ID CSEN_HUMAN Reviewed; 256 AA. AC Q9Y2W7; H7BY46; Q3YAC3; Q3YAC4; Q53TJ5; Q96T40; Q9UJ84; Q9UJ85; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1999, sequence version 1. DT 24-JAN-2024, entry version 201. DE RecName: Full=Calsenilin; DE AltName: Full=A-type potassium channel modulatory protein 3; DE AltName: Full=DRE-antagonist modulator; DE Short=DREAM; DE AltName: Full=Kv channel-interacting protein 3; DE Short=KChIP3; GN Name=KCNIP3; Synonyms=CSEN, DREAM, KCHIP3; 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 1), AND FUNCTION IN PRESENILIN RP REGULATION. RX PubMed=9771752; DOI=10.1038/2673; RA Buxbaum J.D., Choi E.K., Luo Y., Lilliehook C., Crowley A.C., Merriam D.E., RA Wasco W.; RT "Calsenilin: a calcium-binding protein that interacts with the presenilins RT and regulates the levels of a presenilin fragment."; RL Nat. Med. 4:1177-1181(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN TRANSCRIPTION RP REGULATION. RC TISSUE=Caudate nucleus; RX PubMed=10078534; DOI=10.1038/18044; RA Carrion A.M., Link W.A., Ledo F., Mellstrom B., Naranjo J.R.; RT "DREAM is a Ca2+-regulated transcriptional repressor."; RL Nature 398:80-84(1999). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION IN POTASSIUM RP TRANSPORT. 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 [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3), 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 [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RA Isbrandt D., Pongs O.; RL Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [9] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [11] RP INTERACTION WITH PSEN2, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND RP MUTAGENESIS OF ASP-61 AND ASP-64. RX PubMed=11278424; DOI=10.1074/jbc.m008597200; RA Choi E.K., Zaidi N.F., Miller J.S., Crowley A.C., Merriam D.E., RA Lilliehook C., Buxbaum J.D., Wasco W.; RT "Calsenilin is a substrate for caspase-3 that preferentially interacts with RT the familial Alzheimer's disease-associated C-terminal fragment of RT presenilin 2."; RL J. Biol. Chem. 276:19197-19204(2001). RN [12] RP FUNCTION IN APOPTOSIS. RX PubMed=11259376; DOI=10.1096/fj.00-0541fje; RA Jo D.G., Kim M.J., Choi Y.H., Kim I.K., Song Y.H., Woo H.N., Chung C.W., RA Jung Y.K.; RT "Pro-apoptotic function of calsenilin/DREAM/KChIP3."; RL FASEB J. 15:589-591(2001). RN [13] RP FUNCTION IN APOPTOSIS. RX PubMed=11988022; DOI=10.1006/mcne.2001.1096; RA Lilliehook C., Chan S., Choi E.K., Zaidi N.F., Wasco W., Mattson M.P., RA Buxbaum J.D.; RT "Calsenilin enhances apoptosis by altering endoplasmic reticulum calcium RT signaling."; RL Mol. Cell. Neurosci. 19:552-559(2002). RN [14] RP FUNCTION IN POTASSIUM TRANSPORT. 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 [15] RP PHOSPHORYLATION AT SER-63. RX PubMed=12837631; DOI=10.1016/s1044-7431(03)00072-1; RA Choi E.K., Miller J.S., Zaidi N.F., Salih E., Buxbaum J.D., Wasco W.; RT "Phosphorylation of calsenilin at Ser63 regulates its cleavage by caspase- RT 3."; RL Mol. Cell. Neurosci. 23:495-506(2003). RN [16] RP INTERACTION WITH KCND2, FUNCTION IN POTASSIUM TRANSPORT, SUBUNIT, AND RP SUBCELLULAR LOCATION. RX PubMed=15485870; DOI=10.1074/jbc.m409721200; RA Kunjilwar K., Strang C., DeRubeis D., Pfaffinger P.J.; RT "KChIP3 rescues the functional expression of Shal channel tetramerization RT mutants."; RL J. Biol. Chem. 279:54542-54551(2004). RN [17] RP TISSUE SPECIFICITY. RX PubMed=14720210; DOI=10.1111/j.1471-4159.2004.02159.x; RA Jo D.G., Lee J.Y., Hong Y.M., Song S., Mook-Jung I., Koh J.Y., Jung Y.K.; RT "Induction of pro-apoptotic calsenilin/DREAM/KChIP3 in Alzheimer's disease RT and cultured neurons after amyloid-beta exposure."; RL J. Neurochem. 