Glutamate receptor ionotropic, NMDA 2A

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

Sites

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	128 – 128	1	ZincBy similarity
<p>Indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.</p><p><a href='../manual/metal' target='_top'>More...</a></p>Metal bindingi	283 – 283	1	ZincBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	518 – 518	1	Glutamate
<p>Describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.</p><p><a href='../manual/site' target='_top'>More...</a></p>Sitei	614 – 614	1	Functional determinant of NMDA receptorsBy similarity
<p>Describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.</p><p><a href='../manual/binding' target='_top'>More...</a></p>Binding sitei	731 – 731	1	Glutamate; via amide nitrogen

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATPase binding Source: RGD

  <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

  • 19406213

• cell adhesion molecule binding Source: RGD

  <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

  • 16540568

• extracellular-glutamate-gated ion channel activity Source: InterPro
• glutamate binding 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

  • 9425000

• glutamate receptor binding Source: RGD

  <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

  • 19298817

• ionotropic glutamate receptor activity Source: RGD

  <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

  • 16477151

• neurotransmitter binding Source: RGD

  <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

  • 16477151

• NMDA glutamate receptor activity Source: RGD

  <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

  • 16477151
  • 22098737
  • 8428958

• protein complex binding Source: RGD

  <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

  • 12618293
  • 20197063

• protein dimerization activity Source: RGD

  <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

  • 22493736

• protein heterodimerization activity Source: RGD

  <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

  • 21544205

• protein kinase binding Source: RGD

  <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

  • 11478920

• receptor binding Source: RGD

  <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

  • 12408866

• scaffold protein 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

  • 20847060

• voltage-gated cation channel activity Source: RGD

  <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

  • 17050728

• zinc ion binding Source: UniProtKB

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

• action potential Source: RGD

  <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

  • 16904707
  • 17655746

• cellular response to amino acid stimulus Source: RGD

  <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

  • 19154422

• cellular response to dsRNA Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19958814

• cellular response to growth factor stimulus Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19958814

• cellular response to lipid Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19819306

• cellular response to magnesium ion Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19154422

• cellular response to manganese ion Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19643132

• cellular response to zinc ion Source: RGD

  <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

  • 19240037

• cerebral cortex development Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19409459

• chemical synaptic transmission Source: RGD

  <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

  • 15306812

• excitatory postsynaptic potential Source: RGD

  <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

  • 20164351

• hippocampus development Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19535712

• ionotropic glutamate receptor signaling pathway Source: RGD

  <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

  • 16477151

• memory 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

  • 16157280

• positive regulation of cell death Source: RGD

  <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

  • 20168047

• positive regulation of excitatory postsynaptic potential 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

  • 12930820

• protein tetramerization Source: RGD

  <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

  • 22493736

• regulation of long-term neuronal synaptic plasticity Source: RGD

  <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

  • 16904707
  • 17655746

• response to amine Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19918184

• response to ammonium ion Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 20084674

• response to calcium ion Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19761817

• response to carbohydrate Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19695778

• response to cocaine Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19322657

• response to drug Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 20084674
  • 20417256

• response to ethanol Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19673743

• response to fungicide Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19591855

• response to light stimulus Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19850826

• response to manganese ion Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 20175136

• response to methylmercury Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19409459

• response to organic cyclic compound Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19322657

• response to other organism Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19563853

• rhythmic process Source: RGD

  <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

  • 16477151

• spinal cord development Source: RGD

  <p>Inferred from Expression Pattern</p> <p>Covers cases where the annotation is inferred from the timing or location of expression of a gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#iep">GO evidence code guide</a></p> Inferred from expression patternⁱ

  • 19446017

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Molecular functionⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Biological processⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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 - Ligandⁱ

Protein family/group databases

<p>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><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

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

Topology

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	23 – 555	533	ExtracellularSequence analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	556 – 576	21	HelicalSequence analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	577 – 633	57	CytoplasmicSequence analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	634 – 654	21	HelicalSequence analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	655 – 816	162	ExtracellularSequence analysis			Add BLAST
<p>Describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.</p><p><a href='../manual/transmem' target='_top'>More...</a></p>Transmembranei	817 – 837	21	HelicalSequence analysis			Add BLAST
<p>Describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.</p><p><a href='../manual/topo_dom' target='_top'>More...</a></p>Topological domaini	838 – 1464	627	CytoplasmicSequence analysis			Add BLAST

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

• cell junction Source: UniProtKB-KW
• dendritic spine Source: MGI

  <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

  • 16221859

• neuron projection 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

  • 12738960

• NMDA selective glutamate receptor complex 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

