Vacuolar protein sorting-associated protein 4B

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityⁱ

• ATP

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  • See the description of this molecule in ChEBI.

  + H₂O

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  = ADP

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  + H⁺

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  + phosphate

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  EC:3.6.4.6
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  • See the description of this EC number in ENZYME.
  Source: Rhea

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  ATP

  • Search proteins in UniProtKB for this molecule.
  • Search chemical reactions in Rhea for this molecule.
  • See the description of this molecule in ChEBI.

  

  +

  H₂O

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  • See the description of this molecule in ChEBI.

  

  =

  ADP

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  +

  H⁺

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  • See the description of this molecule in ChEBI.

  

  +

  phosphate

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Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATPase activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.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.
• ATPase activity, coupled Source: UniProtKBInferred from direct assayⁱ
  • Ref.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.
• ATP binding Source: UniProtKB-KW
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.27

    "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.
• protein-containing complex binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.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.
• protein C-terminus binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.29

    "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.
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.27

    "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.

GO - Biological processⁱ

• cholesterol transport Source: Ensembl
• endosomal transport Source: MGIInferred from direct assayⁱ
  • Ref.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.
• endosome to lysosome transport via multivesicular body sorting pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Role of mammalian vacuolar protein-sorting proteins in endocytic trafficking of a non-ubiquitinated G protein-coupled receptor to lysosomes."
    Hislop J.N., Marley A., Von Zastrow M.
    J. Biol. Chem. 279:22522-22531(2004) [PubMed] [Europe PMC] [Abstract]
• ESCRT III complex disassembly Source: UniProtKBInferred from direct assayⁱ
  • Ref.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.
• late endosomal microautophagy Source: Ensembl
• macroautophagy Source: ParkinsonsUK-UCL <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#nas">GO evidence code guide</a></p> Non-traceable author statementⁱ
  • "Membrane budding and scission by the ESCRT machinery: it's all in the neck."
    Hurley J.H., Hanson P.I.
    Nat. Rev. Mol. Cell Biol. 11:556-566(2010) [PubMed] [Europe PMC] [Abstract]
• midbody abscission Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• mitotic metaphase plate congression Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• multivesicular body assembly Source: ParkinsonsUK-UCLNon-traceable author statementⁱ
  • "Membrane budding and scission by the ESCRT machinery: it's all in the neck."
    Hurley J.H., Hanson P.I.
    Nat. Rev. Mol. Cell Biol. 11:556-566(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of cell death Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of exosomal secretion Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Analysis of ESCRT functions in exosome biogenesis, composition and secretion highlights the heterogeneity of extracellular vesicles."
    Colombo M., Moita C., van Niel G., Kowal J., Vigneron J., Benaroch P., Manel N., Moita L.F., Thery C., Raposo G.
    J. Cell. Sci. 126:5553-5565(2013) [PubMed] [Europe PMC] [Abstract]
• nucleus organization Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of centriole elongation Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of exosomal secretion Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.23

    "Syndecan-syntenin-ALIX regulates the biogenesis of exosomes."
    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.
    Nat. Cell Biol. 14:677-685(2012) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION.
• positive regulation of G2/M transition of mitotic cell cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of viral life cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.27

