CDK18_HUMAN
ID CDK18_HUMAN Reviewed; 474 AA.
AC Q07002; Q5VXQ2; Q6V3A2; Q6V3A3; Q96F90;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Cyclin-dependent kinase 18;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 18;
DE AltName: Full=PCTAIRE-motif protein kinase 3;
DE AltName: Full=Serine/threonine-protein kinase PCTAIRE-3;
GN Name=CDK18; Synonyms=PCTAIRE3, PCTK3;
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 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=15019984; DOI=10.1016/j.gene.2003.12.011;
RA Herskovits A.Z., Davies P.;
RT "Cloning and expression analysis of two novel PCTAIRE 3 transcripts from
RT human brain.";
RL Gene 328:59-67(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT MET-166.
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 3-474 (ISOFORM 1), AND VARIANT
RP MET-166.
RC TISSUE=Colon;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 95-474.
RX PubMed=1639063; DOI=10.1002/j.1460-2075.1992.tb05360.x;
RA Meyerson M., Enders G.H., Wu C.-L., Su L.-K., Gorka C., Nelson C.,
RA Harlow E., Tsai L.-H.;
RT "A family of human cdc2-related protein kinases.";
RL EMBO J. 11:2909-2917(1992).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-89 AND SER-117, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-89 AND SER-132, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-74; SER-89; SER-98 AND
RP SER-117, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [13]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-48; ARG-67 AND MET-166.
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: May play a role in signal transduction cascades in terminally
CC differentiated cells.
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=2.7.11.22;
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=2.7.11.22;
CC -!- INTERACTION:
CC Q07002; Q96MA6: AK8; NbExp=3; IntAct=EBI-746238, EBI-8466265;
CC Q07002; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-746238, EBI-2548012;
CC Q07002; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-746238, EBI-11524851;
CC Q07002; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-746238, EBI-10171570;
CC Q07002; Q86Z20: CCDC125; NbExp=3; IntAct=EBI-746238, EBI-11977221;
CC Q07002; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-746238, EBI-347573;
CC Q07002; P30281: CCND3; NbExp=3; IntAct=EBI-746238, EBI-375013;
CC Q07002; O95273: CCNDBP1; NbExp=3; IntAct=EBI-746238, EBI-748961;
CC Q07002; O75909-2: CCNK; NbExp=3; IntAct=EBI-746238, EBI-12010594;
CC Q07002; Q01850: CDR2; NbExp=3; IntAct=EBI-746238, EBI-1181367;
CC Q07002; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-746238, EBI-742887;
CC Q07002; O00167-2: EYA2; NbExp=3; IntAct=EBI-746238, EBI-12807776;
CC Q07002; O94868-3: FCHSD2; NbExp=3; IntAct=EBI-746238, EBI-11958845;
CC Q07002; A1L4K1: FSD2; NbExp=3; IntAct=EBI-746238, EBI-5661036;
CC Q07002; P51114-2: FXR1; NbExp=3; IntAct=EBI-746238, EBI-11022345;
CC Q07002; Q08379: GOLGA2; NbExp=6; IntAct=EBI-746238, EBI-618309;
CC Q07002; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-746238, EBI-5916454;
CC Q07002; Q9H8Y8: GORASP2; NbExp=3; IntAct=EBI-746238, EBI-739467;
CC Q07002; P54257: HAP1; NbExp=3; IntAct=EBI-746238, EBI-712814;
CC Q07002; Q6NT76: HMBOX1; NbExp=3; IntAct=EBI-746238, EBI-2549423;
CC Q07002; Q9NSC5: HOMER3; NbExp=3; IntAct=EBI-746238, EBI-748420;
CC Q07002; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-746238, EBI-10961706;
CC Q07002; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-746238, EBI-747204;
CC Q07002; Q0VD86: INCA1; NbExp=3; IntAct=EBI-746238, EBI-6509505;
CC Q07002; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-746238, EBI-2556193;
CC Q07002; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-746238, EBI-2125614;
CC Q07002; P19012: KRT15; NbExp=3; IntAct=EBI-746238, EBI-739566;
