UniProtKB - P0DP24 (CALM2_HUMAN)
(max 400 entries)x
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P0DP24|CALM2_HUMAN Calmodulin-2 OS=Homo sapiens OX=9606 GN=CALM2 PE=1 SV=1 MADQLTEEQIAEFKEAFSLFDKDGDGTITTKELGTVMRSLGQNPTEAELQDMINEVDADG NGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDE EVDEMIREADIDGDGQVNYEEFVQMMTAK
- Align
- Format
- Add to basketAdded to basket
- History
- Other tutorials and videos
- Help video
- Feedback
Protein
Calmodulin-2
Gene
CALM2
Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<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
Calmodulin mediates the control of a large number of enzymes, ion channels, aquaporins and other proteins through calcium-binding. Among the enzymes to be stimulated by the calmodulin-calcium complex are a number of protein kinases and phosphatases. Together with CCP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (PubMed:16760425). Mediates calcium-dependent inactivation of CACNA1C (PubMed:26969752). Positively regulates calcium-activated potassium channel activity of KCNN2 (PubMed:27165696).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"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. - Ref.42"Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin Variants in Long QT Syndrome and Functional Characterization of a Novel Long QT Syndrome-Associated Calmodulin Missense Variant, E141G."
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J., Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G., Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.
Circ. Cardiovasc. Genet. 9:136-146(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LQT15 GLY-130 AND VAL-130, FUNCTION. - Ref.43"Arrhythmogenic calmodulin mutations impede activation of small-conductance calcium-activated potassium current."
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M., Everett T.H. IV, George A.L. Jr., Chen P.S.
Heart Rhythm 13:1716-1723(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, FUNCTION.
Miscellaneous
This protein has four functional calcium-binding sites.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Calmodulin structure refined at 1.7 A resolution."
Chattopadhyaya R., Meador W.E., Means A.R., Quiocho F.A.
J. Mol. Biol. 228:1177-1192(1992) [PubMed] [Europe PMC] [Abstract]Cited for: CALCIUM-BINDING SITES.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 21 – 32 | 11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 57 – 68 | 21 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 94 – 105 | 31 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 | |
| <p>This subsection of the ‘Function’ section specifies the position(s) of the calcium-binding region(s) within the protein. One common calcium-binding motif is the EF-hand, but other calcium-binding motifs also exist.<p><a href='/help/ca_bind' target='_top'>More...</a></p>Calcium bindingi | 130 – 141 | 41 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 12 |
<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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- calcium channel inhibitor 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- calcium ion 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
- disordered domain specific 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ion channel binding Source: BHF-UCL <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
- N-terminal myristoylation domain 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein domain specific 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: BHF-UCL <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
- protein phosphatase activator activity Source: BHF-UCL <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
- 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-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- titin binding Source: BHF-UCL <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
<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 - Biological processi
- 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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- G-protein coupled receptor signaling pathway Source: UniProtKB <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
- negative regulation of peptidyl-threonine phosphorylation 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-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- negative regulation of ryanodine-sensitive calcium-release channel 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-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation by host of symbiont cAMP-mediated signal transduction Source: CAFA <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
- positive regulation of cyclic-nucleotide phosphodiesterase activity Source: BHF-UCL <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
- positive regulation of peptidyl-threonine phosphorylation 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-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of phosphoprotein phosphatase activity Source: BHF-UCL <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
- positive regulation of protein autophosphorylation 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-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of protein dephosphorylation Source: BHF-UCL <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
- positive regulation of protein serine/threonine kinase 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-go-evidence-codes#tas">GO evidence code guide</a></p> Traceable author statementi
- positive regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL <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
- regulation of cardiac muscle contraction 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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- 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: 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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of heart rate 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-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum Source: BHF-UCL <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
- response to calcium ion Source: BHF-UCL <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
- substantia nigra development Source: UniProtKBInferred from high throughput expression patterni
<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
| Ligand | Calcium, Metal-binding |
<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
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Calmodulin-2Imported<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:CALM21 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:CAM2, CAMB |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Human Gene Nomenclature Database More...HGNCi | HGNC:1445 CALM2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 114182 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P0DP24 |
<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
Cytoskeleton
- spindle 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"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.
- spindle pole 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"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.
