEU-64.
PubMed=19129480; DOI=10.1091/mbc.E08-05-0474;
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M.,
Ameer-Beg S., Bowers K., Martin-Serrano J.;
"Essential role of hIST1 in cytokinesis.";
Mol. Biol. Cell 20:1374-1387(2009).
[20]
INTERACTION WITH IST1, AND MUTAGENESIS OF VAL-13 AND LEU-64.
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-8, 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]
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).
[23]
INTERACTION WITH CHMP1B; CHMP2A; CHMP3; CHMP4B AND CHMP6.
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).
[24]
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).
[25]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ZFYVE19.
PubMed=24814515; DOI=10.1038/ncb2959;
Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K.,
Andersen J.S., Raiborg C., Stenmark H.;
"ANCHR mediates Aurora-B-dependent abscission checkpoint control
through retention of VPS4.";
Nat. Cell Biol. 16:550-560(2014).
[26]
STRUCTURE BY NMR OF 1-77, INTERACTION WITH CHMP1B, AND MUTAGENESIS OF
LEU-64 AND GLU-68.
PubMed=16174732; DOI=10.1073/pnas.0502165102;
Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J.,
Sundquist W.I.;
"Structure and ESCRT-III protein interactions of the MIT domain of
human VPS4A.";
Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005).
[27]
STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP1A, INTERACTION WITH
CHMP2B, AND MUTAGENESIS OF LEU-64 AND LYS-173.
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).
[28]
STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP6, INTERACTION WITH
CHMP1A, AND MUTAGENESIS OF VAL-13; LEU-64 AND LYS-173.
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).
[29]
VARIANT SER-193 DEL.
PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C.,
Patry L., Massicotte C., Ambalavanan A., Spiegelman D., Diallo O.,
Henrion E., Dionne-Laporte A., Fougerat A., Pshezhetsky A.V.,
Venkateswaran S., Rouleau G.A., Michaud J.L.;
"De novo mutations in moderate or severe intellectual disability.";
PLoS Genet. 10:E1004772-E1004772(2014).
-!- 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). Involved in cytokinesis: retained at the midbody by
ZFYVE19/ANCHR and CHMP4C until abscission checkpoint signaling is
terminated at late cytokinesis. It is then released following
dephosphorylation of CHMP4C, leading to abscission
(PubMed:24814515). VPS4A/B are required for the exosomal release
of SDCBP, CD63 and syndecan (PubMed:22660413).
{ECO:0000269|PubMed:11563910, ECO:0000269|PubMed:11595185,
ECO:0000269|PubMed:15075231, ECO:0000269|PubMed:22660413,
ECO:0000269|PubMed:24814515}.
-!- 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 (By similarity). Interacts with CHMP1A, CHMP1B, CHMP2A,
CHMP2B, CHMP3, CHMP4A, CHMP4B, CHMP4C and CHMP6. Interacts with
VPS4B; the interaction suggests a heteromeric assembly with VPS4B.
Interacts with SPAST. Interacts with IST1. Interacts with
ZFYVE19/ANCHR; leading to retain it at midbody. {ECO:0000250,
ECO:0000269|PubMed:11559748, ECO:0000269|PubMed:11563910,
ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844,
ECO:0000269|PubMed:16174732, ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18606141, ECO:0000269|PubMed:18997780,
ECO:0000269|PubMed:19129479, ECO:0000269|PubMed:19129480,
ECO:0000269|PubMed:21543490, ECO:0000269|PubMed:24814515}.
-!- INTERACTION:
Q9HD42:CHMP1A; NbExp=6; IntAct=EBI-1171942, EBI-1057156;
Q9HD42-1:CHMP1A; NbExp=2; IntAct=EBI-1171942, EBI-15663713;
Q7LBR1:CHMP1B; NbExp=4; IntAct=EBI-1171942, EBI-2118090;
O43633:CHMP2A; NbExp=3; IntAct=EBI-1171942, EBI-2692789;
Q96K21-1:ZFYVE19; NbExp=3; IntAct=EBI-1171942, EBI-16106990;
-!- SUBCELLULAR LOCATION: Prevacuolar compartment membrane; Peripheral
membrane protein. Late endosome membrane {ECO:0000305}; Peripheral
membrane protein {ECO:0000305}. Midbody. Note=Membrane-associated
in the prevacuolar endosomal compartment. Localizes to the midbody
of dividing cells, interaction with ZFYVE19/ANCHR mediates
retention at midbody (PubMed:24814515). Localized in two distinct
rings on either side of the Flemming body.
{ECO:0000269|PubMed:24814515}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:10637304, 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:0000250|UniProtKB:O75351}.
-!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255}.
-!- SEQUENCE CAUTION:
Sequence=AAL75948.1; Type=Frameshift; Positions=123, 133, 157, 163; Evidence={ECO:0000305};
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EMBL; AF255952; AAK52408.1; -; mRNA.
EMBL; AF282903; AAG01470.1; -; Genomic_DNA.
EMBL; AF132747; AAL75948.1; ALT_FRAME; mRNA.
EMBL; AF159063; AAD49227.1; -; mRNA.
EMBL; AF112215; AAF17203.1; -; mRNA.
EMBL; AK315026; BAG37514.1; -; mRNA.
EMBL; CH471092; EAW83263.1; -; Genomic_DNA.
EMBL; BC047932; AAH47932.1; -; mRNA.
EMBL; AF155740; AAD42971.1; -; mRNA.
CCDS; CCDS45517.1; -.
RefSeq; NP_037377.1; NM_013245.2.
UniGene; Hs.128420; -.
PDB; 1YXR; NMR; -; A=1-77.
PDB; 2JQ9; NMR; -; A=1-84.
PDB; 2K3W; NMR; -; A=1-84.
PDBsum; 1YXR; -.
PDBsum; 2JQ9; -.
PDBsum; 2K3W; -.
ProteinModelPortal; Q9UN37; -.
SMR; Q9UN37; -.
BioGrid; 118059; 33.
ComplexPortal; CPX-338; VPS4A/B complex.
DIP; DIP-44585N; -.
IntAct; Q9UN37; 22.
MINT; Q9UN37; -.
STRING; 9606.ENSP00000254950; -.
iPTMnet; Q9UN37; -.
PhosphoSitePlus; Q9UN37; -.
BioMuta; VPS4A; -.
DMDM; 62511240; -.
EPD; Q9UN37; -.
MaxQB; Q9UN37; -.
PaxDb; Q9UN37; -.
PeptideAtlas; Q9UN37; -.
PRIDE; Q9UN37; -.
ProteomicsDB; 85248; -.
DNASU; 27183; -.
Ensembl; ENST00000254950; ENSP00000254950; ENSG00000132612.
GeneID; 27183; -.
KEGG; hsa:27183; -.
UCSC; uc002eww.4; human.
CTD; 27183; -.
DisGeNET; 27183; -.
EuPathDB; HostDB:ENSG00000132612.15; -.
GeneCards; VPS4A; -.
HGNC; HGNC:13488; VPS4A.
HPA; CAB018751; -.
HPA; CAB034411; -.
HPA; HPA060092; -.
MIM; 609982; gene.
neXtProt; NX_Q9UN37; -.
OpenTargets; ENSG00000132612; -.
PharmGKB; PA38362; -.
eggNOG; KOG0739; Eukaryota.
eggNOG; ENOG410XRHN; LUCA.
GeneTree; ENSGT00550000074466; -.
HOGENOM; HOG000225146; -.
HOVERGEN; HBG057074; -.
InParanoid; Q9UN37; -.
KO; K12196; -.
OMA; RAKCMQY; -.
OrthoDB; EOG091G0Q8J; -.
PhylomeDB; Q9UN37; -.
TreeFam; TF105012; -.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
ChiTaRS; VPS4A; human.
EvolutionaryTrace; Q9UN37; -.
GeneWiki; VPS4A; -.
GenomeRNAi; 27183; -.
PRO; PR:Q9UN37; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000132612; -.
CleanEx; HS_VPS4A; -.
ExpressionAtlas; Q9UN37; baseline and differential.
