CTK1_SCHPO
ID CTK1_SCHPO Reviewed; 593 AA.
AC O14098;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 153.
DE RecName: Full=CTD kinase subunit alpha;
DE Short=CTDK-I subunit alpha;
DE EC=2.7.11.23;
DE AltName: Full=CTD kinase subunit 1;
DE AltName: Full=Latrunculin sensitive kinase 1;
GN Name=lsk1 {ECO:0000312|EMBL:CAB16269.1};
GN Synonyms=ctk1 {ECO:0000250|UniProtKB:Q03957}; ORFNames=SPAC2F3.15;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1] {ECO:0000312|EMBL:CAB16269.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=15537703; DOI=10.1091/mbc.e04-06-0502;
RA Karagiannis J., Bimbo A., Rajagopalan S., Liu J., Balasubramanian M.K.;
RT "The nuclear kinase Lsk1p positively regulates the septation initiation
RT network and promotes the successful completion of cytokinesis in response
RT to perturbation of the actomyosin ring in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 16:358-371(2005).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP FUNCTION, INTERACTION WITH CTK2, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP LYS-306.
RX PubMed=17502918; DOI=10.1371/journal.pone.0000433;
RA Karagiannis J., Balasubramanian M.K.;
RT "A cyclin-dependent kinase that promotes cytokinesis through modulating
RT phosphorylation of the carboxy terminal domain of the RNA Pol II Rpb1p sub-
RT unit.";
RL PLoS ONE 2:E433-E433(2007).
RN [5] {ECO:0000305}
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-58; SER-104 AND
RP SER-109, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Catalytic subunit of the CTDK-I complex, which
CC hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of
CC the largest RNA polymerase II subunit. Involved in RNA polymerase II
CC transcriptional elongation and pre-mRNA 3'-end processing (By
CC similarity). Together with ctk2/lsc1, required for the regulation of
CC cytokinesis by phosphorylating 'Ser-2' residues found in the heptad
CC repeats of the CTD. Required for nuclear localization of ctk2/lsc1.
CC Positively regulates the septation initiation network (SIN) and
CC promotes successful completion of cytokinesis in response to
CC perturbation of the actomyosin ring. Acts in parallel to clp1 to
CC promote actomyosin ring stability upon cytokinesis checkpoint
CC activation. {ECO:0000250, ECO:0000269|PubMed:15537703,
CC ECO:0000269|PubMed:17502918}.
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 Evidence={ECO:0000250|UniProtKB:Q03957};
CC -!- SUBUNIT: CTDK-I consists of three subunits, ctk1/lsk1, ctk2/lsc1 and
CC ctk3 (also called alpha, beta and gamma) (By similarity). Interacts
CC with ctk2/lsc1. This interaction is dependent on kinase activity.
CC {ECO:0000250, ECO:0000269|PubMed:17502918}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:15537703,
CC ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17502918}.
CC Note=Localized to nucleus during all cell cycle phases.
CC {ECO:0000269|PubMed:15537703, ECO:0000269|PubMed:16823372}.
CC -!- DISRUPTION PHENOTYPE: Cells display severe cytokinesis defects. They
CC are able to form, but not maintain the integrity of the actomyosin ring
CC and are unable to successfully complete division septum formation upon
CC treatment with low doses (0.3 uM) of actin depolymerizing drug,
CC latrunculin A (LatA). However, deletion mutants are competent to delay
CC nuclear cycle progression after cytokinetic failure upon treatment with
CC LatA. In addition, deletion mutants suppress the lethal, multiseptate
CC phenotype conferred by hyperactivation of the SIN.
CC {ECO:0000269|PubMed:15537703}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. CDC2/CDKX subfamily. {ECO:0000255}.
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DR EMBL; CU329670; CAB16269.1; -; Genomic_DNA.
DR PIR; T38547; T38547.
DR RefSeq; NP_594393.1; NM_001019816.2.