88:604-611(2004). RN [18] RP FUNCTION IN POTASSIUM TRANSPORT. RX PubMed=16123112; DOI=10.1113/jphysiol.2005.087858; RA Jerng H.H., Kunjilwar K., Pfaffinger P.J.; RT "Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel RT complexes with ISA-like properties."; RL J. Physiol. (Lond.) 568:767-788(2005). RN [19] RP FUNCTION IN POTASSIUM TRANSPORT, INTERACTION WITH KCND2, AND SUBCELLULAR RP LOCATION. RX PubMed=18957440; DOI=10.1074/jbc.m806852200; RA Jerng H.H., Pfaffinger P.J.; RT "Multiple Kv channel-interacting proteins contain an N-terminal RT transmembrane domain that regulates Kv4 channel trafficking and gating."; RL J. Biol. Chem. 283:36046-36059(2008). RN [20] RP SUMOYLATION AT LYS-26 AND LYS-90, AND SUBCELLULAR LOCATION. RX PubMed=21070824; DOI=10.1016/j.bbamcr.2010.11.001; RA Palczewska M., Casafont I., Ghimire K., Rojas A.M., Valencia A., RA Lafarga M., Mellstrom B., Naranjo J.R.; RT "Sumoylation regulates nuclear localization of repressor DREAM."; RL Biochim. Biophys. Acta 1813:1050-1058(2011). RN [21] RP STRUCTURE BY NMR OF 161-256, SUBUNIT, AND CALCIUM-BINDING. RX PubMed=17962406; DOI=10.1110/ps.072928007; RA Yu L., Sun C., Mendoza R., Wang J., Matayoshi E.D., Hebert E., RA Pereda-Lopez A., Hajduk P.J., Olejniczak E.T.; RT "Solution structure and calcium-binding properties of EF-hands 3 and 4 of RT calsenilin."; RL Protein Sci. 16:2502-2509(2007). RN [22] RP VARIANTS [LARGE SCALE ANALYSIS] SER-170 AND TYR-179. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Calcium-dependent transcriptional repressor that binds to the CC DRE element of genes including PDYN and FOS. Affinity for DNA is CC reduced upon binding to calcium and enhanced by binding to magnesium. CC Seems to be involved in nociception (By similarity). CC {ECO:0000250|UniProtKB:Q9QXT8}. CC -!- FUNCTION: Regulatory subunit of Kv4/D (Shal)-type voltage-gated rapidly CC inactivating A-type potassium channels, such as KCND2/Kv4.2 and CC KCND3/Kv4.3. Modulates channel expression at the cell membrane, gating CC characteristics, inactivation kinetics and rate of recovery from CC inactivation in a calcium-dependent and isoform-specific manner. CC {ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:12829703, CC ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:16123112, CC ECO:0000269|PubMed:18957440}. CC -!- FUNCTION: May play a role in the regulation of PSEN2 proteolytic CC processing and apoptosis. Together with PSEN2 involved in modulation of CC amyloid-beta formation. {ECO:0000269|PubMed:11259376, CC ECO:0000269|PubMed:11988022, ECO:0000269|PubMed:9771752}. CC -!- SUBUNIT: Binds to DNA as a homomultimer. Dimerization is induced by CC binding to calcium (PubMed:17962406). Interacts with the C-terminus of CC PSEN1 and PSEN2 and with PSEN2 CTF subunit. Associates with KCN1. CC Component of heteromultimeric potassium channels. Identified in CC potassium channel complexes containing KCND1, KCND2, KCND3, KCNIP1, CC KCNIP2, KCNIP3, KCNIP4, DPP6 and DPP10 (By similarity). Interacts with CC KCND2 and KCND3. {ECO:0000250|UniProtKB:Q9QXT8, CC ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:15485870, CC ECO:0000269|PubMed:17962406, ECO:0000269|PubMed:18957440}. CC -!