CTK2_YEAST
ID CTK2_YEAST Reviewed; 323 AA.
AC P46962; D6VWG9;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=CTD kinase subunit beta;
DE Short=CTDK-I subunit beta;
DE AltName: Full=CTD kinase 38 kDa subunit;
DE AltName: Full=CTD kinase subunit 2;
GN Name=CTK2; OrderedLocusNames=YJL006C; ORFNames=J1390;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 217-225, CTD KINASE
RP ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=7565723; DOI=10.1128/mcb.15.10.5716;
RA Sterner D.E., Lee J.M., Hardin S.E., Greenleaf A.L.;
RT "The yeast carboxyl-terminal repeat domain kinase CTDK-I is a divergent
RT cyclin-cyclin-dependent kinase complex.";
RL Mol. Cell. Biol. 15:5716-5724(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=8641269; DOI=10.1002/j.1460-2075.1996.tb00557.x;
RA Galibert F., Alexandraki D., Baur A., Boles E., Chalwatzis N., Chuat J.-C.,
RA Coster F., Cziepluch C., de Haan M., Domdey H., Durand P., Entian K.-D.,
RA Gatius M., Goffeau A., Grivell L.A., Hennemann A., Herbert C.J.,
RA Heumann K., Hilger F., Hollenberg C.P., Huang M.-E., Jacq C.,
RA Jauniaux J.-C., Katsoulou C., Kirchrath L., Kleine K., Kordes E.,
RA Koetter P., Liebl S., Louis E.J., Manus V., Mewes H.-W., Miosga T.,
RA Obermaier B., Perea J., Pohl T.M., Portetelle D., Pujol A., Purnelle B.,
RA Ramezani Rad M., Rasmussen S.W., Rose M., Rossau R.,
RA Schaaff-Gerstenschlaeger I., Smits P.H.M., Scarcez T., Soriano N.,
RA To Van D., Tzermia M., Van Broekhoven A., Vandenbol M., Wedler H.,
RA von Wettstein D., Wambutt R., Zagulski M., Zollner A., Karpfinger-Hartl L.;
RT "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.";
RL EMBO J. 15:2031-2049(1996).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP FUNCTION IN RNA POLYMERASE II TRANSCRIPTION.
RX PubMed=9110987; DOI=10.1074/jbc.272.17.10990;
RA Lee J.M., Greenleaf A.L.;
RT "Modulation of RNA polymerase II elongation efficiency by C-terminal
RT heptapeptide repeat domain kinase I.";
RL J. Biol. Chem. 272:10990-10993(1997).
RN [5]
RP PHOSPHORYLATION, AND UBIQUITINATION.
RX PubMed=10082518; DOI=10.1128/mcb.19.4.2527;
RA Hautbergue G., Goguel V.;
RT "The yeast C-type cyclin Ctk2p is phosphorylated and rapidly degraded by
RT the ubiquitin-proteasome pathway.";
RL Mol. Cell. Biol. 19:2527-2534(1999).
RN [6]
RP CTK1 ACTIVATION, AND INTERACTION WITH CTK1 AND CTK3.
RX PubMed=11118453; DOI=10.1074/jbc.m010162200;
RA Hautbergue G., Goguel V.;
RT "Activation of the cyclin-dependent kinase CTDK-I requires the
RT heterodimerization of two unstable subunits.";
RL J. Biol. Chem. 276:8005-8013(2001).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=12684377; DOI=10.1128/ec.2.2.274-283.2003;
RA Ostapenko D., Solomon M.J.;
RT "Budding yeast CTDK-I is required for DNA damage-induced transcription.";
RL Eukaryot. Cell 2:274-283(2003).
RN [8]
RP FUNCTION IN H3 METHYLATION.
RX PubMed=12629047; DOI=10.1101/gad.1055503;
RA Xiao T., Hall H., Kizer K.O., Shibata Y., Hall M.C., Borchers C.H.,
RA Strahl B.D.;
RT "Phosphorylation of RNA polymerase II CTD regulates H3 methylation in
RT yeast.";
RL Genes Dev. 17:654-663(2003).
RN [9]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [10]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [11]
RP FUNCTION OF THE CTDK-I COMPLEX.
