DCLK1_HUMAN
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 03-AUG-2022, entry version 204.
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 O15075-2; 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};
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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; 91.
DR IntAct; O15075; 36.
DR MINT; O15075; -.
DR STRING; 9606.ENSP00000255448; -.
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; O15075; -.
DR PeptideAtlas; O15075; -.
DR PRIDE; O15075; -.
DR ProteomicsDB; 48428; -. [O15075-1]
DR ProteomicsDB; 48429; -. [O15075-2]
DR ProteomicsDB; 48430; -. [O15075-3]
DR ProteomicsDB; 48431; -. [O15075-4]
DR Antibodypedia; 23046; 438 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; ENST00000615680.4; 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 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; CSKICVY; -.
DR OrthoDB; 330091at2759; -.
DR PhylomeDB; O15075; -.
DR TreeFam; TF318770; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; O15075; -.
DR SignaLink; O15075; -.
DR BioGRID-ORCS; 9201; 12 hits in 1103 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 186 other tissues.
DR ExpressionAtlas; O15075; baseline and differential.
DR Genevisible; O15075; HS.
DR GO; GO:0005887; C:integral component of 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:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
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 Gene3D; 3.10.20.230; -; 2.
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 Pfam; PF03607; DCX; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00537; DCX; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR SUPFAM; SSF89837; SSF89837; 2.
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.
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
