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O75351

- VPS4B_HUMAN

UniProt

O75351 - VPS4B_HUMAN

Protein

Vacuolar protein sorting-associated protein 4B

Gene

VPS4B

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (16 Jan 2004)
      Previous versions | rss
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    Functioni

    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).3 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi174 – 1818ATPSequence Analysis

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATPase activity, coupled Source: UniProtKB
    3. ATP binding Source: UniProtKB
    4. protein binding Source: UniProtKB
    5. protein C-terminus binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: UniProtKB
    2. cell cycle Source: UniProtKB-KW
    3. cell division Source: UniProtKB-KW
    4. endosomal transport Source: UniProtKB
    5. endosome organization Source: Ensembl
    6. endosome to lysosome transport via multivesicular body sorting pathway Source: UniProtKB
    7. intracellular cholesterol transport Source: UniProtKB
    8. membrane organization Source: Reactome
    9. positive regulation of viral release from host cell Source: UniProt
    10. potassium ion transport Source: Ensembl
    11. protein transport Source: UniProtKB-KW
    12. regulation of viral process Source: UniProt
    13. response to lipid Source: UniProtKB
    14. viral life cycle Source: Reactome
    15. viral process Source: Reactome

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, Protein transport, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Names & Taxonomyi

    Protein namesi
    Recommended 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 namesi
    Name:VPS4B
    Synonyms:SKD1, VPS42
    ORF Names:MIG1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:10895. VPS4B.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB
    3. early endosome Source: UniProtKB
    4. endosome Source: MGI
    5. endosome membrane Source: UniProtKB
    6. extracellular vesicular exosome Source: UniProt
    7. late endosome Source: UniProtKB
    8. late endosome membrane Source: UniProtKB-SubCell
    9. lysosome Source: UniProtKB
    10. nucleus Source: UniProtKB
    11. vacuolar membrane Source: UniProtKB

    Keywords - Cellular componenti

    Endosome, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi15 – 151A → D: Reduces HIV-1 release 10-fold; when associated with D-66. 2 Publications
    Mutagenesisi15 – 151A → D: Reduces HIV-1 release 2-fold. 2 Publications
    Mutagenesisi66 – 661L → D: Reduces HIV-1 release 10-fold; when associated with D-15. 2 Publications
    Mutagenesisi66 – 661L → D: Reduces HIV-1 release 3-fold. 2 Publications
    Mutagenesisi208 – 2092WL → AA: Strongly impairs HIV-1 release. 1 Publication
    Mutagenesisi210 – 2101G → A: Impairs HIV-1 release. 2 Publications
    Mutagenesisi235 – 2351E → Q: Defective in vacuolar protein sorting. 2 Publications
    Mutagenesisi390 – 3967Missing: Abolishes interaction with VTA1. 1 Publication

    Organism-specific databases

    PharmGKBiPA35795.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 444444Vacuolar protein sorting-associated protein 4BPRO_0000084767Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei93 – 931Phosphoserine1 Publication
    Modified residuei102 – 1021Phosphoserine6 Publications
    Modified residuei108 – 1081Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO75351.
    PaxDbiO75351.
    PeptideAtlasiO75351.
    PRIDEiO75351.

    PTM databases

    PhosphoSiteiO75351.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiO75351.
    BgeeiO75351.
    CleanExiHS_VPS4B.
    GenevestigatoriO75351.

    Organism-specific databases

    HPAiCAB046445.

    Interactioni

    Subunit structurei

    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 VTA1.7 Publications

    Protein-protein interaction databases

    BioGridi114901. 31 interactions.
    DIPiDIP-53790N.
    IntActiO75351. 1 interaction.
    STRINGi9606.ENSP00000238497.

    Structurei

    Secondary structure

    444
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni1 – 33
    Helixi6 – 2318
    Helixi30 – 4718
    Helixi52 – 554
    Helixi56 – 7217
    Turni73 – 753
    Beta strandi87 – 893
    Beta strandi125 – 1273
    Helixi133 – 1353
    Helixi140 – 15516
    Helixi157 – 1593
    Beta strandi168 – 17811
    Helixi180 – 19011
    Beta strandi195 – 2006
    Helixi213 – 22513
    Beta strandi227 – 2348
    Turni235 – 2373
    Helixi238 – 2403
    Beta strandi243 – 2453
    Helixi250 – 26314
    Beta strandi265 – 2673
    Beta strandi272 – 2798
    Turni281 – 2833
    Helixi286 – 2905
    Beta strandi294 – 2974
    Helixi303 – 31412
    Helixi323 – 3319
    Helixi338 – 34912
    Helixi351 – 3588
    Beta strandi360 – 3689
    Beta strandi375 – 3839
    Beta strandi386 – 3883
    Beta strandi391 – 3933
    Helixi396 – 3983
    Helixi401 – 4033
    Helixi411 – 4199
    Helixi427 – 43812

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1WR0NMR-A1-77[»]
    1XWIX-ray2.80A123-444[»]
    2CPTNMR-A1-104[»]
    2JQHNMR-A1-86[»]
    2JQKNMR-A1-86[»]
    ProteinModelPortaliO75351.
    SMRiO75351. Positions 1-108, 123-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO75351.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini4 – 8279MITAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili19 – 8264Sequence AnalysisAdd
    BLAST

    Domaini

    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).1 Publication

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated
    Contains 1 MIT domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0464.
    HOGENOMiHOG000225146.
    HOVERGENiHBG057074.
    InParanoidiO75351.
    KOiK12196.
    OMAiFRLYQHA.
    OrthoDBiEOG74BJS2.
    PhylomeDBiO75351.
    TreeFamiTF105012.

