CDKC2_ARATH
ID CDKC2_ARATH Reviewed; 513 AA.
AC Q8W4P1; Q9LV82;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Cyclin-dependent kinase C-2;
DE Short=CDKC;2;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
GN Name=CDKC-2; OrderedLocusNames=At5g64960; ORFNames=MXK3.19;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10718197; DOI=10.1093/dnares/7.1.31;
RA Sato S., Nakamura Y., Kaneko T., Katoh T., Asamizu E., Kotani H.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. X. Sequence
RT features of the regions of 3,076,755 bp covered by sixty P1 and TAC
RT clones.";
RL DNA Res. 7:31-63(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11971144; DOI=10.1105/tpc.010445;
RA Vandepoele K., Raes J., de Veylder L., Rouze P., Rombauts S., Inze D.;
RT "Genome-wide analysis of core cell cycle genes in Arabidopsis.";
RL Plant Cell 14:903-916(2002).
RN [5]
RP TISSUE SPECIFICITY, AND INTERACTION WITH CYCT1-3.
RX PubMed=12678503; DOI=10.1007/s000180300033;
RA Barroco R.M., de Veylder L., Magyar Z., Engler G., Inze D., Mironov V.;
RT "Novel complexes of cyclin-dependent kinases and a cyclin-like protein from
RT Arabidopsis thaliana with a function unrelated to cell division.";
RL Cell. Mol. Life Sci. 60:401-412(2003).
RN [6]
RP REVIEW.
RX PubMed=17094738; DOI=10.1146/annurev.genet.40.110405.090431;
RA Inze D., de Veylder L.;
RT "Cell cycle regulation in plant development.";
RL Annu. Rev. Genet. 40:77-105(2006).
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 -!- CATALYTIC ACTIVITY:
CC Reaction=[DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-
CC [DNA-directed RNA polymerase]; Xref=Rhea:RHEA:10216, Rhea:RHEA-
CC COMP:11321, Rhea:RHEA-COMP:11322, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546,
CC ChEBI:CHEBI:456216; EC=2.7.11.23;
CC -!- SUBUNIT: Interacts with CYCT1-3. {ECO:0000269|PubMed:12678503}.
CC -!- INTERACTION:
CC Q8W4P1; Q8LBC0: CYCT1-3; NbExp=2; IntAct=EBI-2025894, EBI-2025764;
CC Q8W4P1; Q84MB2: TIFY8; NbExp=3; IntAct=EBI-2025894, EBI-4426557;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8W4P1-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Highly expressed in flowers. Expressed in
CC seedlings, roots, rosettes and stems. {ECO:0000269|PubMed:12678503}.
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; AB019236; BAA97308.1; -; Genomic_DNA.
DR EMBL; CP002688; AED97975.1; -; Genomic_DNA.
DR EMBL; AF360134; AAK25844.1; -; mRNA.
DR EMBL; AY039990; AAK64067.1; -; mRNA.
DR EMBL; AY062449; AAL32527.1; -; mRNA.
DR EMBL; BT002565; AAO00925.1; -; mRNA.
DR RefSeq; NP_201301.1; NM_125895.5. [Q8W4P1-1]
DR AlphaFoldDB; Q8W4P1; -.
DR SMR; Q8W4P1; -.
DR BioGRID; 21862; 21.
DR IntAct; Q8W4P1; 13.
DR STRING; 3702.AT5G64960.1; -.
DR iPTMnet; Q8W4P1; -.
DR PaxDb; Q8W4P1; -.
DR PRIDE; Q8W4P1; -.
DR ProteomicsDB; 223975; -. [Q8W4P1-1]
DR EnsemblPlants; AT5G64960.1; AT5G64960.1; AT5G64960. [Q8W4P1-1]
DR GeneID; 836620; -.
DR Gramene; AT5G64960.1; AT5G64960.1; AT5G64960. [Q8W4P1-1]
DR KEGG; ath:AT5G64960; -.
DR Araport; AT5G64960; -.
DR TAIR; locus:2177744; AT5G64960.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q8W4P1; -.
DR OMA; MDALKHP; -.
DR OrthoDB; 925637at2759; -.
DR PhylomeDB; Q8W4P1; -.
DR BRENDA; 2.7.11.22; 399.
DR PRO; PR:Q8W4P1; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8W4P1; baseline and differential.
DR Genevisible; Q8W4P1; AT.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0016604; C:nuclear body; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0048440; P:carpel development; IGI:TAIR.
DR GO; GO:0009908; P:flower development; IMP:TAIR.
DR GO; GO:0006397; P:mRNA processing; IMP:TAIR.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0050792; P:regulation of viral process; IMP:TAIR.
DR GO; GO:0009615; P:response to virus; IEP:TAIR.
DR GO; GO:0009414; P:response to water deprivation; IMP:TAIR.
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..513
FT /note="Cyclin-dependent kinase C-2"
FT /id="PRO_0000293118"
FT DOMAIN 26..325
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 337..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..367
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..451
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 32..40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 37
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P24100"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9C9M7"
FT CONFLICT 26
FT /note="F -> Y (in Ref. 3; AAL32527/AAO00925)"
FT /evidence="ECO:0000305"
FT CONFLICT 188
FT /note="S -> P (in Ref. 3; AAL32527/AAO00925)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 513 AA; 57129 MW; F348F40377CA3756 CRC64;
MAAAAFGQLN LEEPPPIWGS RSVDCFEKLE QIGEGTYGQV YMAKEIKTGE IVALKKIRMD
NEREGFPITA IREIKILKKL HHENVIHLKE IVTSPGRDRD DQGKPDNNKY KGGIYMVFEY
MDHDLTGLAD RPGLRFTVPQ IKCYMKQLLT GLHYCHVNQV LHRDIKGSNL LIDNEGNLKL
ADFGLARSYS HDHTGNLTNR VITLWYRPPE LLLGATKYGP AIDMWSVGCI FAELLNGKPI
LPGKTENEQL NKIYELCGSP DESNWPGVSK MPWYNQMKSS RPLKRRVREI YRHFDRHALE
LLEKMLVLDP SQRICAKDAL DAEYFWTDPL PCDPKSLPTY ESSHEFQTKK KRQQMRHNEE
AAKKQKLQHP QQQHSRLPPQ QHGVGQSHAA PLWPAGPNHP MNNNAPPPQI PAGGHYYGGK
PRGGAPVPNR YPPSGNQTGG YNNQSRGGYS SGAYPPQGRG APYGAGPRGP SGGYGVGPPN
YSQGGGQYGG SGGSGRGQNP MGGARNQQYG WQP
