ID DCLK1_HUMAN Reviewed; 740 AA. AC O15075; B7Z3E9; Q5VZY8; Q5VZZ0; Q5VZZ1; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 27-MAR-2024, entry version 213. DE RecName: Full=Serine/threonine-protein kinase DCLK1; DE EC=2.7.11.1; DE AltName: Full=Doublecortin domain-containing protein 3A; DE AltName: Full=Doublecortin-like and CAM kinase-like 1; DE AltName: Full=Doublecortin-like kinase 1; GN Name=DCLK1; Synonyms=DCAMKL1, DCDC3A, KIAA0369; 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] (ISOFORMS 1; 2; 3 AND 4). RX PubMed=9747029; DOI=10.1007/s100380050063; RA Omori Y., Suzuki M., Ozaki K., Harada Y., Nakamura Y., Takahashi E., RA Fujiwara T.; RT "Expression and chromosomal localization of KIAA0369, a putative kinase RT structurally related to Doublecortin."; RL J. Hum. Genet. 43:169-177(1998). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2). RC TISSUE=Fetal brain; RX PubMed=10036192; DOI=10.1006/geno.1998.5718; RA Sossey-Alaoui K., Srivastava A.K.; RT "DCAMKL1, a brain-specific transmembrane protein on 13q12.3 that is similar RT to doublecortin (DCX)."; RL Genomics 56:121-126(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=9205841; DOI=10.1093/dnares/4.2.141; RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., RA Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. VII. The RT complete sequences of 100 new cDNA clones from brain which can code for RT large proteins in vitro."; RL DNA Res. 4:141-150(1997). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Hippocampus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057823; DOI=10.1038/nature02379; RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L., RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., RA Frankish A.G., Frankland J., French L., Garner P., Garnett J., RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., RA Rogers J., Ross M.T.; RT "The DNA sequence and analysis of human chromosome 13."; RL Nature 428:522-528(2004). RN [6] 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 (FEB-2008) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [8] RP TISSUE SPECIFICITY. RX PubMed=10051403; DOI=10.1006/geno.1998.5673; RA Matsumoto N., Pilz D.T., Ledbetter D.H.; RT "Genomic structure, chromosomal mapping, and expression pattern of human RT DCAMKL1 (KIAA0369), a homologue of DCX (XLIS)."; RL Genomics 56:179-183(1999). RN [9] RP INDUCTION, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=16548883; DOI=10.1111/j.1462-5822.2005.00644.x; RA Leong W.F., Chow V.T.; RT "Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal RT differential cellular gene expression in response to enterovirus 71 RT infection."; RL Cell. Microbiol. 8:565-580(2006). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] RP STRUCTURE BY NMR OF 51-156. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the N-terminal DCX domain of human doublecortin-like RT kinase."; RL Submitted (NOV-2003) to the PDB data bank. RN [12] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-29; MET-46; GLN-93; PHE-291 AND RP HIS-292. 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: Probable kinase that may be involved in a calcium-signaling CC pathway controlling neuronal migration in the developing brain. May CC also participate in functions of the mature nervous system. 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=2.7.11.1; 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=2.7.11.1; CC -!