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Protein

Potassium voltage-gated channel subfamily C member 4

Gene

KCNC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This protein mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.

GO - Molecular functioni

  • delayed rectifier potassium channel activity Source: GO_Central
  • potassium channel activity Source: ProtInc
  • voltage-gated potassium channel activity Source: ProtInc

GO - Biological processi

  • potassium ion transport Source: ProtInc
  • protein homooligomerization Source: InterPro
  • regulation of neurotransmitter secretion Source: Ensembl
  • synaptic transmission Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Potassium channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

ReactomeiR-HSA-1296072. Voltage gated Potassium channels.
SIGNORiQ03721.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily C member 4
Alternative name(s):
KSHIIIC
Voltage-gated potassium channel subunit Kv3.4
Gene namesi
Name:KCNC4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6236. KCNC4.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 226226CytoplasmicSequence analysisAdd
BLAST
Transmembranei227 – 24721Helical; Name=Segment S1Sequence analysisAdd
BLAST
Transmembranei278 – 29821Helical; Name=Segment S2Sequence analysisAdd
BLAST
Topological domaini299 – 31214CytoplasmicSequence analysisAdd
BLAST
Transmembranei313 – 33321Helical; Name=Segment S3Sequence analysisAdd
BLAST
Transmembranei345 – 36420Helical; Voltage-sensor; Name=Segment S4Sequence analysisAdd
BLAST
Topological domaini365 – 38016CytoplasmicSequence analysisAdd
BLAST
Transmembranei381 – 40121Helical; Name=Segment S5Sequence analysisAdd
BLAST
Transmembranei452 – 47221Helical; Name=Segment S6Sequence analysisAdd
BLAST
Topological domaini473 – 635163CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • axon terminus Source: Ensembl
  • neuromuscular junction Source: Ensembl
  • plasma membrane Source: Reactome
  • voltage-gated potassium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81S → A: Decreased inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-9. 1 Publication
Mutagenesisi8 – 81S → D: Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-9; D-15 and D-21. 1 Publication
Mutagenesisi9 – 91S → A: Strong decrease of inhibition of channel closure by PKC. Inhibition of channel closure is nearly abolished; when associated with A-8. 1 Publication
Mutagenesisi9 – 91S → D: Decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-15 and D-21. 1 Publication
Mutagenesisi15 – 151S → A: Decreased inhibition of channel closure by PKC. 2 Publications
Mutagenesisi15 – 151S → D: Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-21. 2 Publications
Mutagenesisi21 – 211S → A: Decreased inhibition of channel closure by PKC. 2 Publications
Mutagenesisi21 – 211S → D: Slightly decreased rate of channel inactivation. Loss of channel inactivation; when associated with D-8; D-9 and D-15. 2 Publications

Organism-specific databases

PharmGKBiPA30028.

Chemistry

ChEMBLiCHEMBL2362996.

Polymorphism and mutation databases

BioMutaiKCNC4.
DMDMi66774206.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 635635Potassium voltage-gated channel subfamily C member 4PRO_0000054058Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Phosphoserine1 Publication
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei15 – 151Phosphoserine1 Publication
Modified residuei21 – 211Phosphoserine1 Publication
Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence analysis
Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence analysis

Post-translational modificationi

Phosphorylation of serine residues in the inactivation gate inhibits rapid channel closure.2 Publications

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiQ03721.
PRIDEiQ03721.
TopDownProteomicsiQ03721-3. [Q03721-3]

PTM databases

iPTMnetiQ03721.
PhosphoSiteiQ03721.

Expressioni

Gene expression databases

BgeeiQ03721.
CleanExiHS_KCNC4.
ExpressionAtlasiQ03721. baseline and differential.
GenevisibleiQ03721. HS.

Organism-specific databases

HPAiHPA014740.

Interactioni

Subunit structurei

Homotetramer (Probable). Heterotetramer of potassium channel proteins (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridi109951. 27 interactions.
IntActiQ03721. 1 interaction.
STRINGi9606.ENSP00000358802.

Structurei

Secondary structure

1
635
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 53Combined sources
Beta strandi14 – 163Combined sources
Beta strandi19 – 213Combined sources
Turni26 – 294Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4GNMR-A1-30[»]
1B4INMR-A1-30[»]
1ZTNNMR-A1-30[»]
ProteinModelPortaliQ03721.
SMRiQ03721. Positions 1-30, 35-479.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ03721.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2828Inactivation gateAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi436 – 4416Selectivity filterBy similarity

Domaini

The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position.
The tail may be important in modulation of channel activity and/or targeting of the channel to specific subcellular compartments.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3713. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231012.
HOVERGENiHBG105862.
InParanoidiQ03721.
KOiK04890.
OMAiGCEFFFD.
OrthoDBiEOG7CRTPP.
PhylomeDBiQ03721.
TreeFamiTF352511.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003968. K_chnl_volt-dep_Kv.
IPR003974. K_chnl_volt-dep_Kv3.
IPR005405. K_chnl_volt-dep_Kv3.4.
IPR021105. K_chnl_volt-dep_Kv3_ID.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11404. Potassium_chann. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01583. KV34CHANNEL.
PR01491. KVCHANNEL.
PR01498. SHAWCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q03721-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MISSVCVSSY RGRKSGNKPP SKTCLKEEMA KGEASEKIII NVGGTRHETY
60 70 80 90 100
RSTLRTLPGT RLAWLADPDG GGRPETDGGG VGSSGSSGGG GCEFFFDRHP
110 120 130 140 150
GVFAYVLNYY RTGKLHCPAD VCGPLFEEEL TFWGIDETDV EPCCWMTYRQ
160 170 180 190 200
HRDAEEALDI FESPDGGGSG AGPSDEAGDD ERELALQRLG PHEGGAGHGA
210 220 230 240 250
GSGGCRGWQP RMWALFEDPY SSRAARVVAF ASLFFILVSI TTFCLETHEA
260 270 280 290 300
FNIDRNVTEI LRVGNITSVH FRREVETEPI LTYIEGVCVL WFTLEFLVRI
310 320 330 340 350
VCCPDTLDFV KNLLNIIDFV AILPFYLEVG LSGLSSKAAR DVLGFLRVVR
360 370 380 390 400
FVRILRIFKL TRHFVGLRVL GHTLRASTNE FLLLIIFLAL GVLIFATMIY
410 420 430 440 450
YAERIGARPS DPRGNDHTDF KNIPIGFWWA VVTMTTLGYG DMYPKTWSGM
460 470 480 490 500
LVGALCALAG VLTIAMPVPV IVNNFGMYYS LAMAKQKLPK KRKKHVPRPA
510 520 530 540 550
QLESPMYCKS EETSPRDSTC SDTSPPAREE GMIERKRADS KQNGDANAVL
560 570 580 590 600
SDEEGAGLTQ PLASSPTPEE RRALRRSTTR DRNKKAAACF LLSTGDYACA
610 620 630
DGSVRKGTFV LRDLPLQHSP EAACPPTAGT LFLPH
Length:635
Mass (Da):69,767
Last modified:May 24, 2005 - v2
Checksum:i8A36F0A16AD17722
GO
Isoform 2 (identifier: Q03721-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     539-582: DSKQNGDANA...ALRRSTTRDR → GEIRGWEGKS...GFPKHKDVPL
     583-635: Missing.

Note: Could be a cloning artifact.
Show »
Length:582
Mass (Da):64,547
Checksum:i427587A53154E5E0
GO
Isoform 3 (identifier: Q03721-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     607-635: GTFVLRDLPLQHSPEAACPPTAGTLFLPH → ETCQDALSSNYAQAEVLTLS

Note: Gene prediction based on EST data.
Show »
Length:626
Mass (Da):68,824
Checksum:i25385AD738077B52
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861S → T in AAA57263 (PubMed:1381835).Curated
Sequence conflicti351 – 3511F → I in AAA57263 (PubMed:1381835).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti318 – 3181D → Y.
Corresponds to variant rs35167146 [ dbSNP | Ensembl ].
VAR_034051
Natural varianti516 – 5161R → Q.
Corresponds to variant rs59123361 [ dbSNP | Ensembl ].
VAR_062185
Natural varianti520 – 5201C → Y.
Corresponds to variant rs12411176 [ dbSNP | Ensembl ].
VAR_027505

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei539 – 58244DSKQN…TTRDR → GEIRGWEGKSLFPQWPREFP NGPQTLGFGMCFVWGFPKHK DVPL in isoform 2. 2 PublicationsVSP_020581Add
BLAST
Alternative sequencei583 – 63553Missing in isoform 2. 2 PublicationsVSP_020582Add
BLAST
Alternative sequencei607 – 63529GTFVL…LFLPH → ETCQDALSSNYAQAEVLTLS in isoform 3. CuratedVSP_040033Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64676 mRNA. Translation: AAA57263.1.
AL137790 Genomic DNA. Translation: CAI18831.1.
BC019010 mRNA. No translation available.
BC101769 mRNA. Translation: AAI01770.1.
CCDSiCCDS44193.1. [Q03721-3]
CCDS821.1. [Q03721-1]
RefSeqiNP_001034663.1. NM_001039574.2. [Q03721-3]
NP_004969.2. NM_004978.4. [Q03721-1]
UniGeneiHs.153521.

Genome annotation databases

EnsembliENST00000369787; ENSP00000358802; ENSG00000116396. [Q03721-1]
ENST00000438661; ENSP00000393655; ENSG00000116396. [Q03721-3]
ENST00000469655; ENSP00000436656; ENSG00000116396. [Q03721-1]
GeneIDi3749.
KEGGihsa:3749.
UCSCiuc001dzg.4. human. [Q03721-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M64676 mRNA. Translation: AAA57263.1.
AL137790 Genomic DNA. Translation: CAI18831.1.
BC019010 mRNA. No translation available.
BC101769 mRNA. Translation: AAI01770.1.
CCDSiCCDS44193.1. [Q03721-3]
CCDS821.1. [Q03721-1]
RefSeqiNP_001034663.1. NM_001039574.2. [Q03721-3]
NP_004969.2. NM_004978.4. [Q03721-1]
UniGeneiHs.153521.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1B4GNMR-A1-30[»]
1B4INMR-A1-30[»]
1ZTNNMR-A1-30[»]
ProteinModelPortaliQ03721.
SMRiQ03721. Positions 1-30, 35-479.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109951. 27 interactions.
IntActiQ03721. 1 interaction.
STRINGi9606.ENSP00000358802.

