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 27-MAR-2024, entry version 219. 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; P62258: YWHAE; NbExp=3; IntAct=EBI-746238, EBI-356498; CC Q07002; P63104: YWHAZ; NbExp=3; 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}. 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; 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 RefSeq; XP_011507904.1; XM_011509602.2. [Q07002-2] DR RefSeq; XP_016856912.1; XM_017001423.1. [Q07002-3] DR AlphaFoldDB; Q07002; -. DR SMR; Q07002; -. DR BioGRID; 111156; 134. DR IntAct; Q07002; 107. DR MINT; Q07002; -. DR STRING; 9606.ENSP00000423665; -. DR BindingDB; Q07002; -. DR ChEMBL; CHEMBL5316; -. DR DrugCentral; Q07002; -. DR GlyGen; Q07002; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q07002; -. DR PhosphoSitePlus; Q07002; -. DR SwissPalm; Q07002; -. DR BioMuta; CDK18; -. DR DMDM; 116242704; -. DR CPTAC; non-CPTAC-2857; -. DR CPTAC; non-CPTAC-2858; -. DR CPTAC; non-CPTAC-5665; -. DR EPD; Q07002; -. DR jPOST; Q07002; -. DR MassIVE; Q07002; -. DR MaxQB; Q07002; -. DR PaxDb; 9606-ENSP00000423665; -. DR PeptideAtlas; Q07002; -. DR ProteomicsDB; 58496; -. [Q07002-2] DR ProteomicsDB; 58497; -. [Q07002-3] DR Pumba; Q07002; -. DR Antibodypedia; 34567; 209 antibodies from 27 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 AGR; HGNC:8751; -. DR CTD; 5129; -. DR DisGeNET; 5129; -. DR GeneCards; CDK18; -. DR HGNC; HGNC:8751; CDK18. DR HPA; ENSG00000117266; Group enriched (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; CHKSKIL; -. DR OrthoDB; 244018at2759; -. 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; 10 hits in 1181 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 145 other cell types or tissues. DR ExpressionAtlas; Q07002; baseline and differential. 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; IBA:GO_Central. DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR CDD; cd07871; STKc_PCTAIRE3; 1. DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1. 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 PANTHER; PTHR24056; CELL DIVISION PROTEIN KINASE; 1. DR PANTHER; PTHR24056:SF52; CYCLIN-DEPENDENT KINASE 18; 1. DR Pfam; PF00069; Pkinase; 1. DR SMART; SM00220; S_TKc; 1. DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1. DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1. DR Genevisible; Q07002; HS. 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 //