Note: Distributed throughout the cell during interphase, but during mitosis becomes dramatically localized to the spindle poles and the spindle microtubules.- spindle 1 Publication
Cytoskeleton
- centrosome 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
- spindle microtubule 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
- spindle pole 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
Nucleus
Plasma Membrane
- plasma membrane Source: UniProtKB <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
Other locations
- calcium channel complex Source: BHF-UCL <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
- catalytic complex Source: CAFA <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
- cytoplasm 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
- protein-containing complex Source: CAFA <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
- sarcomere Source: BHF-UCL <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
- vesicle Source: UniProtKBInferred from high throughput direct assayi
<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>Keywords - Cellular componenti
Cytoplasm, Cytoskeleton<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
Long QT syndrome 15 (LQT15)6 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More...</a></p>
Manual assertion based on experiment ini
- Ref.37"Calmodulin mutations associated with recurrent cardiac arrest in infants."
Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M., Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M., Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W., Kaab S. , Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J., George A.L. Jr.
Circulation 127:1009-1017(2013) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN LQT15, VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96. - Ref.38"Novel calmodulin mutations associated with congenital arrhythmia susceptibility."
Makita N., Yagihara N., Crotti L., Johnson C.N., Beckmann B.M., Roh M.S., Shigemizu D., Lichtner P., Ishikawa T., Aiba T., Homfray T., Behr E.R., Klug D., Denjoy I., Mastantuono E., Theisen D., Tsunoda T., Satake W. , Toda T., Nakagawa H., Tsuji Y., Tsuchiya T., Yamamoto H., Miyamoto Y., Endo N., Kimura A., Ozaki K., Motomura H., Suda K., Tanaka T., Schwartz P.J., Meitinger T., Kaeaeb S., Guicheney P., Shimizu W., Bhuiyan Z.A., Watanabe H., Chazin W.J., George A.L. Jr.
Circ. Cardiovasc. Genet. 7:466-474(2014) [PubMed] [Europe PMC] [Abstract]Cited for: INVOLVEMENT IN LQT15, VARIANTS LQT15 ILE-98; SER-98; GLU-132; HIS-134 AND PRO-136, CHARACTERIZATION OF VARIANTS LQT15 ILE-98; GLU-132; HIS-134 AND PRO-136. - Ref.40"Distinctive malfunctions of calmodulin mutations associated with heart RyR2-mediated arrhythmic disease."
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H., Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E., Nounesis G., Lai F.A., Nomikos M.
Biochim. Biophys. Acta 1850:2168-2176(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2. - Ref.41"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 LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2. - Ref.42"Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin Variants in Long QT Syndrome and Functional Characterization of a Novel Long QT Syndrome-Associated Calmodulin Missense Variant, E141G."
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J., Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G., Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.
Circ. Cardiovasc. Genet. 9:136-146(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANTS LQT15 GLY-130 AND VAL-130, FUNCTION. - Ref.43"Arrhythmogenic calmodulin mutations impede activation of small-conductance calcium-activated potassium current."
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M., Everett T.H. IV, George A.L. Jr., Chen P.S.
Heart Rhythm 13:1716-1723(2016) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, FUNCTION.
Ref.37
"Calmodulin mutations associated with recurrent cardiac arrest in infants."
Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M., Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M., Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W., Kaab S. , Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J., George A.L. Jr.
Circulation 127:1009-1017(2013) [PubMed] [Europe PMC] [Abstract]
Crotti L., Johnson C.N., Graf E., De Ferrari G.M., Cuneo B.F., Ovadia M., Papagiannis J., Feldkamp M.D., Rathi S.G., Kunic J.D., Pedrazzini M., Wieland T., Lichtner P., Beckmann B.M., Clark T., Shaffer C., Benson D.W., Kaab S. , Meitinger T., Strom T.M., Chazin W.J., Schwartz P.J., George A.L. Jr.
Circulation 127:1009-1017(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LQT15, VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96.
Ref.38
"Novel calmodulin mutations associated with congenital arrhythmia susceptibility."
Makita N., Yagihara N., Crotti L., Johnson C.N., Beckmann B.M., Roh M.S., Shigemizu D., Lichtner P., Ishikawa T., Aiba T., Homfray T., Behr E.R., Klug D., Denjoy I., Mastantuono E., Theisen D., Tsunoda T., Satake W. , Toda T., Nakagawa H., Tsuji Y., Tsuchiya T., Yamamoto H., Miyamoto Y., Endo N., Kimura A., Ozaki K., Motomura H., Suda K., Tanaka T., Schwartz P.J., Meitinger T., Kaeaeb S., Guicheney P., Shimizu W., Bhuiyan Z.A., Watanabe H., Chazin W.J., George A.L. Jr.
