Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 173 (13 Feb 2019)
Sequence version 2 (07 Nov 2003)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Potassium voltage-gated channel subfamily D member 2

Gene

KCND2

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>

<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

Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for action potentials. It regulates neuronal excitability, prolongs the latency before the first spike in a series of action potentials, regulates the frequency of repetitive action potential firing, shortens the duration of action potentials and regulates the back-propagation of action potentials from the neuronal cell body to the dendrites. Contributes to the regulation of the circadian rhythm of action potential firing in suprachiasmatic nucleus neurons, which regulates the circadian rhythm of locomotor activity (By similarity). Functions downstream of the metabotropic glutamate receptor GRM5 and plays a role in neuronal excitability and in nociception mediated by activation of GRM5 (By similarity). Mediates the transient outward current I(to) in rodent heart left ventricle apex cells, but not in human heart, where this current is mediated by another family member. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient (PubMed:10551270, PubMed:15454437, PubMed:14695263, PubMed:14623880, PubMed:14980201, PubMed:16934482, PubMed:24811166, PubMed:24501278). The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:11507158). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCND2 and KCND3; channel properties depend on the type of pore-forming alpha subunits that are part of the channel. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes. Interaction with specific isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression at the cell surface and thereby increases channel activity; it modulates the kinetics of channel activation and inactivation, shifts the threshold for channel activation to more negative voltage values, shifts the threshold for inactivation to less negative voltages and accelerates recovery after inactivation (PubMed:15454437, PubMed:14623880, PubMed:14980201, PubMed:19171772, PubMed:24501278, PubMed:24811166). Likewise, interaction with DPP6 or DPP10 promotes expression at the cell membrane and regulates both channel characteristics and activity (By similarity).By similarity11 Publications

Miscellaneous

The transient neuronal A-type potassium current called I(SA) is triggered at membrane potentials that are below the threshold for action potentials. It inactivates rapidly and recovers rapidly from inactivation. It regulates the firing of action potentials and plays a role in synaptic integration and plasticity. Potassium channels containing KCND2 account for about 80% of the neuronal A-type potassium current. In contrast, the potassium channel responsible for the cardiac I(to) current differs between species; it is mediated by KCND2 in rodents. In human and other non-rodents KCND3 may play an equivalent role.2 Publications1 Publication
Is specifically and reversibly inhibited by the scorpion toxin Ts8 (AC P69940).By similarity

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Homotetrameric channels activate rapidly, i.e within a few msec. After that, they inactivate rapidly, i.e within about 50-100 msec. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system and the presence or absence of ancillary subunits. Homotetrameric channels have a unitary conductance of about 4 pS when expressed in a heterologous system. For the activation of homotetrameric channels expressed in xenopus oocytes, the voltage at half-maximal amplitude is about -10 mV. The time constant for inactivation is about 20 msec. For inactivation, the voltage at half-maximal amplitude is -62 mV. The time constant for recovery after inactivation is about 70 msec.2 Publications

      Sites

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi105Zinc; via pros nitrogenBy similarity1
      Metal bindingi132ZincBy similarity1
      Metal bindingi133ZincBy similarity1

      <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

      • A-type (transient outward) potassium channel activity Source: UniProtKB
      • metal ion binding Source: UniProtKB-KW
      • voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential Source: GO_Central
      • voltage-gated potassium channel activity Source: UniProtKB

      GO - Biological processi

      <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

      Molecular functionIon channel, Potassium channel, Voltage-gated channel
      Biological processIon transport, Potassium transport, Transport
      LigandMetal-binding, Potassium, Zinc

      Enzyme and pathway databases

      Reactome - a knowledgebase of biological pathways and processes

      More...
      Reactomei
      R-HSA-1296072 Voltage gated Potassium channels
      R-HSA-5576894 Phase 1 - inactivation of fast Na+ channels

      Protein family/group databases

      Transport Classification Database

      More...
      TCDBi
      1.A.1.2.5 the voltage-gated ion channel (vic) superfamily

      <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:
      Potassium voltage-gated channel subfamily D member 2
      Alternative name(s):
      Voltage-gated potassium channel subunit Kv4.2
      <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:KCND2
      Synonyms:KIAA1044
      <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>OrganismiHomo 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 identifieri9606 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      <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
      • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 7

