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Q9UK17 (KCND3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium voltage-gated channel subfamily D member 3
Alternative name(s):
Voltage-gated potassium channel subunit Kv4.3
Gene names
Name:KCND3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length655 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Pore-forming (alpha) subunit of voltage-gated rapidly inactivating A-type potassium channels. May contribute to I(To) current in heart and I(Sa) current in neurons. Channel properties are modulated by interactions with other alpha subunits and with regulatory subunits. Ref.1 Ref.2

Subunit structure

Homotetramer or heterotetramer with KCND1 and/or KCND2. Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4 By similarity. Interacts with KCNE1, KCNE2, SCN1B and KCNAB1 and DLG1. Ref.8 Ref.9 Ref.11 Ref.12

Subcellular location

Membrane; Multi-pass membrane protein. Cell membranesarcolemma By similarity. Cell projectiondendrite By similarity.

Tissue specificity

Highly expressed in heart and brain, in particular in cortex, cerebellum, amygdala and caudate nucleus. Detected at lower levels in liver, skeletal muscle, kidney and pancreas. Isoform 1 predominates in most tissues. Isoform 1 and isoform 2 are detected at similar levels in brain, skeletal muscle and pancreas. Ref.1 Ref.2 Ref.4

Domain

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.

Post-translational modification

Regulated through phosphorylation at Ser-569 by CaMK2D By similarity.

Involvement in disease

Spinocerebellar ataxia 19 (SCA19) [MIM:607346]: A form of spinocerebellar ataxia, a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA19 is a relatively mild, cerebellar ataxic syndrome with cognitive impairment, pyramidal tract involvement, tremor and peripheral neuropathy, and mild atrophy of the cerebellar hemispheres and vermis.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15

KCND3 rare variants may confer risk for lethal ventricular arrhytmias and be associated with autopsy-negative sudden unexplained death syndrome (SUDS). Ref.10

Sequence similarities

Belongs to the potassium channel family. D (Shal) (TC 1.A.1.2) subfamily. Kv4.3/KCND3 sub-subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Potassium transport
Transport
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Neurodegeneration
Spinocerebellar ataxia
   DomainTransmembrane
Transmembrane helix
   LigandMetal-binding
Potassium
Zinc
   Molecular functionIon channel
Potassium channel
Voltage-gated channel
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell death

Inferred from electronic annotation. Source: UniProtKB-KW

membrane repolarization

Inferred from direct assay PubMed 21493962. Source: BHF-UCL

potassium ion export

Inferred from direct assay PubMed 21493962. Source: BHF-UCL

potassium ion transport

Traceable author statement PubMed 8734615. Source: ProtInc

protein homooligomerization

Inferred from electronic annotation. Source: InterPro

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentdendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

perinuclear endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

sarcolemma

Inferred from electronic annotation. Source: UniProtKB-SubCell

voltage-gated potassium channel complex

Inferred from direct assay PubMed 21493962. Source: BHF-UCL

   Molecular_functionA-type (transient outward) potassium channel activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

ion channel binding

Inferred from physical interaction PubMed 21493962. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UK17-1)

Also known as: KCND3L; Long;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9UK17-2)

Also known as: KCND3S; Short;

The sequence of this isoform differs from the canonical sequence as follows:
     488-506: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 655655Potassium voltage-gated channel subfamily D member 3
PRO_0000054068

Regions

Topological domain1 – 181181Cytoplasmic Potential
Transmembrane182 – 20221Helical; Name=Segment S1; Potential
Transmembrane222 – 24221Helical; Name=Segment S2; Potential
Topological domain243 – 25614Cytoplasmic Potential
Transmembrane257 – 27721Helical; Name=Segment S3; Potential
Transmembrane287 – 30721Helical; Voltage-sensor; Name=Segment S4; Potential
Topological domain308 – 32013Cytoplasmic Potential
Transmembrane321 – 34121Helical; Name=Segment S5; Potential
Intramembrane360 – 38021Pore-forming; Name=Segment H5; Potential
Transmembrane382 – 40221Helical; Name=Segment S6; Potential
Topological domain403 – 655253Cytoplasmic Potential
Region2 – 2019Interaction with KCNIP2 By similarity
Region472 – 48716Mediates dendritic targeting By similarity
Motif367 – 3726Selectivity filter By similarity