    Family and domain databases

    Gene3Di1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view]
    SUPFAMiSSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O75351-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ    50
    GDKAKQSIRA KCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN 100
    DSDGEGESDD PEKKKLQNQL QGAIVIERPN VKWSDVAGLE GAKEALKEAV 150
    ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK SYLAKAVATE ANNSTFFSIS 200
    SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC GSRSENESEA 250
    ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL 300
    PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM 350
    QPVRKVQSAT HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP 400
    GDKLLEPVVS MSDMLRSLSN TKPTVNEHDL LKLKKFTEDF GQEG 444
    Length:444
    Mass (Da):49,302
    Last modified:January 16, 2004 - v2
    Checksum:i9D565E4B20AF73FB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti114 – 1141K → R in AAC39874. (PubMed:9653160)Curated
    Sequence conflicti127 – 1271E → D in AAC39874. (PubMed:9653160)Curated
    Sequence conflicti342 – 3421S → G in AAC39874. (PubMed:9653160)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti58 – 581I → M Common polymorphism; induces thermal instability. 1 Publication
    Corresponds to variant rs17688948 [ dbSNP | Ensembl ].
    VAR_023385

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11983.1.
    RefSeqiNP_004860.2. NM_004869.3.
    UniGeneiHs.126550.

    Genome annotation databases

    EnsembliENST00000238497; ENSP00000238497; ENSG00000119541.
    GeneIDi9525.
    KEGGihsa:9525.
    UCSCiuc002lix.3. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS11983.1.
    RefSeqi NP_004860.2. NM_004869.3.
    UniGenei Hs.126550.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1WR0 NMR - A 1-77 [» ]
    1XWI X-ray 2.80 A 123-444 [» ]
    2CPT NMR - A 1-104 [» ]
    2JQH NMR - A 1-86 [» ]
    2JQK NMR - A 1-86 [» ]
    ProteinModelPortali O75351.
    SMRi O75351. Positions 1-108, 123-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114901. 31 interactions.
    DIPi DIP-53790N.
    IntActi O75351. 1 interaction.
    STRINGi 9606.ENSP00000238497.

    Chemistry

    ChEMBLi CHEMBL2311229.

    PTM databases

    PhosphoSitei O75351.

    Proteomic databases

    MaxQBi O75351.
    PaxDbi O75351.
    PeptideAtlasi O75351.
    PRIDEi O75351.

    Protocols and materials databases

    DNASUi 9525.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000238497 ; ENSP00000238497 ; ENSG00000119541 .
    GeneIDi 9525.
    KEGGi hsa:9525.
    UCSCi uc002lix.3. human.

    Organism-specific databases

    CTDi 9525.
    GeneCardsi GC18M061056.
    HGNCi HGNC:10895. VPS4B.
    HPAi CAB046445.
    MIMi 609983. gene.
    neXtProti NX_O75351.
    PharmGKBi PA35795.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0464.
    HOGENOMi HOG000225146.
    HOVERGENi HBG057074.
    InParanoidi O75351.
    KOi K12196.
    OMAi FRLYQHA.
    OrthoDBi EOG74BJS2.
    PhylomeDBi O75351.
    TreeFami TF105012.

    Enzyme and pathway databases

    Reactomei REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_6359. Budding and maturation of HIV virion.

    Miscellaneous databases

    EvolutionaryTracei O75351.
    GeneWikii VPS4B.
    GenomeRNAii 9525.
    NextBioi 35700.
    PROi O75351.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O75351.
    Bgeei O75351.
    CleanExi HS_VPS4B.
    Genevestigatori O75351.

    Family and domain databases

    Gene3Di 1.20.58.280. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR007330. MIT.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 1 hit.
    PF04212. MIT. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM00745. MIT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF116846. SSF116846. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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. 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. 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. 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. 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. 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. 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. Cited for: STRUCTURE BY NMR OF 1-77, DOMAIN, VARIANT MET-58.
    24. 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. Cited for: STRUCTURE BY NMR OF 1-86 IN COMPLEX WITH CHMP2B, INTERACTION WITH CHMP1B.

    Entry informationi

    Entry nameiVPS4B_HUMAN
    AccessioniPrimary (citable) accession number: O75351
    Secondary accession number(s): Q69HW4, Q9GZS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 16, 2004
    Last modified: October 1, 2014
    This is version 141 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 18
      Human chromosome 18: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3