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Protein

Small conductance calcium-activated potassium channel protein 2

Gene

KCNN2

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

Functioni

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.

GO - Molecular functioni

  1. alpha-actinin binding Source: BHF-UCL
  2. calcium-activated potassium channel activity Source: BHF-UCL
  3. calmodulin binding Source: GO_Central
  4. protein homodimerization activity Source: BHF-UCL
  5. small conductance calcium-activated potassium channel activity Source: UniProtKB

GO - Biological processi

  1. potassium ion transmembrane transport Source: BHF-UCL
  2. potassium ion transport Source: UniProtKB
  3. regulation of potassium ion transmembrane transport Source: BHF-UCL
  4. synaptic transmission Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

ReactomeiREACT_75896. Ca2+ activated K+ channels.

Protein family/group databases

TCDBi1.A.1.16.1. the voltage-gated ion channel (vic) superfamily.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:KCNN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:6291. KCNN2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei138 – 15821Helical; Name=Segment S1Sequence AnalysisAdd
BLAST
Transmembranei168 – 18821Helical; Name=Segment S2Sequence AnalysisAdd
BLAST
Transmembranei214 – 23421Helical; Name=Segment S3Sequence AnalysisAdd
BLAST
Transmembranei256 – 27621Helical; Name=Segment S4Sequence AnalysisAdd
BLAST
Transmembranei305 – 32521Helical; Name=Segment S5Sequence AnalysisAdd
BLAST
Intramembranei345 – 36521Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST
Transmembranei374 – 39421Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. dendritic spine Source: GO_Central
  2. integral component of membrane Source: UniProtKB
  3. neuronal cell body Source: GO_Central
  4. plasma membrane Source: GO_Central
  5. smooth endoplasmic reticulum Source: Ensembl
  6. T-tubule Source: Ensembl
  7. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30071.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Small conductance calcium-activated potassium channel protein 2PRO_0000155010Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei160 – 1601PhosphotyrosineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9H2S1.
PaxDbiQ9H2S1.
PRIDEiQ9H2S1.

PTM databases

PhosphoSiteiQ9H2S1.

Expressioni

Tissue specificityi

Expressed in atrial myocytes (at protein level). Widely expressed.1 Publication

Gene expression databases

BgeeiQ9H2S1.
CleanExiHS_KCNN2.
ExpressionAtlasiQ9H2S1. baseline and differential.
GenevestigatoriQ9H2S1.

Organism-specific databases

HPAiHPA038221.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

BioGridi109982. 6 interactions.
DIPiDIP-48997N.
IntActiQ9H2S1. 2 interactions.
STRINGi9606.ENSP00000264773.

Structurei

3D structure databases

ProteinModelPortaliQ9H2S1.
SMRiQ9H2S1. Positions 322-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni412 – 48877Calmodulin-bindingBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi41 – 455Poly-Gly
Compositional biasi51 – 588Poly-Ala
Compositional biasi83 – 886Poly-Gly
Compositional biasi91 – 10212Poly-GlyAdd
BLAST
Compositional biasi563 – 5664Poly-Arg

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000124679.
HOVERGENiHBG052241.
InParanoidiQ9H2S1.
KOiK04943.
OMAiAQMESYD.
PhylomeDBiQ9H2S1.
TreeFamiTF315015.

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9H2S1-1) [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
MSSCRYNGGV MRPLSNLSAS RRNLHEMDSE AQPLQPPASV GGGGGASSPS
60 70 80 90 100
AAAAAAAAVS SSAPEIVVSK PEHNNSNNLA LYGTGGGGST GGGGGGGGSG
110 120 130 140 150
HGSSSGTKSS KKKNQNIGYK LGHRRALFEK RKRLSDYALI FGMFGIVVMV
160 170 180 190 200
IETELSWGAY DKASLYSLAL KCLISLSTII LLGLIIVYHA REIQLFMVDN
210 220 230 240 250
GADDWRIAMT YERIFFICLE ILVCAIHPIP GNYTFTWTAR LAFSYAPSTT
260 270 280 290 300
TADVDIILSI PMFLRLYLIA RVMLLHSKLF TDASSRSIGA LNKINFNTRF
310 320 330 340 350
VMKTLMTICP GTVLLVFSIS LWIIAAWTVR ACERYHDQQD VTSNFLGAMW
360 370 380 390 400
LISITFLSIG YGDMVPNTYC GKGVCLLTGI MGAGCTALVV AVVARKLELT
410 420 430 440 450
KAEKHVHNFM MDTQLTKRVK NAAANVLRET WLIYKNTKLV KKIDHAKVRK
460 470 480 490 500
HQRKFLQAIH QLRSVKMEQR KLNDQANTLV DLAKTQNIMY DMISDLNERS
510 520 530 540 550
EDFEKRIVTL ETKLETLIGS IHALPGLISQ TIRQQQRDFI EAQMESYDKH
560 570
VTYNAERSRS SSRRRRSSST APPTSSESS
Length:579
Mass (Da):63,760
Last modified:October 14, 2008 - v2
Checksum:i2ED87FE13C106183
GO
Isoform 2 (identifier: Q9H2S1-2) [UniParc]FASTAAdd to basket

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

Show »
Length:231
Mass (Da):26,341
Checksum:i89BD2ED1EAD6E54B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501S → SA in AAK84039 (Ref. 3) Curated
Sequence conflicti52 – 521A → D in AAG16728 (PubMed:10991935).Curated
Sequence conflicti58 – 581A → AA in AAP45946 (PubMed:13679367).Curated
Sequence conflicti323 – 3231I → T in AAK84039 (Ref. 3) Curated
Sequence conflicti530 – 5301Q → R in AAP45946 (PubMed:13679367).Curated
Sequence conflicti530 – 5301Q → R in AAK84039 (Ref. 3) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 348348Missing in isoform 2. 1 PublicationVSP_044584Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4114.1. [Q9H2S1-1]
CCDS43352.1. [Q9H2S1-2]
RefSeqiNP_001265133.1. NM_001278204.1. [Q9H2S1-2]
NP_067627.2. NM_021614.3. [Q9H2S1-1]
NP_740721.1. NM_170775.2. [Q9H2S1-2]
UniGeneiHs.98280.

Genome annotation databases

EnsembliENST00000264773; ENSP00000264773; ENSG00000080709. [Q9H2S1-1]
ENST00000503706; ENSP00000421439; ENSG00000080709. [Q9H2S1-2]
ENST00000512097; ENSP00000427120; ENSG00000080709. [Q9H2S1-1]
ENST00000610748; ENSP00000483124; ENSG00000080709. [Q9H2S1-2]
GeneIDi3781.
KEGGihsa:3781.
UCSCiuc003kqo.3. human. [Q9H2S1-1]
uc003kqp.3. human.

Polymorphism databases

DMDMi209572638.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4114.1. [Q9H2S1-1]
CCDS43352.1. [Q9H2S1-2]
RefSeqiNP_001265133.1. NM_001278204.1. [Q9H2S1-2]
NP_067627.2. NM_021614.3. [Q9H2S1-1]
NP_740721.1. NM_170775.2. [Q9H2S1-2]
UniGeneiHs.98280.

3D structure databases

ProteinModelPortaliQ9H2S1.
SMRiQ9H2S1. Positions 322-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi109982. 6 interactions.
DIPiDIP-48997N.
IntActiQ9H2S1. 2 interactions.
STRINGi9606.ENSP00000264773.

Chemistry

BindingDBiQ9H2S1.
ChEMBLiCHEMBL4469.
DrugBankiDB01110. Miconazole.
DB00721. Procaine.
GuidetoPHARMACOLOGYi382.

Protein family/group databases

TCDBi1.A.1.16.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSiteiQ9H2S1.

Polymorphism databases

DMDMi209572638.

Proteomic databases

MaxQBiQ9H2S1.
PaxDbiQ9H2S1.
PRIDEiQ9H2S1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264773; ENSP00000264773; ENSG00000080709. [Q9H2S1-1]
ENST00000503706; ENSP00000421439; ENSG00000080709. [Q9H2S1-2]
ENST00000512097; ENSP00000427120; ENSG00000080709. [Q9H2S1-1]
ENST00000610748; ENSP00000483124; ENSG00000080709. [Q9H2S1-2]
GeneIDi3781.
KEGGihsa:3781.
UCSCiuc003kqo.3. human. [Q9H2S1-1]
uc003kqp.3. human.

Organism-specific databases

CTDi3781.
GeneCardsiGC05P113725.
HGNCiHGNC:6291. KCNN2.
HPAiHPA038221.
MIMi605879. gene.
neXtProtiNX_Q9H2S1.
PharmGKBiPA30071.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG320393.
GeneTreeiENSGT00500000044784.
HOGENOMiHOG000124679.
HOVERGENiHBG052241.
InParanoidiQ9H2S1.
KOiK04943.
OMAiAQMESYD.
PhylomeDBiQ9H2S1.
TreeFamiTF315015.

Enzyme and pathway databases

ReactomeiREACT_75896. Ca2+ activated K+ channels.

Miscellaneous databases

ChiTaRSiKCNN2. human.
GeneWikiiKCNN2.
GenomeRNAii3781.
NextBioi14837.
PROiQ9H2S1.
SOURCEiSearch...

Gene expression databases

BgeeiQ9H2S1.
CleanExiHS_KCNN2.
ExpressionAtlasiQ9H2S1. baseline and differential.
GenevestigatoriQ9H2S1.

Family and domain databases

InterProiIPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view]
PANTHERiPTHR10153. PTHR10153. 1 hit.
PfamiPF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view]
PRINTSiPR01451. SKCHANNEL.
SMARTiSM01053. CaMBD. 1 hit.
[Graphical view]
SUPFAMiSSF81327. SSF81327. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1999) [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(2002) [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 (JUN-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.
    , 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] (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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Brain and Skin.

Entry informationi

Entry nameiKCNN2_HUMAN
AccessioniPrimary (citable) accession number: Q9H2S1
Secondary accession number(s): A6NF94
, Q0VFZ4, Q6PJI0, Q6X2Y2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 16, 2001
Last sequence update: October 14, 2008
Last modified: April 1, 2015
This is version 127 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. 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.