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 25-MAY-2022, entry version 201. 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; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=1704889; DOI=10.1016/s0021-9258(19)67807-5; 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., 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 [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., 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 [5] 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 [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 project: RT 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., Sunderland T., RA 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 BY RP 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT 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 the RT 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 splicing of RT 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 BY RP 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 BY RP 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., Bignell G., RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., RA 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 and CC tyrosine-containing substrates. Phosphorylates serine- and arginine- CC rich (SR) proteins of the spliceosomal complex and may be a constituent CC of a network of regulatory mechanisms that enable SR proteins to CC control RNA splicing. Phosphorylates: SRSF1, SRSF3 and PTPN1. Regulates CC the alternative splicing of tissue factor (F3) pre-mRNA in endothelial CC cells and adenovirus E1A pre-mRNA. {ECO:0000269|PubMed:10480872, CC 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, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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-tyrosyl- CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA- CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.12.1; CC -!- ACTIVITY REGULATION: Regulates splicing of its own pre-mRNA according CC to its kinase activity; increased expression of the catalytically CC active form influences splicing to generate the catalytically inactive CC splicing variant lacking the kinase domain. Leucettine L41 inhibits its CC kinase activity and affects the regulation of alternative splicing CC mediated by phosphorylation of SR proteins (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Interacts with PPIG and UBL5. {ECO:0000269|PubMed:12705895}. CC -!- INTERACTION: CC P49759; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-473775, EBI-10172290; CC P49759; O76083: PDE9A; NbExp=3; IntAct=EBI-473775, EBI-742764; CC P49759-3; Q8N2M8: CLASRP; NbExp=3; IntAct=EBI-11981867, EBI-751069; CC P49759-3; P49760: CLK2; NbExp=5; IntAct=EBI-11981867, EBI-750020; CC P49759-3; Q92997: DVL3; NbExp=3; IntAct=EBI-11981867, EBI-739789; CC P49759-3; P60371: KRTAP10-6; NbExp=3; IntAct=EBI-11981867, EBI-12012928; CC P49759-3; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-11981867, EBI-10172290; CC P49759-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11981867, EBI-739832; CC P49759-3; O76083-2: PDE9A; NbExp=3; IntAct=EBI-11981867, EBI-11524542; CC P49759-3; O14492-2: SH2B2; NbExp=3; IntAct=EBI-11981867, EBI-19952306; CC P49759-3; A7MD48: SRRM4; NbExp=3; IntAct=EBI-11981867, EBI-3867173; CC P49759-3; Q07955: SRSF1; NbExp=3; IntAct=EBI-11981867, EBI-398920; CC P49759-3; O75494: SRSF10; NbExp=3; IntAct=EBI-11981867, EBI-353655; CC P49759-3; P84103: SRSF3; NbExp=3; IntAct=EBI-11981867, EBI-372557; CC P49759-3; Q16629: SRSF7; NbExp=3; IntAct=EBI-11981867, EBI-398885; CC P49759-3; P62995: TRA2B; NbExp=5; IntAct=EBI-11981867, EBI-725485; 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 Name=3; CC IsoId=P49759-3; Sequence=VSP_043578; CC -!- TISSUE SPECIFICITY: Endothelial cells. {ECO:0000269|PubMed:19168442}. CC -!- PTM: Autophosphorylates on all three types of residues. {ECO:0000250}. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks the kinase domain. May be produced at CC very low levels due to a premature stop codon in the mRNA, leading to CC nonsense-mediated mRNA decay. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr CC 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; 6KHD; X-ray; 2.70 A; A/B/C=1-484. 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; 6QTY; X-ray; 1.65 A; A=148-484. DR PDB; 6R3D; X-ray; 1.85 A; A=148-484. DR PDB; 6R6E; X-ray; 2.25 A; A=148-484. DR PDB; 6R6X; X-ray; 2.05 A; A=148-484. DR PDB; 6R8J; X-ray; 1.75 A; A=148-484. DR PDB; 6RAA; X-ray; 2.10 A; A=148-484. DR PDB; 6TW2; X-ray; 1.80 A; E=148-484. DR PDB; 6YTA; X-ray; 2.30 A; A=148-484. DR PDB; 6YTD; X-ray; 2.00 A; A=148-484. DR PDB; 6YTE; X-ray; 2.30 A; C=148-484. DR PDB; 6YTG; X-ray; 1.95 A; A=148-484. DR PDB; 6YTI; X-ray; 2.40 A; A=148-484. DR PDB; 6Z4Z; X-ray; 2.07 A; A/B/C=148-484. DR PDB; 6Z50; X-ray; 1.60 A; A=148-484. DR PDB; 6ZLN; X-ray; 1.70 A; A=148-484. DR PDB; 7AK3; X-ray; 2.50 A; A=148-484. DR PDB; 7OPG; X-ray; 1.93 A; A/B/C=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; 6KHD; -. DR PDBsum; 6Q8K; -. DR PDBsum; 6Q8P; -. DR PDBsum; 6QTY; -. DR PDBsum; 6R3D; -. DR PDBsum; 6R6E; -. DR PDBsum; 6R6X; -. DR PDBsum; 6R8J; -. DR PDBsum; 6RAA; -. DR PDBsum; 6TW2; -. DR PDBsum; 6YTA; -. DR PDBsum; 6YTD; -. DR PDBsum; 6YTE; -. DR PDBsum; 6YTG; -. DR PDBsum; 6YTI; -. DR PDBsum; 6Z4Z; -. DR PDBsum; 6Z50; -. DR PDBsum; 6ZLN; -. DR PDBsum; 7AK3; -. DR PDBsum; 7OPG; -. DR AlphaFoldDB; P49759; -. DR SMR; P49759; -. DR BioGRID; 107606; 196. DR IntAct; P49759; 54. 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 GlyGen; P49759; 1 site, 1 O-linked glycan (1 site). 