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Serine/threonine-protein kinase DCLK2 (EC 2.7.11.1) (CaMK-like CREB regulatory kinase 2) (CL2) (CLICK-II) (CLICK2) (Doublecortin domain-containing protein 3B) (Doublecortin-like and CAM kinase-like 2) (Doublecortin-like kinase 2)

 DCLK2_HUMAN             Reviewed;         766 AA.
Q8N568; C9J5Q9; Q59GC8; Q8N399;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 4.
07-NOV-2018, entry version 146.
RecName: Full=Serine/threonine-protein kinase DCLK2;
EC=2.7.11.1;
AltName: Full=CaMK-like CREB regulatory kinase 2;
Short=CL2;
Short=CLICK-II;
Short=CLICK2;
AltName: Full=Doublecortin domain-containing protein 3B;
AltName: Full=Doublecortin-like and CAM kinase-like 2;
AltName: Full=Doublecortin-like kinase 2;
Name=DCLK2; Synonyms=DCAMKL2, DCDC3B, DCK2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-766 (ISOFORM 3).
TISSUE=Amygdala;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[4]
GENE FAMILY.
PubMed=16869982; DOI=10.1186/1471-2164-7-188;
Reiner O., Coquelle F.M., Peter B., Levy T., Kaplan A., Sapir T.,
Orr I., Barkai N., Eichele G., Bergmann S.;
"The evolving doublecortin (DCX) superfamily.";
BMC Genomics 7:188-188(2006).
[5]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=18075264; DOI=10.1159/000109861;
Tuy F.P.D., Saillour Y., Kappeler C., Chelly J., Francis F.;
"Alternative transcripts of Dclk1 and Dclk2 and their expression in
doublecortin knockout mice.";
Dev. Neurosci. 30:171-186(2008).
[6]
REVIEW, AND GENE FAMILY.
PubMed=20236041; DOI=10.2174/187152410790780118;
Dijkmans T.F., van Hooijdonk L.W.A., Fitzsimons C.P., Vreugdenhil E.;
"The doublecortin gene family and disorders of neuronal structure.";
Cent. Nerv. Syst. Agents Med. Chem. 10:32-46(2010).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61 AND SER-362, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[8]
VARIANTS [LARGE SCALE ANALYSIS] CYS-119; HIS-372 AND VAL-583.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[9]
VARIANT MET-212.
PubMed=25512093; DOI=10.1002/humu.22744;
Peeters K., Bervoets S., Chamova T., Litvinenko I., De Vriendt E.,
Bichev S., Kancheva D., Mitev V., Kennerson M., Timmerman V.,
De Jonghe P., Tournev I., MacMillan J., Jordanova A.;
"Novel mutations in the DYNC1H1 tail domain refine the genetic and
clinical spectrum of dyneinopathies.";
Hum. Mutat. 36:287-291(2015).
-!- FUNCTION: Protein kinase with a significantly reduced C(a2+)/CAM
affinity and dependence compared to other members of the CaMK
family. May play a role in the down-regulation of CRE-dependent
gene activation probably by phosphorylation of the CREB
coactivator CRTC2/TORC2 and the resulting retention of TORC2 in
the cytoplasm (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
-!- SUBUNIT: Binds to and stabilizes microtubules. Interacts with
MAPK8IP1/JIP-1, MAPK8IP2/JIP-2, MAPK9/JNK2, PPP1R9B/NEURABIN-2 and
actin. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Colocalizes
with microtubules. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q8N568-1; Sequence=Displayed;
Name=2;
IsoId=Q8N568-2; Sequence=VSP_012794;
Note=By homology to mouse isoform 2.;
Name=3;
IsoId=Q8N568-3; Sequence=VSP_012793;
-!- TISSUE SPECIFICITY: Expressed in the brain, heart and eyes.
{ECO:0000269|PubMed:18075264}.
-!- DEVELOPMENTAL STAGE: Expressed in fetal brain, and, to a lower
extent, in fetal kidney. {ECO:0000269|PubMed:18075264}.
-!- DOMAIN: The doublecortin domains are involved in the
colocalization with microtubules. {ECO:0000250}.
-!- PTM: Autophosphorylated. {ECO:0000250}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
Ser/Thr protein kinase family. CaMK subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD92418.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AB209181; BAD92418.1; ALT_INIT; mRNA.
EMBL; AC093748; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC105343; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC118064; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL834498; CAD39156.1; -; mRNA.
CCDS; CCDS34076.1; -. [Q8N568-1]
CCDS; CCDS47142.2; -. [Q8N568-3]
RefSeq; NP_001035350.2; NM_001040260.3. [Q8N568-1]
RefSeq; NP_001035351.4; NM_001040261.4. [Q8N568-3]
RefSeq; XP_005262843.1; XM_005262786.2. [Q8N568-2]
UniGene; Hs.591683; -.
ProteinModelPortal; Q8N568; -.
SMR; Q8N568; -.
BioGrid; 127929; 7.
IntAct; Q8N568; 4.
STRING; 9606.ENSP00000303887; -.
BindingDB; Q8N568; -.
ChEMBL; CHEMBL5519; -.
GuidetoPHARMACOLOGY; 2006; -.
iPTMnet; Q8N568; -.
PhosphoSitePlus; Q8N568; -.
BioMuta; DCLK2; -.
DMDM; 296439470; -.
MaxQB; Q8N568; -.
PaxDb; Q8N568; -.
PeptideAtlas; Q8N568; -.
PRIDE; Q8N568; -.
ProteomicsDB; 72008; -.
ProteomicsDB; 72009; -. [Q8N568-2]
ProteomicsDB; 72010; -. [Q8N568-3]
DNASU; 166614; -.
Ensembl; ENST00000296550; ENSP00000296550; ENSG00000170390. [Q8N568-1]
Ensembl; ENST00000302176; ENSP00000303887; ENSG00000170390. [Q8N568-3]
Ensembl; ENST00000506325; ENSP00000427235; ENSG00000170390. [Q8N568-2]
GeneID; 166614; -.
KEGG; hsa:166614; -.
UCSC; uc003ilm.5; human. [Q8N568-1]
CTD; 166614; -.
EuPathDB; HostDB:ENSG00000170390.15; -.
GeneCards; DCLK2; -.
HGNC; HGNC:19002; DCLK2.
HPA; HPA015770; -.
MIM; 613166; gene.
neXtProt; NX_Q8N568; -.
OpenTargets; ENSG00000170390; -.
PharmGKB; PA162383366; -.
eggNOG; KOG0615; Eukaryota.
eggNOG; ENOG410YA63; LUCA.
GeneTree; ENSGT00930000150819; -.
HOGENOM; HOG000230855; -.
HOVERGEN; HBG003790; -.
InParanoid; Q8N568; -.
KO; K08805; -.
OMA; CERAGTW; -.
OrthoDB; EOG091G02RF; -.
PhylomeDB; Q8N568; -.
TreeFam; TF318770; -.
SignaLink; Q8N568; -.
ChiTaRS; DCLK2; human.
GenomeRNAi; 166614; -.
PRO; PR:Q8N568; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000170390; Expressed in 115 organ(s), highest expression level in oocyte.
CleanEx; HS_DCLK2; -.
ExpressionAtlas; Q8N568; baseline and differential.
Genevisible; Q8N568; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0005874; C:microtubule; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
GO; GO:1900181; P:negative regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0018105; P:peptidyl-serine phosphorylation; IEA:Ensembl.
GO; GO:0021860; P:pyramidal neuron development; IEA:Ensembl.
CDD; cd01617; DCX; 2.
Gene3D; 3.10.20.230; -; 2.
InterPro; IPR003533; Doublecortin_dom.
InterPro; IPR036572; Doublecortin_dom_sf.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF03607; DCX; 2.
Pfam; PF00069; Pkinase; 1.
SMART; SM00537; DCX; 2.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
SUPFAM; SSF89837; SSF89837; 2.
PROSITE; PS50309; DC; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Complete proteome; Cytoplasm;
Cytoskeleton; Kinase; Nucleotide-binding; Phosphoprotein;
Polymorphism; Reference proteome; Repeat;
Serine/threonine-protein kinase; Transferase.
CHAIN 1 766 Serine/threonine-protein kinase DCLK2.
/FTId=PRO_0000085922.
DOMAIN 72 158 Doublecortin 1. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 197 280 Doublecortin 2. {ECO:0000255|PROSITE-
ProRule:PRU00072}.
DOMAIN 394 651 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 400 408 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
COMPBIAS 293 362 Ser-rich.
COMPBIAS 713 753 Pro-rich.
ACT_SITE 515 515 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 423 423 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 61 61 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 362 362 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 647 647 Phosphoserine.
{ECO:0000250|UniProtKB:Q5MPA9}.
MOD_RES 666 666 Phosphothreonine.
{ECO:0000250|UniProtKB:Q5MPA9}.
VAR_SEQ 321 321 V -> VKRGGHYSSAYSTAKSPV (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_012793.
VAR_SEQ 353 353 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_012794.
VARIANT 119 119 G -> C (in dbSNP:rs56327537).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040441.
VARIANT 212 212 V -> M (found in a patient with
hereditary motor and sensory neuropathy;
unknown pathological significance;
dbSNP:rs759398144).
{ECO:0000269|PubMed:25512093}.
/FTId=VAR_073158.
VARIANT 372 372 R -> H (in dbSNP:rs34386880).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040442.
VARIANT 583 583 I -> V (in dbSNP:rs35745104).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_040443.
CONFLICT 694 694 A -> V (in Ref. 3; CAD39156).
{ECO:0000305}.
CONFLICT 748 748 P -> C (in Ref. 1; BAD92418 and 3;
CAD39156). {ECO:0000305}.
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


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