Chemistry

ChEMBLiCHEMBL2362996.

PTM databases

iPTMnetiQ03721.
PhosphoSiteiQ03721.

Polymorphism and mutation databases

BioMutaiKCNC4.
DMDMi66774206.

Proteomic databases

PaxDbiQ03721.
PRIDEiQ03721.
TopDownProteomicsiQ03721-3. [Q03721-3]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000369787; ENSP00000358802; ENSG00000116396. [Q03721-1]
ENST00000438661; ENSP00000393655; ENSG00000116396. [Q03721-3]
ENST00000469655; ENSP00000436656; ENSG00000116396. [Q03721-1]
GeneIDi3749.
KEGGihsa:3749.
UCSCiuc001dzg.4. human. [Q03721-1]

Organism-specific databases

CTDi3749.
GeneCardsiKCNC4.
H-InvDBHIX0023584.
HGNCiHGNC:6236. KCNC4.
HPAiHPA014740.
MIMi176265. gene.
neXtProtiNX_Q03721.
PharmGKBiPA30028.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3713. Eukaryota.
COG1226. LUCA.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231012.
HOVERGENiHBG105862.
InParanoidiQ03721.
KOiK04890.
OMAiGCEFFFD.
OrthoDBiEOG7CRTPP.
PhylomeDBiQ03721.
TreeFamiTF352511.

Enzyme and pathway databases

ReactomeiR-HSA-1296072. Voltage gated Potassium channels.
SIGNORiQ03721.

Miscellaneous databases

EvolutionaryTraceiQ03721.
GeneWikiiKCNC4.
GenomeRNAii3749.
PROiQ03721.
SOURCEiSearch...

Gene expression databases

BgeeiQ03721.
CleanExiHS_KCNC4.
ExpressionAtlasiQ03721. baseline and differential.
GenevisibleiQ03721. HS.

Family and domain databases

Gene3Di1.20.120.350. 1 hit.
InterProiIPR000210. BTB/POZ_dom.
IPR027359. Channel_four-helix_dom.
IPR005821. Ion_trans_dom.
IPR003968. K_chnl_volt-dep_Kv.
IPR003974. K_chnl_volt-dep_Kv3.
IPR005405. K_chnl_volt-dep_Kv3.4.
IPR021105. K_chnl_volt-dep_Kv3_ID.
IPR011333. SKP1/BTB/POZ.
IPR003131. T1-type_BTB.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 3 hits.
PfamiPF02214. BTB_2. 1 hit.
PF00520. Ion_trans. 1 hit.
PF11404. Potassium_chann. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01583. KV34CHANNEL.
PR01491. KVCHANNEL.
PR01498. SHAWCHANNEL.
SMARTiSM00225. BTB. 1 hit.
[Graphical view]
SUPFAMiSSF54695. SSF54695. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of ShIII (Shaw-like) cDNAs encoding a novel high-voltage-activating, TEA-sensitive, type-A K+ channel."
    de Miera E.V.-S., Moreno H., Fruhling D., Kentros C., Rudy B.
    Proc. R. Soc. B 248:9-18(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "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.
    , 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].
  3. "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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-635 (ISOFORM 1).
    Tissue: Brain.
  4. "Elimination of rapid potassium channel inactivation by phosphorylation of the inactivation gate."
    Covarrubias M., Wei A., Salkoff L., Vyas T.B.
    Neuron 13:1403-1412(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15 AND SER-21, MUTAGENESIS OF SER-15 AND SER-21.
  5. "Interactions between multiple phosphorylation sites in the inactivation particle of a K+ channel. Insights into the molecular mechanism of protein kinase C action."
    Beck E.J., Sorensen R.G., Slater S.J., Covarrubias M.
    J. Gen. Physiol. 112:71-84(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-8 AND SER-9, MUTAGENESIS OF SER-8; SER-9; SER-15 AND SER-21.
  6. "NMR structure of inactivation gates from mammalian voltage-dependent potassium channels."
    Antz C., Geyer M., Fakler B., Schott M.K., Guy H.R., Frank R., Ruppersberg J.P., Kalbitzer H.R.
    Nature 385:272-275(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-30.
  7. "Control of K+ channel gating by protein phosphorylation: structural switches of the inactivation gate."
    Antz C., Bauer T., Kalbacher H., Frank R., Covarrubias M., Kalbitzer H.R., Ruppersberg J.P., Baukrowitz T., Fakler B.
    Nat. Struct. Biol. 6:146-150(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-30.

Entry informationi

Entry nameiKCNC4_HUMAN
AccessioniPrimary (citable) accession number: Q03721
Secondary accession number(s): Q3MIM4, Q5TBI6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: May 24, 2005
Last modified: June 8, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.