CDK14_PLEMO
ID CDK14_PLEMO Reviewed; 451 AA.
AC B0VXL7;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 Plecturocebus moloch (Dusky titi monkey) (Callicebus moloch).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini;
OC Pitheciidae; Callicebinae; Plecturocebus.
OX NCBI_TaxID=9523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Antonellis A., Ayele K., Benjamin B., Blakesley R.W., Boakye A.,
RA Bouffard G.G., Brinkley C., Brooks S., Chu G., Coleman H., Engle J.,
RA Gestole M., Greene A., Guan X., Gupta J., Haghighi P., Han J., Hansen N.,
RA Ho S.-L., Hu P., Hunter G., Hurle B., Idol J.R., Kwong P., Laric P.,
RA Larson S., Lee-Lin S.-Q., Legaspi R., Madden M., Maduro Q.L., Maduro V.B.,
RA Margulies E.H., Masiello C., Maskeri B., McDowell J., Mojidi H.A.,
RA Mullikin J.C., Oestreicher J.S., Park M., Portnoy M.E., Prasad A., Puri O.,
RA Reddix-Dugue N., Schandler K., Schueler M.G., Sison C., Stantripop S.,
RA Stephen E., Taye A., Thomas J.W., Thomas P.J., Tsipouri V., Ung L.,
RA Vogt J.L., Wetherby K.D., Young A., Green E.D.;
RT "NISC comparative sequencing initiative.";
RL Submitted (NOV-2005) 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 at
CC 'Ser-1490', leading to the activation of the Wnt signaling pathway.
CC Acts as a regulator of cell cycle progression and cell proliferation
CC via its interaction with CCDN3. Phosphorylates RB1 in vitro, however
CC the relevance of such result remains to be confirmed in vivo. May also
CC play a role in meiosis, neuron differentiation and may indirectly act
CC as a negative regulator of insulin-responsive glucose transport (By
CC similarity). {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 -!- ACTIVITY REGULATION: Serine/threonine-protein kinase activity is
CC promoted by associated cyclins CCDN3 and CCNY and repressed by CDKN1A.
CC {ECO:0000250}.
CC -!- SUBUNIT: Found in a complex with LRP6, CCNY and CAPRIN2 during G2/M
CC stage; CAPRIN2 functions as a scaffold for the complex by binding to
CC CCNY via its N terminus and to CDK14 via its C terminus. Interacts with
CC CCNY; CCNY mediates its recruitment to the plasma membrane and promotes
CC phosphorylation of LRP6. Interacts with CCDN3 and CDKN1A. Interacts
CC with SEPT8. Interacts with 14-3-3 proteina YWHAB, YWHAE, YWHAH and
CC YWHAQ. {ECO:0000250|UniProtKB:O94921}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC Note=Recruited to the cell membrane by CCNY. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DP000601; ACA35057.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VXL7; -.
DR SMR; B0VXL7; -.
DR GO; GO:0000308; C:cytoplasmic cyclin-dependent protein kinase holoenzyme complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IEA:InterPro.
DR GO; GO:0060828; P:regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Cytoplasm; Kinase;
KW Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Serine/threonine-protein kinase; Transferase; Wnt signaling pathway.
FT CHAIN 1..451
FT /note="Cyclin-dependent kinase 14"
FT /id="PRO_0000391898"
FT DOMAIN 117..401
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 84..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 123..131
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 146
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94921"
FT MOD_RES 77
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94921"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94921"
SQ SEQUENCE 451 AA; 50690 MW; B436467A7E830EA9 CRC64;
MHGYFGCNAA AEPGYSAFLG TPQICVTKMS TRNCQGMDSV IKPLDTIPED KKVRVQRTQS
TFDPFEKPAN QVKRVHSENN ACINFKTSST GKESPKVRRH SSPSSPTSPK FGKADSYEKL
EKLGEGSYAT VYKGKSKVNG KLVALKVIRL QEEEGTPFTA IREASLLKGL KHANIVLLHD
IIHTKETLTL VFEYVHTDLC QYMDKHPGGL HPDNVKLFLF QLLRGLSYIH QRYILHRDLK
PQNLLISDTG ELKLADFGLA RAKSVPSHTY SNEVVTLWYR PPDVLLGSTE YSTCLDMWGV
GCIFVEMIQG VAAFPGMKDI QDQLERIFLV LGTPNEDTWP GVHSLPHFKP ERFTLYSSKN
LRQAWNKLSY VNHAEDLASK LLQCSPKNRL SAQAALSHEY FSDLPPRLWE LTDMSSIFTI
PNVRLQPEAG ESMRAFGKNN SYGKSLSNSK H
