CDK17_RAT
ID CDK17_RAT Reviewed; 523 AA.
AC O35831;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Cyclin-dependent kinase 17;
DE EC=2.7.11.22;
DE AltName: Full=Cell division protein kinase 17;
DE AltName: Full=PCTAIRE-motif protein kinase 2;
DE AltName: Full=Serine/threonine-protein kinase PCTAIRE-2;
GN Name=Cdk17; Synonyms=Pctaire2, Pctk2;
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 IDENTIFICATION IN A COMPLEX WITH CDK16 AND TDRD7, AND INTERACTION WITH
RP TDRD7.
RX PubMed=10727952; DOI=10.1046/j.1432-1327.2000.01218.x;
RA Hirose T., Kawabuchi M., Tamaru T., Okumura N., Nagai K., Okada M.;
RT "Identification of tudor repeat associator with PCTAIRE 2 (Trap). A novel
RT protein that interacts with the N-terminal domain of PCTAIRE 2 in rat
RT brain.";
RL Eur. J. Biochem. 267:2113-2121(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137, AND IDENTIFICATION BY
RP 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137 AND SER-180, AND
RP 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 terminally differentiated neurons. Has a
CC Ser/Thr-phosphorylating activity for histone H1.
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 -!- SUBUNIT: Found in a complex containing CABLES1, CDK16 and TDRD7.
CC Interacts with TDRD7. {ECO:0000269|PubMed:10727952}.
CC -!- TISSUE SPECIFICITY: Brain specific. Within the brain it is concentrated
CC in the neuronal layers of the hippocampus and olfactory bulb, which
CC mostly consist of post-mitotic neurons.
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; AB005540; BAA22332.1; -; mRNA.
DR AlphaFoldDB; O35831; -.
DR SMR; O35831; -.
DR STRING; 10116.ENSRNOP00000005762; -.
DR iPTMnet; O35831; -.
DR PhosphoSitePlus; O35831; -.
DR jPOST; O35831; -.
DR PaxDb; O35831; -.
DR PRIDE; O35831; -.
DR Ensembl; ENSRNOT00000109496; ENSRNOP00000085940; ENSRNOG00000004148.
DR UCSC; RGD:1565593; rat.
DR RGD; 1565593; Cdk17.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000155834; -.
DR InParanoid; O35831; -.
DR PhylomeDB; O35831; -.
DR BRENDA; 2.7.11.22; 5301.
DR PRO; PR:O35831; -.
DR Proteomes; UP000002494; Chromosome 7.
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..523
FT /note="Cyclin-dependent kinase 17"
FT /id="PRO_0000086489"
FT DOMAIN 192..473
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 31..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 103..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..123
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 313
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 198..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 221
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 80
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 105
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 137
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16641100,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 523 AA; 59432 MW; 1A391555CB3CEF79 CRC64;
MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEESSSKDNE PIVKNGRPPT SHSMHSFLHQ
YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV
QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQISSPPFDQ PMSRRSRRAS
LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS
LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGSIMSMHNV KLFLYQILRG
LAYCHRRKVL HRDLKPQNLL INERGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL
LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGVSSND
EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RAPAEEAMKH VYFRSLGPRI
HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGVFVINHFT CRS
