CDK17_MOUSE
ID CDK17_MOUSE Reviewed; 523 AA.
AC Q8K0D0;
DT 21-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2004, sequence version 2.
DT 03-AUG-2022, entry version 156.
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 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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Limb, and Retina;
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 [2]
RP IDENTIFICATION IN A COMPLEX WITH CABLES1 AND TDRD7.
RX PubMed=11527406; DOI=10.1006/bbrc.2001.5493;
RA Yamochi T., Nishimoto I., Okuda T., Matsuoka M.;
RT "ik3-1/Cables is associated with Trap and Pctaire2.";
RL Biochem. Biophys. Res. Commun. 286:1045-1050(2001).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-137; SER-165 AND SER-180, AND
RP IDENTIFICATION BY 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-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and
RC Spleen;
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 terminally differentiated neurons. Has a
CC Ser/Thr-phosphorylating activity for histone H1 (By similarity).
CC {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 -!- SUBUNIT: Found in a complex containing CABLES1, CDK16 and TDRD7.
CC Interacts with TDRD7. {ECO:0000269|PubMed:11527406}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8K0D0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8K0D0-2; Sequence=VSP_010640, VSP_010641;
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH31778.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC031778; AAH31778.1; ALT_INIT; mRNA.
DR EMBL; BC064815; AAH64815.1; -; mRNA.
DR CCDS; CCDS48670.1; -. [Q8K0D0-1]
DR RefSeq; NP_666351.2; NM_146239.2. [Q8K0D0-1]
DR RefSeq; XP_006513690.1; XM_006513627.2. [Q8K0D0-1]
DR RefSeq; XP_011241749.1; XM_011243447.2. [Q8K0D0-1]
DR AlphaFoldDB; Q8K0D0; -.
DR SMR; Q8K0D0; -.
DR BioGRID; 231880; 3.
DR IntAct; Q8K0D0; 1.
DR MINT; Q8K0D0; -.
DR STRING; 10090.ENSMUSP00000070355; -.
DR iPTMnet; Q8K0D0; -.
DR PhosphoSitePlus; Q8K0D0; -.
DR EPD; Q8K0D0; -.
DR jPOST; Q8K0D0; -.
DR MaxQB; Q8K0D0; -.
DR PaxDb; Q8K0D0; -.
DR PRIDE; Q8K0D0; -.
DR ProteomicsDB; 281295; -. [Q8K0D0-1]
DR ProteomicsDB; 281296; -. [Q8K0D0-2]
DR Antibodypedia; 17666; 156 antibodies from 28 providers.
DR DNASU; 237459; -.
DR Ensembl; ENSMUST00000069965; ENSMUSP00000070355; ENSMUSG00000020015. [Q8K0D0-1]
DR GeneID; 237459; -.
DR KEGG; mmu:237459; -.
DR UCSC; uc007gul.2; mouse. [Q8K0D0-1]
DR CTD; 5128; -.
DR MGI; MGI:97517; Cdk17.
DR VEuPathDB; HostDB:ENSMUSG00000020015; -.
DR eggNOG; KOG0594; Eukaryota.
DR GeneTree; ENSGT00940000155834; -.
DR HOGENOM; CLU_000288_154_3_1; -.
DR InParanoid; Q8K0D0; -.
DR OMA; FQINSPP; -.
DR PhylomeDB; Q8K0D0; -.
DR TreeFam; TF106508; -.
DR BioGRID-ORCS; 237459; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Cdk17; mouse.
DR PRO; PR:Q8K0D0; -.
DR Proteomes; UP000000589; Chromosome 10.
DR RNAct; Q8K0D0; protein.
DR Bgee; ENSMUSG00000020015; Expressed in olfactory tubercle and 222 other tissues.
DR ExpressionAtlas; Q8K0D0; baseline and differential.
DR Genevisible; Q8K0D0; 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 Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..523
FT /note="Cyclin-dependent kinase 17"
FT /id="PRO_0000086488"
FT DOMAIN 192..473
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 30..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 REGION 501..523
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:19144319"
FT MOD_RES 146
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q00537"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..84
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010640"
FT VAR_SEQ 512..523
FT /note="GHGKNRRQSMLF -> ALS (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010641"
SQ SEQUENCE 523 AA; 59506 MW; 847B045A3BCE4628 CRC64;
MKKFKRRLSL TLRGSQTIDE SLSELAEQMT IEESSSKDNE PIVKNGRPPT SHSVHSFLHQ
YTGSFKKPPL RRPHSVIGGS LGSFMAMPRN GSRLDIVHEN LKMGSDGESD QASGTSSDEV
QSPTGVCLRN RIHRRISMED LNKRLSLPAD IRIPDGYLEK LQISSPPFDQ PMSRRSRRAS
LSEIGFGKME TYIKLEKLGE GTYATVYKGR SKLTENLVAL KEIRLEHEEG APCTAIREVS
LLKDLKHANI VTLHDIVHTD KSLTLVFEYL DKDLKQYMDD CGNIMSMHNV KLFLYQILRG
LAYCHRRKVL HRDLKPQNLL INERGELKLA DFGLARAKSV PTKTYSNEVV TLWYRPPDVL
LGSSEYSTQI DMWGVGCIFF EMASGRPLFP GSTVEDELHL IFRLLGTPSQ ETWPGVSSND
EFKNYNFPKY KPQPLINHAP RLDSEGIELI TKFLQYESKK RVPAEEAMKH VYFRSLGPRI
HALPESVSIF SLKEIQLQKD PGFRNSSYPE TGHGKNRRQS MLF