- INTERACTION: CC Q9Y2W7; P05067: APP; NbExp=3; IntAct=EBI-751501, EBI-77613; CC Q9Y2W7; Q12797-6: ASPH; NbExp=3; IntAct=EBI-751501, EBI-12092171; CC Q9Y2W7; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-751501, EBI-2817707; CC Q9Y2W7; Q8N6Q3: CD177; NbExp=9; IntAct=EBI-751501, EBI-747170; CC Q9Y2W7; O14843: FFAR3; NbExp=3; IntAct=EBI-751501, EBI-17762181; CC Q9Y2W7; Q7Z5G4: GOLGA7; NbExp=3; IntAct=EBI-751501, EBI-4403685; CC Q9Y2W7; P08069: IGF1R; NbExp=6; IntAct=EBI-751501, EBI-475981; CC Q9Y2W7; P40189: IL6ST; NbExp=7; IntAct=EBI-751501, EBI-1030834; CC Q9Y2W7; Q17RA0: IL6ST; NbExp=3; IntAct=EBI-751501, EBI-10238517; CC Q9Y2W7; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-751501, EBI-9089060; CC Q9Y2W7; P57682: KLF3; NbExp=3; IntAct=EBI-751501, EBI-8472267; CC Q9Y2W7; Q7Z434: MAVS; NbExp=3; IntAct=EBI-751501, EBI-995373; CC Q9Y2W7; Q8WZ73-3: RFFL; NbExp=3; IntAct=EBI-751501, EBI-25839575; CC Q9Y2W7; P08865: RPSA; NbExp=3; IntAct=EBI-751501, EBI-354112; CC Q9Y2W7; P08294: SOD3; NbExp=6; IntAct=EBI-751501, EBI-10195782; CC Q9Y2W7; Q86TD4-2: SRL; NbExp=3; IntAct=EBI-751501, EBI-12304565; CC Q9Y2W7; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-751501, EBI-12090309; CC Q9Y2W7; Q8IUR5-4: TMTC1; NbExp=3; IntAct=EBI-751501, EBI-9089156; CC Q9Y2W7; O60844: ZG16; NbExp=3; IntAct=EBI-751501, EBI-746479; CC Q9Y2W7; A0A1U9X8X8; NbExp=3; IntAct=EBI-751501, EBI-17234977; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18957440}. Cell CC membrane {ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:18957440}; CC Lipid-anchor {ECO:0000250}. Endoplasmic reticulum CC {ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:18957440}. Golgi CC apparatus {ECO:0000269|PubMed:11278424}. Nucleus CC {ECO:0000269|PubMed:21070824}. Note=Also membrane-bound, associated CC with the plasma membrane (PubMed:15485870). In the presence of PSEN2 CC associated with the endoplasmic reticulum and Golgi. The sumoylated CC form is present only in the nucleus. {ECO:0000269|PubMed:11278424, CC ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:21070824}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=KChIP3.1; CC IsoId=Q9Y2W7-1; Sequence=Displayed; CC Name=2; Synonyms=KChIP3.2, KChIP4.2; CC IsoId=Q9Y2W7-2; Sequence=VSP_015040; CC Name=3; Synonyms=KChip3.x; CC IsoId=Q9Y2W7-3; Sequence=VSP_040982, VSP_040983; CC -!- TISSUE SPECIFICITY: Highly expressed in brain. Widely expressed at CC lower levels. Expression levels are elevated in brain cortex regions CC affected by Alzheimer disease. {ECO:0000269|PubMed:14720210}. CC -!- PTM: Palmitoylated. Palmitoylation enhances association with the plasma CC membrane (By similarity). {ECO:0000250}. CC -!- PTM: Proteolytically cleaved by caspase-3. CC {ECO:0000269|PubMed:11278424}. CC -!- PTM: Phosphorylation at Ser-63 inhibits cleavage by CASP3. CC {ECO:0000269|PubMed:11278424, ECO:0000269|PubMed:12837631}. CC -!- SIMILARITY: Belongs to the recoverin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF120102; AAD20350.1; -; mRNA. DR EMBL; AJ131730; CAB56836.1; -; mRNA. DR EMBL; AJ131730; CAB56835.1; -; mRNA. DR EMBL; AF199599; AAF33684.1; -; mRNA. DR EMBL; DQ148485; AAZ77802.1; -; mRNA. DR EMBL; DQ148486; AAZ77803.1; -; mRNA. DR EMBL; AF367022; AAK53711.1; -; mRNA. DR EMBL; BT020075; AAV38878.1; -; mRNA. DR EMBL; AK315437; BAG37825.1; -; mRNA. DR EMBL; AC009238; AAY14752.1; -; Genomic_DNA. DR EMBL; CH471219; EAX10724.1; -; Genomic_DNA. DR EMBL; BC012850; AAH12850.1; -; mRNA. DR CCDS; CCDS2013.1; -. [Q9Y2W7-1] DR CCDS; CCDS33245.1; -. [Q9Y2W7-3] DR RefSeq; NP_001030086.1; NM_001034914.1. [Q9Y2W7-3] DR RefSeq; NP_038462.1; NM_013434.4. [Q9Y2W7-1] DR PDB; 