CDK14_DASNO
ID CDK14_DASNO Reviewed; 468 AA.
AC C0RW22;
DT 02-MAR-2010, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 49.
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 Dasypus novemcinctus (Nine-banded armadillo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Xenarthra; Cingulata; Dasypodidae; Dasypus.
OX NCBI_TaxID=9361;
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 (SEP-2006) 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}.
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DR EMBL; DP001073; ACN22218.1; -; Genomic_DNA.
DR AlphaFoldDB; C0RW22; -.
DR SMR; C0RW22; -.
DR HOGENOM; CLU_000288_181_6_1; -.
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..468
FT /note="Cyclin-dependent kinase 14"
FT /id="PRO_0000391900"
FT DOMAIN 134..418
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 103..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 448..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 255
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 140..148
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 163
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 24
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 94
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94921"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O94921"
SQ SEQUENCE 468 AA; 52957 MW; E318D639D3E9F80C CRC64;
MCDLIEPQPA EKIGKMKKLR RTLSESFSRI ALKKEDTTFD EICVTKMSTR NCQGMDSVIK
PLDTIPEDKV RVQRTQSTFD PFEKPTNQVK RVHSENNACI NFKTSSAGKE SPKVRRHSSP
SSPTSPKFGK ADSYEKLEKL GEGSYATVYK GKSKVNGKLV ALKVIRLQEE EGTPFTAIRE
ASLLKGLKHA NIVLLHDIIH TKETLTLVFE YVHTDLCQYM DKHPGGLHPE NVKLFLFQLL
RGLSYIHQRY ILHRDLKPQN LLISDTGELK LADFGLARAK SVPSHTYSNE VVTLWYRPPD
VLLGSTEYST CLDMWGVGCI FVEMIQGVAA FPGMKDIQDQ LERIFLVLGT PNEDTWPGVH
SLPHFKPERF TLYSSKNLRQ AWNKLSYVNH AEDLASKLLQ CSPKNRLSAQ AALSHEYFSD
LPPRLWELTD MSSIFTVPNV RLQPEAGESM RAFGKNNSYG KSLSNSKH