  • 8702950

• postsynaptic density Source: RGD

  <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

  • 19339621

• postsynaptic membrane Source: UniProtKB-SubCell
• presynaptic membrane 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

  • 16157280

• synapse 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

  • 16407536

• terminal bouton Source: RGD

  <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

  • 19666514

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

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

Chemistry

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

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Denotes the presence of an N-terminal signal peptide.</p><p><a href='../manual/signal' target='_top'>More...</a></p>Signal peptidei	1 – 22	22	Sequence analysis			Add BLAST
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	23 – 1464	1442	Glutamate receptor ionotropic, NMDA 2A		PRO_0000011576	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	75 – 75	1	N-linked (GlcNAc...)Sequence analysis
<p>Describes the positions of cysteine residues participating in disulfide bonds.</p><p><a href='../manual/disulfid' target='_top'>More...</a></p>Disulfide bondi	87 ↔ 320		By similarity
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	340 – 340	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	443 – 443	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	444 – 444	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).</p><p><a href='../manual/carbohyd' target='_top'>More...</a></p>Glycosylationi	541 – 541	1	N-linked (GlcNAc...)Sequence analysis
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	882 – 882	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	890 – 890	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	929 – 929	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1025 – 1025	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1059 – 1059	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1062 – 1062	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1198 – 1198	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1291 – 1291	1	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 Ref.13 "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues." Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V. Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-882; SER-890; SER-929; SER-1025; SER-1059; SER-1062; SER-1198 AND SER-1291, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Proteomic databases

PTM databases

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

<p>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="/help/function_section">‘Function’</a> section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

<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><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

• ATPase binding Source: RGD

  <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

  • 19406213

• cell adhesion molecule binding Source: RGD

  <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

  • 16540568

• glutamate receptor binding Source: RGD

  <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

  • 19298817

• protein complex binding Source: RGD

  <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

  • 12618293
  • 20197063

• protein dimerization activity Source: RGD

  <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

  • 22493736

• protein heterodimerization activity Source: RGD

  <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

  • 21544205

• protein kinase binding Source: RGD

  <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

  • 11478920

• receptor binding Source: RGD

  <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

  • 12408866

• scaffold protein 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

  • 20847060

Protein-protein interaction databases

Chemistry

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

Secondary structure

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	406 – 410	5	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	414 – 416	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	417 – 421	5	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the <span class="caps">DSSP</span> secondary structure code ‘T’.</p><p><a href='../manual/turn' target='_top'>More...</a></p>Turni	424 – 426	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	434 – 447	14	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	449 – 458	10	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	459 – 471	13	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	475 – 479	5	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	482 – 485	4	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	495 – 501	7	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	506 – 508	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	516 – 519	4	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	522 – 524	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	529 – 531	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	533 – 538	6	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	668 – 671	4	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	673 – 675	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	676 – 678	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	689 – 697	9	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	699 – 705	7	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	706 – 708	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	713 – 721	9	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	726 – 731	6	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	732 – 740	9	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	747 – 751	5	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	752 – 754	3	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 PDB:4NF5
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	755 – 757	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	759 – 761	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined beta strands within the protein sequence.</p><p><a href='../manual/strand' target='_top'>More...</a></p>Beta strandi	764 – 766	3	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	772 – 784	13	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 PDB:4JWX
<p>Is used to indicate the positions of experimentally determined helical regions within the protein sequence.</p><p><a href='../manual/helix' target='_top'>More...</a></p>Helixi	787 – 795	9	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 PDB:4JWX

3D structure databases

Miscellaneous databases

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

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	511 – 513	3	Glutamate binding
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	689 – 690	2	Glutamate binding

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.</p><p><a href='../manual/motif' target='_top'>More...</a></p>Motifi	1462 – 1464	3	PDZ-binding

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Phylogenomic databases

Family and domain databases

<p>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 length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequenceⁱ

<p>Indicates if the <a href="/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

<p>Indicates if the <a href="/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><p><a href='../manual/sequence_processing' target='_top'>More...</a></p>Sequence processingⁱ: The displayed sequence is further processed into a mature form.

