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Serine/threonine-protein kinase crk1 (EC 2.7.11.23) (Mitotic catastrophe suppressor 6)

 CRK1_SCHPO              Reviewed;         335 AA.
Q12126;
06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
25-OCT-2017, entry version 146.
RecName: Full=Serine/threonine-protein kinase crk1;
EC=2.7.11.23;
AltName: Full=Mitotic catastrophe suppressor 6;
Name=crk1; Synonyms=mcs6, mop1; ORFNames=SPBC19F8.07;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH MCS2.
PubMed=8557036;
Damagnez V., Makela T.P., Cottarel G.;
"Schizosaccharomyces pombe Mop1-Mcs2 is related to mammalian CAK.";
EMBO J. 14:6164-6172(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INTERACTION WITH
MCS2.
STRAIN=972 / ATCC 24843;
PubMed=8557037;
Buck V., Russell P., Millar J.B.A.;
"Identification of a cdk-activating kinase in fission yeast.";
EMBO J. 14:6173-6183(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[4]
PHOSPHORYLATION AT SER-165.
PubMed=9857180; DOI=10.1093/emboj/17.24.7230;
Hermand D., Pihlak A., Westerling T., Damagnez V., Vandenhaute J.,
Cottarel G., Makela T.P.;
"Fission yeast Csk1 is a CAK-activating kinase (CAKAK).";
EMBO J. 17:7230-7238(1998).
[5]
SUBUNIT.
PubMed=14534314; DOI=10.1074/jbc.M306750200;
Spaehr H., Khorosjutina O., Baraznenok V., Linder T., Samuelsen C.O.,
Hermand D., Maekelae T.P., Holmberg S., Gustafsson C.M.;
"Mediator influences Schizosaccharomyces pombe RNA polymerase II-
dependent transcription in vitro.";
J. Biol. Chem. 278:51301-51306(2003).
[6]
INTERACTION WITH MCS2 AND TFB3.
PubMed=15555586; DOI=10.1016/j.bbrc.2004.10.190;
Bamps S., Westerling T., Pihlak A., Tafforeau L., Vandenhaute J.,
Maekelae T.P., Hermand D.;
"Mcs2 and a novel CAK subunit Pmh1 associate with Skp1 in fission
yeast.";
Biochem. Biophys. Res. Commun. 325:1424-1432(2004).
[7]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162; SER-165 AND
SER-318, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
-!- FUNCTION: Protein kinase essential for cell proliferation, where
it is required for completion of cytokinesis. Phosphorylates the
C-terminal repeat domain (CTD) of RNA polymerase II.
{ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037}.
-!- CATALYTIC ACTIVITY: ATP + [DNA-directed RNA polymerase] = ADP +
[DNA-directed RNA polymerase] phosphate.
-!- SUBUNIT: One of the nine subunits forming the core-TFIIH basal
transcription factor. Interacts with mcs2 and tfb3.
{ECO:0000269|PubMed:14534314, ECO:0000269|PubMed:15555586,
ECO:0000269|PubMed:8557036, ECO:0000269|PubMed:8557037}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}.
Nucleus {ECO:0000269|PubMed:16823372}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
Ser/Thr protein kinase family. CDC2/CDKX subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L47353; AAB00356.1; -; mRNA.
EMBL; X91239; CAA62621.1; -; Genomic_DNA.
EMBL; CU329671; CAA19127.1; -; Genomic_DNA.
PIR; S66145; S66145.
RefSeq; NP_596349.1; NM_001022269.2.
ProteinModelPortal; Q12126; -.
BioGrid; 276999; 14.
IntAct; Q12126; 2.
MINT; MINT-4699918; -.
STRING; 4896.SPBC19F8.07.1; -.
iPTMnet; Q12126; -.
MaxQB; Q12126; -.
PRIDE; Q12126; -.
EnsemblFungi; SPBC19F8.07.1; SPBC19F8.07.1:pep; SPBC19F8.07.
GeneID; 2540471; -.
KEGG; spo:SPBC19F8.07; -.
EuPathDB; FungiDB:SPBC19F8.07; -.
PomBase; SPBC19F8.07; -.
HOGENOM; HOG000233024; -.
InParanoid; Q12126; -.
KO; K02202; -.
OMA; ADIKAWM; -.
OrthoDB; EOG092C2FL8; -.
PhylomeDB; Q12126; -.
Reactome; R-SPO-113418; Formation of the Early Elongation Complex.
Reactome; R-SPO-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-SPO-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-SPO-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-SPO-6782135; Dual incision in TC-NER.
Reactome; R-SPO-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-SPO-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-SPO-72086; mRNA Capping.
Reactome; R-SPO-73776; RNA Polymerase II Promoter Escape.
Reactome; R-SPO-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-SPO-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-SPO-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-SPO-77075; RNA Pol II CTD phosphorylation and interaction with CE.
PRO; PR:Q12126; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0019907; C:cyclin-dependent protein kinase activating kinase holoenzyme complex; IPI:PomBase.
GO; GO:0005737; C:cytoplasm; IDA:PomBase.
GO; GO:0005829; C:cytosol; IDA:PomBase.
GO; GO:0005675; C:holo TFIIH complex; ISO:PomBase.
GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0070985; C:TFIIK complex; IDA:PomBase.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019912; F:cyclin-dependent protein kinase activating kinase activity; IDA:PomBase.
GO; GO:0097472; F:cyclin-dependent protein kinase activity; IDA:PomBase.
GO; GO:0004693; F:cyclin-dependent protein serine/threonine kinase activity; IDA:PomBase.
GO; GO:0008353; F:RNA polymerase II carboxy-terminal domain kinase activity; IDA:PomBase.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0070817; P:P-TEFb-cap methyltransferase complex localization; IMP:PomBase.
GO; GO:0070816; P:phosphorylation of RNA polymerase II C-terminal domain; IDA:PomBase.
GO; GO:1903655; P:phosphorylation of RNA polymerase II C-terminal domain serine 2 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IMP:PomBase.
GO; GO:0071620; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues; IMP:PomBase.
GO; GO:1903654; P:phosphorylation of RNA polymerase II C-terminal domain serine 5 residues involved in positive regulation of transcription elongation from RNA polymerase II promoter; IMP:PomBase.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR011009; Kinase-like_dom.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR008271; Ser/Thr_kinase_AS.
Pfam; PF00069; Pkinase; 1.
SMART; SM00220; S_TKc; 1.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
ATP-binding; Cell cycle; Cell division; Complete proteome; Cytoplasm;
Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
Reference proteome; Serine/threonine-protein kinase; Transcription;
Transcription regulation; Transferase.
CHAIN 1 335 Serine/threonine-protein kinase crk1.
/FTId=PRO_0000085879.
DOMAIN 11 292 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 17 25 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 133 133 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 40 40 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 162 162 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
MOD_RES 165 165 Phosphoserine; by CAK.
{ECO:0000269|PubMed:18257517,
ECO:0000269|PubMed:9857180}.
MOD_RES 318 318 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
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


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