2E6W; NMR; -; A=161-256. DR PDBsum; 2E6W; -. DR AlphaFoldDB; Q9Y2W7; -. DR SMR; Q9Y2W7; -. DR BioGRID; 119042; 33. DR IntAct; Q9Y2W7; 25. DR STRING; 9606.ENSP00000295225; -. DR TCDB; 8.A.82.2.5; the calmodulin calcium binding protein (calmodulin) family. DR iPTMnet; Q9Y2W7; -. DR PhosphoSitePlus; Q9Y2W7; -. DR BioMuta; KCNIP3; -. DR DMDM; 13431428; -. DR MassIVE; Q9Y2W7; -. DR PaxDb; 9606-ENSP00000295225; -. DR PeptideAtlas; Q9Y2W7; -. DR ProteomicsDB; 43500; -. DR ProteomicsDB; 85919; -. [Q9Y2W7-1] DR ProteomicsDB; 85920; -. [Q9Y2W7-2] DR ProteomicsDB; 85921; -. [Q9Y2W7-3] DR ABCD; Q9Y2W7; 2 sequenced antibodies. DR Antibodypedia; 4181; 600 antibodies from 41 providers. DR DNASU; 30818; -. DR Ensembl; ENST00000295225.10; ENSP00000295225.5; ENSG00000115041.14. [Q9Y2W7-1] DR Ensembl; ENST00000468529.1; ENSP00000417499.1; ENSG00000115041.14. [Q9Y2W7-3] DR GeneID; 30818; -. DR KEGG; hsa:30818; -. DR MANE-Select; ENST00000295225.10; ENSP00000295225.5; NM_013434.5; NP_038462.1. DR UCSC; uc002sup.4; human. [Q9Y2W7-1] DR AGR; HGNC:15523; -. DR CTD; 30818; -. DR DisGeNET; 30818; -. DR GeneCards; KCNIP3; -. DR HGNC; HGNC:15523; KCNIP3. DR HPA; ENSG00000115041; Tissue enhanced (brain, lymphoid tissue, parathyroid gland). DR MIM; 604662; gene. DR neXtProt; NX_Q9Y2W7; -. DR OpenTargets; ENSG00000115041; -. DR PharmGKB; PA26934; -. DR VEuPathDB; HostDB:ENSG00000115041; -. DR eggNOG; KOG0044; Eukaryota. DR GeneTree; ENSGT00940000158782; -. DR HOGENOM; CLU_072366_2_2_1; -. DR InParanoid; Q9Y2W7; -. DR OMA; GMELCAI; -. DR OrthoDB; 339700at2759; -. DR PhylomeDB; Q9Y2W7; -. DR TreeFam; TF318560; -. DR PathwayCommons; Q9Y2W7; -. DR Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels. DR Reactome; R-HSA-9768777; Regulation of NPAS4 gene transcription. DR SignaLink; Q9Y2W7; -. DR SIGNOR; Q9Y2W7; -. DR BioGRID-ORCS; 30818; 22 hits in 1155 CRISPR screens. DR ChiTaRS; KCNIP3; human. DR EvolutionaryTrace; Q9Y2W7; -. DR GeneWiki; Calsenilin; -. DR GenomeRNAi; 30818; -. DR Pharos; Q9Y2W7; Tbio. DR PRO; PR:Q9Y2W7; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9Y2W7; Protein. DR Bgee; ENSG00000115041; Expressed in right frontal lobe and 110 other cell types or tissues. DR ExpressionAtlas; Q9Y2W7; baseline and differential. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; TAS:Reactome. DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:ARUK-UCL. DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW. DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:ARUK-UCL. DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:ARUK-UCL. DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB. DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB. DR GO; GO:0007165; P:signal transduction; TAS:ProtInc. DR CDD; cd00051; EFh; 2. DR Gene3D; 1.10.238.10; EF-hand; 1. 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; CALCIUM BINDING PROTEINS; 1. DR PANTHER; PTHR23055:SF165; CALSENILIN; 1. DR Pfam; PF13499; EF-hand_7; 1. DR Pfam; PF13833; EF-hand_8; 1. DR PRINTS; PR00450; RECOVERIN. DR SMART; SM00054; EFh; 3. DR SUPFAM; SSF47473; EF-hand; 1. DR PROSITE; PS00018; EF_HAND_1; 2. DR PROSITE; PS50222; EF_HAND_2; 3. DR Genevisible; Q9Y2W7; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Calcium; Cell membrane; KW Cytoplasm; Endoplasmic reticulum; Golgi apparatus; Ion channel; KW Ion transport; Isopeptide bond; Lipoprotein; Membrane; Metal-binding; KW Nucleus; Palmitate; Phosphoprotein; Potassium; Potassium channel; KW Potassium transport; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Transport; Ubl