      Organism-specific databases

      Eukaryotic Pathogen Database Resources

      More...
      EuPathDBi
      HostDB:ENSG00000184408.9

      Human Gene Nomenclature Database

      More...
      HGNCi
      HGNC:6238 KCND2

      Online Mendelian Inheritance in Man (OMIM)

      More...
      MIMi
      605410 gene

      neXtProt; the human protein knowledge platform

      More...
      neXtProti
      NX_Q9NZV8

      <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

      Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

      Topology

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 182CytoplasmicBy similarityAdd BLAST182
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section 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><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei183 – 204Helical; Name=Segment S1By similarityAdd BLAST22
      Topological domaini205 – 228ExtracellularBy similarityAdd BLAST24
      Transmembranei229 – 250Helical; Name=Segment S2By similarityAdd BLAST22
      Topological domaini251 – 261CytoplasmicBy similarityAdd BLAST11
      Transmembranei262 – 279Helical; Name=Segment S3By similarityAdd BLAST18
      Topological domaini280 – 286ExtracellularBy similarity7
      Transmembranei287 – 306Helical; Voltage-sensor; Name=Segment S4By similarityAdd BLAST20
      Topological domaini307 – 321CytoplasmicBy similarityAdd BLAST15
      Transmembranei322 – 343Helical; Name=Segment S5By similarityAdd BLAST22
      Topological domaini344 – 357ExtracellularBy similarityAdd BLAST14
      <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a region that is buried within a membrane, but does not cross it.<p><a href='/help/intramem' target='_top'>More...</a></p>Intramembranei358 – 369Helical; Name=Pore helixBy similarityAdd BLAST12
      Intramembranei370 – 377By similarity8
      Topological domaini378 – 384ExtracellularBy similarity7
      Transmembranei385 – 413Helical; Name=Segment S6By similarityAdd BLAST29
      Topological domaini414 – 630CytoplasmicBy similarityAdd BLAST217

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse

      <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

      KNCD2 mutations have been found in a family with autism and epilepsy and may play a role in disease pathogenesis. Autism is a complex multifactorial, pervasive developmental disorder characterized by impairments in reciprocal social interaction and communication, restricted and stereotyped patterns of interests and activities, and the presence of developmental abnormalities by 3 years of age. Epilepsy is characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system.1 Publication
      A KCND2 mutation leading to the production of a C-terminally truncated protein has been identified in a patient with epilepsy. Epilepsy is characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system.1 Publication

      Mutagenesis

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi309G → A: Increases peak current amplitude and causes a negative shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi311R → A: No effect on peak current amplitude, but causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi312I → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi313L → A: Causes a positive shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi314G → A: Loss of channel activity. 1 Publication1
      Mutagenesisi315Y → A: Increases peak current amplitude but has a minor effect on the voltage-dependence of activation. 1 Publication1
      Mutagenesisi316T → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi317L → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi318K → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi319S → A: May impair protein folding. 1 Publication1
      Mutagenesisi320C → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. 1 Publication1
      Mutagenesisi320C → S: Increases peak current amplitude and slows the onset of inactivation at low voltage, but has no effect on the voltage-dependence of activation. 1 Publication1
      Mutagenesisi322S → A: Increases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi323E → A: Slightly increases peak current amplitude and causes a negative shift in the voltage-dependence of activation. May decrease the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi324L → A: May impair protein folding. 1 Publication1
      Mutagenesisi327L → A: Loss of channel activity. 1 Publication1
      Mutagenesisi328L → A: May impair protein folding. 1 Publication1
      Mutagenesisi329F → A: Loss of channel activity. 1 Publication1
      Mutagenesisi397V → A: May impair protein folding. 1 Publication1
      Mutagenesisi398I → A: Loss of channel activity. 1 Publication1
      Mutagenesisi399A → V: May impair protein folding. 1 Publication1
      Mutagenesisi401P → A: May impair protein folding. 1 Publication1
      Mutagenesisi402 – 404VPV → IPI: Increases pak current amplitude and causes a positive shift in the voltage-dependence of activation and steady-state inactivation. May increase the affinity for the closed-inactivated state of the channel. 1 Publication3
      Mutagenesisi403P → A: Loss of channel activity. 1 Publication1
      Mutagenesisi405I → A: Loss of channel activity. 1 Publication1
      Mutagenesisi406V → A: Loss of channel activity. 1 Publication1
      Mutagenesisi407S → A: Increases peak current amplitude but has no effect on the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi408N → A: Decreases peak current amplitude and causes a positive shift in the voltage-dependence of activation. May increase the affinity for the closed-inactivated state of the channel. 1 Publication1
      Mutagenesisi409F → A: May impair protein folding. 1 Publication1
      Mutagenesisi601 – 604PTPP → ATAA: Abolishes interaction with FLNC. 1 Publication4

