CRK1_SCHPO
ID CRK1_SCHPO Reviewed; 335 AA.
AC Q12126;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Serine/threonine-protein kinase crk1;
DE EC=2.7.11.23 {ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037, ECO:0000269|PubMed:9857180};
DE AltName: Full=Mitotic catastrophe suppressor 6;
GN Name=crk1; Synonyms=mcs6, mop1; ORFNames=SPBC19F8.07;
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]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION
RP WITH MCS2.
RX PubMed=8557036; DOI=10.1002/j.1460-2075.1995.tb00307.x;
RA Damagnez V., Makela T.P., Cottarel G.;
RT "Schizosaccharomyces pombe Mop1-Mcs2 is related to mammalian CAK.";
RL EMBO J. 14:6164-6172(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP INTERACTION WITH MCS2.
RC STRAIN=972 / ATCC 24843;
RX PubMed=8557037; DOI=10.1002/j.1460-2075.1995.tb00308.x;
RA Buck V., Russell P., Millar J.B.A.;
RT "Identification of a cdk-activating kinase in fission yeast.";
RL EMBO J. 14:6173-6183(1995).
RN [3]
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 [4]
RP CATALYTIC ACTIVITY, AND PHOSPHORYLATION AT SER-165.
RX PubMed=9857180; DOI=10.1093/emboj/17.24.7230;
RA Hermand D., Pihlak A., Westerling T., Damagnez V., Vandenhaute J.,
RA Cottarel G., Makela T.P.;
RT "Fission yeast Csk1 is a CAK-activating kinase (CAKAK).";
RL EMBO J. 17:7230-7238(1998).
RN [5]
RP SUBUNIT.
RX PubMed=14534314; DOI=10.1074/jbc.m306750200;
RA Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
RA Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
RT "Mediator influences Schizosaccharomyces pombe RNA polymerase II-dependent
RT transcription in vitro.";
RL J. Biol. Chem. 278:51301-51306(2003).
RN [6]
RP INTERACTION WITH MCS2 AND TFB3.
RX PubMed=15555586; DOI=10.1016/j.bbrc.2004.10.190;
RA Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J.,
RA Maekelae T.P., Hermand D.;
RT "Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission yeast.";
RL Biochem. Biophys. Res. Commun. 325:1424-1432(2004).
RN [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-165 AND SER-318, AND
RP 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: Protein kinase essential for cell proliferation, where it is
CC required for completion of cytokinesis. Phosphorylates the C-terminal
CC repeat domain (CTD) of RNA polymerase II. {ECO:0000269|PubMed:8557036,
CC ECO:0000269|PubMed:8557037}.
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:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037,
CC ECO:0000269|PubMed:9857180};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10217;
CC Evidence={ECO:0000305|PubMed:8557036};
CC -!- SUBUNIT: One of the nine subunits forming the core-TFIIH basal
CC transcription factor. Interacts with mcs2 and tfb3.
CC {ECO:0000269|PubMed:14534314, ECO:0000269|PubMed:15555586,
CC ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
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; L47353; AAB00356.1; -; mRNA.
DR EMBL; X91239; CAA62621.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA19127.1; -; Genomic_DNA.
DR PIR; S66145; S66145.
DR RefSeq; NP_596349.1; NM_001022269.2.
DR AlphaFoldDB; Q12126; -.
DR SMR; Q12126; -.
DR BioGRID; 276999; 14.
DR IntAct; Q12126; 2.
DR STRING; 4896.SPBC19F8.07.1; -.
DR iPTMnet; Q12126; -.
DR MaxQB; Q12126; -.
DR PaxDb; Q12126; -.
DR PRIDE; Q12126; -.
DR EnsemblFungi; SPBC19F8.07.1; SPBC19F8.07.1:pep; SPBC19F8.07.
DR GeneID; 2540471; -.
DR KEGG; spo:SPBC19F8.07; -.
DR PomBase; SPBC19F8.07; -.
DR VEuPathDB; FungiDB:SPBC19F8.07; -.
DR eggNOG; KOG0659; Eukaryota.
DR HOGENOM; CLU_000288_181_1_1; -.
DR InParanoid; Q12126; -.
DR OMA; GIHHCHR; -.
DR PhylomeDB; Q12126; -.
DR BRENDA; 2.7.11.23; 5613.
DR Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
DR Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-SPO-6782135; Dual incision in TC-NER.
DR Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-SPO-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-SPO-69202; Cyclin E associated events during G1/S transition.
DR Reactome; R-SPO-69231; Cyclin D associated events in G1.
DR Reactome; R-SPO-69656; Cyclin A:Cdk2-associated events at S phase entry.
DR Reactome; R-SPO-72086; mRNA Capping.
DR Reactome; R-SPO-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-SPO-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR PRO; PR:Q12126; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IDA:PomBase.
DR GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IPI:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0070985; C:transcription factor TFIIK complex; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:PomBase.
DR GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0008353; F:RNA polymerase II CTD heptapeptide repeat kinase activity; IDA:PomBase.
DR GO; GO:0016251; F:RNA polymerase II general transcription initiation factor activity; IC:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; 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; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
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; Transcription; Transcription regulation;
KW Transferase.
FT CHAIN 1..335
FT /note="Serine/threonine-protein kinase crk1"
FT /id="PRO_0000085879"
FT DOMAIN 11..292
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 17..25
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 40
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 165
FT /note="Phosphoserine; by CAK"
FT /evidence="ECO:0000269|PubMed:18257517,
FT ECO:0000269|PubMed:9857180"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 335 AA; 38538 MW; 8AD88A491ACB1671 CRC64;
MDIEKSDKWT YVKERKVGEG TYAVVFLGRQ KETNRRVAIK KIKVGQFKDG IDISALREIK
FLRESRHDNV IELVDVFSTK SNLNIILEFL DSDLEMLIKD KFIVFQPAHI KSWMVMLLRG
LHHIHSRFIL HRDLKPNNLL ISSDGVLKLA DFGLSRDFGT PSHMSHQVIT RWYRPPELFM
GCRSYGTGVD MWSVGCIFAE LMLRTPYLPG ESDLDQLNVI FRALGTPEPE VIKSMQQLPN
YVEMKHIPPP NGGMEALFSA AGHEEIDLLK MMLDYNPYRR PTAQQALEHH YFSALPKPTH
PSLLPRKGGE EGIKHVSSDL QRQNNFPMRA NIKFV