RX PubMed=15047695; DOI=10.1074/jbc.m402218200;
RA Jones J.C., Phatnani H.P., Haystead T.A., MacDonald J.A., Alam S.M.,
RA Greenleaf A.L.;
RT "C-terminal repeat domain kinase I phosphorylates Ser2 and Ser5 of RNA
RT polymerase II C-terminal domain repeats.";
RL J. Biol. Chem. 279:24957-24964(2004).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=15520468; DOI=10.1093/nar/gkh927;
RA Bouchoux C., Hautbergue G., Grenetier S., Carles C., Riva M., Goguel V.;
RT "CTD kinase I is involved in RNA polymerase I transcription.";
RL Nucleic Acids Res. 32:5851-5860(2004).
RN [13]
RP FUNCTION IN ADAPTATION TO ALTERNATIVE CARBON SOURCES.
RX PubMed=16182287; DOI=10.1016/j.febslet.2005.08.057;
RA Van Driessche B., Coddens S., Van Mullem V., Vandenhaute J.;
RT "Glucose deprivation mediates interaction between CTDK-I and Snf1 in
RT Saccharomyces cerevisiae.";
RL FEBS Lett. 579:5318-5324(2005).
RN [14]
RP FUNCTION IN THE INTEGRITY OF RDNA.
RX PubMed=16984969; DOI=10.1093/nar/gkl493;
RA Grenetier S., Bouchoux C., Goguel V.;
RT "CTD kinase I is required for the integrity of the rDNA tandem array.";
RL Nucleic Acids Res. 34:4996-5006(2006).
CC -!- FUNCTION: Cyclin subunit of the CTDK-I complex, which
CC hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of
CC the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if
CC the CTD substrate is not phosphorylated at 'Ser-5', but will
CC phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already
CC phosphorylated. CTDK-I is also more reactive toward substrates that are
CC prephosphorylated at 'Ser-2' or 'Ser-5' compared with an
CC unphosphorylated CTD substrate, therefore efficiently creating doubly
CC phosphorylated CTD repeats. Involved in RNA polymerase II
CC transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA
CC 3'-end processing and SET2 mediated H3K36 methylation. Together with
CC CTK3, required for CTK1 CTD kinase activation. Required for DNA damage
CC induced transcription. Involved in the adaptation to alternative carbon
CC sources, including galactose, glycerol and ethanol, but not raffinose.
CC Required for the integrity of the rDNA locus.
CC {ECO:0000269|PubMed:12629047, ECO:0000269|PubMed:12684377,
CC ECO:0000269|PubMed:15047695, ECO:0000269|PubMed:16182287,
CC ECO:0000269|PubMed:16984969, ECO:0000269|PubMed:9110987}.
CC -!- SUBUNIT: CTDK-I consists of three subunits, CTK1, CTK2 and CTK3 (also
CC called alpha, beta and gamma). Interacts with CTK1. Heterodimerization
CC with CTK3 is required to protect this subunit from degradation.
CC {ECO:0000269|PubMed:11118453, ECO:0000269|PubMed:7565723}.
CC -!- INTERACTION:
CC P46962; Q03957: CTK1; NbExp=9; IntAct=EBI-5236, EBI-5230;
CC P46962; P46963: CTK3; NbExp=10; IntAct=EBI-5236, EBI-5241;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:15520468}.
CC -!- PTM: Phosphorylated. Ubiquitinated. Phosphorylation and ubiquitination
CC lead to degradation in growth-related way by the ubiquitin-proteasome
CC pathway. Neither phosphorylation nor degradation requires association
CC with CTK1. {ECO:0000269|PubMed:10082518}.
CC -!- DISRUPTION PHENOTYPE: Null mutants are viable, but grow more slowly
CC than wild-type cells at 30 degrees Celsius. They are cold-sensitive,
CC failing to grow at 12 degrees Celsius. They display flocculent growth
CC in liquid media and they show abnormal cell morphologies, for example,
CC a significant fraction of the cells are greatly enlarged. Deletion
CC mutant is sensitive to the DNA synthesis inhibitor hydroxyurea (HU) and
CC UV irradiation. {ECO:0000269|PubMed:12684377,
CC ECO:0000269|PubMed:7565723}.
CC -!- MISCELLANEOUS: Present with 1590 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the cyclin family. {ECO:0000305}.
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DR EMBL; U30295; AAC49077.1; -; Genomic_DNA.
DR EMBL; Z49281; CAA89296.1; -; Genomic_DNA.
DR EMBL; BK006943; DAA08785.1; -; Genomic_DNA.
DR PIR; S56777; S56777.
DR RefSeq; NP_012528.1; NM_001181440.1.
