Charged multivesicular body 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

Miscellaneous

<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

• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKB <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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.18

    "Plasma membrane deformation by circular arrays of ESCRT-III protein filaments."
    Hanson P.I., Roth R., Lin Y., Heuser J.E.
    J. Cell Biol. 180:389-402(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SELF-ASSOCIATION, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
• protein homodimerization activity 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ
  • Ref.10

    "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: FUNCTION (MICROBIAL INFECTION), SELF-ASSOCIATION, INTERACTION WITH CHMP2A; CHMP4A; CHMP4C; CHMP6; PDCD6IP AND VPS4A.

GO - Biological processⁱ

• autophagy Source: ParkinsonsUK-UCL <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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Syntaxin 13, a genetic modifier of mutant CHMP2B in frontotemporal dementia, is required for autophagosome maturation."
    Lu Y., Zhang Z., Sun D., Sweeney S.T., Gao F.B.
    Mol. Cell 52:264-271(2013) [PubMed] [Europe PMC] [Abstract]
• endosomal transport Source: Reactome
• exit from mitosis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.30

    "Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
    Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
    Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• macroautophagy Source: ParkinsonsUK-UCL <p>Traceable Author Statement</p> <p>Used for information from review articles where the original experiments are traceable through that article and also for information from text books or dictionaries.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#tas">GO evidence code guide</a></p> 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]
• maintenance of lens transparency Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.32

    "CHMP4B, a novel gene for autosomal dominant cataracts linked to chromosome 20q."
    Shiels A., Bennett T.M., Knopf H.L.S., Yamada K., Yoshiura K., Niikawa N., Shim S., Hanson P.I.
    Am. J. Hum. Genet. 81:596-606(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: VARIANTS CTRCT31 VAL-129 AND LYS-161.
• membrane fission Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.25

    "Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments."
    Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H., Mueller-Reichert T., Gerlich D.W.
    Science 331:1616-1620(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• 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 cytokinesis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.25

    "Cortical constriction during abscission involves helices of ESCRT-III-dependent filaments."
    Guizetti J., Schermelleh L., Maentler J., Maar S., Poser I., Leonhardt H., Mueller-Reichert T., Gerlich D.W.
    Science 331:1616-1620(2011) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• 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-UCLTraceable 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 autophagosome assembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • "ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons."
    Lee J.A., Liu L., Javier R., Kreitzer A.C., Delaloy C., Gao F.B.
    Mol Brain 4:37-37(2011) [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 neuron death Source: UniProtKBInferred from mutant phenotypeⁱ
  • "ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons."
    Lee J.A., Liu L., Javier R., Kreitzer A.C., Delaloy C., Gao F.B.
    Mol Brain 4:37-37(2011) [PubMed] [Europe PMC] [Abstract]
• nuclear envelope reassembly Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.30

    "Spastin and ESCRT-III coordinate mitotic spindle disassembly and nuclear envelope sealing."
    Vietri M., Schink K.O., Campsteijn C., Wegner C.S., Schultz S.W., Christ L., Thoresen S.B., Brech A., Raiborg C., Stenmark H.
    Nature 522:231-235(2015) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SUBCELLULAR LOCATION.
• 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 viral release from host cell Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.9

    "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 (MICROBIAL INFECTION), INTERACTION WITH CHMP6; CHMP4C; PDCD6IP; VPS4A AND VPS4B.
• posttranslational protein targeting to endoplasmic reticulum membrane Source: UniProtKBInferred from mutant phenotypeⁱ
  • "ESCRT-III subunits Snf7-1 and Snf7-2 differentially regulate transmembrane cargos in hESC-derived human neurons."
    Lee J.A., Liu L., Javier R., Kreitzer A.C., Delaloy C., Gao F.B.
    Mol Brain 4:37-37(2011) [PubMed] [Europe PMC] [Abstract]
• protein homooligomerization Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "Plasma membrane deformation by circular arrays of ESCRT-III protein filaments."
    Hanson P.I., Roth R., Lin Y., Heuser J.E.
    J. Cell Biol. 180:389-402(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SELF-ASSOCIATION, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
• 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.9

    "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 (MICROBIAL INFECTION), INTERACTION WITH CHMP6; CHMP4C; PDCD6IP; VPS4A AND VPS4B.
• 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]
• vacuolar transport Source: InterPro
• viral budding Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.32

    "CHMP4B, a novel gene for autosomal dominant cataracts linked to chromosome 20q."
    Shiels A., Bennett T.M., Knopf H.L.S., Yamada K., Yoshiura K., Niikawa N., Shim S., Hanson P.I.
    Am. J. Hum. Genet. 81:596-606(2007) [PubMed] [Europe PMC] [Abstract]

    Cited for: VARIANTS CTRCT31 VAL-129 AND LYS-161.
• viral budding via host ESCRT complex Source: UniProtKBInferred from direct assayⁱ
  • "Structure of cellular ESCRT-III spirals and their relationship to HIV budding."
    Cashikar A.G., Shim S., Roth R., Maldazys M.R., Heuser J.E., Hanson P.I.
    Elife 3:0-0(2014) [PubMed] [Europe PMC] [Abstract]
• viral life cycle Source: Reactome

<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

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseaseⁱ

Keywords - Diseaseⁱ

Organism-specific 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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

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_section">'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_section">'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_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

GO - Molecular functionⁱ

• cadherin binding Source: BHF-UCLInferred from high throughput direct assayⁱ
  • "E-cadherin interactome complexity and robustness resolved by quantitative proteomics."
    Guo Z., Neilson L.J., Zhong H., Murray P.S., Zanivan S., Zaidel-Bar R.
    Sci Signal 7:rs7-rs7(2014) [PubMed] [Europe PMC] [Abstract]
• identical protein binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.18

    "Plasma membrane deformation by circular arrays of ESCRT-III protein filaments."
    Hanson P.I., Roth R., Lin Y., Heuser J.E.
    J. Cell Biol. 180:389-402(2008) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, SELF-ASSOCIATION, STRUCTURE BY ELECTRON CRYOMICROSCOPY.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • Ref.10

    "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: FUNCTION (MICROBIAL INFECTION), SELF-ASSOCIATION, INTERACTION WITH CHMP2A; CHMP4A; CHMP4C; CHMP6; PDCD6IP AND VPS4A.

Protein-protein interaction 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

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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MSVFGKLFGA GGGKAGKGGP TPQEAIQRLR DTEEMLSKKQ EFLEKKIEQE 
        60         70         80         90        100
LTAAKKHGTK NKRAALQALK RKKRYEKQLA QIDGTLSTIE FQREALENAN 
       110        120        130        140        150
TNTEVLKNMG YAAKAMKAAH DNMDIDKVDE LMQDIADQQE LAEEISTAIS 
       160        170        180        190        200
KPVGFGEEFD EDELMAELEE LEQEELDKNL LEISGPETVP LPNVPSIALP 
       210        220 
SKPAKKKEEE DDDMKELENW AGSM                             

Natural variant

Sequence databases

Genome annotation databases

<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

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. Human chromosome 20
   Human chromosome 20: entries, gene names and cross-references to MIM
2. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
3. SIMILARITY comments
   Index of protein domains and families
4. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
5. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
6. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot