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Database: UniProt
Entry: P38938
LinkDB: P38938
Original site: P38938 
ID   CEK1_SCHPO              Reviewed;        1338 AA.
AC   P38938; Q9Y7N8;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2001, sequence version 3.
DT   26-NOV-2014, entry version 120.
DE   RecName: Full=Serine/threonine-protein kinase cek1;
DE            EC=2.7.11.1;
GN   Name=cek1; ORFNames=SPCC1450.11c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales;
OC   Schizosaccharomycetaceae; Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8065367; DOI=10.1128/MCB.14.9.6361;
RA   Samejima I., Yanagida M.;
RT   "Identification of cut8+ and cek1+, a novel protein kinase gene, which
RT   complement a fission yeast mutation that blocks anaphase.";
RL   Mol. Cell. Biol. 14:6361-6371(1994).
RN   [2]
RP   ERRATUM.
RA   Samejima I., Yanagida M.;
RL   Mol. Cell. Biol. 14:7683-7683(1994).
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.,
RA   Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
RA   Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
RA   Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
RA   James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
RA   Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
RA   Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
RA   Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
RA   Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
RA   Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
RA   Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
RA   Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
RA   Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
RA   Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
RA   Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
RA   Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
RA   Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
RA   Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
RA   Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
RA   Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
RA   Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-525; SER-748 AND
RP   SER-1211, 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: May facilitate the progression of anaphase through
CC       direct or indirect interaction with the cut8 protein.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr
CC       protein kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 AGC-kinase C-terminal domain.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00140}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR   EMBL; D31773; BAA06551.1; -; Genomic_DNA.
DR   EMBL; CU329672; CAB40178.1; -; Genomic_DNA.
DR   PIR; T40993; T40993.
DR   RefSeq; NP_588310.1; NM_001023300.2.
DR   ProteinModelPortal; P38938; -.
DR   BioGrid; 275778; 33.
DR   IntAct; P38938; 1.
DR   MINT; MINT-4689362; -.
DR   STRING; 4896.SPCC1450.11c-1; -.
DR   MaxQB; P38938; -.
DR   EnsemblFungi; SPCC1450.11c.1; SPCC1450.11c.1:pep; SPCC1450.11c.
DR   GeneID; 2539208; -.
DR   KEGG; spo:SPCC1450.11c; -.
DR   PomBase; SPCC1450.11c; -.
DR   eggNOG; COG0515; -.
DR   InParanoid; P38938; -.
DR   KO; K08286; -.
DR   OMA; INANHAN; -.
DR   OrthoDB; EOG7Z95VF; -.
DR   PhylomeDB; P38938; -.
DR   BRENDA; 2.7.11.1; 5615.
DR   NextBio; 20800378; -.
DR   PRO; PR:P38938; -.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
DR   GO; GO:0006468; P:protein phosphorylation; IC:PomBase.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IGI:PomBase.
DR   Gene3D; 2.30.29.30; -; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR011993; PH_like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   Pfam; PF00069; Pkinase; 2.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00133; S_TK_X; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 2.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1   1338       Serine/threonine-protein kinase cek1.
FT                                /FTId=PRO_0000085847.
FT   DOMAIN       28     98       PAS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN      589    958       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      959   1057       AGC-kinase C-terminal.
FT   NP_BIND     595    603       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   ACT_SITE    713    713       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING     618    618       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     525    525       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES     748    748       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   MOD_RES    1211   1211       Phosphoserine.
FT                                {ECO:0000269|PubMed:18257517}.
FT   CONFLICT   1297   1338       FVYICEDETCIPTDLQSDGVLLKPITCENIESCLRKLDVWH
FT                                S -> VCIHLRGRDLHSD (in Ref. 1; BAA06551).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1338 AA;  149897 MW;  755DD0A13D3D2762 CRC64;
     MKHIKNEREE VFLEDDQAQH SQAELLSSKD ENLQPSIPLS PVAFELDFSG NFQFISDNSS
     ELLDIPKDKI IGHSVAEVLG TDGYNAFMRA VNCLLKDDSH SYHVRFQHSI NANHANQNYY
     TAKGDLPSDE KITKPFDAIG ILIRHPGSAI PAHTMWVVNP ATNSLGSVSP LVTKLLDVIG
     FGASLLDKYL CDLRTSYHKH NSLDALPLPT PEFCQICERE IQSWFFELHS KFCLSTSTYE
     SVVQAAQDSL LYFRSTLLEI QEGMQKDSSL VPVYKNEPLI VDADDYFFTD ENKQTLSLCS
     FLSQVMYYLE VAIDITIPPV KIIVNFDKVD SLRVQSPRSE KATIELDNYN PSLENCSSAV
     IALWEDIKTA VDTKITGVLR LRNAIYYSER IRLEIDHHVQ EIIDDVVSNL VTNHSSTSLG
     HLESKLAPSI TFPDACDALE AEECITRPGS ATNTPQSDRS LDINDLSRSS SYSRHLSHVS
     LSNPDFAIGS PMSQDSSNYS SPLHRRKASD SNFSDPRFDD LKYLSPNSSP RFVASDGPNR
     PASNGRSSLF SRGRASNLGD VGLRLPSPSP RIHTIVPNSA PEHPSINDYK ILKPISKGAF
     GSVYLAQKRT TGDYFAIKIL KKSNMIAKNQ VINVRAERAI LMSQGESPFV AKLYYTFQSK
     DYLYLVMEYL NGGDCGSLLK TMGVLDLDWI RTYIAETVLC LGDLHDRGII HRDIKPENLL
     ISQNGHLKLT DFGLSRVGYM KRHRRKQSSS IPVLDLRDRS SAISDLSLST ASSVLEAQSL
     ITPERPKRPS LNEKLLSLDG TSIRLAGQSF NYENSAEDSP TATNTPTSQV DESNIFRSTD
     SPRVQPFFEN KDPSKRFIGT PDYIAPEVIL GNPGIKASDW WSLGCVVFEF LFGYPPFNAE
     TPDQVFQNIL ARRINWPAEV FTAESSVALD LIDRLLCMNP ANRLGANGVE EIKAHPFFKS
     VNWDTILEED PPFVPKPFSP EDTVYFDSRG LKGFDFSEYY NQPTVTEAQK LEEERPASSI
     PQHVSGNRKG RLRSNTISTP EFGSFTYRNL DFLNKANRNT IQKLRKEHMA VKSAKTSVDD
     TFSQYMSRFK AKLSTSQSVG PVKSSRRASM ADYEASTTTR VQDITTDSID SIDDFDSLKE
     GRMLSFFDNL ALEDHKGVSS TMSASQSQSS MHTALPDVTE GTSSDEHTTI QKGRIDNLQA
     QSLTHKRNAI SYPGLFQLDR LQMIIPKDEI ELAEILKKIF PKLTLVLIDD PWSILKKLLQ
     NEQFNVVFLH FGNDKVSSSR LMYSVRTSAT INSRVPFVYI CEDETCIPTD LQSDGVLLKP
     ITCENIESCL RKLDVWHS
//
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