KCIP2_HUMAN
ID KCIP2_HUMAN Reviewed; 270 AA.
AC Q9NS61; A6NJE5; A8MQ75; Q3YAC6; Q3YAC8; Q3YAC9; Q7Z6F1; Q96K86; Q96T41;
AC Q96T42; Q96T43; Q96T44; Q9H0N4; Q9HD10; Q9HD11; Q9NS60; Q9NY10; Q9NZI1;
DT 16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Kv channel-interacting protein 2;
DE Short=KChIP2 {ECO:0000303|PubMed:11684073};
DE AltName: Full=A-type potassium channel modulatory protein 2;
DE AltName: Full=Cardiac voltage-gated potassium channel modulatory subunit;
DE AltName: Full=Potassium channel-interacting protein 2;
GN Name=KCNIP2; Synonyms=KCHIP2;
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 [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP KCND2.
RX PubMed=10676964; DOI=10.1038/35000592;
RA An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
RA Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
RT "Modulation of A-type potassium channels by a family of calcium sensors.";
RL Nature 403:553-556(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), AND TISSUE SPECIFICITY.
RC TISSUE=Umbilical vein endothelial cell;
RX PubMed=11263977; DOI=10.1006/bbrc.2001.4558;
RA Ohya S., Morohashi Y., Muraki K., Tomita T., Watanabe M., Iwatsubo T.,
RA Imaizumi Y.;
RT "Molecular cloning and expression of the novel splice variants of K(+)
RT channel-interacting protein 2.";
RL Biochem. Biophys. Res. Commun. 282:96-102(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3),
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11684073; DOI=10.1016/s0008-6363(01)00374-1;
RA Decher N., Uyguner O., Scherer C.R., Karaman B., Yuksel-Apak M.,
RA Busch A.E., Steinmeyer K., Wollnik B.;
RT "hKChIP2 is a functional modifier of hKv4.3 potassium channels: cloning and
RT expression of a short hKChIP2 splice variant.";
RL Cardiovasc. Res. 52:255-264(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP KCND2.
RX PubMed=11287421; DOI=10.1074/jbc.m101320200;
RA Baehring R., Dannenberg J., Peters H.C., Leicher T., Pongs O., Isbrandt D.;
RT "Conserved Kv4 N-terminal domain critical for effects of Kv channel-
RT interacting protein 2.2 on channel expression and gating.";
RL J. Biol. Chem. 276:23888-23894(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 7).
RC TISSUE=Heart;
RA Juang G.J., Tomaselli G.F.;
RT "Modulatory elements of voltage gated potassium channels.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 8 AND 9).
RA Isbrandt D., Pongs O.;
RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 4), AND ALTERNATIVE SPLICING.
RX PubMed=16112838; DOI=10.1016/j.ygeno.2005.07.001;
RA Pruunsild P., Timmusk T.;
RT "Structure, alternative splicing, and expression of the human and mouse
RT KCNIP gene family.";
RL Genomics 86:581-593(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Kidney;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RA Li H., Zhong J., Zhou G., Shen C., Lin L., Yang S.;
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC TISSUE=Brain, and Embryo;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
RN [14]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 213-270.
RC TISSUE=Skeletal muscle;
RA Ievolella C., Trevisan S., Pacchioni B., Stanchi F., Frigimelica E.,
RA Scannapieco P., Corso V., Biasio B., Lanfranchi G.;
RT "Full-length of some muscular transcripts, Telethon (Italy) project B41.";
RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases.
RN [15]
RP FUNCTION, AND INTERACTION WITH KCND3.
RX PubMed=12297301; DOI=10.1016/s0014-5793(02)03296-9;
RA Deschenes I., Tomaselli G.F.;
RT "Modulation of Kv4.3 current by accessory subunits.";
RL FEBS Lett. 528:183-188(2002).
RN [16]
RP FUNCTION.
