ID DCLK2_HUMAN Reviewed; 766 AA. AC Q8N568; Q59GC8; Q8N399; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 3. DT 20-JAN-2009, entry version 55. DE RecName: Full=Serine/threonine-protein kinase DCLK2; DE EC=2.7.11.1; DE AltName: Full=Doublecortin-like and CAM kinase-like 2; DE Short=Doublecortin-like kinase 2; GN Name=DCLK2; Synonyms=DCAMKL2, DCDC3B, DCK2; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-766 (ISOFORM 3). RC TISSUE=Amygdala; RG The German cDNA consortium; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [4] RP VARIANTS [LARGE SCALE ANALYSIS] CYS-119; HIS-372 AND VAL-583. 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 -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q8N568-1; Sequence=Displayed; CC Name=2; CC IsoId=Q8N568-2; Sequence=VSP_012794; CC Note=By homology to mouse isoform 2; CC Name=3; CC IsoId=Q8N568-3; Sequence=VSP_012793; CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK CC Ser/Thr protein kinase family. CaMK subfamily. CC -!- SIMILARITY: Contains 2 doublecortin domains. CC -!- SIMILARITY: Contains 1 protein kinase domain. 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; AB209181; BAD92418.1; ALT_INIT; mRNA. DR EMBL; AC093748; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105343; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC108934; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC118064; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL834498; CAD39156.1; -; mRNA. DR RefSeq; NP_001035350.2; -. DR RefSeq; NP_001035351.3; -. DR UniGene; Hs.591683; -. DR HSSP; O43602; 1MJD. DR SMR; Q8N568; 65-169. DR PhosphoSite; Q8N568; -. DR Ensembl; ENSG00000170390; Homo sapiens. DR GeneID; 166614; -. DR KEGG; hsa:166614; -. DR GeneCards; GC04P151219; -. DR HGNC; HGNC:19002; DCLK2. DR HPA; HPA015770; -. DR HOVERGEN; Q8N568; -. DR BRENDA; 2.7.11.1; 247. DR LinkHub; Q8N568; -. DR NextBio; 88597; -. DR ArrayExpress; Q8N568; -. DR CleanEx; HS_DCLK2; -. DR GermOnline; ENSG00000170390; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:InterPro. DR GO; GO:0007242; P:intracellular signaling cascade; IEA:InterPro. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR003533; DCX. DR InterPro; IPR000719; Prot_kinase_core. DR InterPro; IPR017441; Protein_kinase_ATP_bd_CS. DR InterPro; IPR017442; Se/Thr_pkinase-rel. DR InterPro; IPR008271; Ser_thr_pkin_AS. DR InterPro; IPR002290; Ser_thr_pkinase. DR Pfam; PF03607; DCX; 2. DR Pfam; PF00069; Pkinase; 1. DR ProDom; PD000001; Prot_kinase; 1. DR SMART; SM00537; DCX; 2. DR SMART; SM00220; S_TKc; 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. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding; KW Polymorphism; Repeat; Serine/threonine-protein kinase; Transferase. FT CHAIN 1 766 Serine/threonine-protein kinase DCLK2. FT /FTId=PRO_0000085922. FT DOMAIN 72 158 Doublecortin 1. FT DOMAIN 197 280 Doublecortin 2. FT DOMAIN 394 651 Protein kinase. FT NP_BIND 400 408 ATP (By similarity). FT COMPBIAS 293 362 Ser-rich. FT COMPBIAS 713 753 Pro-rich. FT ACT_SITE 515 515 Proton acceptor (By similarity). FT BINDING 423 423 ATP (By similarity). FT VAR_SEQ 321 321 V -> VKRGGHYSSAYSTAKSPV (in isoform 3). FT /FTId=VSP_012793. FT VAR_SEQ 352 352 Missing (in isoform 2). FT /FTId=VSP_012794. FT VARIANT 119 119 G -> C. FT /FTId=VAR_040441. FT VARIANT 372 372 R -> H. FT /FTId=VAR_040442. FT VARIANT 583 583 I -> V. FT /FTId=VAR_040443. FT CONFLICT 694 694 A -> V (in Ref. 3; CAD39156). SQ SEQUENCE 766 AA; 83612 MW; 024F2DF9174AE83C CRC64; MASTRSIELE HFEERDKRPR PGSRRGAPSS SGGSSSSGPK GNGLIPSPAH SAHCSFYRTR TLQALSSEKK AKKARFYRNG DRYFKGLVFA ISSDRFRSFD ALLIELTRSL SDNVNLPQGV RTIYTIDGSR KVTSLDELLE GESYVCASNE PFRKVDYTKN INPNWSVNIK GGTSRALAAA SSVKSEVKES KDFIKPKLVT VIRSGVKPRK AVRILLNKKT AHSFEQVLTD ITEAIKLDSG VVKRLCTLDG KQVTCLQDFF GDDDVFIACG PEKFRYAQDD FVLDHSECRV LKSSYSRSSA VKYSGSKSPG PSRRSKSPAS VNGTPSSQLS TPKSTKSSSS SPTSPGSFRG LKQISAHGRS SSNVNGGPEL DRCISPEGVN GNRCSESSTL LEKYKIGKVI GDGNFAVVKE CIDRSTGKEF ALKIIDKAKC CGKEHLIENE VSILRRVKHP NIIMLVEEME TATELFLVME LVKGGDLFDA ITSSTKYTER DGSAMVYNLA NALRYLHGLS IVHRDIKPEN LLVCEYPDGT KSLKLGDFGL ATVVEGPLYT VCGTPTYVAP EIIAETGYGL KVDIWAAGVI TYILLCGFPP FRSENNLQED LFDQILAGKL EFPAPYWDNI TDSAKELISQ MLQVNVEARC TAGQILSHPW VSDDASQENN MQAEVTGKLK QHFNNALPKQ NSTTTGVSVI MNTALDKEGQ IFCSKHCQDS GRPGMEPISP VPPSVEEIPV PGEAVPAPTP PESPTPHCPP AAPGGERAGT WRRHRD //