      Keywords - Diseasei

      Autism, Autism spectrum disorder, Disease mutation, Epilepsy

      Organism-specific databases

      DisGeNET

      More...
      DisGeNETi
      3751

      GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

      More...
      GeneReviewsi
      KCND2

      Open Targets

      More...
      OpenTargetsi
      ENSG00000184408

      The Pharmacogenetics and Pharmacogenomics Knowledge Base

      More...
      PharmGKBi
      PA30030

      Chemistry databases

      ChEMBL database of bioactive drug-like small molecules

      More...
      ChEMBLi
      CHEMBL5885

      Drug and drug target database

      More...
      DrugBanki
      DB00321 Amitriptyline
      DB06637 Dalfampridine
      DB00280 Disopyramide
      DB00458 Imipramine

      Polymorphism and mutation databases

      BioMuta curated single-nucleotide variation and disease association database

      More...
      BioMutai
      KCND2

      Domain mapping of disease mutations (DMDM)

      More...
      DMDMi
      38258257

      <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 keyPosition(s)DescriptionActionsGraphical viewLength
      <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_00000540641 – 630Potassium voltage-gated channel subfamily D member 2Add BLAST630

      Amino acid modifications

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <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 residuei38PhosphothreonineBy similarity1
      Modified residuei438PhosphoserineBy similarity1
      Modified residuei548PhosphoserineBy similarity1
      Modified residuei552PhosphoserineBy similarity1
      Modified residuei572PhosphoserineBy similarity1
      Modified residuei575PhosphoserineBy similarity1
      Modified residuei602PhosphothreonineBy similarity1
      Modified residuei607PhosphothreonineBy similarity1
      Modified residuei616PhosphoserineBy similarity1

      <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

      Phosphorylation at Ser-438 in response to MAPK activation is increased in stimulated dendrites. Interaction with KCNIP2 and DPP6 propomtes phosphorylation by PKA at Ser-552. Phosphorylation at Ser-552 has no effect on interaction with KCNIP3, but is required for the regulation of channel activity by KCNIP3. Phosphorylation at Ser-552 leads to KCND2 internalization (By similarity). Phosphorylated by MAPK in response to signaling via the metabotropic glutamate receptor GRM5 (By similarity). Phosphorylation at Ser-616 is required for the down-regulation of neuronal A-type currents in response to signaling via GRM5 (By similarity).By similarity

      Keywords - PTMi

      Phosphoprotein

      Proteomic databases

      Encyclopedia of Proteome Dynamics

      More...
      EPDi
      Q9NZV8

      PaxDb, a database of protein abundance averages across all three domains of life

      More...
      PaxDbi
      Q9NZV8

      PeptideAtlas

      More...
      PeptideAtlasi
      Q9NZV8

      PRoteomics IDEntifications database

      More...
      PRIDEi
      Q9NZV8

      ProteomicsDB human proteome resource

      More...
      ProteomicsDBi
      83521

      PTM databases

      iPTMnet integrated resource for PTMs in systems biology context

      More...
      iPTMneti
      Q9NZV8

      Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

      More...
      PhosphoSitePlusi
      Q9NZV8

      <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

      <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

      Detected in ovary, in corpus luteum and in granulosa and theca cells in the follicle (at protein level) (PubMed:15991246). Highly expressed throughout the brain (PubMed:10551270, PubMed:10729221). Detected in amygdala, caudate nucleus, cerebellum, hippocampus, substantia nigra and thalamus (PubMed:10551270, PubMed:10729221). Expression is not detectable or very low in heart, kidney, liver, lung, pancreas and skeletal muscle (PubMed:10551270, PubMed:10729221). Not detectable in human heart atrium (PubMed:12395204).4 Publications