Sites

Metal binding1041Zinc
Metal binding1311Zinc
Metal binding1321Zinc

Amino acid modifications

Modified residue5691Phosphoserine; by CaMK2D By similarity

Natural variations

Alternative sequence488 – 50619Missing in isoform 2.
VSP_008826
Natural variant941V → M in a colorectal cancer sample; somatic mutation. Ref.13
VAR_035775
Natural variant2271Missing in SCA19; results in reduced channel activity consistent with impaired cell surface expression of the mutant protein. Ref.14
VAR_070785
Natural variant3381V → E in SCA19. Ref.14
VAR_070786
Natural variant3451G → V in SCA19. Ref.14
VAR_070787
Natural variant3521T → P in SCA19; loss of channel activity. Ref.15
VAR_070788
Natural variant3731M → I in SCA19; causes reduced channel activity. Ref.15
VAR_070789
Natural variant3771T → M in SCA19. Ref.14
VAR_070790
Natural variant3901S → N in SCA19; results in impaired cell surface expression. Ref.15
VAR_070791
Natural variant3921V → I Probable disease-associated mutation found in a case of sudden unexplained death syndrome; gain of function. Ref.10
VAR_067694
Natural variant5301S → R Rare variant found in a case of sudden infant death; does not affect the electrophysiological properties of the channel. Ref.10
VAR_067695
Natural variant6001G → R Probable disease-associated mutation found in a case of sudden unexplained death syndrome; gain of function. Ref.10
Corresponds to variant rs149344567 [ dbSNP | Ensembl ].
VAR_067696

Experimental info

Sequence conflict2391V → G in AAC05121. Ref.1
Sequence conflict2391V → G in AAC05122. Ref.1
Sequence conflict2391V → G in AAD38898. Ref.4
Sequence conflict3751P → L in AAC05121. Ref.1
Sequence conflict3751P → L in AAC05122. Ref.1
Sequence conflict3751P → L in AAD38898. Ref.4
Sequence conflict4081R → G in AAF01044. Ref.2
Sequence conflict4081R → G in AAF01045. Ref.2
Sequence conflict4521E → G in AAF01044. Ref.2
Sequence conflict4521E → G in AAF01045. Ref.2
Sequence conflict5311T → Q in AAF01044. Ref.2
Sequence conflict5311T → Q in AAF01045. Ref.2
Sequence conflict5641A → D in AAF01044. Ref.2
Sequence conflict5641A → D in AAF01045. Ref.2
Sequence conflict6461A → T in AAC05121. Ref.1
Sequence conflict6461A → T in AAC05122. Ref.1
Sequence conflict6461A → T in AAF01045. Ref.2
Sequence conflict6461A → T in AAD38898. Ref.4
Sequence conflict6541A → V in AAC05121. Ref.1
Sequence conflict6541A → V in AAC05122. Ref.1
Sequence conflict6541A → V in AAF01044. Ref.2
Sequence conflict6541A → V in AAD38898. Ref.4

Secondary structure

............................. 655
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (KCND3L) (Long) [UniParc].

Last modified March 7, 2006. Version 3.
Checksum: ADD1402A97204764

FASTA65573,451
        10         20         30         40         50         60 
MAAGVAAWLP FARAAAIGWM PVANCPMPLA PADKNKRQDE LIVLNVSGRR FQTWRTTLER 

        70         80         90        100        110        120 
YPDTLLGSTE KEFFFNEDTK EYFFDRDPEV FRCVLNFYRT GKLHYPRYEC ISAYDDELAF 

       130        140        150        160        170        180 
YGILPEIIGD CCYEEYKDRK RENAERLMDD NDSENNQESM PSLSFRQTMW RAFENPHTST 

       190        200        210        220        230        240 
LALVFYYVTG FFIAVSVITN VVETVPCGTV PGSKELPCGE RYSVAFFCLD TACVMIFTVE 

       250        260        270        280        290        300 
YLLRLFAAPS RYRFIRSVMS IIDVVAIMPY YIGLVMTNNE DVSGAFVTLR VFRVFRIFKF 

       310        320        330        340        350        360 
SRHSQGLRIL GYTLKSCASE LGFLLFSLTM AIIIFATVMF YAEKGSSASK FTSIPASFWY 

       370        380        390        400        410        420 
TIVTMTTLGY GDMVPKTIAG KIFGSICSLS GVLVIALPVP VIVSNFSRIY HQNQRADKRR 

       430        440        450        460        470        480 
AQKKARLARI RVAKTGSSNA YLHSKRNGLL NEALELTGTP EEEHMGKTTS LIESQHHHLL 

       490        500        510        520        530        540 
HCLEKTTGLS YLVDDPLLSV RTSTIKNHEF IDEQMFEQNC MESSMQNYPS TRSPSLSSHP 

       550        560        570        580        590        600 
GLTTTCCSRR SKKTTHLPNS NLPATRLRSM QELSTIHIQG SEQPSLTTSR SSLNLKADDG 

       610        620        630        640        650 
LRPNCKTSQI TTAIISIPTP PALTPEGESR PPPASPGPNT NIPSIASNVV KVSAL 

« Hide

Isoform 2 (KCND3S) (Short) [UniParc].