Circ. Cardiovasc. Genet. 7:466-474(2014) [PubMed] [Europe PMC] [Abstract]
Makita N., Yagihara N., Crotti L., Johnson C.N., Beckmann B.M., Roh M.S., Shigemizu D., Lichtner P., Ishikawa T., Aiba T., Homfray T., Behr E.R., Klug D., Denjoy I., Mastantuono E., Theisen D., Tsunoda T., Satake W. , Toda T., Nakagawa H., Tsuji Y., Tsuchiya T., Yamamoto H., Miyamoto Y., Endo N., Kimura A., Ozaki K., Motomura H., Suda K., Tanaka T., Schwartz P.J., Meitinger T., Kaeaeb S., Guicheney P., Shimizu W., Bhuiyan Z.A., Watanabe H., Chazin W.J., George A.L. Jr.
Circ. Cardiovasc. Genet. 7:466-474(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LQT15, VARIANTS LQT15 ILE-98; SER-98; GLU-132; HIS-134 AND PRO-136, CHARACTERIZATION OF VARIANTS LQT15 ILE-98; GLU-132; HIS-134 AND PRO-136.
Ref.40
"Distinctive malfunctions of calmodulin mutations associated with heart RyR2-mediated arrhythmic disease."
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H., Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E., Nounesis G., Lai F.A., Nomikos M.
Biochim. Biophys. Acta 1850:2168-2176(2015) [PubMed] [Europe PMC] [Abstract]
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H., Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E., Nounesis G., Lai F.A., Nomikos M.
Biochim. Biophys. Acta 1850:2168-2176(2015) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2.
Ref.41
"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]
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 LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2.
Ref.42
"Spectrum and Prevalence of CALM1-, CALM2-, and CALM3-Encoded Calmodulin Variants in Long QT Syndrome and Functional Characterization of a Novel Long QT Syndrome-Associated Calmodulin Missense Variant, E141G."
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J., Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G., Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.
Circ. Cardiovasc. Genet. 9:136-146(2016) [PubMed] [Europe PMC] [Abstract]
Boczek N.J., Gomez-Hurtado N., Ye D., Calvert M.L., Tester D.J., Kryshtal D.O., Hwang H.S., Johnson C.N., Chazin W.J., Loporcaro C.G., Shah M., Papez A.L., Lau Y.R., Kanter R., Knollmann B.C., Ackerman M.J.
Circ. Cardiovasc. Genet. 9:136-146(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS LQT15 GLY-130 AND VAL-130, FUNCTION.
Ref.43
"Arrhythmogenic calmodulin mutations impede activation of small-conductance calcium-activated potassium current."
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M., Everett T.H. IV, George A.L. Jr., Chen P.S.
Heart Rhythm 13:1716-1723(2016) [PubMed] [Europe PMC] [Abstract]
Yu C.C., Ko J.S., Ai T., Tsai W.C., Chen Z., Rubart M., Vatta M., Everett T.H. IV, George A.L. Jr., Chen P.S.
Heart Rhythm 13:1716-1723(2016) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, FUNCTION.
The disease is caused by mutations affecting the gene represented in this entry. Mutations in CALM2 are the cause of LQT15.
Disease descriptionA form of long QT syndrome, a heart disorder characterized by a prolonged QT interval on the ECG and polymorphic ventricular arrhythmias. They cause syncope and sudden death in response to exercise or emotional stress, and can present with a sentinel event of sudden cardiac death in infancy.