DR PDB; 7JV7; X-ray; 1.85 A; B=1-323.
DR PDBsum; 7JV7; -.
DR AlphaFoldDB; P46962; -.
DR SMR; P46962; -.
DR BioGRID; 33750; 231.
DR ComplexPortal; CPX-1710; Carboxy-terminal domain protein kinase complex.
DR DIP; DIP-2105N; -.
DR IntAct; P46962; 6.
DR MINT; P46962; -.
DR STRING; 4932.YJL006C; -.
DR iPTMnet; P46962; -.
DR MaxQB; P46962; -.
DR PaxDb; P46962; -.
DR PRIDE; P46962; -.
DR EnsemblFungi; YJL006C_mRNA; YJL006C; YJL006C.
DR GeneID; 853450; -.
DR KEGG; sce:YJL006C; -.
DR SGD; S000003543; CTK2.
DR VEuPathDB; FungiDB:YJL006C; -.
DR eggNOG; KOG0834; Eukaryota.
DR HOGENOM; CLU_842225_0_0_1; -.
DR InParanoid; P46962; -.
DR OMA; LMIPPHC; -.
DR BioCyc; YEAST:G3O-31484-MON; -.
DR Reactome; R-SCE-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SCE-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SCE-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SCE-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SCE-9018519; Estrogen-dependent gene expression.
DR PRO; PR:P46962; -.
DR Proteomes; UP000002311; Chromosome X.
DR RNAct; P46962; protein.
DR GO; GO:0032806; C:carboxy-terminal domain protein kinase complex; IPI:ComplexPortal.
DR GO; GO:0070692; C:CTDK-1 complex; IDA:SGD.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005654; C:nucleoplasm; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0061575; F:cyclin-dependent protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0016538; F:cyclin-dependent protein serine/threonine kinase regulator activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEA:UniProtKB-KW.
DR GO; GO:0031124; P:mRNA 3'-end processing; IDA:ComplexPortal.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:ComplexPortal.
DR GO; GO:0032786; P:positive regulation of DNA-templated transcription, elongation; IDA:SGD.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IDA:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045903; P:positive regulation of translational fidelity; IPI:SGD.
DR GO; GO:0006468; P:protein phosphorylation; IPI:SGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd00043; CYCLIN; 1.
DR InterPro; IPR013763; Cyclin-like.
DR InterPro; IPR036915; Cyclin-like_sf.
DR InterPro; IPR043198; Cyclin/Ssn8.
DR InterPro; IPR006671; Cyclin_N.
DR PANTHER; PTHR10026; PTHR10026; 1.
DR Pfam; PF00134; Cyclin_N; 1.
DR SMART; SM00385; CYCLIN; 1.
DR SUPFAM; SSF47954; SSF47954; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Cyclin; Direct protein sequencing; DNA damage;
KW mRNA processing; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Ubl conjugation.
FT CHAIN 1..323
FT /note="CTD kinase subunit beta"
FT /id="PRO_0000080507"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 18..25
FT /evidence="ECO:0007829|PDB:7JV7"
FT TURN 26..28
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 32..53
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 57..73
FT /evidence="ECO:0007829|PDB:7JV7"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 102..113
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 120..140
FT /evidence="ECO:0007829|PDB:7JV7"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 192..206
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 214..220
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 224..240
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 242..244
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:7JV7"
FT STRAND 299..305
FT /evidence="ECO:0007829|PDB:7JV7"
FT HELIX 307..313
FT /evidence="ECO:0007829|PDB:7JV7"
SQ SEQUENCE 323 AA; 37905 MW; 7C18FA672778D8FD CRC64;
MPSTFESQLF FSRPFLSKRQ IQRAQKNTIS DYRNYNQKKL AVFKFLSDLC VQLKFPRKTL
ETAVYFYQRY HLFNRFETEV CYTVATSCLT LGCKEVETIK KTNDICTLSL RLRNVVKINT
DILENFKKRV FQIELRILES CSFDYRVNNY VHIDEYVIKI GRELSFDYKL CNLAWVIAYD
ALKLETILVI PQHSIALAIL KIAYELLDNK NWSSKRYSLF ETDEKSVNEA YFDIVNFYIN
SFDMCDLQRH LPADLLPIGV ERFMELKKNA GPESGLPQIP DHLLNADPYI TITRDNNVQE
RRYVLSLELI NGESSINSST RHA
