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CDK14_XENTR
ID   CDK14_XENTR             Reviewed;         423 AA.
AC   A4IIW7;
DT   02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 77.
DE   RecName: Full=Cyclin-dependent kinase 14;
DE            EC=2.7.11.22;
DE   AltName: Full=Cell division protein kinase 14;
GN   Name=cdk14; Synonyms=pftk1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serine/threonine-protein kinase involved in the control of
CC       the eukaryotic cell cycle, whose activity is controlled by an
CC       associated cyclin. Acts as a cell-cycle regulator of Wnt signaling
CC       pathway during G2/M phase by mediating the phosphorylation of lrp6,
CC       leading to the activation of the Wnt signaling pathway (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: Interacts with ccny; ccny mediates its recruitment to the
CC       plasma membrane and promotes phosphorylation of lrp6. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}. Note=Recruited to the cell membrane by CCNY.
CC       {ECO:0000250}.
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; BC136183; AAI36184.1; -; mRNA.
DR   RefSeq; NP_001096458.1; NM_001102988.1.
DR   AlphaFoldDB; A4IIW7; -.
DR   SMR; A4IIW7; -.
DR   PaxDb; A4IIW7; -.
DR   DNASU; 100125075; -.
DR   Ensembl; ENSXETT00000007502; ENSXETP00000007502; ENSXETG00000003466.
DR   GeneID; 100125075; -.
DR   KEGG; xtr:100125075; -.
DR   CTD; 5218; -.
DR   Xenbase; XB-GENE-943250; cdk14.
DR   eggNOG; KOG0594; Eukaryota.
DR   HOGENOM; CLU_000288_181_6_1; -.
DR   InParanoid; A4IIW7; -.
DR   OrthoDB; 1010560at2759; -.
DR   Proteomes; UP000008143; Chromosome 6.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000003466; Expressed in brain and 9 other tissues.
DR   ExpressionAtlas; A4IIW7; baseline.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR   GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; ISS:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR   GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; IBA:GO_Central.
DR   GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
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; Cell cycle; Cell division; Cell membrane; Kinase; Membrane;
KW   Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase; Wnt signaling pathway.
FT   CHAIN           1..423
FT                   /note="Cyclin-dependent kinase 14"
FT                   /id="PRO_0000391904"
FT   DOMAIN          89..373
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          62..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         95..103
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         118
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
SQ   SEQUENCE   423 AA;  47680 MW;  4D229A5E1558FDB5 CRC64;
     MSTRNCQGID SVIKPLDTIP EDKKVRVQRT QSSFDPFEKT SNQVKRVHSE NNACINFKSA
     SVGKESPKVR RHSSPSSPTS PKFGKADSYE KLEKLGEGSY ATVYKGKSKV NGKLVALKVI
     RLQEEEGTPF TAIREASLLK GLKHANIVLL HDIIHTKETL TLVFEYVHTD LCQYMDKHPG
     GLNPENVKLF LFQLLRGLSY IHQGHILHRD LKPQNLLISD TGELKLADFG LARAKSVPSH
     TYSNEVVTLW YRPPDVLLGS TDYSTCLDMW GVGCIFVEMI QGVAAFPGMK DIQDQLERIF
     LILGTPNEET WPGVHSLPHF KLERFTQYGP KNLRQAWNKL SYVNHAEDLA SKLLQCFPKN
     RLSAQAALNH DYFSDLPPRL WELSDMSSIF TVPNVKLQPE AGESMRVFGK NNSFSKSLSN
     SKH
 
 
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