See also OMIM:616249| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073276 | 96 | D → V in LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073277 | 98 | N → I in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078543 | 98 | N → S in LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078544 | 130 | D → G in LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of clacium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078262 | 130 | D → V in LQT15. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073279 | 132 | D → E in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073280 | 134 | D → H in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073281 | 136 | Q → P in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<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>Keywords - Diseasei
Disease mutation, Long QT syndromeOrganism-specific databases
MalaCards human disease database More...MalaCardsi | CALM2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 616249 phenotype |
Open Targets More...OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | RemovedCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000439933 | 2 – 149 | Calmodulin-2Add BLAST | 148 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 2 | N-acetylalanineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 22 | N6-acetyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| ||
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes covalent linkages of various types formed between two proteins (interchain cross-links) or between two parts of the same protein (intrachain cross-links), except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki | 22 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | ||
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 45 | Phosphothreonine; by CaMK4By similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 82 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 95 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 100 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 102 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 111 | PhosphothreonineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 116 | N6,N6,N6-trimethyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 116 | N6-methyllysine; alternateCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 139 | PhosphotyrosineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 |
<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
Ubiquitination results in a strongly decreased activity.By similarity
Phosphorylation results in a decreased activity.By similarity
<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>Keywords - PTMi
Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugationPTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P0DP24 |
<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
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P0DP24 baseline and differential |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA044999 |
<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
Interacts with MYO1C, MYO5A and RRAD. Interacts with MYO10 (By similarity). Interacts with CEP97, CCP110, TTN/titin and SRY (PubMed:9804419, PubMed:12871148, PubMed:15746192, PubMed:16760425, PubMed:17719545). Interacts with USP6; the interaction is calcium dependent (PubMed:16127172). Interacts with CDK5RAP2 (PubMed:20466722). Interacts with SCN5A (By similarity). Interacts with RYR1 (PubMed:18650434). Interacts with FCHO1 (PubMed:22484487). Interacts with MIP in a 1:2 stoichiometry; the interaction with the cytoplasmic domains from two MIP subunits promotes MIP water channel closure (By similarity). Interacts with ORAI1; this may play a role in the regulation of ORAI1-mediated calcium transport (By similarity). Interacts with IQCF1 (By similarity). Interacts with SYT7 (By similarity). Interacts with CEACAM1 (via cytoplasmic domain); this interaction is in a calcium dependent manner and reduces homophilic cell adhesion through dissociation of dimer (By similarity). Interacts with RYR2; regulates RYR2 calcium-release channel activity (PubMed:27516456, PubMed:18650434, PubMed:26164367). Interacts with PCP4; regulates calmodulin calcium-binding (PubMed:27876793). Interacts with the heterotetrameric KCNQ2 and KCNQ3 channel; the interaction is calcium-independent, constitutive and participates to the proper assembly of a functional heterotetrameric M channel (PubMed:27564677).By similarity
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
14 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"Structural basis for activation of the titin kinase domain during myofibrillogenesis."
Mayans O., van der Ven P.F.M., Wilm M., Mues A., Young P., Furst D.O., Wilmanns M., Gautel M.
Nature 395:863-869(1998) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH TTN. - Ref.13"Recombinant expression, purification and characterisation of the HMG domain of human SRY."
Kelly S., Yotis J., Macris M., Harley V.
Protein Pept. Lett. 10:281-286(2003) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SRY. - Ref.14"Calcium/calmodulin regulates ubiquitination of the ubiquitin-specific protease TRE17/USP6."
Shen C., Ye Y., Robertson S.E., Lau A.W., Mak D.O., Chou M.M.
J. Biol. Chem. 280:35967-35973(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH USP6. - Ref.15"Defective calmodulin-mediated nuclear transport of the sex-determining region of the Y chromosome (SRY) in XY sex reversal."
Sim H., Rimmer K., Kelly S., Ludbrook L.M., Clayton A.H., Harley V.R.
Mol. Endocrinol. 19:1884-1892(2005) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH SRY. - Ref.17"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. - Ref.18"Cep97 and CP110 suppress a cilia assembly program."
Spektor A., Tsang W.Y., Khoo D., Dynlacht B.D.
Cell 130:678-690(2007) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CEP97 AND CCP110. - Ref.19"S100A1 and calmodulin compete for the same binding site on ryanodine receptor."
Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F., Weber D.J.
J. Biol. Chem. 283:26676-26683(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH RYR1 AND RYR2. - Ref.27"Crystal structure of calmodulin binding domain of orai1 in complex with Ca2+ calmodulin displays a unique binding mode."
Liu Y., Zheng X., Mueller G.A., Sobhany M., DeRose E.F., Zhang Y., London R.E., Birnbaumer L.
J. Biol. Chem. 287:43030-43041(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH ORAI1. - Ref.29"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH FCHO1. - Ref.35"Structural insights into the M-channel proximal C-terminus/calmodulin complex."
Strulovich R., Tobelaim W.S., Attali B., Hirsch J.A.