- INTERACTION: CC O15075; Q96M94: KLHL15; NbExp=2; IntAct=EBI-2684263, EBI-2510129; CC O15075-2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-12324841, EBI-396137; CC O15075-2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-12324841, EBI-2349927; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Comment=Additional isoforms seem to exist. Type A (AS and AL) and CC type B (BS and BL) isoforms differ respectively by the presence or CC absence of the doublecortin domain. An alternative splicing occurring CC in 3' of the mRNA produces the long (L) instead of the short (S) CC isoforms.; CC Name=2; Synonyms=AL; CC IsoId=O15075-1; Sequence=Displayed; CC Name=1; Synonyms=AS; CC IsoId=O15075-2; Sequence=VSP_004907; CC Name=3; Synonyms=BS; CC IsoId=O15075-3; Sequence=VSP_004905, VSP_004906, VSP_004907; CC Name=4; Synonyms=BL; CC IsoId=O15075-4; Sequence=VSP_004905, VSP_004906; CC -!- TISSUE SPECIFICITY: In fetal tissues, highly expressed in brain, CC detectable in lung and liver, but not in kidney. In adult tissues, CC expressed ubiquitously in the brain, detectable in the heart, liver, CC spleen, thymus, prostate, testis, ovary, small intestine and colon. The CC type A isoforms seem to be expressed predominantly in fetal brain CC whereas type B isoforms are expressed abundantly in both fetal and CC adult brain. {ECO:0000269|PubMed:10051403}. CC -!- INDUCTION: Up-regulated in response to enterovirus 71 (EV71) infection CC (at protein level). {ECO:0000269|PubMed:16548883}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr CC protein kinase family. CaMK subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20824.2; Type=Erroneous initiation; Evidence={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; AB002367; BAA20824.2; ALT_INIT; mRNA. DR EMBL; AL157760; CAH70167.1; -; Genomic_DNA. DR EMBL; AL157694; CAH70167.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70167.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70167.1; JOINED; Genomic_DNA. DR EMBL; AL157760; CAH70170.1; -; Genomic_DNA. DR EMBL; AK295777; BAH12185.1; -; mRNA. DR EMBL; AL157760; CAH70168.1; -; Genomic_DNA. DR EMBL; AL157694; CAH70168.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70168.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70168.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70261.1; -; Genomic_DNA. DR EMBL; AL157694; CAH70261.1; JOINED; Genomic_DNA. DR EMBL; AL157760; CAH70261.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70261.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70262.1; -; Genomic_DNA. DR EMBL; AL157694; CAH70262.1; JOINED; Genomic_DNA. DR EMBL; AL157760; CAH70262.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70262.1; JOINED; Genomic_DNA. DR EMBL; AL157694; CAH70656.1; -; Genomic_DNA. DR EMBL; AL157760; CAH70656.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70656.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70656.1; JOINED; Genomic_DNA. DR EMBL; AL157694; CAH70657.1; -; Genomic_DNA. DR EMBL; AL157760; CAH70657.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAH70657.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAH70657.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAI15720.1; -; Genomic_DNA. DR EMBL; AL157694; CAI15720.1; JOINED; Genomic_DNA. DR EMBL; AL157760; CAI15720.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAI15720.1; JOINED; Genomic_DNA. DR EMBL; AL390029; CAI15721.1; -; Genomic_DNA. DR EMBL; AL157694; CAI15721.1; JOINED; Genomic_DNA. DR EMBL; AL157760; CAI15721.1; JOINED; Genomic_DNA. DR EMBL; AL160392; CAI15721.1; JOINED; Genomic_DNA. DR EMBL; CH471075; EAX08550.1; -; Genomic_DNA. DR EMBL; CH471075; EAX08551.1; -; Genomic_DNA. DR EMBL; BC152456; AAI52457.1; -; mRNA. DR CCDS; CCDS55895.1; -. [O15075-4] DR CCDS; CCDS73561.1; -. [O15075-3] DR CCDS; CCDS81762.1; -. [O15075-1] DR CCDS; CCDS9354.1; -. [O15075-2] DR RefSeq; NP_001182344.1; NM_001195415.1. [O15075-3] DR RefSeq; NP_001182345.1; NM_001195416.1. [O15075-4] DR RefSeq; NP_001317000.1; NM_001330071.1. [O15075-1] DR RefSeq; NP_001317001.1; NM_001330072.1. [O15075-1] DR