      Gene expression databases

      Bgee dataBase for Gene Expression Evolution

      More...
      Bgeei
      ENSG00000184408 Expressed in 133 organ(s), highest expression level in caudate nucleus

      ExpressionAtlas, Differential and Baseline Expression

      More...
      ExpressionAtlasi
      Q9NZV8 baseline and differential

      Genevisible search portal to normalized and curated expression data from Genevestigator

      More...
      Genevisiblei
      Q9NZV8 HS

      Organism-specific databases

      Human Protein Atlas

      More...
      HPAi
      HPA029068

      <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

      Homotetramer or heterotetramer with KCND1 or KCND3 (PubMed:14980201, PubMed:16934482, PubMed:24811166). Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 (PubMed:10676964, PubMed:11287421, PubMed:11847232, PubMed:12451113, PubMed:15358149, PubMed:14623880, PubMed:14980201, PubMed:14980207, PubMed:24811166). In vivo, probably exists as heteromeric complex containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19171772). The tetrameric channel can associate with up to four regulatory subunits, such as KCNIP2 or KCNIP4 (PubMed:14623880, PubMed:14980201, PubMed:24811166). Interaction with four KCNIP4 chains does not reduce interaction with DPP10 (PubMed:24811166). Interacts with DLG4 and NCS1/FREQ (By similarity). Interacts with DLG1 (PubMed:19213956). Probably part of a complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (PubMed:15358149). Interacts with FLNA, FLNC, DPP6 and DPP10 (PubMed:11102480, PubMed:15454437, PubMed:24811166).By similarity1 Publication13 Publications

      <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

      Protein-protein interaction databases

      The Biological General Repository for Interaction Datasets (BioGrid)

      More...
      BioGridi
      109953, 18 interactors

      ComplexPortal: manually curated resource of macromolecular complexes

      More...
      ComplexPortali
      CPX-3239 Kv4.2-KChIP2 channel complex

      CORUM comprehensive resource of mammalian protein complexes

      More...
      CORUMi
      Q9NZV8

      Protein interaction database and analysis system

      More...
      IntActi
      Q9NZV8, 2 interactors

      STRING: functional protein association networks

      More...
      STRINGi
      9606.ENSP00000333496

      <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

      3D structure databases

      Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

      More...
      ProteinModelPortali
      Q9NZV8

      SWISS-MODEL Repository - a database of annotated 3D protein structure models

      More...
      SMRi
      Q9NZV8

      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

      Region

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <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>Regioni2 – 20Interaction with KCNIP1, KCNIP2, and other family membersBy similarityAdd BLAST19
      Regioni71 – 90Interaction with KCNIP1By similarityAdd BLAST20
      Regioni308 – 321S4-S5 linkerBy similarityAdd BLAST14
      Regioni474 – 630Important for normal channel activation and inactivation, for interaction with KCNIP2, and probably other family members as wellBy similarity1 PublicationAdd BLAST157
      Regioni474 – 489Required for dendritic targetingBy similarityAdd BLAST16

      Motif

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi370 – 375Selectivity filterBy similarity6
      Motifi627 – 630PDZ-bindingBy similarity4

      <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

      The transmembrane segment S4 functions as voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Channel opening and closing is effected by a conformation change that affects the position and orientation of the voltage-sensor paddle formed by S3 and S4 within the membrane. A transmembrane electric field that is positive inside would push the positively charged S4 segment outwards, thereby opening the pore, while a field that is negative inside would pull the S4 segment inwards and close the pore. Changes in the position and orientation of S4 are then transmitted to the activation gate formed by the inner helix bundle via the S4-S5 linker region.By similarity
      The N-terminal cytoplasmic region can mediate N-type inactivation by physically blocking the channel (PubMed:14695263). This probably does not happen in vivo, where the N-terminal region mediates interaction with regulatory subunits, such as KCNIP1 and KCNIP2 (PubMed:15358149). The zinc binding sites in the N-terminal domain are important for tetramerization and assembly of a functional channel complex (By similarity). Most likely, the channel undergoes closed-state inactivation, where a subtle conformation change would render the protein less sensitive to activation.By similarity4 Publications
      The C-terminal cytoplasmic region is important for normal expression at the cell membrane and modulates the voltage-dependence of channel activation and inactivation (PubMed:16934482). It is required for interaction with KCNIP2, and probably other family members as well (By similarity).By similarity1 Publication

