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Q9H2S1 (KCNN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Small conductance calcium-activated potassium channel protein 2
Short name=SK2
Short name=SKCa 2
Short name=SKCa2
Alternative name(s):
KCa2.2
Gene names
Name:KCNN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization. The channel is blocked by apamin.

Subunit structure

Heterooligomer. The complex is composed of 4 channel subunits each of which binds to a calmodulin subunit which regulates the channel activity through calcium-binding By similarity.

Subcellular location

Membrane; Multi-pass membrane protein.

Tissue specificity

Expressed in atrial myocytes (at protein level). Widely expressed. Ref.2

Sequence similarities

Belongs to the potassium channel KCNN family. KCa2.2/KCNN2 subfamily.

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandCalmodulin-binding
   Molecular functionIon channel
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpotassium ion transmembrane transport

Inferred from direct assay PubMed 17110593. Source: BHF-UCL

potassium ion transport

Non-traceable author statement Ref.1. Source: UniProtKB

regulation of potassium ion transmembrane transport

Inferred from direct assay PubMed 17110593. Source: BHF-UCL

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentT-tubule

Inferred from electronic annotation. Source: Ensembl

Z disc

Inferred from electronic annotation. Source: Ensembl

dendritic spine

Inferred from Biological aspect of Ancestor. Source: RefGenome

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

neuronal cell body

Inferred from Biological aspect of Ancestor. Source: RefGenome

plasma membrane

Inferred from Biological aspect of Ancestor. Source: RefGenome

smooth endoplasmic reticulum

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionalpha-actinin binding

Inferred from physical interaction PubMed 17110593. Source: BHF-UCL

calcium-activated potassium channel activity

Inferred from direct assay PubMed 17110593. Source: BHF-UCL

calmodulin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homodimerization activity

Inferred from physical interaction PubMed 17110593. Source: BHF-UCL

small conductance calcium-activated potassium channel activity

Traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H2S1-1)

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: Q9H2S1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-348: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Small conductance calcium-activated potassium channel protein 2
PRO_0000155010

Regions

Transmembrane138 – 15821Helical; Name=Segment S1; Potential
Transmembrane168 – 18821Helical; Name=Segment S2; Potential
Transmembrane214 – 23421Helical; Name=Segment S3; Potential
Transmembrane256 – 27621Helical; Name=Segment S4; Potential
Transmembrane305 – 32521Helical; Name=Segment S5; Potential
Intramembrane345 – 36521Pore-forming; Name=Segment H5; Potential
Transmembrane374 – 39421Helical; Name=Segment S6; Potential
Region412 – 48877Calmodulin-binding By similarity
Compositional bias41 – 455Poly-Gly
Compositional bias51 – 588Poly-Ala
Compositional bias83 – 886Poly-Gly
Compositional bias91 – 10212Poly-Gly
Compositional bias563 – 5664Poly-Arg

Amino acid modifications

Modified residue1601Phosphotyrosine By similarity

Natural variations

Alternative sequence1 – 348348Missing in isoform 2.
VSP_044584

Experimental info

Sequence conflict501S → SA in AAK84039. Ref.3
Sequence conflict521A → D in AAG16728. Ref.1
Sequence conflict581A → AA in AAP45946. Ref.2
Sequence conflict3231I → T in AAK84039. Ref.3
Sequence conflict5301Q → R in AAP45946. Ref.2
Sequence conflict5301Q → R in AAK84039. Ref.3

Sequences

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

Last modified October 14, 2008. Version 2.
Checksum: 2ED87FE13C106183

FASTA57963,760
        10         20         30         40         50         60 
MSSCRYNGGV MRPLSNLSAS RRNLHEMDSE AQPLQPPASV GGGGGASSPS AAAAAAAAVS 

        70         80         90        100        110        120 
SSAPEIVVSK PEHNNSNNLA LYGTGGGGST GGGGGGGGSG HGSSSGTKSS KKKNQNIGYK 

       130        140        150        160        170        180 
LGHRRALFEK RKRLSDYALI FGMFGIVVMV IETELSWGAY DKASLYSLAL KCLISLSTII 

       190        200        210        220        230        240 
LLGLIIVYHA REIQLFMVDN GADDWRIAMT YERIFFICLE ILVCAIHPIP GNYTFTWTAR 

       250        260        270        280        290        300 
LAFSYAPSTT TADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA LNKINFNTRF 

       310        320        330        340        350        360 
VMKTLMTICP GTVLLVFSIS LWIIAAWTVR ACERYHDQQD VTSNFLGAMW LISITFLSIG 

       370        380        390        400        410        420 
YGDMVPNTYC GKGVCLLTGI MGAGCTALVV AVVARKLELT KAEKHVHNFM MDTQLTKRVK 

       430        440        450        460        470        480 
NAAANVLRET WLIYKNTKLV KKIDHAKVRK HQRKFLQAIH QLRSVKMEQR KLNDQANTLV 

       490        500        510        520        530        540 
DLAKTQNIMY DMISDLNERS EDFEKRIVTL ETKLETLIGS IHALPGLISQ TIRQQQRDFI 

       550        560        570 
EAQMESYDKH VTYNAERSRS SSRRRRSSST APPTSSESS

« Hide

Isoform 2 [UniParc].

