Calmodulin-3

<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

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

• adenylate cyclase activator activity 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
  • "Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
    Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
    Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
• adenylate cyclase binding Source: CAFA <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
  • "Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
    Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
    Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
• calcium-dependent protein binding Source: Ensembl
• calcium ion binding Source: UniProtKBInferred from direct assayⁱ
  • Ref.37

    "Novel CPVT-Associated Calmodulin Mutation in CALM3 (CALM3-A103V) Activates Arrhythmogenic Ca Waves and Sparks."
    Gomez-Hurtado N., Boczek N.J., Kryshtal D.O., Johnson C.N., Sun J., Nitu F.R., Cornea R.L., Chazin W.J., Calvert M.L., Tester D.J., Ackerman M.J., Knollmann B.C.
    Circ. Arrhythm. Electrophysiol. 9:0-0(2016) [PubMed] [Europe PMC] [Abstract]

    Cited for: VARIANT CPVT VAL-103, CHARACTERIZATION OF VARIANT CPVT VAL-103, INTERACTION WITH RYR2.
• disordered domain specific binding Source: CAFAInferred from physical interactionⁱ
  • "Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule."
    Majava V., Wang C., Myllykoski M., Kangas S.M., Kang S.U., Hayashi N., Baumgartel P., Heape A.M., Lubec G., Kursula P.
    Amino Acids 39:59-71(2010) [PubMed] [Europe PMC] [Abstract]
• enzyme regulator activity 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]
• ion channel binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5."
    Chagot B., Chazin W.J.
    J. Mol. Biol. 406:106-119(2011) [PubMed] [Europe PMC] [Abstract]
  • "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
    Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
    Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
• nitric-oxide synthase binding Source: Ensembl
• nitric-oxide synthase regulator activity Source: Ensembl
• N-terminal myristoylation domain binding Source: UniProtKBInferred from physical interactionⁱ
  • "Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo."
    Matsubara M., Jing T., Kawamura K., Shimojo N., Titani K., Hashimoto K., Hayashi N.
    Protein Sci. 14:494-503(2005) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol 3-kinase binding Source: Ensembl
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • "The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins."
    Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y., Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S., Kingsmore S.F.
    Mol. Med. 8:56-64(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• protein phosphatase activator activity Source: BHF-UCLInferred from direct assayⁱ
  • "Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds."
    Tan R.Y., Mabuchi Y., Grabarek Z.
    J. Biol. Chem. 271:7479-7483(1996) [PubMed] [Europe PMC] [Abstract]
• protein serine/threonine kinase activator activity Source: BHF-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%2Dgo%2Devidence%2Dcodes#tas">GO evidence code guide</a></p> Traceable author statementⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• titin binding Source: BHF-UCLInferred from physical interactionⁱ
  • "A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase."
    Gautel M., Castiglione Morelli M.A., Pfuhl M., Motta A., Pastore A.
    Eur. J. Biochem. 230:752-759(1995) [PubMed] [Europe PMC] [Abstract]
• type 3 metabotropic glutamate receptor binding Source: Ensembl

GO - Biological processⁱ

• activation of adenylate cyclase activity Source: Ensembl
• calcium-mediated signaling 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• detection of calcium ion Source: BHF-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%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ
  • "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
    Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
    Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
• establishment of protein localization to mitochondrial membrane Source: Ensembl
• G2/M transition of mitotic cell cycle Source: Ensembl
• G protein-coupled receptor signaling pathway Source: UniProtKBTraceable author statementⁱ
  • "Calmodulin regulation of basal and agonist-stimulated G protein coupling by the mu-opioid receptor (OP(3)) in morphine-pretreated cell."
    Wang D., Surratt C.K., Sadee W.
    J. Neurochem. 75:763-771(2000) [PubMed] [Europe PMC] [Abstract]
• microtubule cytoskeleton organization 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. Bioinformatics 12:449-462(2011) [PubMed] [Europe PMC] [Abstract]
• negative regulation of peptidyl-threonine phosphorylation Source: BHF-UCLTraceable author statementⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• negative regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
• positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCLInferred from direct assayⁱ
  • "Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds."
    Tan R.Y., Mabuchi Y., Grabarek Z.
    J. Biol. Chem. 271:7479-7483(1996) [PubMed] [Europe PMC] [Abstract]
• positive regulation of DNA binding Source: Ensembl
• positive regulation of nitric-oxide synthase activity Source: Ensembl
• positive regulation of peptidyl-threonine phosphorylation Source: BHF-UCLTraceable author statementⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of phosphoprotein phosphatase activity Source: BHF-UCLInferred from direct assayⁱ
  • "Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds."
    Tan R.Y., Mabuchi Y., Grabarek Z.
    J. Biol. Chem. 271:7479-7483(1996) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein autophosphorylation Source: BHF-UCLTraceable author statementⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein dephosphorylation Source: BHF-UCLInferred from direct assayⁱ
  • "Blocking the Ca2+-induced conformational transitions in calmodulin with disulfide bonds."
    Tan R.Y., Mabuchi Y., Grabarek Z.
    J. Biol. Chem. 271:7479-7483(1996) [PubMed] [Europe PMC] [Abstract]
• positive regulation of protein serine/threonine kinase activity Source: BHF-UCLTraceable author statementⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCLInferred from direct assayⁱ
  • "Defective calmodulin binding to the cardiac ryanodine receptor plays a key role in CPVT-associated channel dysfunction."
    Xu X., Yano M., Uchinoumi H., Hino A., Suetomi T., Ono M., Tateishi H., Oda T., Okuda S., Doi M., Kobayashi S., Yamamoto T., Ikeda Y., Ikemoto N., Matsuzaki M.
    Biochem. Biophys. Res. Commun. 394:660-666(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of cardiac muscle contraction Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
    Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
    Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion Source: BHF-UCL
• regulation of cell communication by electrical coupling involved in cardiac conduction Source: BHF-UCL
• regulation of cytokinesis Source: UniProtKBInferred from mutant phenotypeⁱ
  • Ref.16