      <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      evolutionary genealogy of genes: Non-supervised Orthologous Groups

      More...
      eggNOGi
      KOG4390 Eukaryota
      COG1226 LUCA

      Ensembl GeneTree

      More...
      GeneTreei
      ENSGT00940000155472

      The HOVERGEN Database of Homologous Vertebrate Genes

      More...
      HOVERGENi
      HBG106687

      InParanoid: Eukaryotic Ortholog Groups

      More...
      InParanoidi
      Q9NZV8

      KEGG Orthology (KO)

      More...
      KOi
      K04892

      Identification of Orthologs from Complete Genome Data

      More...
      OMAi
      GIQFQTW

      Database of Orthologous Groups

      More...
      OrthoDBi
      469107at2759

      Database for complete collections of gene phylogenies

      More...
      PhylomeDBi
      Q9NZV8

      TreeFam database of animal gene trees

      More...
      TreeFami
      TF313103

      Family and domain databases

      Gene3D Structural and Functional Annotation of Protein Families

      More...
      Gene3Di
      1.20.120.350, 1 hit

      Integrated resource of protein families, domains and functional sites

      More...
      InterProi
      View protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003975 K_chnl_volt-dep_Kv4
      IPR004055 K_chnl_volt-dep_Kv4.2
      IPR024587 K_chnl_volt-dep_Kv4_C
      IPR021645 Shal-type_N
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf

      The PANTHER Classification System

      More...
      PANTHERi
      PTHR11537 PTHR11537, 1 hit

      Pfam protein domain database

      More...
      Pfami
      View protein in Pfam
      PF02214 BTB_2, 1 hit
      PF11879 DUF3399, 1 hit
      PF00520 Ion_trans, 1 hit
      PF11601 Shal-type, 1 hit

      Protein Motif fingerprint database; a protein domain database

      More...
      PRINTSi
      PR00169 KCHANNEL
      PR01517 KV42CHANNEL
      PR01491 KVCHANNEL
      PR01497 SHALCHANNEL

      Simple Modular Architecture Research Tool; a protein domain database

      More...
      SMARTi
      View protein in SMART
      SM00225 BTB, 1 hit

      Superfamily database of structural and functional annotation

      More...
      SUPFAMi
      SSF54695 SSF54695, 1 hit

      <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>Sequence (1+)i

      <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.

      This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

      Q9NZV8-1 [UniParc]FASTAAdd to basket
      « Hide
              10         20         30         40         50
      MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT
      60 70 80 90 100
      RFQTWQDTLE RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR
      110 120 130 140 150
      TGKLHYPRHE CISAYDEELA FFGLIPEIIG DCCYEEYKDR RRENAERLQD
      160 170 180 190 200
      DADTDTAGES ALPTMTARQR VWRAFENPHT STMALVFYYV TGFFIAVSVI
      210 220 230 240 250
      ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF TVEYLLRLAA
      260 270 280 290 300
      APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
      310 320 330 340 350
      FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS
      360 370 380 390 400
      ASKFTSIPAA FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL
      410 420 430 440 450
      PVPVIVSNFS RIYHQNQRAD KRRAQKKARL ARIRAAKSGS ANAYMQSKRN
      460 470 480 490 500
      GLLSNQLQSS EDEQAFVSKS GSSFETQHHH LLHCLEKTTN HEFVDEQVFE
      510 520 530 540 550
      ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKTFRI PNANVSGSHQ
      560 570 580 590 600
      GSIQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
      610 620 630
      PTPPVTTPEG DDRPESPEYS GGNIVRVSAL
      Length:630
      Mass (Da):70,537
      Last modified:November 7, 2003 - v2
      <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:i0C11E62FFA220421
      GO

      <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

      There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
      EntryEntry nameProtein names
      Gene namesLengthAnnotation
      H7C445H7C445_HUMAN
      Potassium voltage-gated channel sub...
      KCND2
      177Annotation score:

