CDKD2_ARATH
ID CDKD2_ARATH Reviewed; 348 AA.
AC Q9C9M7;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Cyclin-dependent kinase D-2;
DE Short=CDKD;2;
DE EC=2.7.11.22;
DE EC=2.7.11.23;
DE AltName: Full=CDK-activating kinase 4-At;
DE Short=CAK4-At;
GN Name=CDKD-2; OrderedLocusNames=At1g66750; ORFNames=F4N21.12;
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 [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12527363; DOI=10.1016/s0014-5793(02)03780-8;
RA Shimotohno A., Matsubayashi S., Yamaguchi M., Uchimiya H., Umeda M.;
RT "Differential phosphorylation activities of CDK-activating kinases in
RT Arabidopsis thaliana.";
RL FEBS Lett. 534:69-74(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
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 [5]
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 [6]
RP FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, INTERACTION WITH
RP CYCH1-1, PHOSPHORYLATION AT SER-162 AND THR-168, AND MUTAGENESIS OF LYS-42;
RP SER-162 AND THR-168.
RX PubMed=15486101; DOI=10.1105/tpc.104.025601;
RA Shimotohno A., Umeda-Hara C., Bisova K., Uchimiya H., Umeda M.;
RT "The plant-specific kinase CDKF;1 is involved in activating phosphorylation
RT of cyclin-dependent kinase-activating kinases in Arabidopsis.";
RL Plant Cell 16:2954-2966(2004).
RN [7]
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).
RN [8]
RP FUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT TYR-24, INTERACTION WITH
RP CYCH1-1, AND MUTAGENESIS OF TYR-24.
RX PubMed=16856985; DOI=10.1111/j.1365-313x.2006.02820.x;
RA Shimotohno A., Ohno R., Bisova K., Sakaguchi N., Huang J., Koncz C.,
RA Uchimiya H., Umeda M.;
RT "Diverse phosphoregulatory mechanisms controlling cyclin-dependent kinase-
RT activating kinases in Arabidopsis.";
RL Plant J. 47:701-710(2006).
CC -!- FUNCTION: Forms a stable complex with cyclin CYCH1-1 that
CC phosphorylates human CDK2 and the C-terminal domain (CTD) of the large
CC subunit of RNA polymerase II. {ECO:0000269|PubMed:15486101,
CC ECO:0000269|PubMed:16856985}.
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 -!- ACTIVITY REGULATION: Activated by phosphorylation by CDKF-1. Down-
CC regulated by phosphorylation by WEE1. {ECO:0000269|PubMed:15486101,
CC ECO:0000269|PubMed:16856985}.
CC -!- SUBUNIT: Interacts with CYCH1-1. Binding to CYCH1-1 activates CDK
CC kinase. {ECO:0000269|PubMed:15486101, ECO:0000269|PubMed:16856985}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15486101}. Nucleus
CC {ECO:0000269|PubMed:15486101}.
CC -!- TISSUE SPECIFICITY: Expressed in suspension cell culture, but not in
CC plant organs. {ECO:0000269|PubMed:12527363}.
CC -!- PTM: Phosphorylated by CDKF-1 at Ser-162 and Thr-168. Phosphorylated by
CC WEE1 at Tyr-24. Autophosphorylated. {ECO:0000269|PubMed:15486101,
CC ECO:0000269|PubMed:16856985}.
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; AB074116; BAB91558.1; -; mRNA.
DR EMBL; AC013288; AAG60076.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE34551.1; -; Genomic_DNA.
DR EMBL; AY136355; AAM97021.1; -; mRNA.
DR EMBL; BT000198; AAN15517.1; -; mRNA.
DR RefSeq; NP_176847.1; NM_105345.5.
DR AlphaFoldDB; Q9C9M7; -.
DR SMR; Q9C9M7; -.
DR BioGRID; 28214; 43.
DR IntAct; Q9C9M7; 21.
DR STRING; 3702.AT1G66750.1; -.
DR iPTMnet; Q9C9M7; -.
DR PaxDb; Q9C9M7; -.
DR PRIDE; Q9C9M7; -.
DR ProteomicsDB; 224393; -.
DR EnsemblPlants; AT1G66750.1; AT1G66750.1; AT1G66750.
DR GeneID; 842993; -.
DR Gramene; AT1G66750.1; AT1G66750.1; AT1G66750.
DR KEGG; ath:AT1G66750; -.
DR Araport; AT1G66750; -.
DR TAIR; locus:2033349; AT1G66750.
DR eggNOG; KOG0659; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q9C9M7; -.
DR OMA; LAKMFIY; -.
DR OrthoDB; 1367115at2759; -.
DR PhylomeDB; Q9C9M7; -.
DR PRO; PR:Q9C9M7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9C9M7; baseline and differential.
DR Genevisible; Q9C9M7; AT.
DR GO; GO:0005737; C:cytoplasm; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IPI:TAIR.
DR GO; GO:0070985; C:transcription factor TFIIK complex; 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; IBA:GO_Central.
DR GO; GO:0004672; F:protein kinase activity; IDA:TAIR.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; TAS:TAIR.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0048578; P:positive regulation of long-day photoperiodism, flowering; IMP:TAIR.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0000079; P:regulation of cyclin-dependent protein serine/threonine kinase activity; TAS:TAIR.
DR CDD; cd07841; STKc_CDK7; 1.
DR InterPro; IPR037770; CDK7.
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 ATP-binding; Cell cycle; Cell division; Cytoplasm; Kinase;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..348
FT /note="Cyclin-dependent kinase D-2"
FT /id="PRO_0000293120"
FT DOMAIN 13..293
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 293..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 135
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 19..27
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 42
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
FT MOD_RES 24
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:16856985"
FT MOD_RES 162
FT /note="Phosphoserine; by CAK"
FT /evidence="ECO:0000269|PubMed:15486101"
FT MOD_RES 168
FT /note="Phosphothreonine; by CAK"
FT /evidence="ECO:0000269|PubMed:15486101"
FT MUTAGEN 24
FT /note="Y->F: Abolishes phosphorylation by WEE1."
FT /evidence="ECO:0000269|PubMed:16856985"
FT MUTAGEN 42
FT /note="K->R: Prevents autophosphorylation."
FT /evidence="ECO:0000269|PubMed:15486101"
FT MUTAGEN 162
FT /note="S->A: Reduces phosphorylation by CDKF-1 by 30%."
FT /evidence="ECO:0000269|PubMed:15486101"
FT MUTAGEN 168
FT /note="T->A: Almost abolishes phosphorylation by CDKF-1.
FT Loss of CTD-kinase activity."
FT /evidence="ECO:0000269|PubMed:15486101"
SQ SEQUENCE 348 AA; 39201 MW; A32CA3E98204DDAD CRC64;
MSKSGDNQPV DRYLRRQILG EGTYGVVYKA TDTKTGKTVA VKKIRLGNQK EGVNFTALRE
IKLLKELNHP HIVELIDAFP HDGSLHLVFE YMQTDLEAVI RDRNIFLSPG DIKSYMLMTL
KGLAYCHKKW VLHRDMKPNN LLIGENGLLK LADFGLARLF GSPNRRFTHQ VFATWYRAPE
LLFGSRQYGA GVDVWAAGCI FAELLLRRPF LPGSTEIDQL GKIFQAFGTP VPSQWSDMIY
LPDYMEFSYT PAPPLRTIFP MASDDALDLL AKMFIYDPRQ RITIQQALDH RYFSSSPSPT
EPGKLQIPAS KGDALEPKAS EQNQHGNSPA VLSPPGKMRR VMGPEGFT