        10         20         30         40         50
MGRLGYWTLL VLPALLVWRD PAQNAAAEKG PPALNIAVLL GHSHDVTERE 
        60         70         80         90        100
LRNLWGPEQA TGLPLDVNVV ALLMNRTDPK SLITHVCDLM SGARIHGLVF 
       110        120        130        140        150
GDDTDQEAVA QMLDFISSQT FIPILGIHGG ASMIMADKDP TSTFFQFGAS 
       160        170        180        190        200
IQQQATVMLK IMQDYDWHVF SLVTTIFPGY RDFISFIKTT VDNSFVGWDM 
       210        220        230        240        250
QNVITLDTSF EDAKTQVQLK KIHSSVILLY CSKDEAVLIL SEARSLGLTG 
       260        270        280        290        300
YDFFWIVPSL VSGNTELIPK EFPSGLISVS YDDWDYSLEA RVRDGLGILT 
       310        320        330        340        350
TAASSMLEKF SYIPEAKASC YGQAEKPETP LHTLHQFMVN VTWDGKDLSF 
       360        370        380        390        400
TEEGYQVHPR LVVIVLNKDR EWEKVGKWEN QTLSLRHAVW PRYKSFSDCE 
       410        420        430        440        450
PDDNHLSIVT LEEAPFVIVE DIDPLTETCV RNTVPCRKFV KINNSTNEGM 
       460        470        480        490        500
NVKKCCKGFC IDILKKLSRT VKFTYDLYLV TNGKHGKKVN NVWNGMIGEV 
       510        520        530        540        550
VYQRAVMAVG SLTINEERSE VVDFSVPFVE TGISVMVSRS NGTVSPSAFL 
       560        570        580        590        600
EPFSASVWVM MFVMLLIVSA IAVFVFEYFS PVGYNRNLAK GKAPHGPSFT 
       610        620        630        640        650
IGKAIWLLWG LVFNNSVPVQ NPKGTTSKIM VSVWAFFAVI FLASYTANLA 
       660        670        680        690        700
AFMIQEEFVD QVTGLSDKKF QRPHDYSPPF RFGTVPNGST ERNIRNNYPY 
       710        720        730        740        750
MHQYMTRFNQ RGVEDALVSL KTGKLDAFIY DAAVLNYKAG RDEGCKLVTI 
       760        770        780        790        800
GSGYIFASTG YGIALQKGSP WKRQIDLALL QFVGDGEMEE LETLWLTGIC 
       810        820        830        840        850
HNEKNEVMSS QLDIDNMAGV FYMLAAAMAL SLITFIWEHL FYWKLRFCFT 
       860        870        880        890        900
GVCSDRPGLL FSISRGIYSC IHGVHIEEKK KSPDFNLTGS QSNMLKLLRS 
       910        920        930        940        950
AKNISNMSNM NSSRMDSPKR ATDFIQRGSL IVDMVSDKGN LIYSDNRSFQ 
       960        970        980        990       1000
GKDSIFGDNM NELQTFVANR HKDNLSNYVF QGQHPLTLNE SNPNTVEVAV 
      1010       1020       1030       1040       1050
STESKGNSRP RQLWKKSMES LRQDSLNQNP VSQRDEKTAE NRTHSLKSPR 
      1060       1070       1080       1090       1100
YLPEEVAHSD ISETSSRATC HREPDNNKNH KTKDNFKRSM ASKYPKDCSD 
      1110       1120       1130       1140       1150
VDRTYMKTKA SSPRDKIYTI DGEKEPSFHL DPPQFVENIT LPENVGFPDT 
      1160       1170       1180       1190       1200
YQDHNENFRK GDSTLPMNRN PLHNEDGLPN NDQYKLYAKH FTLKDKGSPH 
      1210       1220       1230       1240       1250
SEGSDRYRQN STHCRSCLSN LPTYSGHFTM RSPFKCDACL RMGNLYDIDE 
      1260       1270       1280       1290       1300
DQMLQETGNP ATREEVYQQD WSQNNALQFQ KNKLRINRQH SYDNILDKPR 
      1310       1320       1330       1340       1350
EIDLSRPSRS ISLKDRERLL EGNLYGSLFS VPSSKLLGNK SSLFPQGLED 
      1360       1370       1380       1390       1400
SKRSKSLLPD HASDNPFLHT YGDDQRLVIG RCPSDPYKHS LPSQAVNDSY 
      1410       1420       1430       1440       1450
LRSSLRSTAS YCSRDSRGHS DVYISEHVMP YAANKNTMYS TPRVLNSCSN 
      1460 
RRVYKKMPSI ESDV                                  

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	246 – 246	1	L → F in BAA02498 (PubMed:8428958).Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	758 – 758	1	S → T in BAA02498 (PubMed:8428958).Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	758 – 758	1	S → T in AAB58801 (Ref. 4) Curated
<p>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><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	990 – 990	1	E → D in AAB58801 (Ref. 4) Curated

Sequence databases

Genome annotation databases

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

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/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

Documents

1. PDB cross-references
   Index of Protein Data Bank (PDB) cross-references
2. SIMILARITY comments
   Index of protein domains and families

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