      Annotation score:1 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>

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

      The sequence BAA82996 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

      Experimental Info

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <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 conflicti450N → S in AAD22053 (PubMed:9843794).Curated1
      Sequence conflicti464Q → P in AAD22053 (PubMed:9843794).Curated1
      Sequence conflicti550Q → R in AAD22053 (PubMed:9843794).Curated1
      Sequence conflicti553I → V in AAD22053 (PubMed:9843794).Curated1

      Natural variant

      Feature keyPosition(s)DescriptionActionsGraphical viewLength
      <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_072076404V → M Probable disease-associated mutation found in a family with atypical autism and severe epilepsy; disrupts potassium current inactivation. 1 PublicationCorresponds to variant dbSNP:rs587777631EnsemblClinVar.1

      Sequence databases

      Select the link destinations:

      EMBL nucleotide sequence database

      More...
      EMBLi

      GenBank nucleotide sequence database

      More...
      GenBanki

      DNA Data Bank of Japan; a nucleotide sequence database

      More...
      DDBJi
      Links Updated
      AF121104 mRNA Translation: AAD22053.1
      AB028967 mRNA Translation: BAA82996.2 Different initiation.
      AJ010969 mRNA Translation: CAB56841.1
      AF166008, AF166007 Genomic DNA Translation: AAF65618.1
      AC004888 Genomic DNA Translation: AAC83405.1
      AC004946 Genomic DNA No translation available.
      AF142568 Genomic DNA Translation: AAD52159.1
      BC110449 mRNA Translation: AAI10450.1
      BC110450 mRNA Translation: AAI10451.1

      The Consensus CDS (CCDS) project

      More...
      CCDSi
      CCDS5776.1

      NCBI Reference Sequences

      More...
      RefSeqi
      NP_036413.1, NM_012281.2

      UniGene gene-oriented nucleotide sequence clusters

      More...
      UniGenei
      Hs.654739

      Genome annotation databases

      Ensembl eukaryotic genome annotation project

      More...
      Ensembli
      ENST00000331113; ENSP00000333496; ENSG00000184408

      Database of genes from NCBI RefSeq genomes

      More...
      GeneIDi
      3751

      KEGG: Kyoto Encyclopedia of Genes and Genomes

      More...
      KEGGi
      hsa:3751

      UCSC genome browser

      More...
      UCSCi
      uc003vjj.2 human

      <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

      <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:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF121104 mRNA Translation: AAD22053.1
      AB028967 mRNA Translation: BAA82996.2 Different initiation.
      AJ010969 mRNA Translation: CAB56841.1
      AF166008, AF166007 Genomic DNA Translation: AAF65618.1
      AC004888 Genomic DNA Translation: AAC83405.1
      AC004946 Genomic DNA No translation available.
      AF142568 Genomic DNA Translation: AAD52159.1
      BC110449 mRNA Translation: AAI10450.1
      BC110450 mRNA Translation: AAI10451.1
      CCDSiCCDS5776.1
      RefSeqiNP_036413.1, NM_012281.2
      UniGeneiHs.654739

      3D structure databases

      ProteinModelPortaliQ9NZV8
      SMRiQ9NZV8
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi109953, 18 interactors
      ComplexPortaliCPX-3239 Kv4.2-KChIP2 channel complex
      CORUMiQ9NZV8
      IntActiQ9NZV8, 2 interactors
      STRINGi9606.ENSP00000333496

      Chemistry databases

      ChEMBLiCHEMBL5885
      DrugBankiDB00321 Amitriptyline
      DB06637 Dalfampridine
      DB00280 Disopyramide
      DB00458 Imipramine

      Protein family/group databases

      TCDBi1.A.1.2.5 the voltage-gated ion channel (vic) superfamily

      PTM databases

      iPTMnetiQ9NZV8
      PhosphoSitePlusiQ9NZV8

      Polymorphism and mutation databases

      BioMutaiKCND2
      DMDMi38258257

      Proteomic databases

      EPDiQ9NZV8
      PaxDbiQ9NZV8
      PeptideAtlasiQ9NZV8
      PRIDEiQ9NZV8
      ProteomicsDBi83521

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENST00000331113; ENSP00000333496; ENSG00000184408
      GeneIDi3751
      KEGGihsa:3751
      UCSCiuc003vjj.2 human

