CDK18_PONAB
ID CDK18_PONAB Reviewed; 474 AA.
AC Q5RD01;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 28-MAR-2018, sequence version 3.
DT 03-AUG-2022, entry version 104.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play a role in signal transduction cascades in terminally
CC differentiated cells. {ECO:0000250}.
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 -!- 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; CR858117; CAH90356.1; -; mRNA.
DR RefSeq; NP_001127275.1; NM_001133803.1.
DR RefSeq; XP_009236983.1; XM_009238708.1.
DR RefSeq; XP_009236987.1; XM_009238712.1.
DR AlphaFoldDB; Q5RD01; -.
DR SMR; Q5RD01; -.
DR STRING; 9601.ENSPPYP00000000327; -.
DR GeneID; 100174332; -.
DR KEGG; pon:100174332; -.
DR CTD; 5129; -.
DR eggNOG; KOG0594; Eukaryota.
DR HOGENOM; CLU_000288_154_3_1; -.
DR InParanoid; Q5RD01; -.
DR TreeFam; TF106508; -.
DR Proteomes; UP000001595; Chromosome 1.
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; IEA:InterPro.
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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..474
FT /note="Cyclin-dependent kinase 18"
FT /id="PRO_0000086492"
FT DOMAIN 144..425
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 44..87
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:0000250|UniProtKB:Q07002"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
FT MOD_RES 132
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q07002"
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"
SQ SEQUENCE 474 AA; 54469 MW; 5AD43E03D4511893 CRC64;
MIMNKMKNFK RRFSLSVPRT ETIEESLAEF TEQFNQLHNR RNEDLQLGPL GRDPLQECST
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 RYLPQPLISH APRLDTDGIQ LLSSLLLYES KSRMSAEAAL
SHPYFRSLGE RVHQLEDTAS IFSLKEIQLQ KDPGYRGLAF QQPGRGKNRR QSIF
