CDK18_RAT
ID CDK18_RAT Reviewed; 451 AA.
AC O35832;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
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 Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9370357; DOI=10.1111/j.1432-1033.1997.t01-1-00481.x;
RA Hirose T., Tamaru T., Okumura N., Nagai K., Okada M.;
RT "PCTAIRE 2, a Cdc2-related serine/threonine kinase, is predominantly
RT expressed in terminally differentiated neurons.";
RL Eur. J. Biochem. 249:481-488(1997).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51 AND SER-66, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16641100; DOI=10.1073/pnas.0600895103;
RA Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
RT "Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
RT regulation of aquaporin-2 phosphorylation at two sites.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-51; SER-66; SER-417 AND
RP SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; AB005541; BAA21472.1; -; mRNA.
DR RefSeq; NP_001093976.1; NM_001100506.1.
DR RefSeq; XP_006249813.1; XM_006249751.3.
DR AlphaFoldDB; O35832; -.
DR SMR; O35832; -.
DR STRING; 10116.ENSRNOP00000010976; -.
DR iPTMnet; O35832; -.
DR PhosphoSitePlus; O35832; -.
DR jPOST; O35832; -.
DR PaxDb; O35832; -.
DR PRIDE; O35832; -.
DR GeneID; 289019; -.
DR KEGG; rno:289019; -.
DR UCSC; RGD:1309523; rat.
DR CTD; 5129; -.
DR RGD; 1309523; Cdk18.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_154_3_1; -.
DR InParanoid; O35832; -.
DR PhylomeDB; O35832; -.
DR TreeFam; TF106508; -.
DR BRENDA; 2.7.11.22; 5301.
DR PRO; PR:O35832; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; O35832; RN.
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_0000086493"
FT DOMAIN 121..402
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 39..61
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 51
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04899"
FT MOD_RES 417
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 451 AA; 51882 MW; C3E4688F51B142E8 CRC64;
MNKMKNFKRR LSLSVPRPET IEESLTEFTE QFNQLHTQRN EDGRDEPGQL SPGVQYQQRQ
NQRRFSMEDL NKRLSLPMDI RLPQEFLQKL QLENPGLPKP LTRMSRRASL SDIGFGKLET
YVKLDKLGEG TYATVFKGRS KLTENLVALK EIRLEHEEGA PCTAIREVSL LKDLKHANIV
TLHDLIHTDR SLTLVFEYLD SDLKQYLDHC GNLMNMHNVK IFMFQLLRGL AYCHRRKILH
RDLKPQNLLI NERGELKLAD FGLARAKSVP TKTYSNEVVT LWYRPPDVLL GSTEYSTPID
MWGVGCILYE MATGKPLFPG STVKEELHLI FRLLGTPTEE SWPGVTSISE FRAYNFPRYL
PQPLLSHAPR LDTEGINLLT SLLLYESKSR MSAEAALSHP YFQSLGERVH QLDDTASIFS
LKEIQLQKDP GYRGLAFQHP GRGKSRRQSI F