Biochemistry 55:5353-5365(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH KCNQ2 AND KCNQ3. - Ref.36"PEP-19 modulates calcium binding to calmodulin by electrostatic steering."
Wang X., Putkey J.A.
Nat. Commun. 7:13583-13583(2016) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH PCP4, REGION. - Ref.40"Distinctive malfunctions of calmodulin mutations associated with heart RyR2-mediated arrhythmic disease."
Vassilakopoulou V., Calver B.L., Thanassoulas A., Beck K., Hu H., Buntwal L., Smith A., Theodoridou M., Kashir J., Blayney L., Livaniou E., Nounesis G., Lai F.A., Nomikos M.
Biochim. Biophys. Acta 1850:2168-2176(2015) [PubMed] [Europe PMC] [Abstract]Cited for: VARIANT LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2. - Ref.41"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 LQT15 VAL-96, CHARACTERIZATION OF VARIANT LQT15 VAL-96, INTERACTION WITH RYR2.
<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 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- disordered domain specific 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- ion channel binding Source: BHF-UCL <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
- N-terminal myristoylation domain 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein domain specific 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-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: BHF-UCL <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
- titin binding Source: BHF-UCL <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
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P0DP24 |
<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
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 7 – 20 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 14 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 25 – 28 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 30 – 39 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 46 – 56 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 61 – 65 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 66 – 73 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 77 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 83 – 93 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 98 – 102 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 103 – 112 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 113 – 115 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 119 – 129 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 134 – 138 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 139 – 147 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0DP24 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<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
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 8 – 43 | EF-hand 1PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 36 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 44 – 79 | EF-hand 2PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 36 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 81 – 116 | EF-hand 3PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 36 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 117 – 149 | EF-hand 4PROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 33 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 77 – 149 | Necessary and sufficient for interaction with PCP41 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 73 |
<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
Belongs to the calmodulin family.Curated
<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>Keywords - Domaini
RepeatPhylogenomic databases
KEGG Orthology (KO) More...KOi | K02183 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00051 EFh, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR039030 Calmodulin IPR011992 EF-hand-dom_pair IPR018247 EF_Hand_1_Ca_BS IPR002048 EF_hand_dom |
The PANTHER Classification System More...PANTHERi | PTHR23050:SF311 PTHR23050:SF311, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF13499 EF-hand_7, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00054 EFh, 4 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47473 SSF47473, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00018 EF_HAND_1, 4 hits PS50222 EF_HAND_2, 4 hits |
<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.
P0DP24-1 [UniParc]FASTAAdd to basketAdded to basketShow »
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
Length:149
Mass (Da):16,838
Last modified:May 10, 2017 - v1
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i6B4BC3FCDE10727B
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 124 | E → Q in AAH08437 (PubMed:15489334).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073276 | 96 | D → V in LQT15; reduction in calcium affinity; highly decreased calcium-dependent inactivation of L-type calcium channel; increased action potential duration; not changed protein abundance; not changed structure; increased thermal stability in absence of calcium; decreased thermal stability in presence of calcium; significantly increased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073277 | 98 | N → I in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078543 | 98 | N → S in LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078544 | 130 | D → G in LQT15; reduction in calcium affinity; not changed protein abundance; not changed structure; significantly decreased thermal stability in presence of clacium; significantly decreased RYR2 interaction; increased ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078262 | 130 | D → V in LQT15. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073279 | 132 | D → E in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073280 | 134 | D → H in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_073281 | 136 | Q → P in LQT15; reduction in calcium affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M19311 mRNA Translation: AAA35641.1 D45887 mRNA Translation: BAA08302.1 U94728, U94725, U94726 Genomic DNA Translation: AAC83174.1 BT009916 mRNA Translation: AAP88918.1 CR541990 mRNA Translation: CAG46787.1 CR542021 mRNA Translation: CAG46818.1 AC073283 Genomic DNA Translation: AAY24085.1 BC003354 mRNA Translation: AAH03354.1 BC006464 mRNA Translation: AAH06464.1 BC008437 mRNA Translation: AAH08437.1 BC017385 mRNA Translation: AAH17385.1 BC018677 mRNA Translation: AAH18677.1 BC026065 mRNA Translation: AAH26065.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1832.1 |
