ID DCLK2_HUMAN Reviewed; 766 AA. AC Q8N568; Q59GC8; Q8N399; DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 4. DT 18-MAY-2010, entry version 69. 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 AltName: Full=Doublecortin-like kinase 2; DE AltName: Full=Doublecortin domain-containing protein 3B; DE AltName: Full=CaMK-like CREB regulatory kinase 2; DE Short=CLICK2; DE Short=CLICK-II; DE Short=CL2; 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; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). 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 -!- FUNCTION: Protein kinase with a significantly reduced Ca2+/CAM CC affinity and dependence compared to other members of the CaMK CC family. May play a role in the down-regulation of CRE-dependent CC gene activation probably by phosphorylation of the CREB CC coactivator CRTC2/TORC2 and the resulting retention of TORC2 in CC the cytoplasm (By similarity). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SUBUNIT: Binds to and stabilizes microtubules (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes CC with microtubules (By similarity). 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 -!- DOMAIN: The doublecortin domains are involved in the CC colocalization with microtubules (By similarity). 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 -!- SEQUENCE CAUTION: CC Sequence=BAD92418.1; Type=Erroneous initiation; Note=Translation N-terminally shortened; 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 IPI; IPI00296360; -. DR IPI; IPI00552471; -. DR IPI; IPI00552604; -. DR RefSeq; NP_001035350.2; -. DR RefSeq; NP_001035351.3; -. DR UniGene; Hs.591683; -. DR SMR; Q8N568; 64-169, 191-293, 386-687. DR PhosphoSite; Q8N568; -. DR Ensembl; ENST00000296550; ENSP00000296550; ENSG00000170390; Homo sapiens. DR GeneID; 166614; -. DR KEGG; hsa:166614; -. DR UCSC; uc003ilm.2; human. DR UCSC; uc003ilo.2; human. DR CTD; 166614; -. DR GeneCards; GC04P151219; -. DR H-InvDB; HIX0004559; -. DR HGNC; HGNC:19002; DCLK2. DR HPA; HPA015770; -. DR MIM; 613166; gene. DR HOVERGEN; HBG003790; -. DR BRENDA; 2.7.11.1; 247. DR NextBio; 88597; -. DR ArrayExpress; Q8N568; -. DR Bgee; Q8N568; -. DR CleanEx; HS_DCLK2; -. DR Genevestigator; Q8N568; -. DR GermOnline; ENSG00000170390; Homo sapiens. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0007242; P:intracellular signaling cascade; IEA:InterPro. DR GO; GO:0006468; P:protein amino acid phosphorylation; IEA:InterPro. DR InterPro; IPR020636; Ca/CaM-dep_prot_kinase-like. DR InterPro; IPR003533; DCX. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_cat_dom. DR InterPro; IPR017441; Protein_kinase_ATP_BS. DR InterPro; IPR017442; Se/Thr_prot_kinase-like_dom. DR InterPro; IPR008271; Ser/Thr_prot_kinase_AS. DR InterPro; IPR020649; Ser/Thr_prot_kinase_DCLK. DR InterPro; IPR002290; Ser/Thr_prot_kinase_dom. DR PANTHER; PTHR22982; Ca/CaM-dep_prot_kinase-like; 1. DR PANTHER; PTHR22982:SF27; Ser/Thr_prot_kinase_DCLK; 1. DR Pfam; PF03607; DCX; 2. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00537; DCX; 2. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Kinase_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. PE 2: Evidence at transcript level; KW Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; KW Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein; 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 MOD_RES 6 6 Phosphoserine (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 (in dbSNP:rs56327537). FT /FTId=VAR_040441. FT VARIANT 372 372 R -> H (in dbSNP:rs34386880). FT /FTId=VAR_040442. FT VARIANT 583 583 I -> V (in dbSNP:rs35745104). FT /FTId=VAR_040443. FT CONFLICT 694 694 A -> V (in Ref. 3; CAD39156). FT CONFLICT 748 748 P -> C (in Ref. 1; BAD92418 and 3; FT CAD39156). SQ SEQUENCE 766 AA; 83606 MW; 024F3223874AE83C 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 PESPTPHPPP AAPGGERAGT WRRHRD //