DR AlphaFoldDB; O14098; -.
DR SMR; O14098; -.
DR BioGRID; 278168; 247.
DR STRING; 4896.SPAC2F3.15.1; -.
DR iPTMnet; O14098; -.
DR SwissPalm; O14098; -.
DR MaxQB; O14098; -.
DR PaxDb; O14098; -.
DR PRIDE; O14098; -.
DR EnsemblFungi; SPAC2F3.15.1; SPAC2F3.15.1:pep; SPAC2F3.15.
DR GeneID; 2541672; -.
DR KEGG; spo:SPAC2F3.15; -.
DR PomBase; SPAC2F3.15; lsk1.
DR VEuPathDB; FungiDB:SPAC2F3.15; -.
DR eggNOG; KOG0600; Eukaryota.
DR HOGENOM; CLU_000288_181_17_1; -.
DR InParanoid; O14098; -.
DR OMA; HIPNERR; -.
DR PhylomeDB; O14098; -.
DR BRENDA; 2.7.11.23; 5613.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-9018519; Estrogen-dependent gene expression.
DR PRO; PR:O14098; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0070692; C:CTDK-1 complex; IPI:PomBase.
DR GO; GO:0000307; C:cyclin-dependent protein kinase holoenzyme complex; IBA:GO_Central.
DR GO; GO:0008024; C:cyclin/CDK positive transcription elongation factor complex; IBA:GO_Central.
DR GO; GO:0019908; C:nuclear cyclin-dependent protein kinase holoenzyme complex; IPI:PomBase.
DR GO; GO:0005730; C:nucleolus; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0030332; F:cyclin binding; IBA:GO_Central.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IMP:PomBase.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:PomBase.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:PomBase.
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:0023052; P:signaling; NAS:PomBase.
DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central.
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; Kinase; mRNA processing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transcription; Transferase.
FT CHAIN 1..593
FT /note="CTD kinase subunit alpha"
FT /id="PRO_0000338603"
FT DOMAIN 277..561
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..29
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..103
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P24941,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 283..291
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24941,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 306
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P24941,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 58
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 104
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MUTAGEN 306
FT /note="K->R: No kinase activity. No interaction with
FT ctk2/lsc1. Mislocalization of ctk2/lsc1."
FT /evidence="ECO:0000269|PubMed:17502918"
SQ SEQUENCE 593 AA; 67366 MW; E37DD7AA762F0713 CRC64;
MSYSKSTIYR RQGTEPNSHF RRTVEEKSQL SGTNEESLGG HTLSSNAFKN NSSSISPSSS
AKDPREQRKR TFPLNDTHSS RARQHERPFR SRKSRRRKGK KAFSPRPGSP PSPSFYRSGS
QKRARNLTTK DYFAKRSESS SSASVSPISP SANRNDSKRQ ASSFRRSPPS SVHMKPSAFN
GRKVSRRPSS SPPPIPSIPH ETTSSDTQKK SSVSSGFPEN KHGKFHFHIP NERRSRFDQP
PSKRMALTST ARESVPAPLP SPPSGPIYTY TYPKPAYEKI DQIGEGTYGK VYKAINTVTG
DLVALKRIRL EQEKDGFPIT TVREVKILQR LRHKNIVRLL EIMVEKSSVY MVFEYMDHDL
TGVLLNSQLH FTPGNIKHLS KQIFEALAYL HHRGVLHRDI KGSNILLNNN GDLKFADFGL
ARFNTSSKSA NYTNRVITLW FRPPELLLGE TAYDTAVDIW SAGCIVMELF TGKPFFQGRD
EISQLEVIYD MMGTPDVHSW PEVKNLPWYE LLKPVEEKKS RFVETFKEIL SPAAIDLCQK
LLALNPFCRP SAHETLMHEY FTSESPPPEP AVILKNMQGS WHEWESKKRK SKR