NCBI Reference Sequences More...RefSeqi | NP_001292553.1, NM_001305624.1 NP_001292554.1, NM_001305625.1 NP_001292555.1, NM_001305626.1 NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.282410 Hs.468442 Hs.515487 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272298; ENSP00000272298; ENSG00000143933 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 801 805 808 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:801 hsa:805 hsa:808 |
<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>Keywords - Coding sequence diversityi
Polymorphism<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
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0DP24 | Calmodulin-1 | ) | 149 | ||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin | ) | 149 | |||
| +276 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0DP24 | Calmodulin-1 | ) | 149 | ||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin | ) | 149 | |||
| +276 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0DP24 | Calmodulin-1 | ) | 149 | ||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin-1 | ) | 149 | |||
| Calmodulin | ) | 149 | |||
| +277 | |||||
<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
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | M19311 mRNA Translation: AAA35641.1 D45887 mRNA Translation: BAA08302.1 U94728, U94725, U94726 Genomic DNA Translation: AAC83174.1 BT009916 mRNA Translation: AAP88918.1 CR541990 mRNA Translation: CAG46787.1 CR542021 mRNA Translation: CAG46818.1 AC073283 Genomic DNA Translation: AAY24085.1 BC003354 mRNA Translation: AAH03354.1 BC006464 mRNA Translation: AAH06464.1 BC008437 mRNA Translation: AAH08437.1 BC017385 mRNA Translation: AAH17385.1 BC018677 mRNA Translation: AAH18677.1 BC026065 mRNA Translation: AAH26065.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS1832.1 |
NCBI Reference Sequences More...RefSeqi | NP_001292553.1, NM_001305624.1 NP_001292554.1, NM_001305625.1 NP_001292555.1, NM_001305626.1 NP_001316851.1, NM_001329922.1 NP_001734.1, NM_001743.5 NP_005175.2, NM_005184.3 NP_008819.1, NM_006888.4 |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.282410 Hs.468442 Hs.515487 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 3O77 | X-ray | 2.35 | A | 45-149 | [»] | |
| 3O78 | X-ray | 2.60 | A/B | 45-149 | [»] | |
| 5COC | X-ray | 2.67 | A | 10-78 | [»] | |
| 5J03 | X-ray | 2.00 | B | 1-149 | [»] | |
| 5NIN | X-ray | 1.70 | A/B | 1-149 | [»] | |
| 5VMS | electron microscopy | 3.70 | B | 1-149 | [»] | |
| 5WSU | X-ray | 3.00 | A/B | 2-149 | [»] | |
| 5WSV | X-ray | 2.33 | A/C | 1-147 | [»] | |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0DP24 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P0DP24 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P0DP24 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000272298; ENSP00000272298; ENSG00000143933 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 801 805 808 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:801 hsa:805 hsa:808 |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 801 805 808 |
GeneCards: human genes, protein and diseases More...GeneCardsi | CALM2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:1445 CALM2 |
Human Protein Atlas More...HPAi | HPA044999 |
MalaCards human disease database More...MalaCardsi | CALM2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 114182 gene 616249 phenotype |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P0DP24 |
Open Targets More...OpenTargetsi | ENSG00000143933 ENSG00000160014 ENSG00000198668 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
KEGG Orthology (KO) More...KOi | K02183 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | CALM2 human |
Protein Ontology More...PROi | PR:P0DP24 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P0DP24 baseline and differential |
Family and domain databases
Conserved Domains Database More...CDDi | cd00051 EFh, 2 hits |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR039030 Calmodulin IPR011992 EF-hand-dom_pair IPR018247 EF_Hand_1_Ca_BS IPR002048 EF_hand_dom |
The PANTHER Classification System More...PANTHERi | PTHR23050:SF311 PTHR23050:SF311, 1 hit |
Pfam protein domain database More...Pfami | View protein in Pfam PF13499 EF-hand_7, 2 hits |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00054 EFh, 4 hits |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF47473 SSF47473, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00018 EF_HAND_1, 4 hits PS50222 EF_HAND_2, 4 hits |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<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 subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | CALM2_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0DP24Primary (citable) accession number: P0DP24 Secondary accession number(s): P02593 , P62158, P70667, P99014, Q13942, Q53S29, Q61379, Q61380, Q96HK3 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 10, 2017 |
| Last sequence update: | May 10, 2017 | |
| Last modified: | July 18, 2018 | |
| This is version 13 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | |
<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
<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>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 2
Human chromosome 2: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