Checksum: 9414269BB8A53D29
Show »

FASTA63671,392

References

« Hide 'large scale' references
[1]"Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing."
Kong W., Po S., Yamagishi T., Ashen M.D., Stetten G., Tomaselli G.F.
Am. J. Physiol. 275:H1963-H1970(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY, FUNCTION.
Tissue: Heart.
[2]"Cloning and expression of the human Kv4.3 potassium channel."
Dilks D., Ling H.-P., Cockett M., Sokol P., Numann R.
J. Neurophysiol. 81:1974-1977(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY.
Tissue: Brain and Heart.
[3]"Long and short human isoforms of the Kv4.3 channel: cloning, expression, electrophysiology, pharmacology and phosphorylation by protein kinase C."
Calmels T.P.G., Faivre J.-F., Javre J.-L., Cheval B., Rouanet S., Bril A.
Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Heart.
[4]"Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA)."
Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U., Michel U., Sauter K., Pongs O.
Genomics 64:144-154(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
Tissue: Brain cortex.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Heart and Lung.
[8]"Modulation of Kv4.3 current by accessory subunits."
Deschenes I., Tomaselli G.F.
FEBS Lett. 528:183-188(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KCNIP2; KCNE1; KCNE2; SCN1B AND KCNAB1.
[9]"Kv4 potassium channels form a tripartite complex with the anchoring protein SAP97 and CaMKII in cardiac myocytes."
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H., Coulombe A., Jeromin A., Hatem S.N.
Circ. Res. 104:758-769(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DLG1.
[10]"Novel mutations in the KCND3-encoded Kv4.3 K+ channel associated with autopsy-negative sudden unexplained death."
Giudicessi J.R., Ye D., Kritzberger C.J., Nesterenko V.V., Tester D.J., Antzelevitch C., Ackerman M.J.
Hum. Mutat. 33:989-997(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SUDS, VARIANTS ILE-392; ARG-530 AND ARG-600, CHARACTERIZATION OF VARIANTS ILE-392; ARG-530 AND ARG-600.
[11]"Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1."
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W., Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M., Stahl M., Malakian K., Somers W., Mosyak L. expand/collapse author list , Bowlby M.R., Chanda P., Rhodes K.J.
Neuron 41:587-598(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 29-143, INTERACTION WITH KCNIP1.
[12]"Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits."
Wang H., Yan Y., Liu Q., Huang Y., Shen Y., Chen L., Chen Y., Yang Q., Hao Q., Wang K., Chai J.
Nat. Neurosci. 10:32-39(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 6-145 IN COMPLEX WITH KCNIP1, SUBUNIT.
[13]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] MET-94.
[14]"Mutations in KCND3 cause spinocerebellar ataxia type 22."
Lee Y.C., Durr A., Majczenko K., Huang Y.H., Liu Y.C., Lien C.C., Tsai P.C., Ichikawa Y., Goto J., Monin M.L., Li J.Z., Chung M.Y., Mundwiller E., Shakkottai V., Liu T.T., Tesson C., Lu Y.C., Brice A. expand/collapse author list , Tsuji S., Burmeister M., Stevanin G., Soong B.W.
Ann. Neurol. 72:859-869(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCA19 PHE-227 DEL; GLU-338; VAL-345 AND MET-377, CHARACTERIZATION OF VARIANT PHE-227 DEL.
[15]"Mutations in potassium channel kcnd3 cause spinocerebellar ataxia type 19."
Duarri A., Jezierska J., Fokkens M., Meijer M., Schelhaas H.J., den Dunnen W.F., van Dijk F., Verschuuren-Bemelmans C., Hageman G., van de Vlies P., Kusters B., van de Warrenburg B.P., Kremer B., Wijmenga C., Sinke R.J., Swertz M.A., Kampinga H.H., Boddeke E., Verbeek D.S.
Ann. Neurol. 72:870-880(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS SCA19 PRO-352; ILE-373 AND ASN-390, CHARACTERIZATION OF VARIANTS SCA19 PRO-352; ILE-373 AND ASN-390.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF048712 mRNA. Translation: AAC05121.1.
AF048713 mRNA. Translation: AAC05122.1.
AF187963 mRNA. Translation: AAF01044.1.
AF187964 mRNA. Translation: AAF01045.1.
AF205856 mRNA. Translation: AAF20924.1.
AF205857 mRNA. Translation: AAF20925.1.
AF120491 mRNA. Translation: AAD38898.1.
AF166011, AF166009, AF166010 Genomic DNA. Translation: AAF68177.1.
AF166011, AF166009, AF166010 Genomic DNA. Translation: AAF68178.1.
AL512665, AL049557, AL450997 Genomic DNA. Translation: CAI16956.1.
AL450997, AL049557, AL512665 Genomic DNA. Translation: CAI19096.1.
AL049557, AL450997, AL512665 Genomic DNA. Translation: CAI22711.1.
CH471122 Genomic DNA. Translation: EAW56511.1.
BC113475 mRNA. Translation: AAI13476.1.
BC113477 mRNA. Translation: AAI13478.1.
CCDSCCDS843.1. [Q9UK17-1]
CCDS844.1. [Q9UK17-2]
RefSeqNP_004971.2. NM_004980.4. [Q9UK17-1]
NP_751948.1. NM_172198.2. [Q9UK17-2]
XP_005270908.1. XM_005270851.2. [Q9UK17-1]
XP_006710692.1. XM_006710629.1. [Q9UK17-1]
XP_006710693.1. XM_006710630.1. [Q9UK17-2]
UniGeneHs.666367.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1GX-ray2.60A/B29-143[»]
2NZ0X-ray3.20B/D6-145[»]
ProteinModelPortalQ9UK17.
SMRQ9UK17. Positions 6-412.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109954. 33 interactions.
STRING9606.ENSP00000319591.

Chemistry

BindingDBQ9UK17.
ChEMBLCHEMBL1964.

Protein family/group databases

TCDB1.A.1.2.19. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ9UK17.

Polymorphism databases

DMDM92090984.

Proteomic databases

PaxDbQ9UK17.
PRIDEQ9UK17.

Protocols and materials databases

DNASU3752.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302127; ENSP00000306923; ENSG00000171385. [Q9UK17-2]
ENST00000315987; ENSP00000319591; ENSG00000171385. [Q9UK17-1]
ENST00000369697; ENSP00000358711; ENSG00000171385. [Q9UK17-2]
GeneID3752.
KEGGhsa:3752.
UCSCuc001ebu.1. human. [Q9UK17-1]
uc001ebv.1. human.

Organism-specific databases

CTD3752.
GeneCardsGC01M112313.
HGNCHGNC:6239. KCND3.
HPAHPA029452.
MIM605411. gene.
607346. phenotype.
neXtProtNX_Q9UK17.
Orphanet130. Brugada syndrome.
98772. Spinocerebellar ataxia type 19/22.
PharmGKBPA210.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1226.
HOVERGENHBG106687.
InParanoidQ9UK17.
KOK04893.
OMAPEVFRCI.
OrthoDBEOG7SR4MG.
PhylomeDBQ9UK17.
TreeFamTF313103.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ9UK17.
BgeeQ9UK17.
CleanExHS_KCND3.
GenevestigatorQ9UK17.

Family and domain databases

Gene3D1.20.120.350. 1 hit.
3.30.710.10. 1 hit.
InterProIPR000210. BTB/POZ-like.
IPR011333. BTB/POZ_fold.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003968. K_chnl_volt-dep_Kv.
IPR003975. K_chnl_volt-dep_Kv4.
IPR004056. K_chnl_volt-dep_Kv4.3.
IPR024587. K_chnl_volt-dep_Kv4_C.
IPR021645. Shal-type.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERPTHR11537. PTHR11537. 1 hit.
PfamPF02214. BTB_2. 1 hit.
PF11879. DUF3399. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11601. Shal-type. 1 hit.
[Graphical view]
PRINTSPR00169. KCHANNEL.
PR01518. KV43CHANNEL.
PR01491. KVCHANNEL.
PR01497. SHALCHANNEL.
SMARTSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMSSF54695. SSF54695. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9UK17.
GeneWikiKCND3.
GenomeRNAi3752.
NextBio14691.
PROQ9UK17.
SOURCESearch...

Entry information

Entry nameKCND3_HUMAN
AccessionPrimary (citable) accession number: Q9UK17
Secondary accession number(s): O60576 expand/collapse secondary AC list , O60577, Q14D71, Q5T0M0, Q9UH85, Q9UH86, Q9UK16
Entry history
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM