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O75351 (VPS4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 136. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 4B

EC=3.6.4.6
Alternative name(s):
Cell migration-inducing gene 1 protein
Suppressor of K(+) transport growth defect 1
Short name=Protein SKD1
Gene names
Name:VPS4B
Synonyms:SKD1, VPS42
ORF Names:MIG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
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). Ref.1 Ref.8 Ref.16

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. 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. Ref.1 Ref.7 Ref.8 Ref.13 Ref.18 Ref.24 Ref.26

Subcellular location

Prevacuolar compartment membrane; Peripheral membrane protein. Late endosome membrane; Peripheral membrane protein Probable. Note: Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells. Ref.1 Ref.8

Tissue specificity

Ubiquitously expressed. Ref.1

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). Ref.23

Sequence similarities

Belongs to the AAA ATPase family.

Contains 1 MIT domain.

Ontologies

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

Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB

cell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

endosomal transport

Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB

endosome organization

Inferred from electronic annotation. Source: Ensembl

endosome to lysosome transport via multivesicular body sorting pathway

Inferred from mutant phenotype PubMed 15024011. Source: UniProtKB

intracellular cholesterol transport

Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

potassium ion transport

Inferred from electronic annotation. Source: Ensembl

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

response to lipid

Inferred from direct assay PubMed 16757520. Source: UniProtKB

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 16757520. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 10637304. Source: UniProtKB

early endosome

Inferred from direct assay PubMed 10637304. Source: UniProtKB

endosome

Inferred from direct assay Ref.1. Source: MGI

endosome membrane

Inferred from direct assay PubMed 16757520. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

late endosome

Inferred from direct assay PubMed 10637304. Source: UniProtKB

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosome

Inferred from direct assay PubMed 10637304. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 16757520. Source: UniProtKB

vacuolar membrane

Inferred from direct assay PubMed 10637304. Source: UniProtKB

   Molecular_functionATP binding

Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB

ATPase activity

Inferred from mutant phenotype PubMed 10637304. Source: UniProtKB

ATPase activity, coupled

Non-traceable author statement PubMed 16174732. Source: UniProtKB

protein C-terminus binding

Inferred from physical interaction Ref.26. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Vacuolar protein sorting-associated protein 4B
PRO_0000084767

Regions

Domain4 – 8279MIT
Nucleotide binding174 – 1818ATP Potential
Coiled coil19 – 8264 Potential

Amino acid modifications

Modified residue931Phosphoserine Ref.20
Modified residue1021Phosphoserine Ref.9 Ref.12 Ref.14 Ref.15 Ref.20 Ref.22
Modified residue1081Phosphoserine Ref.20

Natural variations

Natural variant581I → M Common polymorphism; induces thermal instability. Ref.23
Corresponds to variant rs17688948 [ dbSNP | Ensembl ].
VAR_023385

Experimental info

Mutagenesis151A → D: Reduces HIV-1 release 10-fold; when associated with D-66. Ref.11
Mutagenesis151A → D: Reduces HIV-1 release 2-fold. Ref.11
Mutagenesis661L → D: Reduces HIV-1 release 10-fold; when associated with D-15. Ref.11
Mutagenesis661L → D: Reduces HIV-1 release 3-fold. Ref.11
Mutagenesis208 – 2092WL → AA: Strongly impairs HIV-1 release.
Mutagenesis2101G → A: Impairs HIV-1 release. Ref.24
Mutagenesis2351E → Q: Defective in vacuolar protein sorting. Ref.1
Mutagenesis390 – 3967Missing: Abolishes interaction with VTA1. Ref.13
Sequence conflict1141K → R in AAC39874. Ref.3
Sequence conflict1271E → D in AAC39874. Ref.3
Sequence conflict3421S → G in AAC39874. Ref.3

Secondary structure

...................................................................... 444
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75351 [UniParc].

Last modified January 16, 2004. Version 2.
Checksum: 9D565E4B20AF73FB

FASTA44449,302
        10         20         30         40         50         60 
MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ GDKAKQSIRA 

        70         80         90        100        110        120 
KCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN DSDGEGESDD PEKKKLQNQL 

       130        140        150        160        170        180 
QGAIVIERPN VKWSDVAGLE GAKEALKEAV ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK 

       190        200        210        220        230        240 
SYLAKAVATE ANNSTFFSIS SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC 

       250        260        270        280        290        300 
GSRSENESEA ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL 

       310        320        330        340        350        360 
PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM QPVRKVQSAT 

       370        380        390        400        410        420 
HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP GDKLLEPVVS MSDMLRSLSN 

       430        440 
TKPTVNEHDL LKLKKFTEDF GQEG 

« 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, INTERACTION WITH VPS4A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-235.
[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].
Tissue: Skin.
[3]"Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
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.
Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Umbilical cord blood.
[4]"Identification of a human cell migration gene 1."
Kim J.W.
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]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].
[6]"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].
Tissue: Testis.
[7]"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 CHMP2A.
[8]"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: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP1A; CHMP1B CHMP2A; CHMP4B AND CHMP6, SUBCELLULAR LOCATION.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
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.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[11]"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: MUTAGENESIS OF ALA-15 AND LEU-66.
[12]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[13]"Novel interactions of ESCRT-III with LIP5 and VPS4 and their implications for ESCRT-III disassembly."
Shim S., Merrill S.A., Hanson P.I.
Mol. Biol. Cell 19:2661-2672(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH VTA1, MUTAGENESIS OF 390-GLY--TRP-396.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography."
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.
Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[16]"Helical structures of ESCRT-III are disassembled by VPS4."
Lata S., Schoehn G., Jain A., Pires R., Piehler J., Goettlinger H.G., Weissenhorn W.
Science 321:1354-1357(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH THE CHMP2A-CHMP3 POLYMER, ELECTRON MICROSCOPY.
[17]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
[19]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102 AND SER-108, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[21]"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].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Structural characterization of the MIT domain from human Vps4b."
Takasu H., Jee J.G., Ohno A., Goda N., Fujiwara K., Tochio H., Shirakawa M., Hiroaki H.
Biochem. Biophys. Res. Commun. 334:460-465(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-77, DOMAIN, VARIANT MET-58.
[24]"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: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 123-444, SUBUNIT, INTERACTION WITH VTA1, MUTAGENESIS OF 208-TRP-LEU-209 AND GLY-210.
[25]"Solution structure of MIT domain from human SKD1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-108.
[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 1-86 IN COMPLEX WITH CHMP2B, INTERACTION WITH CHMP1B.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF195514 mRNA. Translation: AAG33022.1.
AF282904 Genomic DNA. Translation: AAG01471.1.
AF038960 mRNA. Translation: AAC39874.1.
AY232629 mRNA. Translation: AAP59551.1.
CH471096 Genomic DNA. Translation: EAW63143.1.
BC039574 mRNA. Translation: AAH39574.1.
RefSeqNP_004860.2. NM_004869.3.
UniGeneHs.126550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WR0NMR-A1-77[»]
1XWIX-ray2.80A123-444[»]
2CPTNMR-A1-104[»]
2JQHNMR-A1-86[»]
2JQKNMR-A1-86[»]
ProteinModelPortalO75351.
SMRO75351. Positions 1-108, 123-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114901. 31 interactions.
DIPDIP-53790N.
IntActO75351. 1 interaction.
STRING9606.ENSP00000238497.

Chemistry

ChEMBLCHEMBL2311229.

PTM databases

PhosphoSiteO75351.

Proteomic databases

PaxDbO75351.
PeptideAtlasO75351.
PRIDEO75351.

Protocols and materials databases

DNASU9525.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000238497; ENSP00000238497; ENSG00000119541.
GeneID9525.
KEGGhsa:9525.
UCSCuc002lix.3. human.

Organism-specific databases

CTD9525.
GeneCardsGC18M061056.
HGNCHGNC:10895. VPS4B.
HPACAB046445.
MIM609983. gene.
neXtProtNX_O75351.
PharmGKBPA35795.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0464.
HOGENOMHOG000225146.
HOVERGENHBG057074.
InParanoidO75351.
KOK12196.
OMARADPNKI.
OrthoDBEOG74BJS2.
PhylomeDBO75351.
TreeFamTF105012.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.
REACT_116125. Disease.

Gene expression databases

ArrayExpressO75351.
BgeeO75351.
CleanExHS_VPS4B.
GenevestigatorO75351.

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

EvolutionaryTraceO75351.
GeneWikiVPS4B.
GenomeRNAi9525.
NextBio35700.
PROO75351.
SOURCESearch...

Entry information

Entry nameVPS4B_HUMAN
AccessionPrimary (citable) accession number: O75351
Secondary accession number(s): Q69HW4, Q9GZS7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 16, 2004
Last modified: April 16, 2014
This is version 136 of the entry and version 2 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM