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KCNS2_HUMAN
ID   KCNS2_HUMAN             Reviewed;         477 AA.
AC   Q9ULS6; A8KAN1;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 2.
DT   03-AUG-2022, entry version 168.
DE   RecName: Full=Potassium voltage-gated channel subfamily S member 2;
DE   AltName: Full=Delayed-rectifier K(+) channel alpha subunit 2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv9.2;
GN   Name=KCNS2; Synonyms=KIAA1144;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=10574461; DOI=10.1093/dnares/6.5.329;
RA   Hirosawa M., Nagase T., Ishikawa K., Kikuno R., Nomura N., Ohara O.;
RT   "Characterization of cDNA clones selected by the GeneMark analysis from
RT   size-fractionated cDNA libraries from human brain.";
RL   DNA Res. 6:329-336(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: Potassium channel subunit that does not form functional
CC       channels by itself. Can form functional heterotetrameric channels with
CC       KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated
CC       potassium channel activation and deactivation rates of KCNB1 and KCNB2.
CC       {ECO:0000250|UniProtKB:O35174}.
CC   -!- SUBUNIT: Heterotetramer with KCNB1 and KCNB2. Does not form
CC       homomultimers. {ECO:0000250|UniProtKB:O35174}.
CC   -!- INTERACTION:
CC       Q9ULS6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-10323864, EBI-3867333;
CC       Q9ULS6; Q969F0: FATE1; NbExp=6; IntAct=EBI-10323864, EBI-743099;
CC       Q9ULS6; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-10323864, EBI-22310682;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35174};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:O35174}. Note=May
CC       not reach the plasma membrane but remain in an intracellular
CC       compartment in the absence of KCNB1 or KCNB2.
CC       {ECO:0000250|UniProtKB:O35174}.
CC   -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC       characterized by a series of positively charged amino acids at every
CC       third position. Channel opening and closing is effected by a
CC       conformation change that affects the position and orientation of the
CC       voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC       transmembrane electric field that is positive inside would push the
CC       positively charged S4 segment outwards, thereby opening the pore, while
CC       a field that is negative inside would pull the S4 segment inwards and
CC       close the pore. Changes in the position and orientation of S4 are then
CC       transmitted to the activation gate formed by the inner helix bundle via
CC       the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2)
CC       subfamily. Kv9.2/KCNS2 sub-subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA86458.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AB032970; BAA86458.1; ALT_INIT; mRNA.
DR   EMBL; AK293096; BAF85785.1; -; mRNA.
DR   EMBL; CH471060; EAW91780.1; -; Genomic_DNA.
DR   EMBL; BC027932; AAH27932.1; -; mRNA.
DR   EMBL; BC034778; AAH34778.1; -; mRNA.
DR   CCDS; CCDS6279.1; -.
DR   RefSeq; NP_065748.1; NM_020697.3.
DR   AlphaFoldDB; Q9ULS6; -.
DR   SMR; Q9ULS6; -.
DR   BioGRID; 109989; 5.
DR   IntAct; Q9ULS6; 3.
DR   STRING; 9606.ENSP00000287042; -.
DR   ChEMBL; CHEMBL2362996; -.
DR   DrugCentral; Q9ULS6; -.
DR   TCDB; 1.A.1.2.16; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; Q9ULS6; -.
DR   PhosphoSitePlus; Q9ULS6; -.
DR   BioMuta; KCNS2; -.
DR   DMDM; 24418481; -.
DR   MassIVE; Q9ULS6; -.
DR   PaxDb; Q9ULS6; -.
DR   PeptideAtlas; Q9ULS6; -.
DR   PRIDE; Q9ULS6; -.
DR   ProteomicsDB; 85103; -.
DR   Antibodypedia; 26073; 191 antibodies from 26 providers.
DR   DNASU; 3788; -.
DR   Ensembl; ENST00000287042.5; ENSP00000287042.4; ENSG00000156486.8.
DR   Ensembl; ENST00000521839.1; ENSP00000430712.1; ENSG00000156486.8.
DR   GeneID; 3788; -.
DR   KEGG; hsa:3788; -.
DR   MANE-Select; ENST00000287042.5; ENSP00000287042.4; NM_020697.4; NP_065748.1.
DR   UCSC; uc003yin.4; human.
DR   CTD; 3788; -.
DR   DisGeNET; 3788; -.
DR   GeneCards; KCNS2; -.
DR   HGNC; HGNC:6301; KCNS2.
DR   HPA; ENSG00000156486; Tissue enhanced (brain).
DR   MIM; 602906; gene.
DR   neXtProt; NX_Q9ULS6; -.
DR   OpenTargets; ENSG00000156486; -.
DR   PharmGKB; PA30079; -.
DR   VEuPathDB; HostDB:ENSG00000156486; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000160344; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; Q9ULS6; -.
DR   OMA; STIPACW; -.
DR   OrthoDB; 818306at2759; -.
DR   PhylomeDB; Q9ULS6; -.
DR   TreeFam; TF313103; -.
DR   PathwayCommons; Q9ULS6; -.
DR   Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR   SignaLink; Q9ULS6; -.
DR   BioGRID-ORCS; 3788; 8 hits in 1064 CRISPR screens.
DR   GeneWiki; KCNS2; -.
DR   GenomeRNAi; 3788; -.
DR   Pharos; Q9ULS6; Tclin.
DR   PRO; PR:Q9ULS6; -.
DR   Proteomes; UP000005640; Chromosome 8.
DR   RNAct; Q9ULS6; protein.
DR   Bgee; ENSG00000156486; Expressed in endothelial cell and 105 other tissues.
DR   Genevisible; Q9ULS6; HS.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   Gene3D; 1.20.120.350; -; 1.
DR   Gene3D; 3.30.710.10; -; 1.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv9.
DR   InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..477
FT                   /note="Potassium voltage-gated channel subfamily S member
FT                   2"
FT                   /id="PRO_0000054084"
FT   TOPO_DOM        1..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        185..206
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        207..225
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        226..248
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        249..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        281..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        291..311
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        312..326
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        327..348
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        349..361
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        362..373
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        374..381
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        382..388
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        389..417
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        418..477
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   MOTIF           374..379
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
SQ   SEQUENCE   477 AA;  54237 MW;  F231AD99EC02EB46 CRC64;
     MTGQSLWDVS EANVEDGEIR INVGGFKRRL RSHTLLRFPE TRLGRLLLCH SREAILELCD
     DYDDVQREFY FDRNPELFPY VLHFYHTGKL HVMAELCVFS FSQEIEYWGI NEFFIDSCCS
     YSYHGRKVEP EQEKWDEQSD QESTTSSFDE ILAFYNDASK FDGQPLGNFR RQLWLALDNP
     GYSVLSRVFS ILSILVVMGS IITMCLNSLP DFQIPDSQGN PGEDPRFEIV EHFGIAWFTF
     ELVARFAVAP DFLKFFKNAL NLIDLMSIVP FYITLVVNLV VESTPTLANL GRVAQVLRLM
     RIFRILKLAR HSTGLRSLGA TLKYSYKEVG LLLLYLSVGI SIFSVVAYTI EKEENEGLAT
     IPACWWWATV SMTTVGYGDV VPGTTAGKLT ASACILAGIL VVVLPITLIF NKFSHFYRRQ
     KQLESAMRSC DFGDGMKEVP SVNLRDYYAH KVKSLMASLT NMSRSSPSEL SLNDSLR
 
 
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