RefSeq; NP_004725.1; NM_004734.4. [O15075-2] DR PDB; 1MFW; X-ray; 1.60 A; A=49-154. DR PDB; 1MG4; X-ray; 1.50 A; A=49-154. DR PDB; 1UF0; NMR; -; A=54-156. DR PDB; 5JZJ; X-ray; 1.71 A; A/B=372-649. DR PDB; 5JZN; X-ray; 2.85 A; A/B=372-649. DR PDB; 6KYQ; X-ray; 2.14 A; A/B=379-704. DR PDB; 6KYR; X-ray; 2.21 A; A/B=379-704. DR PDB; 7F3G; X-ray; 2.10 A; A/B=372-649. DR PDB; 7KX6; X-ray; 2.50 A; A/B=372-649. DR PDB; 7KX8; X-ray; 3.10 A; A/B=372-686. DR PDB; 7KXW; X-ray; 3.00 A; A/B=372-649. DR PDBsum; 1MFW; -. DR PDBsum; 1MG4; -. DR PDBsum; 1UF0; -. DR PDBsum; 5JZJ; -. DR PDBsum; 5JZN; -. DR PDBsum; 6KYQ; -. DR PDBsum; 6KYR; -. DR PDBsum; 7F3G; -. DR PDBsum; 7KX6; -. DR PDBsum; 7KX8; -. DR PDBsum; 7KXW; -. DR AlphaFoldDB; O15075; -. DR SMR; O15075; -. DR BioGRID; 114635; 118. DR IntAct; O15075; 47. DR MINT; O15075; -. DR STRING; 9606.ENSP00000353846; -. DR BindingDB; O15075; -. DR ChEMBL; CHEMBL5683; -. DR DrugBank; DB12010; Fostamatinib. DR DrugCentral; O15075; -. DR GuidetoPHARMACOLOGY; 2005; -. DR CarbonylDB; O15075; -. DR iPTMnet; O15075; -. DR PhosphoSitePlus; O15075; -. DR SwissPalm; O15075; -. DR BioMuta; DCLK1; -. DR EPD; O15075; -. DR jPOST; O15075; -. DR MassIVE; O15075; -. DR MaxQB; O15075; -. DR PaxDb; 9606-ENSP00000255448; -. DR PeptideAtlas; O15075; -. DR ProteomicsDB; 48428; -. [O15075-1] DR ProteomicsDB; 48429; -. [O15075-2] DR ProteomicsDB; 48430; -. [O15075-3] DR ProteomicsDB; 48431; -. [O15075-4] DR Pumba; O15075; -. DR Antibodypedia; 23046; 500 antibodies from 39 providers. DR DNASU; 9201; -. DR Ensembl; ENST00000255448.8; ENSP00000255448.4; ENSG00000133083.15. [O15075-2] DR Ensembl; ENST00000360631.8; ENSP00000353846.3; ENSG00000133083.15. [O15075-1] DR Ensembl; ENST00000379893.5; ENSP00000369223.1; ENSG00000133083.15. [O15075-4] DR Ensembl; ENST00000615680.5; ENSP00000484452.1; ENSG00000133083.15. [O15075-3] DR GeneID; 9201; -. DR KEGG; hsa:9201; -. DR MANE-Select; ENST00000360631.8; ENSP00000353846.3; NM_001330071.2; NP_001317000.1. DR UCSC; uc001uve.4; human. [O15075-1] DR AGR; HGNC:2700; -. DR CTD; 9201; -. DR DisGeNET; 9201; -. DR GeneCards; DCLK1; -. DR HGNC; HGNC:2700; DCLK1. DR HPA; ENSG00000133083; Tissue enhanced (brain). DR MIM; 604742; gene. DR neXtProt; NX_O15075; -. DR OpenTargets; ENSG00000133083; -. DR PharmGKB; PA162383325; -. DR VEuPathDB; HostDB:ENSG00000133083; -. DR eggNOG; KOG0032; Eukaryota. DR eggNOG; KOG3757; Eukaryota. DR GeneTree; ENSGT00940000154956; -. DR HOGENOM; CLU_000288_63_0_1; -. DR InParanoid; O15075; -. DR OMA; FLLDESX; -. DR OrthoDB; 2956627at2759; -. DR PhylomeDB; O15075; -. DR TreeFam; TF318770; -. DR BRENDA; 2.7.11.1; 2681. DR PathwayCommons; O15075; -. DR SignaLink; O15075; -. DR BioGRID-ORCS; 9201; 13 hits in 1181 CRISPR screens. DR ChiTaRS; DCLK1; human. DR EvolutionaryTrace; O15075; -. DR GeneWiki; DCLK1; -. DR GenomeRNAi; 9201; -. DR Pharos; O15075; Tchem. DR PRO; PR:O15075; -. DR Proteomes; UP000005640; Chromosome 13. DR RNAct; O15075; Protein. DR Bgee; ENSG00000133083; Expressed in endothelial cell and 188 other cell types or tissues. DR ExpressionAtlas; O15075; baseline and differential. DR GO; GO:0005886; C:plasma membrane; TAS:ProtInc. DR GO; GO:0014069; C:postsynaptic density; IEA:Ensembl. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004672; F:protein 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; IEA:UniProtKB-KW. DR GO; GO:0048675; P:axon extension; IEA:Ensembl. DR GO; GO:0007417; P:central nervous system development; TAS:ProtInc. DR GO; GO:0021952; P:central nervous system projection neuron axonogenesis; IEA:Ensembl. DR GO; GO:0048813; P:dendrite morphogenesis; IEA:Ensembl. DR GO; GO:0016197; P:endosomal transport; NAS:UniProtKB. DR GO; GO:0030900; P:forebrain development; IEA:Ensembl. DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro. DR GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0048812; P:neuron projection morphogenesis; IBA:GO_Central. DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl. DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc. DR GO; GO:0009615; P:response to virus; IEP:UniProtKB. DR CDD; cd17140; DCX1_DCLK1; 1. DR CDD; cd17069; DCX2; 1. DR CDD; cd14183; STKc_DCKL1; 1. DR Gene3D; 3.10.20.230; Doublecortin domain; 2. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. DR InterPro; IPR003533; Doublecortin_dom. DR InterPro; IPR036572; Doublecortin_dom_sf. 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 PANTHER; PTHR24347; SERINE/THREONINE-PROTEIN KINASE; 1. DR PANTHER; PTHR24347:SF401; SERINE_THREONINE-PROTEIN KINASE DCLK1; 1. DR Pfam; PF03607; DCX; 2. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00537; DCX; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF89837; Doublecortin (DC); 2. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS50309; DC; 2. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; O15075; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; ATP-binding; Developmental protein; KW Differentiation; Kinase; Neurogenesis; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase. FT CHAIN 1..740 FT /note="Serine/threonine-protein kinase DCLK1" FT /id="PRO_0000085919" FT DOMAIN 57..143 FT /note="Doublecortin 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072" FT DOMAIN 186..269 FT /note="Doublecortin 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072" FT DOMAIN 390..647 FT /note="Protein kinase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT REGION 287..378 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 697..740 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..365 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 719..740 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 511 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159, FT ECO:0000255|PROSITE-ProRule:PRU10027" FT BINDING 396..404 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT BINDING 419 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159" FT MOD_RES 32 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 46 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 305 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 307 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 330 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 332 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 334 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 352 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 353 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:O08875" FT MOD_RES 355 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 364 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 376 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 520 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 726 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 735 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT MOD_RES 738 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9JLM8" FT VAR_SEQ 1..307 FT /note="Missing (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9747029" FT /id="VSP_004905" FT VAR_SEQ 308..313 FT /note="PASTSS -> MLELIE (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:9747029" FT /id="VSP_004906" FT VAR_SEQ 687..740 FT /note="TTALDKERQVFRRRRNQDVRSRYKAQPAPPELNSESEDYSPSSSETVRSPNS FT PF -> LDHGFTIKRSGSLDYYQQPGMYWIRPPLLIRRGRFSDEDATRM (in FT isoform 1 and isoform 3)" FT /evidence="ECO:0000303|PubMed:10036192, FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9205841, ECO:0000303|PubMed:9747029" FT /id="VSP_004907" FT VARIANT 29 FT /note="G -> C (in a