    "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.
• positive regulation of viral process Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Involvement of vacuolar protein sorting pathway in Ebola virus release independent of TSG101 interaction."
    Silvestri L.S., Ruthel G., Kallstrom G., Warfield K.L., Swenson D.L., Nelle T., Iversen P.L., Bavari S., Aman M.J.
    J. Infect. Dis. 196 Suppl 2:S264-70(2007) [PubMed] [Europe PMC] [Abstract]
• positive regulation of viral release from host cell Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.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.
• potassium ion transport Source: Ensembl
• protein depolymerization Source: UniProtKBInferred from direct assayⁱ
  • Ref.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.
• protein transport Source: UniProtKB-KW
• regulation of centrosome duplication Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of mitotic spindle assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • "Human ESCRT-III and VPS4 proteins are required for centrosome and spindle maintenance."
    Morita E., Colf L.A., Karren M.A., Sandrin V., Rodesch C.K., Sundquist W.I.
    Proc. Natl. Acad. Sci. U.S.A. 107:12889-12894(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of viral process Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.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.
• response to lipid Source: UniProtKBInferred from direct assayⁱ
  • "Cholesterol depletion facilitates ubiquitylation of NPC1 and its association with SKD1/Vps4."
    Ohsaki Y., Sugimoto Y., Suzuki M., Hosokawa H., Yoshimori T., Davies J.P., Ioannou Y.A., Vanier M.T., Ohno K., Ninomiya H.
    J. Cell. Sci. 119:2643-2653(2006) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "ALIX binds a YPX(3)L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting."
    Dores M.R., Chen B., Lin H., Soh U.J., Paing M.M., Montagne W.A., Meerloo T., Trejo J.
    J. Cell Biol. 197:407-419(2012) [PubMed] [Europe PMC] [Abstract]
• ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKBInferred from mutant phenotypeⁱ
  • "ALIX binds a YPX(3)L motif of the GPCR PAR1 and mediates ubiquitin-independent ESCRT-III/MVB sorting."
    Dores M.R., Chen B., Lin H., Soh U.J., Paing M.M., Montagne W.A., Meerloo T., Trejo J.
    J. Cell Biol. 197:407-419(2012) [PubMed] [Europe PMC] [Abstract]
• vacuole organization Source: GO_Central <p>Inferred from Biological aspect of Ancestor</p> <p>A type of phylogenetic evidence whereby an aspect of a descendent is inferred through the characterization of an aspect of a ancestral gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#iba">GO evidence code guide</a></p> Inferred from biological aspect of ancestorⁱ
  • "Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium."
    Gaudet P., Livstone M.S., Lewis S.E., Thomas P.D.
    Brief. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• viral budding via host ESCRT complex Source: UniProtKB <p>Inferred from Genetic Interaction</p> <p>Used to describe "traditional" genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ
  • "ESCRT requirements for EIAV budding."
    Sandrin V., Sundquist W.I.
    Retrovirology 10:104-104(2013) [PubMed] [Europe PMC] [Abstract]
• viral life cycle Source: Reactome
• viral release from host cell Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.27

    "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.

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsⁱ

Enzyme and pathway databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

Keywords - Cellular componentⁱ

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Mutagenesis

Organism-specific databases

Miscellaneous databases

Chemistry databases

Polymorphism and mutation databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Amino acid modifications

Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressionⁱ

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityⁱ

Gene expression databases

Organism-specific databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.27

    "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.
• protein C-terminus binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.29

    "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.
• protein homodimerization activity Source: UniProtKBInferred from direct assayⁱ
  • Ref.27

    "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.

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Domains and Repeats

Coiled coil

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domainⁱ

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Keywords - Domainⁱ

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)ⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MSSTSPNLQK AIDLASKAAQ EDKAGNYEEA LQLYQHAVQY FLHVVKYEAQ 
        60         70         80         90        100
GDKAKQSIRA KCTEYLDRAE KLKEYLKNKE KKAQKPVKEG QPSPADEKGN 
       110        120        130        140        150
DSDGEGESDD PEKKKLQNQL QGAIVIERPN VKWSDVAGLE GAKEALKEAV 
       160        170        180        190        200
ILPIKFPHLF TGKRTPWRGI LLFGPPGTGK SYLAKAVATE ANNSTFFSIS 
       210        220        230        240        250
SSDLVSKWLG ESEKLVKNLF QLARENKPSI IFIDEIDSLC GSRSENESEA 
       260        270        280        290        300
ARRIKTEFLV QMQGVGVDND GILVLGATNI PWVLDSAIRR RFEKRIYIPL 
       310        320        330        340        350
PEPHARAAMF KLHLGTTQNS LTEADFRELG RKTDGYSGAD ISIIVRDALM 
       360        370        380        390        400
QPVRKVQSAT HFKKVRGPSR ADPNHLVDDL LTPCSPGDPG AIEMTWMDVP 
       410        420        430        440 
GDKLLEPVVS MSDMLRSLSN TKPTVNEHDL LKLKKFTEDF GQEG       

Experimental Info

Natural variant

Sequence databases

Genome annotation databases

Keywords - Coding sequence diversityⁱ

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ

• 100% Identity
• 90% Identity
• 50% Identity

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

Keywords - Technical termⁱ

Documents

1. SIMILARITY comments
   Index of protein domains and families
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. Human chromosome 18
   Human chromosome 18: entries, gene names and cross-references to MIM
6. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references