Charged multivesicular body protein 1a

<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

Caution

<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

• identical protein binding Source: IntAct <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
  • "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
    Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
    Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• metallopeptidase activity Source: ProtInc <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%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • Ref.1

    "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)."
    Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R., Callen D.F., Prockop D.J., Peltonen L., Kadler K.E.
    Gene 174:135-143(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, TISSUE SPECIFICITY.
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.18

    "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 180-196 IN COMPLEX WITH VPS4A.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • 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: INTERACTION WITH CHMP1B; VPS4A AND VPS4B.
  • Ref.9

    "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: SELF-ASSOCIATION, INTERACTION WITH CHMP1B AND VPS4A.
• zinc ion binding Source: ProtIncTraceable author statementⁱ
  • Ref.1

    "Molecular cloning, expression and chromosomal localization of a human gene encoding a 33 kDa putative metallopeptidase (PRSM1)."
    Scott I.C., Halila R., Jenkins J.M., Mehan S., Apostolou S., Winqvist R., Callen D.F., Prockop D.J., Peltonen L., Kadler K.E.
    Gene 174:135-143(1996) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PRELIMINARY FUNCTION, TISSUE SPECIFICITY.

GO - Biological processⁱ

• cell division 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
  • Ref.13

    "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: FUNCTION, INTERACTION WITH IST1, MUTAGENESIS OF LEU-191 AND LEU-194.
• endosome transport via multivesicular body sorting pathway 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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• ESCRT III complex disassembly 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]
• gene silencing 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%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ
  • Ref.2

    "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
    Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
    J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
• late endosome to vacuole transport Source: GO_CentralInferred 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 Bioinform 12:449-462(2011) [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 chromosome condensation Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
    Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
    J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
• 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 cycle Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.2

    "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
    Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
    J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
• negative regulation of transcription, DNA-templated Source: UniProtKBInferred from direct assayⁱ
  • Ref.2

    "CHMP1 is a novel nuclear matrix protein affecting chromatin structure and cell-cycle progression."
    Stauffer D.R., Howard T.L., Nyun T., Hollenberg S.M.
    J. Cell Sci. 114:2383-2393(2001) [PubMed] [Europe PMC] [Abstract]

    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
• 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]
• protein transport Source: GO_CentralInferred 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 Bioinform 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• 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]
• vesicle-mediated transport Source: UniProtKBInferred from direct assayⁱ
  • Ref.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: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH VPS4A.
• viral budding via host ESCRT complex 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]
• viral process 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

Protein family/group 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

• UniProt annotation
• GO - Cellular component

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

Mutagenesis

Keywords - Diseaseⁱ

Organism-specific databases

Miscellaneous databases

Genetic variation 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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductionⁱ

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">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: IntActInferred from physical interactionⁱ
  • "A systematic analysis of human CHMP protein interactions: additional MIT domain-containing proteins bind to multiple components of the human ESCRT III complex."
    Tsang H.T.H., Connell J.W., Brown S.E., Thompson A., Reid E., Sanderson C.M.
    Genomics 88:333-346(2006) [PubMed] [Europe PMC] [Abstract]
  • "A reference map of the human binary protein interactome."
    Luck K., Kim D.K., Lambourne L., Spirohn K., Begg B.E., Bian W., Brignall R., Cafarelli T., Campos-Laborie F.J., Charloteaux B., Choi D., Cote A.G., Daley M., Deimling S., Desbuleux A., Dricot A., Gebbia M., Hardy M.F.

    , Kishore N., Knapp J.J., Kovacs I.A., Lemmens I., Mee M.W., Mellor J.C., Pollis C., Pons C., Richardson A.D., Schlabach S., Teeking B., Yadav A., Babor M., Balcha D., Basha O., Bowman-Colin C., Chin S.F., Choi S.G., Colabella C., Coppin G., D'Amata C., De Ridder D., De Rouck S., Duran-Frigola M., Ennajdaoui H., Goebels F., Goehring L., Gopal A., Haddad G., Hatchi E., Helmy M., Jacob Y., Kassa Y., Landini S., Li R., van Lieshout N., MacWilliams A., Markey D., Paulson J.N., Rangarajan S., Rasla J., Rayhan A., Rolland T., San-Miguel A., Shen Y., Sheykhkarimli D., Sheynkman G.M., Simonovsky E., Tasan M., Tejeda A., Tropepe V., Twizere J.C., Wang Y., Weatheritt R.J., Weile J., Xia Y., Yang X., Yeger-Lotem E., Zhong Q., Aloy P., Bader G.D., De Las Rivas J., Gaudet S., Hao T., Rak J., Tavernier J., Hill D.E., Vidal M., Roth F.P., Calderwood M.A.
    Nature 580:402-408(2020) [PubMed] [Europe PMC] [Abstract]
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • Ref.18

    "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 180-196 IN COMPLEX WITH VPS4A.
• protein homodimerization activity Source: UniProtKBInferred from physical interactionⁱ
  • 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: INTERACTION WITH CHMP1B; VPS4A AND VPS4B.
  • Ref.9

    "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: SELF-ASSOCIATION, INTERACTION WITH CHMP1B AND VPS4A.

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

Coiled coil

Motif

<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>Sequences (2+)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 2 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

        10         20         30         40         50
MDDTLFQLKF TAKQLEKLAK KAEKDSKAEQ AKVKKALLQK NVECARVYAE 
        60         70         80         90        100
NAIRKKNEGV NWLRMASRVD AVASKVQTAV TMKGVTKNMA QVTKALDKAL 
       110        120        130        140        150
STMDLQKVSS VMDRFEQQVQ NLDVHTSVME DSMSSATTLT TPQEQVDSLI 
       160        170        180        190 
MQIAEENGLE VLDQLSQLPE GASAVGESSV RSQEDQLSRR LAALRN     

        10         20         30         40         50
MEDSMSSATT LTTPQEQVDS LIMQIAEENG LEVLDQLSQL PEGASAVGES 
        60 
SVRSQEDQLS RRLAALRN                                    

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Alternative sequence

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

Protein family/group databases

PTM databases

Genetic variation 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 16
   Human chromosome 16: entries, gene names and cross-references to MIM
2. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
3. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
4. SIMILARITY comments
   Index of protein domains and families