gastric adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045673" FT VARIANT 46 FT /note="T -> M (in a gastric adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045674" FT VARIANT 93 FT /note="R -> Q (in a gastric adenocarcinoma sample; somatic FT mutation; dbSNP:rs1366698690)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045675" FT VARIANT 291 FT /note="S -> F (in a gastric adenocarcinoma sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045676" FT VARIANT 292 FT /note="R -> H (in dbSNP:rs56185003)" FT /evidence="ECO:0000269|PubMed:17344846" FT /id="VAR_045677" FT HELIX 53..55 FT /evidence="ECO:0007829|PDB:1MFW" FT STRAND 56..63 FT /evidence="ECO:0007829|PDB:1MG4" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:1MG4" FT TURN 78..80 FT /evidence="ECO:0007829|PDB:1MG4" FT HELIX 84..95 FT /evidence="ECO:0007829|PDB:1MG4" FT STRAND 98..101 FT /evidence="ECO:0007829|PDB:1MG4" FT STRAND 107..110 FT /evidence="ECO:0007829|PDB:1MG4" FT HELIX 120..122 FT /evidence="ECO:0007829|PDB:1MG4" FT STRAND 128..135 FT /evidence="ECO:0007829|PDB:1MG4" FT TURN 142..145 FT /evidence="ECO:0007829|PDB:1MG4" FT HELIX 148..151 FT /evidence="ECO:0007829|PDB:1MG4" FT HELIX 384..389 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 390..398 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 400..409 FT /evidence="ECO:0007829|PDB:5JZJ" FT TURN 410..412 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 415..422 FT /evidence="ECO:0007829|PDB:5JZJ" FT TURN 423..425 FT /evidence="ECO:0007829|PDB:6KYQ" FT STRAND 427..429 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 436..440 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 451..456 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 458..466 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 473..480 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 485..504 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 514..516 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 517..521 FT /evidence="ECO:0007829|PDB:5JZJ" FT STRAND 523..525 FT /evidence="ECO:0007829|PDB:7KX6" FT STRAND 527..531 FT /evidence="ECO:0007829|PDB:5JZJ" FT TURN 551..553 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 556..560 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 568..582 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 596..603 FT /evidence="ECO:0007829|PDB:5JZJ" FT TURN 610..615 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 618..627 FT /evidence="ECO:0007829|PDB:5JZJ" FT TURN 632..634 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 638..643 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 645..647 FT /evidence="ECO:0007829|PDB:5JZJ" FT HELIX 662..668 FT /evidence="ECO:0007829|PDB:6KYQ" FT TURN 678..682 FT /evidence="ECO:0007829|PDB:6KYQ" FT HELIX 683..686 FT /evidence="ECO:0007829|PDB:6KYQ" FT HELIX 689..691 FT /evidence="ECO:0007829|PDB:6KYQ" SQ SEQUENCE 740 AA; 82224 MW; D7B6D855099A315C CRC64; MSFGRDMELE HFDERDKAQR YSRGSRVNGL PSPTHSAHCS FYRTRTLQTL SSEKKAKKVR FYRNGDRYFK GIVYAISPDR FRSFEALLAD LTRTLSDNVN LPQGVRTIYT IDGLKKISSL DQLVEGESYV CGSIEPFKKL EYTKNVNPNW SVNVKTTSAS RAVSSLATAK GSPSEVRENK DFIRPKLVTI IRSGVKPRKA VRILLNKKTA HSFEQVLTDI TDAIKLDSGV VKRLYTLDGK QVMCLQDFFG DDDIFIACGP EKFRYQDDFL LDESECRVVK STSYTKIASS SRRSTTKSPG PSRRSKSPAS TSSVNGTPGS QLSTPRSGKS PSPSPTSPGS LRKQRSSQHG GSSTSLASTK VCSSMDENDG PGEEVSEEGF QIPATITERY KVGRTIGDGN FAVVKECVER STAREYALKI IKKSKCRGKE HMIQNEVSIL RRVKHPNIVL LIEEMDVPTE LYLVMELVKG GDLFDAITST NKYTERDASG MLYNLASAIK YLHSLNIVHR DIKPENLLVY EHQDGSKSLK LGDFGLATIV DGPLYTVCGT PTYVAPEIIA ETGYGLKVDI WAAGVITYIL LCGFPPFRGS GDDQEVLFDQ ILMGQVDFPS PYWDNVSDSA KELITMMLLV DVDQRFSAVQ VLEHPWVNDD GLPENEHQLS VAGKIKKHFN TGPKPNSTAA GVSVIATTAL DKERQVFRRR RNQDVRSRYK AQPAPPELNS ESEDYSPSSS ETVRSPNSPF //