conjugation; KW Voltage-gated channel. FT CHAIN 1..256 FT /note="Calsenilin" FT /id="PRO_0000073814" FT DOMAIN 67..123 FT /note="EF-hand 1; degenerate" FT /evidence="ECO:0000305" FT DOMAIN 126..161 FT /note="EF-hand 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 162..197 FT /note="EF-hand 3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT DOMAIN 210..245 FT /note="EF-hand 4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 243..256 FT /note="Interaction with KCND2" FT /evidence="ECO:0000250" FT BINDING 175 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 177 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 179 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 181 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 186 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 223 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 225 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 227 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT BINDING 234 FT /ligand="Ca(2+)" FT /ligand_id="ChEBI:CHEBI:29108" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448" FT MOD_RES 14 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JM47" FT MOD_RES 60 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9QXT8" FT MOD_RES 63 FT /note="Phosphoserine; by CK1" FT /evidence="ECO:0000269|PubMed:12837631" FT LIPID 45 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT LIPID 46 FT /note="S-palmitoyl cysteine" FT /evidence="ECO:0000250" FT CROSSLNK 26 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:21070824" FT CROSSLNK 90 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO1)" FT /evidence="ECO:0000269|PubMed:21070824" FT VAR_SEQ 1..26 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16112838" FT /id="VSP_040982" FT VAR_SEQ 27..60 FT /note="KEGIKWQRPRLSRQALMRCCLVKWILSSTAPQGS -> MGIQGMELCAMAVV FT VLLFIAVLKQFGILEPISME (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16112838" FT /id="VSP_040983" FT VAR_SEQ 103..124 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|Ref.5" FT /id="VSP_015040" FT VARIANT 119 FT /note="A -> V (in dbSNP:rs35658670)" FT /id="VAR_048663" FT VARIANT 170 FT /note="A -> S (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035463" FT VARIANT 179 FT /note="D -> Y (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_035464" FT MUTAGEN 61 FT /note="D->A: Abolishes cleavage by caspase-3." FT /evidence="ECO:0000269|PubMed:11278424" FT MUTAGEN 64 FT /note="D->A: Abolishes cleavage by caspase-3." FT /evidence="ECO:0000269|PubMed:11278424" FT CONFLICT 182 FT /note="I -> V (in Ref. 2; CAB56836/CAB56835)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="R -> Q (in Ref. 2; CAB56836/CAB56835)" FT /evidence="ECO:0000305" FT HELIX 164..174 FT /evidence="ECO:0007829|PDB:2E6W" FT STRAND 179..182 FT /evidence="ECO:0007829|PDB:2E6W" FT HELIX 184..193 FT /evidence="ECO:0007829|PDB:2E6W" FT STRAND 211..213 FT /evidence="ECO:0007829|PDB:2E6W" FT HELIX 214..222 FT /evidence="ECO:0007829|PDB:2E6W" FT STRAND 227..231 FT /evidence="ECO:0007829|PDB:2E6W" FT HELIX 232..239 FT /evidence="ECO:0007829|PDB:2E6W" FT HELIX 243..254 FT /evidence="ECO:0007829|PDB:2E6W" SQ SEQUENCE 256 AA; 29231 MW; 635C3EDF8B91E1C5 CRC64; MQPAKEVTKA SDGSLLGDLG HTPLSKKEGI KWQRPRLSRQ ALMRCCLVKW ILSSTAPQGS DSSDSELELS TVRHQPEGLD QLQAQTKFTK KELQSLYRGF KNECPTGLVD EDTFKLIYAQ FFPQGDATTY AHFLFNAFDA DGNGAIHFED FVVGLSILLR GTVHEKLKWA FNLYDINKDG YITKEEMLAI MKSIYDMMGR HTYPILREDA PAEHVERFFE KMDRNQDGVV TIEEFLEACQ KDENIMSSMQ LFENVI //