RX PubMed=12829703; DOI=10.1074/jbc.m306142200;
RA Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A.,
RA Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.;
RT "A fundamental role for KChIPs in determining the molecular properties and
RT trafficking of Kv4.2 potassium channels.";
RL J. Biol. Chem. 278:36445-36454(2003).
RN [17]
RP INTERACTION WITH KCNIP1 AND KCDN2, AND HOMOOLIGOMERIZATION.
RX PubMed=15358149; DOI=10.1016/j.bbrc.2004.07.006;
RA Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S.;
RT "Protein-protein interactions of KChIP proteins and Kv4.2.";
RL Biochem. Biophys. Res. Commun. 321:606-610(2004).
RN [18]
RP FUNCTION, COMPOSITION OF THE KCND2-KCNIP2 COMPLEX, AND SUBUNIT.
RX PubMed=14623880; DOI=10.1074/jbc.m311332200;
RA Kim L.A., Furst J., Butler M.H., Xu S., Grigorieff N., Goldstein S.A.;
RT "Ito channels are octameric complexes with four subunits of each Kv4.2 and
RT K+ channel-interacting protein 2.";
RL J. Biol. Chem. 279:5549-5554(2004).
RN [19]
RP TISSUE SPECIFICITY, AND INTERACTION WITH KCND2.
RX PubMed=15356203; DOI=10.1523/jneurosci.0776-04.2004;
RA Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M.,
RA Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F.,
RA Trimmer J.S.;
RT "KChIPs and Kv4 alpha subunits as integral components of A-type potassium
RT channels in mammalian brain.";
RL J. Neurosci. 24:7903-7915(2004).
RN [20]
RP STRUCTURE BY ELECTRON MICROSCOPY (21 ANGSTROMS) OF THE KCND2-KCNIP2
RP COMPLEX, AND SUBUNIT.
RX PubMed=14980201; DOI=10.1016/s0896-6273(04)00050-9;
RA Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A.,
RA Grigorieff N.;
RT "Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by
RT electron microscopy at 21 Angstrom resolution.";
RL Neuron 41:513-519(2004).
CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly
CC inactivating A-type potassium channels. Modulates channel density,
CC inactivation kinetics and rate of recovery from inactivation in a
CC calcium-dependent and isoform-specific manner. In vitro, modulates
CC KCND2/Kv4.2 and KCND3/Kv4.3 currents. Involved in KCND2 and KCND3
CC trafficking to the cell surface. May be required for the expression of
CC I(To) currents in the heart (By similarity).
CC {ECO:0000250|UniProtKB:Q9JJ69, ECO:0000269|PubMed:10676964,
CC ECO:0000269|PubMed:11287421, ECO:0000269|PubMed:11684073,
CC ECO:0000269|PubMed:12297301, ECO:0000269|PubMed:12829703,
CC ECO:0000269|PubMed:14623880}.
CC -!- SUBUNIT: Component of heteromultimeric potassium channels. Identified
CC in potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1,
CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). The KCND2-
CC KCNIP2 channel complex contains four KCND2 and four KCNIP2 subunits
CC (PubMed:14623880, PubMed:14980201). Interacts with KCND2
CC (PubMed:10676964, PubMed:14623880, PubMed:14980201). Isoform 1 and
CC isoform 3 interact with KCND3 isoform 1. Probably part of a complex
CC consisting of KCNIP1, KCNIP2 isoform 3 and KCND2. At least isoform 2
CC and isoform 3 can self-associate to form homodimers and homotetramers.
CC Isoform 3 interacts with KCNIP1 in a calcium-dependent manner.
CC {ECO:0000250|UniProtKB:Q9JJ69, ECO:0000269|PubMed:10676964,
CC ECO:0000269|PubMed:11287421, ECO:0000269|PubMed:12297301,
CC ECO:0000269|PubMed:14623880, ECO:0000269|PubMed:14980201,
CC ECO:0000269|PubMed:15356203, ECO:0000269|PubMed:15358149}.
CC -!- INTERACTION:
CC Q9NS61; Q9NZV8: KCND2; NbExp=3; IntAct=EBI-1052975, EBI-1646745;
CC Q9NS61-2; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-1053003, EBI-4403685;
CC Q9NS61-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1053003, EBI-5235340;
CC Q9NS61-3; Q9NZV8: KCND2; NbExp=3; IntAct=EBI-1053010, EBI-1646745;
CC Q9NS61-3; Q9NZI2: KCNIP1; NbExp=4; IntAct=EBI-1053010, EBI-2120635;
CC Q9NS61-3; Q9NS61-3: KCNIP2; NbExp=2; IntAct=EBI-1053010, EBI-1053010;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9JM59}. Note=Detected on lipid rafts (By
CC similarity). {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cell membrane
CC {ECO:0000250|UniProtKB:Q9JM59}; Lipid-anchor
CC {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=9;
CC Name=1; Synonyms=KChIP2a, KChIP2b, KCHIP2.4, KCHIP2L;
CC IsoId=Q9NS61-1; Sequence=Displayed;
CC Name=2; Synonyms=3, KChIP2.1, KChIP2b;
CC IsoId=Q9NS61-2; Sequence=VSP_015052;
CC Name=3; Synonyms=2, KChIP2.2, KChIP2c, KCHIP2S;
CC IsoId=Q9NS61-3; Sequence=VSP_015051;
CC Name=4;
CC IsoId=Q9NS61-4; Sequence=VSP_015050;
CC Name=5;
CC IsoId=Q9NS61-5; Sequence=VSP_015051, VSP_015056;
CC Name=6; Synonyms=KCHIP4.2;
CC IsoId=Q9NS61-6; Sequence=VSP_015053;
CC Name=7;
CC IsoId=Q9NS61-7; Sequence=VSP_015051, VSP_015055;
CC Name=8; Synonyms=KCHIP2.6;
CC IsoId=Q9NS61-8; Sequence=VSP_015049, VSP_015054;
CC Name=9; Synonyms=KCHIP2.5;
CC IsoId=Q9NS61-9; Sequence=VSP_015051, VSP_015057, VSP_015058;
CC -!- TISSUE SPECIFICITY: Expressed in brain. Colocalizes with KCND2 in
CC excitatory neurons including cortical and hippocampal CA1 pyramidal
CC cells. Isoform 3 is expressed in heart and in umbilical vein
CC endothelial cells. Not expressed in fetal heart.
CC {ECO:0000269|PubMed:11263977, ECO:0000269|PubMed:11684073,
CC ECO:0000269|PubMed:15356203}.
CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma
CC membrane. {ECO:0000250|UniProtKB:Q9JM59}.
CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}.
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DR EMBL; AF199598; AAF33683.1; -; mRNA.
DR EMBL; AB044584; BAA96740.1; -; mRNA.
DR EMBL; AB044585; BAA96741.1; -; mRNA.
DR EMBL; AY026328; AAK07674.1; -; mRNA.
DR EMBL; AY026331; AAK21972.1; -; Genomic_DNA.
DR EMBL; AY026329; AAK21972.1; JOINED; Genomic_DNA.
DR EMBL; AY026330; AAK21972.1; JOINED; Genomic_DNA.
DR EMBL; AF347114; AAK70356.1; -; mRNA.
DR EMBL; AF295076; AAG02120.1; -; mRNA.
DR EMBL; AF295530; AAG02121.1; -; mRNA.
DR EMBL; AF367018; AAK53707.1; -; mRNA.
DR EMBL; AF367019; AAK53708.1; -; mRNA.
DR EMBL; AF367020; AAK53709.1; -; mRNA.
DR EMBL; AF367021; AAK53710.1; -; mRNA.
DR EMBL; DQ148480; AAZ77797.1; -; mRNA.