Genevisible; Q9UN37; HS.
GO; GO:0005813; C:centrosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0090543; C:Flemming body; IDA:UniProtKB.
GO; GO:0005770; C:late endosome; IDA:UniProtKB.
GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
GO; GO:0005774; C:vacuolar membrane; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IMP:UniProtKB.
GO; GO:0016887; F:ATPase activity; IMP:UniProtKB.
GO; GO:0042623; F:ATPase activity, coupled; NAS:UniProtKB.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0009838; P:abscission; IMP:UniProtKB.
GO; GO:0000916; P:actomyosin contractile ring contraction; TAS:ARUK-UCL.
GO; GO:0051301; P:cell division; IDA:UniProtKB.
GO; GO:0000920; P:cell separation after cytokinesis; IMP:UniProtKB.
GO; GO:0061640; P:cytoskeleton-dependent cytokinesis; TAS:ARUK-UCL.
GO; GO:0016197; P:endosomal transport; IMP:UniProtKB.
GO; GO:0034058; P:endosomal vesicle fusion; IMP:UniProtKB.
GO; GO:1904896; P:ESCRT complex disassembly; NAS:ParkinsonsUK-UCL.
GO; GO:1904903; P:ESCRT III complex disassembly; NAS:ParkinsonsUK-UCL.
GO; GO:0032367; P:intracellular cholesterol transport; IMP:UniProtKB.
GO; GO:0061738; P:late endosomal microautophagy; ISS:ParkinsonsUK-UCL.
GO; GO:0016236; P:macroautophagy; NAS:ParkinsonsUK-UCL.
GO; GO:0044878; P:mitotic cytokinesis checkpoint; IMP:UniProtKB.
GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
GO; GO:0036258; P:multivesicular body assembly; ISS:ParkinsonsUK-UCL.
GO; GO:0032466; P:negative regulation of cytokinesis; IMP:UniProtKB.
GO; GO:0006998; P:nuclear envelope organization; TAS:ARUK-UCL.
GO; GO:0031468; P:nuclear envelope reassembly; TAS:ARUK-UCL.
GO; GO:0006997; P:nucleus organization; IMP:UniProtKB.
GO; GO:1903543; P:positive regulation of exosomal secretion; IMP:UniProtKB.
GO; GO:1903774; P:positive regulation of viral budding via host ESCRT complex; IMP:UniProtKB.
GO; GO:1903902; P:positive regulation of viral life cycle; IMP:UniProtKB.
GO; GO:1902188; P:positive regulation of viral release from host cell; IMP:UniProtKB.
GO; GO:0006622; P:protein targeting to lysosome; IMP:UniProtKB.
GO; GO:0032880; P:regulation of protein localization; IDA:UniProtKB.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IMP: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:0006900; P:vesicle budding from membrane; IMP:UniProtKB.
GO; GO:0072319; P:vesicle uncoating; IMP:UniProtKB.
GO; GO:0016192; P:vesicle-mediated transport; IDA: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;
Complete proteome; Disease mutation; Endosome; Hydrolase; Membrane;
Nucleotide-binding; Phosphoprotein; Protein transport;
Reference proteome; Transport.
CHAIN 1 437 Vacuolar protein sorting-associated
protein 4A.
/FTId=PRO_0000084765.
DOMAIN 2 80 MIT.
NP_BIND 167 174 ATP. {ECO:0000305}.
REGION 1 84 Interaction with CHMP1B.
MOD_RES 8 8 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 95 95 Phosphoserine.
{ECO:0000250|UniProtKB:Q793F9}.
MOD_RES 97 97 Phosphoserine.
{ECO:0000250|UniProtKB:Q793F9}.
VARIANT 193 193 Missing (probable disease-associated
mutation found in a patient with severe
intellecutal disabillity and
microcephaly).
{ECO:0000269|PubMed:25356899}.
/FTId=VAR_078655.
MUTAGEN 13 13 V->A,D: Diminishes interaction with IST1.
{ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479}.
MUTAGEN 13 13 V->D: Abolishes interaction with CHMP6,
no effect on interaction with CHMP1A.
{ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479}.
MUTAGEN 13 13 V->D: Greatly diminishes localization to
punctate class E compartments; when
associated with Q-173.
{ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479}.
MUTAGEN 64 64 L->A,D: Abolishes interaction with
CHMP1B; diminishes interaction with IST1.
{ECO:0000269|PubMed:16174732,
ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479,
ECO:0000269|PubMed:19129480}.
MUTAGEN 64 64 L->D: Greatly diminishes localization to
punctate class E compartments and
partially restores HIV-1 release; when
associated with Q-173.
{ECO:0000269|PubMed:16174732,
ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479,
ECO:0000269|PubMed:19129480}.
MUTAGEN 64 64 L->D: Modestly reduces interaction with
CHMP6. {ECO:0000269|PubMed:16174732,
ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18606141,
ECO:0000269|PubMed:19129479,
ECO:0000269|PubMed:19129480}.
MUTAGEN 68 68 E->D: Diminishes interaction with CHMP1B.
{ECO:0000269|PubMed:16174732}.
MUTAGEN 173 173 K->Q: Defective in ATP-binding. Causes
membrane association. Induces vacuolation
of endosomal compartments and impairs
cholesterol sorting. Inhibits HIV-1
release. Greatly diminishes localization
to punctate class E compartments and
partially restores HIV-1 release; when
associated with D-64. Greatly diminishes
localization to punctate class E
compartments; when associated with D-173.
{ECO:0000269|PubMed:10637304,
ECO:0000269|PubMed:11595185,
ECO:0000269|PubMed:17928862,
ECO:0000269|PubMed:18606141}.
MUTAGEN 201 202 WL->AA: Strongly impairs HIV-1 release.
{ECO:0000269|PubMed:16193069}.
MUTAGEN 203 203 G->A: Impairs HIV-1 release.
{ECO:0000269|PubMed:16193069}.
MUTAGEN 228 228 E->Q: Defective in ATP-hydrolysis. Causes
membrane association. Induces vacuolation
of endosomal compartments and impairs
cholesterol and protein sorting. Inhibits
HIV-1 release. Increases binding to
CHMP1. {ECO:0000269|PubMed:10637304,
ECO:0000269|PubMed:11559748,
ECO:0000269|PubMed:11563910,
ECO:0000269|PubMed:11595185,
ECO:0000269|PubMed:15075231}.
CONFLICT 79 79 K -> E (in Ref. 3; AAL75948 and 5;
AAF17203). {ECO:0000305}.
CONFLICT 185 185 N -> T (in Ref. 3; AAL75948).
{ECO:0000305}.
CONFLICT 284 284 R -> K (in Ref. 8; AAD42971).
{ECO:0000305}.
HELIX 5 21 {ECO:0000244|PDB:1YXR}.
HELIX 25 45 {ECO:0000244|PDB:1YXR}.
HELIX 50 76 {ECO:0000244|PDB:1YXR}.
SEQUENCE 437 AA; 48898 MW; C3CC556FB84F105C CRC64;
MTTSTLQKAI DLVTKATEED KAKNYEEALR LYQHAVEYFL HAIKYEAHSD KAKESIRAKC
VQYLDRAEKL KDYLRSKEKH GKKPVKENQS EGKGSDSDSE GDNPEKKKLQ EQLMGAVVME
KPNIRWNDVA GLEGAKEALK EAVILPIKFP HLFTGKRTPW RGILLFGPPG TGKSYLAKAV
ATEANNSTFF SVSSSDLMSK WLGESEKLVK NLFELARQHK PSIIFIDEVD SLCGSRNENE
SEAARRIKTE FLVQMQGVGN NNDGTLVLGA TNIPWVLDSA IRRRFEKRIY IPLPEEAARA
QMFRLHLGST PHNLTDANIH ELARKTEGYS GADISIIVRD SLMQPVRKVQ SATHFKKVCG
PSRTNPSMMI DDLLTPCSPG DPGAMEMTWM DVPGDKLLEP VVCMSDMLRS LATTRPTVNA
DDLLKVKKFS EDFGQES


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