      Organism-specific databases

      Comparative Toxicogenomics Database

      More...
      CTDi
      3751
      DisGeNETi3751
      EuPathDBiHostDB:ENSG00000184408.9

      GeneCards: human genes, protein and diseases

      More...
      GeneCardsi
      KCND2
      GeneReviewsiKCND2
      HGNCiHGNC:6238 KCND2
      HPAiHPA029068
      MIMi605410 gene
      neXtProtiNX_Q9NZV8
      OpenTargetsiENSG00000184408
      PharmGKBiPA30030

      Human Unidentified Gene-Encoded large proteins database

      More...
      HUGEi
      Search...

      GenAtlas: human gene database

      More...
      GenAtlasi
      Search...

      Phylogenomic databases

      eggNOGiKOG4390 Eukaryota
      COG1226 LUCA
      GeneTreeiENSGT00940000155472
      HOVERGENiHBG106687
      InParanoidiQ9NZV8
      KOiK04892
      OMAiGIQFQTW
      OrthoDBi469107at2759
      PhylomeDBiQ9NZV8
      TreeFamiTF313103

      Enzyme and pathway databases

      ReactomeiR-HSA-1296072 Voltage gated Potassium channels
      R-HSA-5576894 Phase 1 - inactivation of fast Na+ channels

      Miscellaneous databases

      ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

      More...
      ChiTaRSi
      KCND2 human

      The Gene Wiki collection of pages on human genes and proteins

      More...
      GeneWikii
      KCND2

      Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

      More...
      GenomeRNAii
      3751

      Protein Ontology

      More...
      PROi
      PR:Q9NZV8

      The Stanford Online Universal Resource for Clones and ESTs

      More...
      SOURCEi
      Search...

      Gene expression databases

      BgeeiENSG00000184408 Expressed in 133 organ(s), highest expression level in caudate nucleus
      ExpressionAtlasiQ9NZV8 baseline and differential
      GenevisibleiQ9NZV8 HS

      Family and domain databases

      Gene3Di1.20.120.350, 1 hit
      InterProiView protein in InterPro
      IPR000210 BTB/POZ_dom
      IPR005821 Ion_trans_dom
      IPR003968 K_chnl_volt-dep_Kv
      IPR003975 K_chnl_volt-dep_Kv4
      IPR004055 K_chnl_volt-dep_Kv4.2
      IPR024587 K_chnl_volt-dep_Kv4_C
      IPR021645 Shal-type_N
      IPR011333 SKP1/BTB/POZ_sf
      IPR003131 T1-type_BTB
      IPR028325 VG_K_chnl
      IPR027359 Volt_channel_dom_sf
      PANTHERiPTHR11537 PTHR11537, 1 hit
      PfamiView protein in Pfam
      PF02214 BTB_2, 1 hit
      PF11879 DUF3399, 1 hit
      PF00520 Ion_trans, 1 hit
      PF11601 Shal-type, 1 hit
      PRINTSiPR00169 KCHANNEL
      PR01517 KV42CHANNEL
      PR01491 KVCHANNEL
      PR01497 SHALCHANNEL
      SMARTiView protein in SMART
      SM00225 BTB, 1 hit
      SUPFAMiSSF54695 SSF54695, 1 hit

      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 nameiKCND2_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>AccessioniPrimary (citable) accession number: Q9NZV8
      Secondary accession number(s): O95012
      , O95021, Q2TBD3, Q9UBY7, Q9UN98, Q9UNH9
      <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 historyiIntegrated into UniProtKB/Swiss-Prot: November 7, 2003
      Last sequence update: November 7, 2003
      Last modified: February 13, 2019
      This is version 173 of the entry and version 2 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 statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program
      DisclaimerAny 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

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. SIMILARITY comments
        Index of protein domains and families
      2. Human chromosome 7
        Human chromosome 7: entries, gene names and cross-references to MIM
      3. Human polymorphisms and disease mutations
        Index of human polymorphisms and disease mutations
      4. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      5. Human entries with polymorphisms or disease mutations
        List of human entries with polymorphisms or disease mutations
      UniProt is an ELIXIR core data resource
      Main funding by: National Institutes of Health

      We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

      Do not show this banner again