DR EMBL; DQ148481; AAZ77798.1; -; mRNA.
DR EMBL; DQ148483; AAZ77800.1; -; mRNA.
DR EMBL; AL136722; CAB66656.1; -; mRNA.
DR EMBL; AY302141; AAP57633.1; -; mRNA.
DR EMBL; AK027347; BAB55052.1; -; mRNA.
DR EMBL; AK315042; BAG37523.1; -; mRNA.
DR EMBL; AC010789; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49733.1; -; Genomic_DNA.
DR EMBL; BC034685; AAH34685.1; -; mRNA.
DR EMBL; AJ276317; CAB77054.1; -; mRNA.
DR CCDS; CCDS41562.1; -. [Q9NS61-2]
DR CCDS; CCDS7521.1; -. [Q9NS61-6]
DR CCDS; CCDS7522.1; -. [Q9NS61-1]
DR CCDS; CCDS7523.1; -. [Q9NS61-7]
DR CCDS; CCDS7524.1; -. [Q9NS61-3]
DR CCDS; CCDS7525.1; -. [Q9NS61-4]
DR CCDS; CCDS7526.1; -. [Q9NS61-9]
DR RefSeq; NP_055406.2; NM_014591.4. [Q9NS61-6]
DR RefSeq; NP_775283.1; NM_173191.2. [Q9NS61-1]
DR RefSeq; NP_775284.1; NM_173192.2. [Q9NS61-2]
DR RefSeq; NP_775285.1; NM_173193.2. [Q9NS61-7]
DR RefSeq; NP_775286.1; NM_173194.2. [Q9NS61-4]
DR RefSeq; NP_775287.1; NM_173195.2. [Q9NS61-3]
DR RefSeq; NP_775289.1; NM_173197.2. [Q9NS61-9]
DR AlphaFoldDB; Q9NS61; -.
DR SMR; Q9NS61; -.
DR BioGRID; 119043; 14.
DR ComplexPortal; CPX-3239; Kv4.2-KChIP2 channel complex.
DR IntAct; Q9NS61; 10.
DR STRING; 9606.ENSP00000420040; -.
DR BindingDB; Q9NS61; -.
DR ChEMBL; CHEMBL2189164; -.
DR TCDB; 8.A.82.2.4; the calmodulin calcium binding protein (calmodulin) family.
DR iPTMnet; Q9NS61; -.
DR PhosphoSitePlus; Q9NS61; -.
DR SwissPalm; Q9NS61; -.
DR BioMuta; KCNIP2; -.
DR DMDM; 338817979; -.
DR MassIVE; Q9NS61; -.
DR PeptideAtlas; Q9NS61; -.
DR PRIDE; Q9NS61; -.
DR ProteomicsDB; 82483; -. [Q9NS61-1]
DR ProteomicsDB; 82484; -. [Q9NS61-2]
DR ProteomicsDB; 82485; -. [Q9NS61-3]
DR ProteomicsDB; 82486; -. [Q9NS61-4]
DR ProteomicsDB; 82487; -. [Q9NS61-5]
DR ProteomicsDB; 82488; -. [Q9NS61-6]
DR ProteomicsDB; 82489; -. [Q9NS61-7]
DR ProteomicsDB; 82490; -. [Q9NS61-8]
DR ProteomicsDB; 82491; -. [Q9NS61-9]
DR ABCD; Q9NS61; 2 sequenced antibodies.
DR Antibodypedia; 17919; 435 antibodies from 30 providers.
DR DNASU; 30819; -.
DR Ensembl; ENST00000239117.3; ENSP00000239117.3; ENSG00000120049.20. [Q9NS61-9]
DR Ensembl; ENST00000343195.8; ENSP00000344169.4; ENSG00000120049.20. [Q9NS61-3]
DR Ensembl; ENST00000348850.9; ENSP00000239118.6; ENSG00000120049.20. [Q9NS61-4]
DR Ensembl; ENST00000353068.7; ENSP00000341624.3; ENSG00000120049.20. [Q9NS61-7]
DR Ensembl; ENST00000356640.7; ENSP00000349055.2; ENSG00000120049.20. [Q9NS61-1]
DR Ensembl; ENST00000358038.7; ENSP00000350733.3; ENSG00000120049.20. [Q9NS61-2]
DR Ensembl; ENST00000434163.5; ENSP00000411679.1; ENSG00000120049.20. [Q9NS61-8]
DR Ensembl; ENST00000461105.5; ENSP00000420040.1; ENSG00000120049.20. [Q9NS61-6]
DR GeneID; 30819; -.
DR KEGG; hsa:30819; -.
DR MANE-Select; ENST00000356640.7; ENSP00000349055.2; NM_173191.3; NP_775283.1.
DR UCSC; uc001ktz.4; human. [Q9NS61-1]
DR CTD; 30819; -.
DR DisGeNET; 30819; -.
DR GeneCards; KCNIP2; -.
DR HGNC; HGNC:15522; KCNIP2.
DR HPA; ENSG00000120049; Tissue enhanced (adipose tissue, brain, heart muscle).
DR MIM; 604661; gene.
DR neXtProt; NX_Q9NS61; -.
DR OpenTargets; ENSG00000120049; -.
DR PharmGKB; PA30042; -.
DR VEuPathDB; HostDB:ENSG00000120049; -.
DR eggNOG; KOG0044; Eukaryota.
DR GeneTree; ENSGT00940000157798; -.
DR HOGENOM; CLU_1517380_0_0_1; -.
DR InParanoid; Q9NS61; -.
DR OMA; ELWEVVI; -.
DR TreeFam; TF318560; -.
DR PathwayCommons; Q9NS61; -.
DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels.
DR SignaLink; Q9NS61; -.
DR BioGRID-ORCS; 30819; 12 hits in 1072 CRISPR screens.
DR ChiTaRS; KCNIP2; human.
DR GeneWiki; KCNIP2; -.
DR GenomeRNAi; 30819; -.
DR Pharos; Q9NS61; Tbio.
DR PRO; PR:Q9NS61; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NS61; protein.
DR Bgee; ENSG00000120049; Expressed in apex of heart and 136 other tissues.
DR ExpressionAtlas; Q9NS61; baseline and differential.
DR Genevisible; Q9NS61; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0030425; C:dendrite; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034705; C:potassium channel complex; TAS:BHF-UCL.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
DR GO; GO:0046923; F:ER retention sequence binding; NAS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IDA:UniProtKB.
DR GO; GO:0005513; P:detection of calcium ion; TAS:ProtInc.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; TAS:BHF-UCL.
DR GO; GO:0006936; P:muscle contraction; NAS:UniProtKB.
DR GO; GO:1903766; P:positive regulation of potassium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; TAS:BHF-UCL.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0006813; P:potassium ion transport; TAS:UniProtKB.
DR GO; GO:0008016; P:regulation of heart contraction; TAS:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR028846; Recoverin.
DR PANTHER; PTHR23055; PTHR23055; 1.
DR Pfam; PF13499; EF-hand_7; 1.
DR Pfam; PF13833; EF-hand_8; 1.
DR SMART; SM00054; EFh; 3.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 3.
DR PROSITE; PS50222; EF_HAND_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Cell membrane; Ion channel; Ion transport;
KW Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Repeat;
KW Transport; Voltage-gated channel.
FT CHAIN 1..270
FT /note="Kv channel-interacting protein 2"
FT /id="PRO_0000073821"
FT DOMAIN 81..137
FT /note="EF-hand 1; degenerate"
FT /evidence="ECO:0000305"
FT DOMAIN 140..175
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 176..211
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 224..259
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..270
FT /note="Interaction with KCND2"
FT /evidence="ECO:0000250|UniProtKB:Q8R426"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 155
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 157
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 159
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 164
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 189
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 191
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 193
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 195
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 200
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 237
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 241
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 248
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT LIPID 45
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT LIPID 46
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:Q9JM59"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015049"
FT VAR_SEQ 1..73
FT /note="MRGQGRKESLSDSRDLDGSYDQLTGHPPGPTKKALKQRFLKLLPCCGPQALP
FT SVSETLAAPASLRPHRPRLLD -> MNRCPRRCRSPLGQAARSLYQLVTGSLS (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:11230166,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:16112838"
FT /id="VSP_015050"
FT VAR_SEQ 25..74
FT /note="Missing (in isoform 3, isoform 5, isoform 7 and
FT isoform 9)"
FT /evidence="ECO:0000303|PubMed:10676964,
FT ECO:0000303|PubMed:11263977, ECO:0000303|PubMed:11287421,
FT ECO:0000303|PubMed:11684073, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16112838,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6, ECO:0000303|Ref.9"
FT /id="VSP_015051"
FT VAR_SEQ 57..75
FT /note="TLAAPASLRPHRPRLLDPD -> N (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10676964,
FT ECO:0000303|PubMed:11263977, ECO:0000303|PubMed:11287421,
FT ECO:0000303|PubMed:11684073, ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16112838,
FT ECO:0000303|Ref.5"
FT /id="VSP_015052"
FT VAR_SEQ 57
FT /note="T -> IGRVFRFLGDSSLPSA (in isoform 6)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015053"
FT VAR_SEQ 94..162
FT /note="EQLQEQTKFTRKELQVLYRGFKNECPSGIVNEENFKQIYSQFFPQGDSSTYA
FT TFLFNAFDTNHDGSVSF -> MWLSWTAWTMNLNCPPCVTGLRVWSSCRSKPNSRARSC
FT RSCTGASRTNVPAELSMRRTSSRFTPSSFLK (in isoform 8)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015054"
FT VAR_SEQ 116
FT /note="N -> NPGALSFQ (in isoform 7)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_015055"
FT VAR_SEQ 160..163
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_015056"
FT VAR_SEQ 163..198
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015057"
FT VAR_SEQ 256..270
FT /note="DENIMRSMQLFDNVI -> VQLPALYITLTWTQA (in isoform 9)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_015058"
FT CONFLICT 50
FT /note="A -> V (in Ref. 2; BAA96740)"
FT /evidence="ECO:0000305"
FT CONFLICT 71
FT /note="L -> P (in Ref. 2; BAA96740)"
FT /evidence="ECO:0000305"
FT CONFLICT 75
FT /note="D -> V (in Ref. 2; BAA96741)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="S -> R (in Ref. 10; BAB55052)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="D -> E (in Ref. 2; BAA96740)"
FT /evidence="ECO:0000305"
FT CONFLICT 83
FT /note="L -> S (in Ref. 8; CAB66656)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="A -> P (in Ref. 2; BAA96740/BAA96741)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="N -> S (in Ref. 9; AAP57633)"
FT /evidence="ECO:0000305"
FT CONFLICT 246
FT /note="I -> N (in Ref. 8; CAB66656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 270 AA; 30907 MW; B75AD02B9E273243 CRC64;
MRGQGRKESL SDSRDLDGSY DQLTGHPPGP TKKALKQRFL KLLPCCGPQA LPSVSETLAA
PASLRPHRPR LLDPDSVDDE FELSTVCHRP EGLEQLQEQT KFTRKELQVL YRGFKNECPS
GIVNEENFKQ IYSQFFPQGD SSTYATFLFN AFDTNHDGSV SFEDFVAGLS VILRGTVDDR
LNWAFNLYDL NKDGCITKEE MLDIMKSIYD MMGKYTYPAL REEAPREHVE SFFQKMDRNK
DGVVTIEEFI ESCQKDENIM RSMQLFDNVI
