Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Potassium voltage-gated channel subfamily KQT member 5

Gene

KCNQ5

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

Functioni

Probably important in the regulation of neuronal excitability. Associates with KCNQ3 to form a potassium channel which contributes to M-type current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons. May contribute, with other potassium channels, to the molecular diversity of a heterogeneous population of M-channels, varying in kinetic and pharmacological properties, which underlie this physiologically important current. Insensitive to tetraethylammonium, but inhibited by barium, linopirdine and XE991. Activated by niflumic acid and the anticonvulsant retigabine. Muscarine suppresses KCNQ5 current in Xenopus oocytes in which cloned KCNQ5 channels were coexpressed with M1 muscarinic receptors.

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: GO_Central
  2. inward rectifier potassium channel activity Source: ProtInc

GO - Biological processi

  1. potassium ion transmembrane transport Source: GO_Central
  2. protein complex assembly Source: ProtInc
  3. synaptic transmission Source: Reactome
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

ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily KQT member 5
Alternative name(s):
KQT-like 5
Potassium channel subunit alpha KvLQT5
Voltage-gated potassium channel subunit Kv7.5
Gene namesi
Name:KCNQ5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6299. KCNQ5.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei126 – 14621Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei157 – 17721Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei201 – 22121Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei230 – 25223Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei267 – 28721Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Intramembranei299 – 31921Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Transmembranei326 – 34621Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. integral component of membrane Source: GO_Central
  2. plasma membrane Source: Reactome
  3. voltage-gated potassium channel complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30077.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 932932Potassium voltage-gated channel subfamily KQT member 5PRO_0000054040Add
BLAST

Proteomic databases

PaxDbiQ9NR82.
PRIDEiQ9NR82.

PTM databases

PhosphoSiteiQ9NR82.

Expressioni

Tissue specificityi

Strongly expressed in brain and skeletal muscle. In brain, expressed in cerebral cortex, occipital pole, frontal lobe and temporal lobe. Lower levels in hippocampus and putamen. Low to undetectable levels in medulla, cerebellum and thalamus.

Gene expression databases

BgeeiQ9NR82.
CleanExiHS_KCNQ5.
ExpressionAtlasiQ9NR82. baseline and differential.
GenevestigatoriQ9NR82.

Organism-specific databases

HPAiHPA016655.

Interactioni

Subunit structurei

Heteromultimer with KCNQ3.

Protein-protein interaction databases

BioGridi121149. 5 interactions.
STRINGi9606.ENSP00000359425.

Structurei

3D structure databases

ProteinModelPortaliQ9NR82.
SMRiQ9NR82. Positions 160-350, 598-627.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi311 – 3166Selectivity 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.By similarity

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiQ9NR82.
KOiK04930.
OMAiYTSSQSC.
OrthoDBiEOG73804Z.
PhylomeDBiQ9NR82.
TreeFamiTF315186.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01459. KCNQCHANNEL.

Sequences (7)i

Sequence statusi: Complete.

This entry describes 7 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NR82-1) [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
MPRHHAGGEE GGAAGLWVKS GAAAAAAGGG RLGSGMKDVE SGRGRVLLNS
60 70 80 90 100
AAARGDGLLL LGTRAATLGG GGGGLRESRR GKQGARMSLL GKPLSYTSSQ
110 120 130 140 150
SCRRNVKYRR VQNYLYNVLE RPRGWAFIYH AFVFLLVFGC LILSVFSTIP
160 170 180 190 200
EHTKLASSCL LILEFVMIVV FGLEFIIRIW SAGCCCRYRG WQGRLRFARK
210 220 230 240 250
PFCVIDTIVL IASIAVVSAK TQGNIFATSA LRSLRFLQIL RMVRMDRRGG
260 270 280 290 300
TWKLLGSVVY AHSKELITAW YIGFLVLIFS SFLVYLVEKD ANKEFSTYAD
310 320 330 340 350
ALWWGTITLT TIGYGDKTPL TWLGRLLSAG FALLGISFFA LPAGILGSGF
360 370 380 390 400
ALKVQEQHRQ KHFEKRRNPA ANLIQCVWRS YAADEKSVSI ATWKPHLKAL
410 420 430 440 450
HTCSPTKKEQ GEASSSQKLS FKERVRMASP RGQSIKSRQA SVGDRRSPST
460 470 480 490 500
DITAEGSPTK VQKSWSFNDR TRFRPSLRLK SSQPKPVIDA DTALGTDDVY
510 520 530 540 550
DEKGCQCDVS VEDLTPPLKT VIRAIRIMKF HVAKRKFKET LRPYDVKDVI
560 570 580 590 600
EQYSAGHLDM LCRIKSLQTR VDQILGKGQI TSDKKSREKI TAEHETTDDL
610 620 630 640 650
SMLGRVVKVE KQVQSIESKL DCLLDIYQQV LRKGSASALA LASFQIPPFE
660 670 680 690 700
CEQTSDYQSP VDSKDLSGSA QNSGCLSRST SANISRGLQF ILTPNEFSAQ
710 720 730 740 750
TFYALSPTMH SQATQVPISQ SDGSAVAATN TIANQINTAP KPAAPTTLQI
760 770 780 790 800
PPPLPAIKHL PRPETLHPNP AGLQESISDV TTCLVASKEN VQVAQSNLTK
810 820 830 840 850
DRSMRKSFDM GGETLLSVCP MVPKDLGKSL SVQNLIRSTE ELNIQLSGSE
860 870 880 890 900
SSGSRGSQDF YPKWRESKLF ITDEEVGPEE TETDTFDAAP QPAREAAFAS
910 920 930
DSLRTGRSRS SQSICKAGES TDALSLPHVK LK
Length:932
Mass (Da):102,179
Last modified:January 8, 2007 - v3
Checksum:iCB41C243FD2B00FC
GO
Isoform 2 (identifier: Q9NR82-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-416: KKEQGEASSS → N

Show »
Length:923
Mass (Da):101,261
Checksum:i3471634490A35B18
GO
Isoform 3 (identifier: Q9NR82-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-416: KKEQGEASSS → NKFCSNKQKLFRMYTSRKQS

Show »
Length:942
Mass (Da):103,624
Checksum:iF7580704F95D1CC3
GO
Isoform 4 (identifier: Q9NR82-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-427: SQKLSFKERVRM → RFVISLLLHVCL
     428-932: Missing.

Note: No experimental confirmation available.

Show »
Length:427
Mass (Da):46,943
Checksum:i175F91B7BB48836B
GO
Isoform 5 (identifier: Q9NR82-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-525: Missing.

Note: No experimental confirmation available.

Show »
Length:822
Mass (Da):89,987
Checksum:iEC339886F1755506
GO
Isoform 6 (identifier: Q9NR82-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     416-416: S → SKFCSNKQKLFRMYTSRKQS

Note: No experimental confirmation available.

Show »
Length:951
Mass (Da):104,542
Checksum:iDB6CFDB0C6267F6F
GO
Isoform 7 (identifier: Q9NR82-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-416: KEQGEASSS → QNQQGESQSC

Note: No experimental confirmation available.

Show »
Length:933
Mass (Da):102,365
Checksum:i6B39865CBDB05D2E
GO

Sequence cautioni

The sequence BAG61495.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 932KP → SR in AAF91335 (PubMed:10787416).Curated
Sequence conflicti109 – 1091R → Q in BAG61495 (PubMed:14702039).Curated
Sequence conflicti129 – 1291Y → H in AAF73446 (Ref. 7) Curated
Sequence conflicti727 – 7271A → V in AAF73446 (Ref. 7) Curated
Sequence conflicti799 – 7991T → P in AAF73446 (Ref. 7) Curated
Sequence conflicti857 – 8571S → R in AAF73446 (Ref. 7) Curated
Sequence conflicti909 – 9091R → Q in AAF73446 (Ref. 7) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti191 – 1911W → G in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035772
Natural varianti244 – 2441R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035773