Checksum: 89BD2ED1EAD6E54B
Show »

FASTA23126,341

References

« Hide 'large scale' references
[1]"Ca2+-activated K+ channels in human leukemic Jurkat T cells. Molecular cloning, biochemical and functional characterization."
Desai R., Peretz A., Idelson H., Lazarovici P., Attali B.
J. Biol. Chem. 275:39954-39963(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Molecular identification and functional roles of a Ca(2+)-activated K+ channel in human and mouse hearts."
Xu Y., Tuteja D., Zhang Z., Xu D., Zhang Y., Rodriguez J., Nie L., Tuxson H.R., Young J.N., Glatter K.A., Vazquez A.E., Yamoah E.N., Chiamvimonvat N.
J. Biol. Chem. 278:49085-49094(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
Tissue: Heart.
[3]"Characterization of calcium-activated potassium channels in human myometrium."
Mazzone J.N., Kaiser R.A., Buxton I.L.O.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Myometrium.
[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. expand/collapse author list , 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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[5]"The DNA sequence and comparative analysis of human chromosome 5."
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. expand/collapse author list , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.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 (SEP-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] (ISOFORMS 1 AND 2).
Tissue: Brain and Skin.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF239613 mRNA. Translation: AAG16728.1.
AY258141 mRNA. Translation: AAP45946.1.
AF397175 mRNA. Translation: AAK84039.1.
AK289948 mRNA. Translation: BAF82637.1.
AC025761 Genomic DNA. No translation available.
AC109482 Genomic DNA. No translation available.
CH471086 Genomic DNA. Translation: EAW48975.1.
CH471086 Genomic DNA. Translation: EAW48976.1.
BC015371 mRNA. Translation: AAH15371.1.
BC117454 mRNA. Translation: AAI17455.1.
BC117456 mRNA. Translation: AAI17457.1.
CCDSCCDS4114.1. [Q9H2S1-1]
CCDS43352.1. [Q9H2S1-2]
RefSeqNP_001265133.1. NM_001278204.1. [Q9H2S1-2]
NP_067627.2. NM_021614.3. [Q9H2S1-1]
NP_740721.1. NM_170775.2. [Q9H2S1-2]
UniGeneHs.98280.

3D structure databases

ProteinModelPortalQ9H2S1.
SMRQ9H2S1. Positions 322-525.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109982. 6 interactions.
DIPDIP-48997N.
IntActQ9H2S1. 2 interactions.
STRING9606.ENSP00000264773.

Chemistry

BindingDBQ9H2S1.
ChEMBLCHEMBL4469.
GuidetoPHARMACOLOGY382.

Protein family/group databases

TCDB1.A.1.16.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteQ9H2S1.

Polymorphism databases

DMDM209572638.

Proteomic databases

MaxQBQ9H2S1.
PaxDbQ9H2S1.
PRIDEQ9H2S1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264773; ENSP00000264773; ENSG00000080709. [Q9H2S1-1]
ENST00000503706; ENSP00000421439; ENSG00000080709. [Q9H2S1-2]
ENST00000512097; ENSP00000427120; ENSG00000080709. [Q9H2S1-1]
GeneID3781.
KEGGhsa:3781.
UCSCuc003kqo.3. human. [Q9H2S1-1]
uc003kqp.3. human.

Organism-specific databases

CTD3781.
GeneCardsGC05P113725.
HGNCHGNC:6291. KCNN2.
HPAHPA038221.
MIM605879. gene.
neXtProtNX_Q9H2S1.
PharmGKBPA30071.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320393.
HOVERGENHBG052241.
InParanoidQ9H2S1.
KOK04943.
OMAAQMESYD.
PhylomeDBQ9H2S1.
TreeFamTF315015.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ9H2S1.
BgeeQ9H2S1.
CleanExHS_KCNN2.
GenevestigatorQ9H2S1.

Family and domain databases

InterProIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERPTHR10153. PTHR10153. 1 hit.
PfamPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSPR01451. SKCHANNEL.
SMARTSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMSSF81327. SSF81327. 1 hit.
ProtoNetSearch...

Other

GeneWikiKCNN2.
GenomeRNAi3781.
NextBio14837.
PROQ9H2S1.
SOURCESearch...

Entry information

Entry nameKCNN2_HUMAN
AccessionPrimary (citable) accession number: Q9H2S1
Secondary accession number(s): A6NF94 expand/collapse secondary AC list , Q0VFZ4, Q6PJI0, Q6X2Y2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 14, 2008
Last modified: July 9, 2014
This is version 119 of the entry and version 2 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

MIM cross-references

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

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents