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Q9H2S1

- KCNN2_HUMAN

UniProt

Q9H2S1 - KCNN2_HUMAN

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Protein

Small conductance calcium-activated potassium channel protein 2

Gene

KCNN2

Organism
Homo sapiens (Human)
Status
Reviewed - 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: RefGenome
  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: Chromosome 5

Organism-specific databases

HGNCiHGNC:6291. KCNN2.

Subcellular locationi

GO - Cellular componenti

  1. dendritic spine Source: RefGenome
  2. integral component of membrane Source: UniProtKB
  3. neuronal cell body Source: RefGenome
  4. plasma membrane Source: RefGenome
  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...

Intramembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Intramembranei345 – 36521Pore-forming; Name=Segment H5Sequence AnalysisAdd
BLAST

Transmembrane

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
Transmembranei374 – 39421Helical; Name=Segment S6Sequence AnalysisAdd
BLAST

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.
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. Align

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. 1 PublicationCurated
Sequence conflicti52 – 521A → D in AAG16728. (PubMed:10991935)Curated
Sequence conflicti58 – 581A → AA in AAP45946. (PubMed:13679367)Curated
Sequence conflicti323 – 3231I → T in AAK84039. 1 PublicationCurated
Sequence conflicti530 – 5301Q → R in AAP45946. (PubMed:13679367)Curated
Sequence conflicti530 – 5301Q → R in AAK84039. 1 PublicationCurated

Alternative sequence

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS4114.1. [Q9H2S1-1 ]
CCDS43352.1. [Q9H2S1-2 ]
RefSeqi NP_001265133.1. NM_001278204.1. [Q9H2S1-2 ]
NP_067627.2. NM_021614.3. [Q9H2S1-1 ]
NP_740721.1. NM_170775.2. [Q9H2S1-2 ]
UniGenei Hs.98280.

3D structure databases

ProteinModelPortali Q9H2S1.
SMRi Q9H2S1. Positions 322-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109982. 6 interactions.
DIPi DIP-48997N.
IntActi Q9H2S1. 2 interactions.
STRINGi 9606.ENSP00000264773.

Chemistry

BindingDBi Q9H2S1.
ChEMBLi CHEMBL4469.
DrugBanki DB01110. Miconazole.
DB00721. Procaine.
GuidetoPHARMACOLOGYi 382.

Protein family/group databases

TCDBi 1.A.1.16.1. the voltage-gated ion channel (vic) superfamily.

PTM databases

PhosphoSitei Q9H2S1.

Polymorphism databases

DMDMi 209572638.

Proteomic databases

MaxQBi Q9H2S1.
PaxDbi Q9H2S1.
PRIDEi Q9H2S1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264773 ; ENSP00000264773 ; ENSG00000080709 . [Q9H2S1-1 ]
ENST00000503706 ; ENSP00000421439 ; ENSG00000080709 . [Q9H2S1-2 ]
ENST00000512097 ; ENSP00000427120 ; ENSG00000080709 . [Q9H2S1-1 ]
ENST00000610748 ; ENSP00000483124 ; ENSG00000080709 . [Q9H2S1-2 ]
GeneIDi 3781.
KEGGi hsa:3781.
UCSCi uc003kqo.3. human. [Q9H2S1-1 ]
uc003kqp.3. human.

Organism-specific databases

CTDi 3781.
GeneCardsi GC05P113725.
HGNCi HGNC:6291. KCNN2.
HPAi HPA038221.
MIMi 605879. gene.
neXtProti NX_Q9H2S1.
PharmGKBi PA30071.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG320393.
GeneTreei ENSGT00500000044784.
HOVERGENi HBG052241.
InParanoidi Q9H2S1.
KOi K04943.
OMAi AQMESYD.
PhylomeDBi Q9H2S1.
TreeFami TF315015.

Enzyme and pathway databases

Reactomei REACT_75896. Ca2+ activated K+ channels.

Miscellaneous databases

GeneWikii KCNN2.
GenomeRNAii 3781.
NextBioi 14837.
PROi Q9H2S1.
SOURCEi Search...

Gene expression databases

Bgeei Q9H2S1.
CleanExi HS_KCNN2.
ExpressionAtlasi Q9H2S1. baseline and differential.
Genevestigatori Q9H2S1.

Family and domain databases

InterProi IPR013099. 2pore_dom_K_chnl_dom.
IPR004178. CaM-bd_dom.
IPR015449. K_chnl_Ca-activ_SK.
[Graphical view ]
PANTHERi PTHR10153. PTHR10153. 1 hit.
Pfami PF02888. CaMBD. 1 hit.
PF07885. Ion_trans_2. 1 hit.
PF03530. SK_channel. 1 hit.
[Graphical view ]
PRINTSi PR01451. SKCHANNEL.
SMARTi SM01053. CaMBD. 1 hit.
[Graphical view ]
SUPFAMi SSF81327. SSF81327. 1 hit.
ProtoNeti Search...

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(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.
    , 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.
    , 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. 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.

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: October 29, 2014
This is version 122 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