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Q9UN37 (VPS4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Vacuolar protein sorting-associated protein 4A

EC=3.6.4.6
Alternative name(s):
Protein SKD2
VPS4-1
Short name=hVPS4
Gene names
Name:VPS4A
Synonyms:VPS4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length437 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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 (Ref.24). Ref.1 Ref.10 Ref.15 Ref.24

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.1 Ref.11 Ref.12 Ref.13 Ref.18 Ref.19 Ref.20 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27

Subcellular location

Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein Probable. Midbody. Note: Membrane-associated in the prevacuolar endosomal compartment. Localizes to the midbody of dividing cells, interaction with ZFYVE19/ANCHR mediates retention at midbody (Ref.24). Localized in two distinct rings on either side of the Fleming body. Ref.1 Ref.9 Ref.17 Ref.24

Tissue specificity

Ubiquitously expressed. Ref.1 Ref.9

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).

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 MIT domain.

Sequence caution

The sequence AAL75948.1 differs from that shown. Reason: Frameshift at positions 123, 133, 157 and 163.

Ontologies

Keywords
   Biological processCell cycle
Cell division
Protein transport
Transport
   Cellular componentEndosome
Membrane
   LigandATP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Non-traceable author statement Ref.25. Source: GOC

cytokinesis

Inferred from direct assay Ref.17. Source: UniProtKB

endosomal transport

Inferred from mutant phenotype Ref.11. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

vesicle-mediated transport

Inferred from direct assay Ref.1. Source: UniProtKB

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay Ref.17Ref.20Ref.24. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity, coupled

Non-traceable author statement Ref.25. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.26. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.11Ref.1Ref.20Ref.19Ref.23Ref.24. Source: UniProtKB

protein domain specific binding

Inferred from physical interaction Ref.27. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.21
Chain2 – 437436Vacuolar protein sorting-associated protein 4A
PRO_0000084765

Regions

Domain2 – 8079MIT
Nucleotide binding167 – 1748ATP Potential
Region2 – 8483Interaction with CHMP1B

Amino acid modifications

Modified residue21N-acetylthreonine Ref.21
Modified residue81N6-acetyllysine Ref.21

Experimental info

Mutagenesis131V → A or D: Diminishes interaction with IST1. Ref.20 Ref.27
Mutagenesis131V → D: Abolishes interaction with CHMP6, no effect on interaction with CHMP1A. Ref.20 Ref.27
Mutagenesis131V → D: Greatly diminishes localization to punctate class E compartments; when associated with Q-173. Ref.20 Ref.27
Mutagenesis641L → A or D: Abolishes interaction with CHMP1B; diminishes interaction with IST1. Ref.19 Ref.20 Ref.25 Ref.26 Ref.27
Mutagenesis641L → D: Greatly diminishes localization to punctate class E compartments and partially restores HIV-1 release; when associated with Q-173. Ref.19 Ref.20 Ref.25 Ref.26 Ref.27
Mutagenesis641L → D: Modestly reduces interaction with CHMP6. Ref.19 Ref.20 Ref.25 Ref.26 Ref.27
Mutagenesis681E → D: Diminishes interaction with CHMP1B. Ref.25
Mutagenesis1731K → 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. Ref.9 Ref.10 Ref.26 Ref.27
Mutagenesis201 – 2022WL → AA: Strongly impairs HIV-1 release.
Mutagenesis2031G → A: Impairs HIV-1 release. Ref.16
Mutagenesis2281E → 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. Ref.1 Ref.9 Ref.10 Ref.11 Ref.15
Sequence conflict791K → E in AAL75948. Ref.3
Sequence conflict791K → E in AAF17203. Ref.5
Sequence conflict1851N → T in AAL75948. Ref.3
Sequence conflict2841R → K in AAD42971. Ref.8

Secondary structure

....... 437
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9UN37 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: C3CC556FB84F105C

FASTA43748,898
        10         20         30         40         50         60 
MTTSTLQKAI DLVTKATEED KAKNYEEALR LYQHAVEYFL HAIKYEAHSD KAKESIRAKC 

        70         80         90        100        110        120 
VQYLDRAEKL KDYLRSKEKH GKKPVKENQS EGKGSDSDSE GDNPEKKKLQ EQLMGAVVME 

       130        140        150        160        170        180 
KPNIRWNDVA GLEGAKEALK EAVILPIKFP HLFTGKRTPW RGILLFGPPG TGKSYLAKAV 

       190        200        210        220        230        240 
ATEANNSTFF SVSSSDLMSK WLGESEKLVK NLFELARQHK PSIIFIDEVD SLCGSRNENE 

       250        260        270        280        290        300 
SEAARRIKTE FLVQMQGVGN NNDGTLVLGA TNIPWVLDSA IRRRFEKRIY IPLPEEAARA 

       310        320        330        340        350        360 
QMFRLHLGST PHNLTDANIH ELARKTEGYS GADISIIVRD SLMQPVRKVQ SATHFKKVCG 

       370        380        390        400        410        420 
PSRTNPSMMI DDLLTPCSPG DPGAMEMTWM DVPGDKLLEP VVCMSDMLRS LATTRPTVNA 

       430 
DDLLKVKKFS EDFGQES 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian cells express two VPS4 proteins both of which are involved in intracellular protein trafficking."
Scheuring S., Roehricht R.A., Schoening-Burkhardt B., Beyer A., Mueller S., Abts H.F., Koehrer K.
J. Mol. Biol. 312:469-480(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH VPS4B, MUTAGENESIS OF GLU-228.
Tissue: Keratinocyte.
[2]"Comparative sequence and expression analyses of four mammalian VPS4 genes."
Beyer A., Scheuring S., Mueller S., Mincheva A., Lichter P., Koehrer K.
Gene 305:47-59(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of a new human cDNA homologous to Homo sapiens SKD1 protein."
Ding J.B., Yu L., Zhao S.Y.
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Isolation of a homolog of SKD1."
Patejunas G.
Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[5]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
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. expand/collapse author list , 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.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hypothalamus.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[9]"ATPase-defective mammalian VPS4 localizes to aberrant endosomes and impairs cholesterol trafficking."
Bishop N., Woodman P.
Mol. Biol. Cell 11:227-239(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-437, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF LYS-173 AND GLU-228.
Tissue: Brain.
[10]"Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding."
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.
Cell 107:55-65(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VIRUS RELEASE, MUTAGENESIS OF LYS-173 AND GLU-228.
[11]"CHMP1 functions as a member of a newly defined family of vesicle trafficking proteins."
Howard T.L., Stauffer D.R., Degnin C.R., Hollenberg S.M.
J. Cell Sci. 114:2395-2404(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1A, MUTAGENESIS OF GLU-228.
[12]"The protein network of HIV budding."
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.
Cell 114:701-713(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP4A; CHMP4B; CHMP4C AND CHMP6.
[13]"Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1A; CHMP1B; CHMP2A; CHMP2B AND CHMP3.
[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]"ATPase-deficient hVPS4 impairs formation of internal endosomal vesicles and stabilizes bilayered clathrin coats on endosomal vacuoles."
Sachse M., Strous G.J., Klumperman J.
J. Cell Sci. 117:1699-1708(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF GLU-228.
[16]"Structural and mechanistic studies of VPS4 proteins."
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.
EMBO J. 24:3658-3669(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF 201-TRP-LEU-202 AND GLY-203.
[17]"Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[18]"Structural basis for midbody targeting of spastin by the ESCRT-III protein CHMP1B."
Yang D., Rismanchi N., Renvoise B., Lippincott-Schwartz J., Blackstone C., Hurley J.H.
Nat. Struct. Mol. Biol. 15:1278-1286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPAST.
[19]"Essential role of hIST1 in cytokinesis."
Agromayor M., Carlton J.G., Phelan J.P., Matthews D.R., Carlin L.M., Ameer-Beg S., Bowers K., Martin-Serrano J.
Mol. Biol. Cell 20:1374-1387(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IST1, MUTAGENESIS OF LEU-64.
[20]"Biochemical analyses of human IST1 and its function in cytokinesis."
Bajorek M., Morita E., Skalicky J.J., Morham S.G., Babst M., Sundquist W.I.
Mol. Biol. Cell 20:1360-1373(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH IST1, MUTAGENESIS OF VAL-13 AND LEU-64.
[21]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 AND LYS-8, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Mechanism of inhibition of retrovirus release from cells by interferon-induced gene ISG15."
Kuang Z., Seo E.J., Leis J.
J. Virol. 85:7153-7161(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CHMP1B; CHMP2A; CHMP3; CHMP4B AND CHMP6.
[24]"ANCHR mediates Aurora-B-dependent abscission checkpoint control through retention of VPS4."
Thoresen S.B., Campsteijn C., Vietri M., Schink K.O., Liestoel K., Andersen J.S., Raiborg C., Stenmark H.
Nat. Cell Biol. 0:0-0(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZFYVE19.
[25]"Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A."
Scott A., Gaspar J., Stuchell-Brereton M.D., Alam S.L., Skalicky J.J., Sundquist W.I.
Proc. Natl. Acad. Sci. U.S.A. 102:13813-13818(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-77, INTERACTION WITH CHMP1B, MUTAGENESIS OF LEU-64 AND GLU-68.
[26]"ESCRT-III recognition by VPS4 ATPases."
Stuchell-Brereton M.D., Skalicky J.J., Kieffer C., Karren M.A., Ghaffarian S., Sundquist W.I.
Nature 449:740-744(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP1A, INTERACTION WITH CHMP2B, MUTAGENESIS OF LEU-64 AND LYS-173.
[27]"Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding."
Kieffer C., Skalicky J.J., Morita E., De Domenico I., Ward D.M., Kaplan J., Sundquist W.I.
Dev. Cell 15:62-73(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-84 IN COMPLEX WITH CHMP6, INTERACTION WITH CHMP1A, MUTAGENESIS OF VAL-13; LEU-64 AND LYS-173.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF255952 mRNA. Translation: AAK52408.1.
AF282903 Genomic DNA. Translation: AAG01470.1.
AF132747 mRNA. Translation: AAL75948.1. Frameshift.
AF159063 mRNA. Translation: AAD49227.1.
AF112215 mRNA. Translation: AAF17203.1.
AK315026 mRNA. Translation: BAG37514.1.
CH471092 Genomic DNA. Translation: EAW83263.1.
BC047932 mRNA. Translation: AAH47932.1.
AF155740 mRNA. Translation: AAD42971.1.
CCDSCCDS45517.1.
RefSeqNP_037377.1. NM_013245.2.
UniGeneHs.128420.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YXRNMR-A1-77[»]
2JQ9NMR-A1-84[»]
2K3WNMR-A1-84[»]
ProteinModelPortalQ9UN37.
SMRQ9UN37. Positions 1-101, 116-436.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118059. 18 interactions.
DIPDIP-44585N.
IntActQ9UN37. 5 interactions.
STRING9606.ENSP00000254950.

PTM databases

PhosphoSiteQ9UN37.

Polymorphism databases

DMDM62511240.

Proteomic databases

MaxQBQ9UN37.
PaxDbQ9UN37.
PRIDEQ9UN37.

Protocols and materials databases

DNASU27183.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254950; ENSP00000254950; ENSG00000132612.
GeneID27183.
KEGGhsa:27183.
UCSCuc002eww.3. human.

Organism-specific databases

CTD27183.
GeneCardsGC16P069335.
HGNCHGNC:13488. VPS4A.
HPACAB018751.
MIM609982. gene.
neXtProtNX_Q9UN37.
PharmGKBPA38362.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000225146.
HOVERGENHBG057074.
InParanoidQ9UN37.
KOK12196.
OMAARTQMFR.
OrthoDBEOG74BJS2.
PhylomeDBQ9UN37.
TreeFamTF105012.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpressQ9UN37.
BgeeQ9UN37.
CleanExHS_VPS4A.
GenevestigatorQ9UN37.

Family and domain databases

Gene3D1.20.58.280. 1 hit.
3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR007330. MIT.
IPR027417. P-loop_NTPase.
IPR015415. Vps4_C.
[Graphical view]
PfamPF00004. AAA. 1 hit.
PF04212. MIT. 1 hit.
PF09336. Vps4_C. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM00745. MIT. 1 hit.
[Graphical view]
SUPFAMSSF116846. SSF116846. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSVPS4A. human.
EvolutionaryTraceQ9UN37.
GeneWikiVPS4A.
GenomeRNAi27183.
NextBio50017.
PROQ9UN37.
SOURCESearch...

Entry information

Entry nameVPS4A_HUMAN
AccessionPrimary (citable) accession number: Q9UN37
Secondary accession number(s): B2RCB7 expand/collapse secondary AC list , Q8TF07, Q9UI03, Q9Y582
Entry history
Integrated into UniProtKB/Swiss-Prot: April 12, 2005
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM