CDK18_MOUSE
ID CDK18_MOUSE Reviewed; 451 AA.
AC Q04899;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 170.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fibroblast;
RX PubMed=1437147;
RA Okuda T., Cleveland J.L., Downing J.R.;
RT "PCTAIRE-1 and PCTAIRE-3, two members of a novel cdc2/CDC28-related protein
RT kinase gene family.";
RL Oncogene 7:2249-2258(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-109, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 -!- TISSUE SPECIFICITY: In brain, kidney, intestine and at a much lower
CC level, in fetal tissues.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-4 is the initiator.
CC {ECO:0000305}.
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DR EMBL; X69026; CAA48788.1; -; mRNA.
DR EMBL; AK004998; BAB23732.1; -; mRNA.
DR CCDS; CCDS15281.1; -.
DR PIR; S30436; S30436.
DR RefSeq; NP_032821.1; NM_008795.2.
DR AlphaFoldDB; Q04899; -.
DR SMR; Q04899; -.
DR BioGRID; 202065; 2.
DR IntAct; Q04899; 1.
DR MINT; Q04899; -.
DR STRING; 10090.ENSMUSP00000027697; -.
DR iPTMnet; Q04899; -.
DR PhosphoSitePlus; Q04899; -.
DR jPOST; Q04899; -.
DR PaxDb; Q04899; -.
DR PeptideAtlas; Q04899; -.
DR PRIDE; Q04899; -.
DR ProteomicsDB; 281297; -.
DR Antibodypedia; 34567; 186 antibodies from 26 providers.
DR DNASU; 18557; -.
DR Ensembl; ENSMUST00000027697; ENSMUSP00000027697; ENSMUSG00000026437.
DR Ensembl; ENSMUST00000112362; ENSMUSP00000107981; ENSMUSG00000026437.
DR GeneID; 18557; -.
DR KEGG; mmu:18557; -.
DR UCSC; uc007coh.2; mouse.
DR CTD; 5129; -.
DR MGI; MGI:97518; Cdk18.
DR VEuPathDB; HostDB:ENSMUSG00000026437; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000159482; -.
DR HOGENOM; CLU_000288_154_3_1; -.
DR InParanoid; Q04899; -.
DR OMA; YRRRQNQ; -.
DR OrthoDB; 1010560at2759; -.
DR PhylomeDB; Q04899; -.
DR TreeFam; TF106508; -.
DR BRENDA; 2.7.11.22; 3474.
DR BioGRID-ORCS; 18557; 2 hits in 74 CRISPR screens.
DR ChiTaRS; Cdk18; mouse.
DR PRO; PR:Q04899; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q04899; protein.
DR Bgee; ENSMUSG00000026437; Expressed in small intestine Peyer's patch and 150 other tissues.
DR ExpressionAtlas; Q04899; baseline and differential.
DR Genevisible; Q04899; MM.
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 ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..451
FT /note="Cyclin-dependent kinase 18"
FT /id="PRO_0000086491"
FT DOMAIN 121..402
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 242
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 127..135
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 150
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 51
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35832"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35832"
SQ SEQUENCE 451 AA; 51848 MW; 3FC500519714F7E0 CRC64;
MNKMKNFKRR LSLSVPRPET IEESLAEFTE QFNQLHTQTN EDGTDEPEQL SPGMQYQQRQ
NQRRFSMEDL NKRLSLPMDI RLPQEFLQKL QLENPGLPKP LTRMSRRASL SDIGFGKLET
YVKLDKLGEG TYATVFKGRS KLTENLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV
TLHDLIHTDR SLTLVFEYLD SDLKQYLDHC GNLMNMHNVK IFMFQLLRGL AYCHHRKILH
RDLKPQNLLI NERGELKLAD FGLARAKSVP TKTYSNEVVT LWYRPPDVLL GSTEYSTPID
MWGVGCILYE MATGKPLFPG STVKEELHLI FRLLGTPTEE SWPGVTSISE FRAYNFPRYL
PQPLLSHAPR LDTEGINLLS SLLLYESKSR MSAEAALNHP YFQSLGDRVH QLHDTASIFS
LKEIQLQKDP GYRGLAFQHP GRGKSRRQSI F