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 Antibodypedia; 34923; 223 antibodies from 29 providers. DR DNASU; 1195; -. DR Ensembl; ENST00000321356.9; ENSP00000326830.4; ENSG00000013441.17. DR Ensembl; ENST00000432425.5; ENSP00000400487.1; ENSG00000013441.17. [P49759-2] DR Ensembl; ENST00000434813.3; ENSP00000394734.2; ENSG00000013441.17. [P49759-3] DR GeneID; 1195; -. DR KEGG; hsa:1195; -. DR MANE-Select; ENST00000321356.9; ENSP00000326830.4; NM_004071.4; NP_004062.2. DR UCSC; uc002uwe.3; human. [P49759-1] DR CTD; 1195; -. DR DisGeNET; 1195; -. DR GeneCards; CLK1; -. DR HGNC; HGNC:2068; CLK1. DR HPA; ENSG00000013441; Low tissue specificity. DR MIM; 601951; gene. DR neXtProt; NX_P49759; -. DR OpenTargets; ENSG00000013441; -. DR PharmGKB; PA26594; -. DR VEuPathDB; HostDB:ENSG00000013441; -. DR eggNOG; KOG0671; Eukaryota. DR GeneTree; ENSGT00940000159722; -. DR HOGENOM; CLU_126079_0_0_1; -. DR InParanoid; P49759; -. DR OMA; YHNHSSK; -. DR OrthoDB; 915778at2759; -. DR PhylomeDB; P49759; -. DR TreeFam; TF101041; -. DR BRENDA; 2.7.12.1; 2681. DR PathwayCommons; P49759; -. DR SignaLink; P49759; -. DR SIGNOR; P49759; -. DR BioGRID-ORCS; 1195; 8 hits in 1113 CRISPR screens. DR ChiTaRS; CLK1; human. DR EvolutionaryTrace; P49759; -. DR GeneWiki; CLK1; -. DR GenomeRNAi; 1195; -. DR Pharos; P49759; Tchem. DR PRO; PR:P49759; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; P49759; protein. DR Bgee; ENSG00000013441; Expressed in left lobe of thyroid gland and 244 other tissues. 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:0106310; F:protein serine kinase activity; IEA:RHEA. 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; Kinase; KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase. FT CHAIN 1..484 FT /note="Dual specificity protein kinase CLK1" FT /id="PRO_0000085866" FT DOMAIN 161..477 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT NP_BIND 167..175 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 79..146 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..24 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 79..100 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 110..136 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 288 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 191 FT /note="ATP" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 61 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18691976" FT MOD_RES 138 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 140 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163" FT VAR_SEQ 1 FT /note="M -> MAAGRRPASALWPERRGSPLRGDLLGFQNVREPSSCGETLSGM (in FT isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_043578" FT VAR_SEQ 131..136 FT /note="KSHRRK -> MKLLIL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7990150" FT /id="VSP_004852" FT VAR_SEQ 137..484 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7990150" FT /id="VSP_004853" FT VARIANT 61 FT /note="S -> F (in dbSNP:rs55989135)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040409" FT VARIANT 99 FT /note="N -> D (in dbSNP:rs6735666)" FT /id="VAR_046551" FT VARIANT 118 FT /note="R -> G (in dbSNP:rs56135616)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040410" FT VARIANT 307 FT /note="P -> S (in dbSNP:rs35412475)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040411" FT VARIANT 440 FT /note="M -> T (in dbSNP:rs35393352)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_040412" FT VARIANT 459 FT /note="E -> G (in dbSNP:rs12709)" FT /id="VAR_051620" FT CONFLICT 432 FT /note="R -> A (in Ref. 1; AAA61480)" FT /evidence="ECO:0000305" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:6FT8" FT TURN 158..160 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 161..170 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 173..180 FT /evidence="ECO:0007829|PDB:6FT8" FT TURN 181..185 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 187..193 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 197..216 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 222..224 FT /evidence="ECO:0007829|PDB:6Z50" FT STRAND 227..233 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 236..242 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 248..254 FT /evidence="ECO:0007829|PDB:6FT8" FT TURN 255..257 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 262..281 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 291..293 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 294..297 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 301..306 FT /evidence="ECO:0007829|PDB:6FT8" FT TURN 307..310 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 311..317 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 321..323 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 330..334 FT /evidence="ECO:0007829|PDB:6YTE" FT HELIX 343..345 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 348..351 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 359..374 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 384..395 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 400..405 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 409..411 FT /evidence="ECO:0007829|PDB:6FT8" FT STRAND 421..423 FT /evidence="ECO:0007829|PDB:6YTI" FT HELIX 424..432 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 436..439 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 445..457 FT /evidence="ECO:0007829|PDB:6FT8" FT TURN 462..464 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 468..471 FT /evidence="ECO:0007829|PDB:6FT8" FT HELIX 475..481 FT /evidence="ECO:0007829|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 //