ID CLK1_HUMAN Reviewed; 484 AA. AC P49759; B4DFW7; Q0P694; Q8N5V8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 2. DT 18-SEP-2019, entry version 186. DE RecName: Full=Dual specificity protein kinase CLK1; DE EC=2.7.12.1; DE AltName: Full=CDC-like kinase 1; GN Name=CLK1; Synonyms=CLK; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1704889; RA Johnson K.W., Smith K.A.; RT "Molecular cloning of a novel human cdc2/CDC28-like protein kinase."; RL J. Biol. Chem. 266:3402-3407(1991). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RX PubMed=7990150; DOI=10.1006/jmbi.1994.1763; RA Hanes J.J., der Kammer H., Klaudiny J.J., Scheit K.H.; RT "Characterization by cDNA cloning of two new human protein kinases. RT Evidence by sequence comparison of a new family of mammalian protein RT kinases."; RL J. Mol. Biol. 244:665-672(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3). RC TISSUE=Amygdala; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4] 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., RA Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., RA Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., RA Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., RA Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., RA Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., RA Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., RA Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., RA Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., RA 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., RA Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., RA Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., RA Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., RA Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., RA Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., RA Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., RA Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., RA Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., RA 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., RA Waterston R.H., Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 RT and 4."; RL Nature 434:724-731(2005). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Blood, and Bone; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [7] RP FUNCTION. RX PubMed=10480872; DOI=10.1074/jbc.274.38.26697; RA Moeslein F.M., Myers M.P., Landreth G.E.; RT "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the RT tyrosine phosphatase, PTP-1B."; RL J. Biol. Chem. 274:26697-26704(1999). RN [8] RP INTERACTION WITH UBL5. RX PubMed=12705895; DOI=10.1016/s0006-291x(03)00549-7; RA Kantham L., Kerr-Bayles L., Godde N., Quick M., Webb R., RA Sunderland T., Bond J., Walder K., Augert G., Collier G.; RT "Beacon interacts with cdc2/cdc28-like kinases."; RL Biochem. Biophys. Res. Commun. 304:125-129(2003). RN [9] RP SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S). RX PubMed=14759258; DOI=10.1186/gb-2004-5-2-r8; RA Hillman R.T., Green R.E., Brenner S.E.; RT "An unappreciated role for RNA surveillance."; RL Genome Biol. 5:R8.1-R8.16(2004). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61 AND SER-140, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007; RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., RA Greff Z., Keri G., Stemmann O., Mann M.; RT "Kinase-selective enrichment enables quantitative phosphoproteomics of RT the kinome across the cell cycle."; RL Mol. Cell 31:438-448(2008). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-138 AND SER-140, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [13] RP FUNCTION, ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY. RX PubMed=19168442; DOI=10.1161/circresaha.108.183905; RA Eisenreich A., Bogdanov V.Y., Zakrzewicz A., Pries A., Antoniak S., RA Poller W., Schultheiss H.P., Rauch U.; RT "Cdc2-like kinases and DNA topoisomerase I regulate alternative RT splicing of tissue factor in human endothelial cells."; RL Circ. Res. 104:589-599(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200; RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., RA Mann M., Daub H.; RT "Large-scale proteomics analysis of the human kinome."; RL Mol. Cell. Proteomics 8:1751-1764(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [16] RP VARIANTS [LARGE SCALE ANALYSIS] PHE-61; GLY-118; SER-307 AND THR-440. RX PubMed=17344846; DOI=10.1038/nature05610; RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., RA Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., RA O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., RA Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., RA Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., RA Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., RA Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., RA West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., RA Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., RA DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., RA Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., RA Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; RT "Patterns of somatic mutation in human cancer genomes."; RL Nature 446:153-158(2007). CC -!- FUNCTION: Dual specificity kinase acting on both serine/threonine CC and tyrosine-containing substrates. Phosphorylates serine- and CC arginine-rich (SR) proteins of the spliceosomal complex and may be CC a constituent of a network of regulatory mechanisms that enable SR CC proteins to control RNA splicing. Phosphorylates: SRSF1, SRSF3 and CC PTPN1. Regulates the alternative splicing of tissue factor (F3) CC pre-mRNA in endothelial cells and adenovirus E1A pre-mRNA. CC {ECO:0000269|PubMed:10480872, ECO:0000269|PubMed:19168442}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA- CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; CC EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; CC EC=2.7.12.1; CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L- CC tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, CC Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; CC EC=2.7.12.1; CC -!- ACTIVITY REGULATION: Regulates splicing of its own pre-mRNA CC according to its kinase activity; increased expression of the CC catalytically active form influences splicing to generate the CC catalytically inactive splicing variant lacking the kinase domain. CC Leucettine L41 inhibits its kinase activity and affects the CC regulation of alternative splicing mediated by phosphorylation of CC SR proteins (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with PPIG and UBL5. CC {ECO:0000269|PubMed:12705895}. CC -!- INTERACTION: CC P49760:CLK2; NbExp=4; IntAct=EBI-11981867, EBI-750020; CC P60409:KRTAP10-7; NbExp=3; IntAct=EBI-473775, EBI-10172290; CC O76083:PDE9A; NbExp=3; IntAct=EBI-473775, EBI-742764; CC -!- SUBCELLULAR LOCATION: Nucleus. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=Long; CC IsoId=P49759-1; Sequence=Displayed; CC Name=2; Synonyms=Short; CC IsoId=P49759-2; Sequence=VSP_004852, VSP_004853; CC Note=Lacks the kinase domain. May be produced at very low levels CC due to a premature stop codon in the mRNA, leading to CC nonsense-mediated mRNA decay.; CC Name=3; CC IsoId=P49759-3; Sequence=VSP_043578; CC Note=No experimental confirmation available.; CC -!- TISSUE SPECIFICITY: Endothelial cells. CC {ECO:0000269|PubMed:19168442}. CC -!- PTM: Autophosphorylates on all three types of residues. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC CC Ser/Thr protein kinase family. Lammer subfamily. {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; L29219; AAA61480.1; -; mRNA. DR EMBL; L29222; AAB59459.1; -; mRNA. DR EMBL; AK289365; BAF82054.1; -; mRNA. DR EMBL; AK294295; BAG57578.1; -; mRNA. DR EMBL; AC005037; AAY14722.1; -; Genomic_DNA. DR EMBL; CH471063; EAW70217.1; -; Genomic_DNA. DR EMBL; BC028149; AAH28149.1; -; mRNA. DR EMBL; BC031549; AAH31549.1; -; mRNA. DR CCDS; CCDS2331.1; -. [P49759-1] DR CCDS; CCDS54427.1; -. [P49759-3] DR PIR; S53641; S53641. DR RefSeq; NP_001155879.1; NM_001162407.1. [P49759-3] DR RefSeq; NP_004062.2; NM_004071.3. [P49759-1] DR PDB; 1Z57; X-ray; 1.70 A; A=148-484. DR PDB; 2VAG; X-ray; 1.80 A; A=148-484. DR PDB; 5J1V; X-ray; 2.52 A; A/B/C=148-484. DR PDB; 5J1W; X-ray; 2.42 A; A/B/C=148-484. DR PDB; 5X8I; X-ray; 1.90 A; A/B=148-484. DR PDB; 6FT8; X-ray; 1.45 A; A=148-484. DR PDB; 6FT9; X-ray; 1.87 A; A/B/C=148-484. DR PDB; 6FYO; X-ray; 2.32 A; A=148-484. DR PDB; 6G33; X-ray; 2.05 A; A/B/C=148-484. DR PDB; 6I5H; X-ray; 1.49 A; A=148-484. DR PDB; 6I5I; X-ray; 1.60 A; A=148-484. DR PDB; 6I5K; X-ray; 2.30 A; A/B/C=148-484. DR PDB; 6I5L; X-ray; 2.55 A; A/B/C=148-484. DR PDB; 6Q8K; X-ray; 2.29 A; A=148-484. DR PDB; 6Q8P; X-ray; 3.00 A; A/B/C=148-484. DR PDB; 6RAA; X-ray; 2.10 A; A=148-484. DR PDBsum; 1Z57; -. DR PDBsum; 2VAG; -. DR PDBsum; 5J1V; -. DR PDBsum; 5J1W; -. DR PDBsum; 5X8I; -. DR PDBsum; 6FT8; -. DR PDBsum; 6FT9; -. DR PDBsum; 6FYO; -. DR PDBsum; 6G33; -. DR PDBsum; 6I5H; -. DR PDBsum; 6I5I; -. DR PDBsum; 6I5K; -. DR PDBsum; 6I5L; -. DR PDBsum; 6Q8K; -. DR PDBsum; 6Q8P; -. DR PDBsum; 6RAA; -. DR SMR; P49759; -. DR BioGrid; 107606; 170. DR IntAct; P49759; 37. DR MINT; P49759; -. DR STRING; 9606.ENSP00000394734; -. DR BindingDB; P49759; -. DR ChEMBL; CHEMBL4224; -. DR DrugBank; DB06376; CHGN111. DR DrugBank; DB04367; Debromohymenialdisine. DR DrugBank; DB08691; ethyl 3-[(E)-2-amino-1-cyanoethenyl]-6,7-dichloro-1-methyl-1H-indole-2-carboxylate. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; P49759; -. DR GuidetoPHARMACOLOGY; 1990; -. DR iPTMnet; P49759; -. DR PhosphoSitePlus; P49759; -. DR BioMuta; CLK1; -. DR DMDM; 206729857; -. DR EPD; P49759; -. DR jPOST; P49759; -. DR MassIVE; P49759; -. DR MaxQB; P49759; -. DR PaxDb; P49759; -. DR PeptideAtlas; P49759; -. DR PRIDE; P49759; -. DR ProteomicsDB; 56090; -. [P49759-1] DR ProteomicsDB; 56091; -. [P49759-2] DR ProteomicsDB; 56092; -. [P49759-3] DR DNASU; 1195; -. DR Ensembl; ENST00000321356; ENSP00000326830; ENSG00000013441. [P49759-1] DR Ensembl; ENST00000432425; ENSP00000400487; ENSG00000013441. [P49759-2] DR Ensembl; ENST00000434813; ENSP00000394734; ENSG00000013441. [P49759-3] DR GeneID; 1195; -. DR KEGG; hsa:1195; -. DR UCSC; uc002uwe.3; human. [P49759-1] DR CTD; 1195; -. DR DisGeNET; 1195; -. DR GeneCards; CLK1; -. DR HGNC; HGNC:2068; CLK1. DR HPA; CAB033141; -. DR HPA; HPA062405; -. DR MIM; 601951; gene. DR neXtProt; NX_P49759; -. DR OpenTargets; ENSG00000013441; -. DR PharmGKB; PA26594; -. DR eggNOG; KOG0671; Eukaryota. DR eggNOG; ENOG410XQF2; LUCA. DR GeneTree; ENSGT00940000159722; -. DR HOGENOM; HOG000203417; -. DR InParanoid; P49759; -. DR KO; K08823; -. DR OMA; RHRDHES; -. DR OrthoDB; 1314811at2759; -. DR PhylomeDB; P49759; -. DR TreeFam; TF101041; -. DR BRENDA; 2.7.12.1; 2681. DR SignaLink; P49759; -. DR SIGNOR; P49759; -. DR ChiTaRS; CLK1; human. DR EvolutionaryTrace; P49759; -. DR GeneWiki; CLK1; -. DR GenomeRNAi; 1195; -. DR Pharos; P49759; -. DR PRO; PR:P49759; -. DR Proteomes; UP000005640; Chromosome 2. DR Bgee; ENSG00000013441; Expressed in 236 organ(s), highest expression level in left lobe of thyroid gland. DR ExpressionAtlas; P49759; baseline and differential. DR Genevisible; P49759; HS. DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; TAS:ProtInc. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl. DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IEA:Ensembl. DR GO; GO:0046777; P:protein autophosphorylation; IEA:Ensembl. DR GO; GO:0043484; P:regulation of RNA splicing; IMP:UniProtKB. DR InterPro; IPR011009; Kinase-like_dom_sf. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR008271; Ser/Thr_kinase_AS. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome; KW Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; KW Reference proteome; Serine/threonine-protein kinase; Transferase; KW Tyrosine-protein kinase. FT CHAIN 1 484 Dual specificity protein kinase CLK1. FT /FTId=PRO_0000085866. FT DOMAIN 161 477 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 167 175 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 288 288 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159, ECO:0000255|PROSITE- FT ProRule:PRU10027}. FT BINDING 191 191 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT MOD_RES 61 61 Phosphoserine. FT {ECO:0000244|PubMed:18691976}. FT MOD_RES 138 138 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 140 140 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:18691976, FT ECO:0000244|PubMed:19369195, FT ECO:0000244|PubMed:23186163}. FT VAR_SEQ 1 1 M -> MAAGRRPASALWPERRGSPLRGDLLGFQNVREPSSC FT GETLSGM (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_043578. FT VAR_SEQ 131 136 KSHRRK -> MKLLIL (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7990150}. FT /FTId=VSP_004852. FT VAR_SEQ 137 484 Missing (in isoform 2). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:7990150}. FT /FTId=VSP_004853. FT VARIANT 61 61 S -> F (in dbSNP:rs55989135). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040409. FT VARIANT 99 99 N -> D (in dbSNP:rs6735666). FT /FTId=VAR_046551. FT VARIANT 118 118 R -> G (in dbSNP:rs56135616). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040410. FT VARIANT 307 307 P -> S (in dbSNP:rs35412475). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040411. FT VARIANT 440 440 M -> T (in dbSNP:rs35393352). FT {ECO:0000269|PubMed:17344846}. FT /FTId=VAR_040412. FT VARIANT 459 459 E -> G (in dbSNP:rs12709). FT /FTId=VAR_051620. FT CONFLICT 432 432 R -> A (in Ref. 1; AAA61480). FT {ECO:0000305}. FT HELIX 148 150 {ECO:0000244|PDB:6FT8}. FT TURN 158 160 {ECO:0000244|PDB:6FT8}. FT STRAND 161 170 {ECO:0000244|PDB:6FT8}. FT STRAND 173 180 {ECO:0000244|PDB:6FT8}. FT TURN 181 185 {ECO:0000244|PDB:6FT8}. FT STRAND 187 193 {ECO:0000244|PDB:6FT8}. FT HELIX 197 216 {ECO:0000244|PDB:6FT8}. FT STRAND 227 233 {ECO:0000244|PDB:6FT8}. FT STRAND 236 242 {ECO:0000244|PDB:6FT8}. FT HELIX 248 254 {ECO:0000244|PDB:6FT8}. FT TURN 255 257 {ECO:0000244|PDB:6FT8}. FT HELIX 262 281 {ECO:0000244|PDB:6FT8}. FT HELIX 291 293 {ECO:0000244|PDB:6FT8}. FT STRAND 294 297 {ECO:0000244|PDB:6FT8}. FT STRAND 301 306 {ECO:0000244|PDB:6FT8}. FT TURN 307 310 {ECO:0000244|PDB:6FT8}. FT STRAND 311 317 {ECO:0000244|PDB:6FT8}. FT STRAND 321 323 {ECO:0000244|PDB:6FT8}. FT STRAND 330 334 {ECO:0000244|PDB:6Q8P}. FT HELIX 343 345 {ECO:0000244|PDB:6FT8}. FT HELIX 348 351 {ECO:0000244|PDB:6FT8}. FT HELIX 359 374 {ECO:0000244|PDB:6FT8}. FT HELIX 384 395 {ECO:0000244|PDB:6FT8}. FT HELIX 400 405 {ECO:0000244|PDB:6FT8}. FT HELIX 409 411 {ECO:0000244|PDB:6FT8}. FT HELIX 424 432 {ECO:0000244|PDB:6FT8}. FT HELIX 436 439 {ECO:0000244|PDB:6FT8}. FT HELIX 445 457 {ECO:0000244|PDB:6FT8}. FT TURN 462 464 {ECO:0000244|PDB:6FT8}. FT HELIX 468 471 {ECO:0000244|PDB:6FT8}. FT HELIX 475 481 {ECO:0000244|PDB:6FT8}. SQ SEQUENCE 484 AA; 57291 MW; F34B5B44988BD118 CRC64; MRHSKRTYCP DWDDKDWDYG KWRSSSSHKR RKRSHSSAQE NKRCKYNHSK MCDSHYLESR SINEKDYHSR RYIDEYRNDY TQGCEPGHRQ RDHESRYQNH SSKSSGRSGR SSYKSKHRIH HSTSHRRSHG KSHRRKRTRS VEDDEEGHLI CQSGDVLSAR YEIVDTLGEG AFGKVVECID HKAGGRHVAV KIVKNVDRYC EAARSEIQVL EHLNTTDPNS TFRCVQMLEW FEHHGHICIV FELLGLSTYD FIKENGFLPF RLDHIRKMAY QICKSVNFLH SNKLTHTDLK PENILFVQSD YTEAYNPKIK RDERTLINPD IKVVDFGSAT YDDEHHSTLV STRHYRAPEV ILALGWSQPC DVWSIGCILI EYYLGFTVFP THDSKEHLAM MERILGPLPK HMIQKTRKRK YFHHDRLDWD EHSSAGRYVS RRCKPLKEFM LSQDVEHERL FDLIQKMLEY DPAKRITLRE ALKHPFFDLL KKSI //