CC Q07002; P08779: KRT16; NbExp=3; IntAct=EBI-746238, EBI-356410;
CC Q07002; Q15323: KRT31; NbExp=6; IntAct=EBI-746238, EBI-948001;
CC Q07002; O76011: KRT34; NbExp=3; IntAct=EBI-746238, EBI-1047093;
CC Q07002; Q6A162: KRT40; NbExp=3; IntAct=EBI-746238, EBI-10171697;
CC Q07002; O95678: KRT75; NbExp=3; IntAct=EBI-746238, EBI-2949715;
CC Q07002; O43790: KRT86; NbExp=3; IntAct=EBI-746238, EBI-9996498;
CC Q07002; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-746238, EBI-741037;
CC Q07002; Q9Y6D9: MAD1L1; NbExp=3; IntAct=EBI-746238, EBI-742610;
CC Q07002; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-746238, EBI-10172526;
CC Q07002; Q8TD10: MIPOL1; NbExp=3; IntAct=EBI-746238, EBI-2548751;
CC Q07002; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-746238, EBI-742948;
CC Q07002; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-746238, EBI-11522433;
CC Q07002; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-746238, EBI-14066006;
CC Q07002; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-746238, EBI-302345;
CC Q07002; Q13136: PPFIA1; NbExp=3; IntAct=EBI-746238, EBI-745426;
CC Q07002; Q15276: RABEP1; NbExp=3; IntAct=EBI-746238, EBI-447043;
CC Q07002; Q04864-2: REL; NbExp=3; IntAct=EBI-746238, EBI-10829018;
CC Q07002; Q13077: TRAF1; NbExp=3; IntAct=EBI-746238, EBI-359224;
CC Q07002; Q12933: TRAF2; NbExp=3; IntAct=EBI-746238, EBI-355744;
CC Q07002; P14373: TRIM27; NbExp=3; IntAct=EBI-746238, EBI-719493;
CC Q07002; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-746238, EBI-9867283;
CC Q07002; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-746238, EBI-2130429;
CC Q07002; Q9BZW7: TSGA10; NbExp=3; IntAct=EBI-746238, EBI-744794;
CC Q07002; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-746238, EBI-9090990;
CC Q07002; Q9UK41-2: VPS28; NbExp=3; IntAct=EBI-746238, EBI-12146727;
CC Q07002; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-746238, EBI-2799833;
CC Q07002; P63104: YWHAZ; NbExp=2; IntAct=EBI-746238, EBI-347088;
CC Q07002; Q9BUY5: ZNF426; NbExp=3; IntAct=EBI-746238, EBI-743265;
CC Q07002; Q7Z4V0: ZNF438; NbExp=3; IntAct=EBI-746238, EBI-11962468;
CC Q07002; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-746238, EBI-10251462;
CC Q07002; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-746238, EBI-527853;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=3a {ECO:0000303|PubMed:15019984};
CC IsoId=Q07002-2; Sequence=Displayed;
CC Name=2; Synonyms=3b {ECO:0000303|PubMed:15019984};
CC IsoId=Q07002-3; Sequence=VSP_035889;
CC -!- TISSUE SPECIFICITY: Isoform 2 expression is limited to several
CC subcortical nuclei of the basal gangli and the spinal cord. Isoform 1
CC is widely expressed. {ECO:0000269|PubMed:15019984}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
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DR EMBL; AY353237; AAR13065.1; -; mRNA.
DR EMBL; AY353238; AAR13066.1; -; mRNA.
DR EMBL; BT007299; AAP35963.1; -; mRNA.
DR EMBL; AL357131; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW91559.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW91560.1; -; Genomic_DNA.
DR EMBL; BC011526; AAH11526.1; -; mRNA.
DR EMBL; X66362; CAA47005.1; -; mRNA.
DR CCDS; CCDS1454.1; -. [Q07002-3]
DR CCDS; CCDS44300.1; -. [Q07002-2]
DR PIR; S32831; S32831.
DR RefSeq; NP_002587.2; NM_002596.3. [Q07002-2]
DR RefSeq; NP_997667.1; NM_212502.2. [Q07002-2]
DR RefSeq; NP_997668.1; NM_212503.2. [Q07002-3]
DR AlphaFoldDB; Q07002; -.
DR SMR; Q07002; -.
DR BioGRID; 111156; 118.
DR IntAct; Q07002; 103.
DR MINT; Q07002; -.
DR STRING; 9606.ENSP00000423665; -.
DR BindingDB; Q07002; -.
DR ChEMBL; CHEMBL5316; -.
DR DrugCentral; Q07002; -.
DR iPTMnet; Q07002; -.
DR PhosphoSitePlus; Q07002; -.
DR BioMuta; CDK18; -.
DR DMDM; 116242704; -.
DR EPD; Q07002; -.
DR jPOST; Q07002; -.
DR MassIVE; Q07002; -.
DR MaxQB; Q07002; -.
DR PeptideAtlas; Q07002; -.
DR PRIDE; Q07002; -.
DR ProteomicsDB; 58496; -. [Q07002-2]
DR ProteomicsDB; 58497; -. [Q07002-3]
DR Antibodypedia; 34567; 186 antibodies from 26 providers.
DR DNASU; 5129; -.
DR Ensembl; ENST00000360066.6; ENSP00000353176.2; ENSG00000117266.16. [Q07002-2]
DR Ensembl; ENST00000429964.7; ENSP00000399082.2; ENSG00000117266.16. [Q07002-2]
DR Ensembl; ENST00000506784.5; ENSP00000423665.1; ENSG00000117266.16. [Q07002-3]
DR GeneID; 5129; -.
DR KEGG; hsa:5129; -.
DR MANE-Select; ENST00000429964.7; ENSP00000399082.2; NM_212502.3; NP_997667.1.
DR UCSC; uc001hcp.4; human. [Q07002-2]
DR CTD; 5129; -.
DR DisGeNET; 5129; -.
DR GeneCards; CDK18; -.
DR HGNC; HGNC:8751; CDK18.
DR HPA; ENSG00000117266; Tissue enhanced (brain, heart muscle).
DR MIM; 169190; gene.
DR neXtProt; NX_Q07002; -.
DR OpenTargets; ENSG00000117266; -.
DR PharmGKB; PA33097; -.
DR VEuPathDB; HostDB:ENSG00000117266; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000159482; -.
DR HOGENOM; CLU_000288_154_3_1; -.
DR InParanoid; Q07002; -.
DR OMA; YRRRQNQ; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q07002; -.
DR TreeFam; TF106508; -.
DR BRENDA; 2.7.11.22; 2681.
DR PathwayCommons; Q07002; -.
DR SignaLink; Q07002; -.
DR SIGNOR; Q07002; -.
DR BioGRID-ORCS; 5129; 9 hits in 1105 CRISPR screens.
DR ChiTaRS; CDK18; human.
DR GeneWiki; PCTK3; -.
DR GenomeRNAi; 5129; -.
DR Pharos; Q07002; Tchem.
DR PRO; PR:Q07002; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q07002; protein.
DR Bgee; ENSG00000117266; Expressed in C1 segment of cervical spinal cord and 143 other tissues.
DR ExpressionAtlas; Q07002; baseline and differential.
DR Genevisible; Q07002; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
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; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..474
FT /note="Cyclin-dependent kinase 18"
FT /id="PRO_0000086490"
FT DOMAIN 144..425
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 44..93
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 265
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 150..158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 173
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19369195"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19369195"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 440
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35832"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35832"
FT VAR_SEQ 91
FT /note="E -> EVRASGALPRQVAGCTHKGVHRRAAALQPDF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15019984"
FT /id="VSP_035889"
FT VARIANT 48
FT /note="G -> S (in dbSNP:rs35134237)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_047802"
FT VARIANT 67
FT /note="G -> R (in dbSNP:rs4623769)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_047803"
FT VARIANT 166
FT /note="T -> M (in dbSNP:rs17850752)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.2"
FT /id="VAR_047804"
FT CONFLICT 258
FT /note="H -> T (in Ref. 6; CAA47005)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="D -> A (in Ref. 6; CAA47005)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="L -> V (in Ref. 6; CAA47005)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 54424 MW; 43C83A573A595476 CRC64;
MIMNKMKNFK RRFSLSVPRT ETIEESLAEF TEQFNQLHNR RNENLQLGPL GRDPPQECST
FSPTDSGEEP GQLSPGVQFQ RRQNQRRFSM EDVSKRLSLP MDIRLPQEFL QKLQMESPDL
PKPLSRMSRR ASLSDIGFGK LETYVKLDKL GEGTYATVFK GRSKLTENLV ALKEIRLEHE
EGAPCTAIRE VSLLKNLKHA NIVTLHDLIH TDRSLTLVFE YLDSDLKQYL DHCGNLMSMH
NVKIFMFQLL RGLAYCHHRK ILHRDLKPQN LLINERGELK LADFGLARAK SVPTKTYSNE
VVTLWYRPPD VLLGSTEYST PIDMWGVGCI HYEMATGRPL FPGSTVKEEL HLIFRLLGTP
TEETWPGVTA FSEFRTYSFP CYLPQPLINH APRLDTDGIH LLSSLLLYES KSRMSAEAAL
SHSYFRSLGE RVHQLEDTAS IFSLKEIQLQ KDPGYRGLAF QQPGRGKNRR QSIF