    "CP110 cooperates with two calcium-binding proteins to regulate cytokinesis and genome stability."
    Tsang W.Y., Spektor A., Luciano D.J., Indjeian V.B., Chen Z., Salisbury J.L., Sanchez I., Dynlacht B.D.
    Mol. Biol. Cell 17:3423-3434(2006) [PubMed] [Europe PMC] [Abstract]

    Cited for: FUNCTION, INTERACTION WITH CCP110, SUBCELLULAR LOCATION.
• regulation of heart rate Source: BHF-UCLInferred from mutant phenotypeⁱ
  • "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
    Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
    Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
• regulation of high voltage-gated calcium channel activity Source: Ensembl
• regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCLInferred from direct assayⁱ
  • "Defective calmodulin binding to the cardiac ryanodine receptor plays a key role in CPVT-associated channel dysfunction."
    Xu X., Yano M., Uchinoumi H., Hino A., Suetomi T., Ono M., Tateishi H., Oda T., Okuda S., Doi M., Kobayashi S., Yamamoto T., Ikeda Y., Ikemoto N., Matsuzaki M.
    Biochem. Biophys. Res. Commun. 394:660-666(2010) [PubMed] [Europe PMC] [Abstract]
• regulation of synaptic vesicle endocytosis Source: Ensembl
• regulation of synaptic vesicle exocytosis Source: Ensembl
• response to amphetamine Source: Ensembl
• response to calcium ion Source: BHF-UCLInferred from direct assayⁱ
  • "A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase."
    Gautel M., Castiglione Morelli M.A., Pfuhl M., Motta A., Pastore A.
    Eur. J. Biochem. 230:752-759(1995) [PubMed] [Europe PMC] [Abstract]
• response to corticosterone Source: Ensembl
• substantia nigra development Source: UniProtKBInferred from high throughput expression patternⁱ
  • "Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis."
    Chen S., Lu F.F., Seeman P., Liu F.
    Neurochem. Res. 37:2805-2813(2012) [PubMed] [Europe PMC] [Abstract]

<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

<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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

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

• adenylate cyclase binding Source: CAFAInferred from physical interactionⁱ
  • "Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
    Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
    Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
• calcium-dependent protein binding Source: Ensembl
• disordered domain specific binding Source: CAFAInferred from physical interactionⁱ
  • "Structural analysis of the complex between calmodulin and full-length myelin basic protein, an intrinsically disordered molecule."
    Majava V., Wang C., Myllykoski M., Kangas S.M., Kang S.U., Hayashi N., Baumgartel P., Heape A.M., Lubec G., Kursula P.
    Amino Acids 39:59-71(2010) [PubMed] [Europe PMC] [Abstract]
• ion channel binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Solution NMR structure of Apo-calmodulin in complex with the IQ motif of human cardiac sodium channel NaV1.5."
    Chagot B., Chazin W.J.
    J. Mol. Biol. 406:106-119(2011) [PubMed] [Europe PMC] [Abstract]
  • "Mutations in calmodulin cause ventricular tachycardia and sudden cardiac death."
    Nyegaard M., Overgaard M.T., Sondergaard M.T., Vranas M., Behr E.R., Hildebrandt L.L., Lund J., Hedley P.L., Camm A.J., Wettrell G., Fosdal I., Christiansen M., Borglum A.D.
    Am. J. Hum. Genet. 91:703-712(2012) [PubMed] [Europe PMC] [Abstract]
• nitric-oxide synthase binding Source: Ensembl
• N-terminal myristoylation domain binding Source: UniProtKBInferred from physical interactionⁱ
  • "Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo."
    Matsubara M., Jing T., Kawamura K., Shimojo N., Titani K., Hashimoto K., Hayashi N.
    Protein Sci. 14:494-503(2005) [PubMed] [Europe PMC] [Abstract]
• phosphatidylinositol 3-kinase binding Source: Ensembl
• protein domain specific binding Source: UniProtKBInferred from physical interactionⁱ
  • "The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins."
    Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y., Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S., Kingsmore S.F.
    Mol. Med. 8:56-64(2002) [PubMed] [Europe PMC] [Abstract]
• protein kinase binding Source: BHF-UCLInferred from physical interactionⁱ
  • "Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation."
    Rellos P., Pike A.C., Niesen F.H., Salah E., Lee W.H., von Delft F., Knapp S.
    PLoS Biol. 8:E1000426-E1000426(2010) [PubMed] [Europe PMC] [Abstract]
• titin binding Source: BHF-UCLInferred from physical interactionⁱ
  • "A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase."
    Gautel M., Castiglione Morelli M.A., Pfuhl M., Motta A., Pastore A.
    Eur. J. Biochem. 230:752-759(1995) [PubMed] [Europe PMC] [Abstract]
• type 3 metabotropic glutamate receptor binding Source: Ensembl

Protein-protein interaction databases

Chemistry 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

<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

Region

<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>Sequenceⁱ

<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.

<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 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
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ 
        60         70         80         90        100
DMINEVDADG NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY 
       110        120        130        140 
ISAAELRHVM TNLGEKLTDE EVDEMIREAD IDGDGQVNYE EFVQMMTAK  

<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

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

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. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families
3. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
4. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
5. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
6. Human chromosome 19
   Human chromosome 19: entries, gene names and cross-references to MIM