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei407 – 41610KKEQGEASSS → N in isoform 2. 2 PublicationsVSP_001014
Alternative sequencei407 – 41610KKEQGEASSS → NKFCSNKQKLFRMYTSRKQS in isoform 3. 1 PublicationVSP_001015
Alternative sequencei408 – 4169KEQGEASSS → QNQQGESQSC in isoform 7. CuratedVSP_056730
Alternative sequencei416 – 525110Missing in isoform 5. 1 PublicationVSP_045487Add
BLAST
Alternative sequencei416 – 42712SQKLS…ERVRM → RFVISLLLHVCL in isoform 4. 1 PublicationVSP_022318Add
BLAST
Alternative sequencei416 – 4161S → SKFCSNKQKLFRMYTSRKQS in isoform 6. CuratedVSP_056731
Alternative sequencei428 – 932505Missing in isoform 4. 1 PublicationVSP_022319Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249278 mRNA. Translation: AAF91335.1.
AL445569 Genomic DNA. No translation available.
AL049845 Genomic DNA. No translation available.
AL360232 Genomic DNA. No translation available.
AL360236 Genomic DNA. No translation available.
AL365232 Genomic DNA. No translation available.
FO393414 Genomic DNA. No translation available.
AL513522 Genomic DNA. No translation available.
AL671823 Genomic DNA. No translation available.
BC050689 mRNA. Translation: AAH50689.1.
BC117359 mRNA. Translation: AAI17360.1.
BC143554 mRNA. Translation: AAI43555.1.
AK299550 mRNA. Translation: BAG61495.1. Different initiation.
AF202977 mRNA. Translation: AAF69797.1.
AJ272506
, AJ272507, AJ272508, AJ272509, AJ272510, AJ272511, AJ272512, AJ272513, AJ272514, AJ272515, AJ272516, AJ272517, AJ272518, AJ272519 Genomic DNA. Translation: CAC88112.1.
AF263835 mRNA. Translation: AAF73446.1.
CCDSiCCDS4976.1. [Q9NR82-1]
CCDS55034.1. [Q9NR82-6]
CCDS55036.1. [Q9NR82-3]
RefSeqiNP_001153602.1. NM_001160130.1. [Q9NR82-2]
NP_001153604.1. NM_001160132.1. [Q9NR82-3]
NP_001153605.1. NM_001160133.1. [Q9NR82-6]
NP_001153606.1. NM_001160134.1. [Q9NR82-5]
NP_062816.2. NM_019842.3. [Q9NR82-1]
UniGeneiHs.445324.

Genome annotation databases

EnsembliENST00000342056; ENSP00000345055; ENSG00000185760. [Q9NR82-6]
ENST00000370392; ENSP00000359419; ENSG00000185760. [Q9NR82-4]
ENST00000370398; ENSP00000359425; ENSG00000185760. [Q9NR82-1]
GeneIDi56479.
KEGGihsa:56479.
UCSCiuc003pgj.4. human. [Q9NR82-4]
uc003pgk.3. human. [Q9NR82-1]
uc010kat.3. human. [Q9NR82-2]
uc011dyi.2. human. [Q9NR82-3]
uc011dyj.2. human.

Polymorphism databases

DMDMi122065285.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF249278 mRNA. Translation: AAF91335.1.
AL445569 Genomic DNA. No translation available.
AL049845 Genomic DNA. No translation available.
AL360232 Genomic DNA. No translation available.
AL360236 Genomic DNA. No translation available.
AL365232 Genomic DNA. No translation available.
FO393414 Genomic DNA. No translation available.
AL513522 Genomic DNA. No translation available.
AL671823 Genomic DNA. No translation available.
BC050689 mRNA. Translation: AAH50689.1.
BC117359 mRNA. Translation: AAI17360.1.
BC143554 mRNA. Translation: AAI43555.1.
AK299550 mRNA. Translation: BAG61495.1. Different initiation.
AF202977 mRNA. Translation: AAF69797.1.
AJ272506
, AJ272507, AJ272508, AJ272509, AJ272510, AJ272511, AJ272512, AJ272513, AJ272514, AJ272515, AJ272516, AJ272517, AJ272518, AJ272519 Genomic DNA. Translation: CAC88112.1.
AF263835 mRNA. Translation: AAF73446.1.
CCDSiCCDS4976.1. [Q9NR82-1]
CCDS55034.1. [Q9NR82-6]
CCDS55036.1. [Q9NR82-3]
RefSeqiNP_001153602.1. NM_001160130.1. [Q9NR82-2]
NP_001153604.1. NM_001160132.1. [Q9NR82-3]
NP_001153605.1. NM_001160133.1. [Q9NR82-6]
NP_001153606.1. NM_001160134.1. [Q9NR82-5]
NP_062816.2. NM_019842.3. [Q9NR82-1]
UniGeneiHs.445324.

3D structure databases

ProteinModelPortaliQ9NR82.
SMRiQ9NR82. Positions 160-350, 598-627.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121149. 5 interactions.
STRINGi9606.ENSP00000359425.

Chemistry

BindingDBiQ9NR82.
ChEMBLiCHEMBL2362996.
DrugBankiDB04953. Ezogabine.
GuidetoPHARMACOLOGYi564.

PTM databases

PhosphoSiteiQ9NR82.

Polymorphism databases

DMDMi122065285.

Proteomic databases

PaxDbiQ9NR82.
PRIDEiQ9NR82.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000342056; ENSP00000345055; ENSG00000185760. [Q9NR82-6]
ENST00000370392; ENSP00000359419; ENSG00000185760. [Q9NR82-4]
ENST00000370398; ENSP00000359425; ENSG00000185760. [Q9NR82-1]
GeneIDi56479.
KEGGihsa:56479.
UCSCiuc003pgj.4. human. [Q9NR82-4]
uc003pgk.3. human. [Q9NR82-1]
uc010kat.3. human. [Q9NR82-2]
uc011dyi.2. human. [Q9NR82-3]
uc011dyj.2. human.

Organism-specific databases

CTDi56479.
GeneCardsiGC06P073331.
HGNCiHGNC:6299. KCNQ5.
HPAiHPA016655.
MIMi607357. gene.
neXtProtiNX_Q9NR82.
PharmGKBiPA30077.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00550000074513.
HOGENOMiHOG000220839.
HOVERGENiHBG059014.
InParanoidiQ9NR82.
KOiK04930.
OMAiYTSSQSC.
OrthoDBiEOG73804Z.
PhylomeDBiQ9NR82.
TreeFamiTF315186.

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKCNQ5. human.
GeneWikiiKCNQ5.
GenomeRNAii56479.
NextBioi35464823.
PROiQ9NR82.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR82.
CleanExiHS_KCNQ5.
ExpressionAtlasiQ9NR82. baseline and differential.
GenevestigatoriQ9NR82.

Family and domain databases

InterProiIPR005821. Ion_trans_dom.
IPR003091. K_chnl.
IPR003937. K_chnl_volt-dep_KCNQ.
IPR013821. K_chnl_volt-dep_KCNQ_C.
IPR028325. VG_K_chnl.
[Graphical view]
PANTHERiPTHR11537. PTHR11537. 1 hit.
PfamiPF00520. Ion_trans. 1 hit.
PF03520. KCNQ_channel. 1 hit.
[Graphical view]
PRINTSiPR00169. KCHANNEL.
PR01459. KCNQCHANNEL.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and functional expression of KCNQ5, a potassium channel subunit that may contribute to neuronal M-current diversity."
    Lerche C., Scherer C.R., Seebohm G., Derst C., Wei A.D., Busch A.E., Steinmeyer K.
    J. Biol. Chem. 275:22395-22400(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Brain.
  2. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2002) [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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
    Tissue: Placenta.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 19-822 (ISOFORM 5).
    Tissue: Brain.
  5. "KCNQ5, a novel potassium channel broadly expressed in brain, mediates M-type currents."
    Schroeder B.C., Hechenberger M., Weinreich F., Kubisch C., Jentsch T.J.
    J. Biol. Chem. 275:24089-24095(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 36-932 (ISOFORMS 1; 2 AND 3).
    Tissue: Brain.
  6. "The new voltage gated potassium channel KCNQ5 and early infantile convulsions."
    Kananura C., Biervert B., Hechenberger M., Engels H., Steinlein O.K.
    Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-932.
  7. "A new gene of the voltage-gated potassium channel KCNQ family, KCNQ5, is a candidate gene for retinal disorders."
    Kniazeva M., Han M.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 72-932 (ISOFORM 1).
    Tissue: Brain and Retina.
  8. "Characterization of KCNQ5/Q3 potassium channels expressed in mammalian cells."
    Wickenden A.D., Zou A., Wagoner P.K., Jegla T.
    Br. J. Pharmacol. 132:381-384(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION, ACTIVATION BY RETICABINE.
  9. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLY-191 AND CYS-244.

Entry informationi

Entry nameiKCNQ5_HUMAN
AccessioniPrimary (citable) accession number: Q9NR82
Secondary accession number(s): A6NKT6
, A6PVT6, A8MSQ5, B4DS33, B5MC83, B7ZL37, F5GZV0, Q17RE1, Q5VVP3, Q86W40, Q9NRN0, Q9NYA6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 31, 2001
Last sequence update: January 8, 2007
Last modified: March 3, 2015
This is version 127 of the entry and version 3 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.