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Database: UniProt/SWISS-PROT
Entry: SPK1_SCHPO
LinkDB: SPK1_SCHPO
Original site: SPK1_SCHPO 
ID   SPK1_SCHPO              Reviewed;         372 AA.
AC   P27638;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   05-DEC-2018, entry version 171.
DE   RecName: Full=Mitogen-activated protein kinase spk1;
DE            Short=MAP kinase spk1;
DE            Short=MAPK;
DE            EC=2.7.11.24;
GN   Name=spk1; ORFNames=SPAC31G5.09c;
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=1899230; DOI=10.1101/gad.5.1.60;
RA   Toda T., Shimanuki M., Yanagida M.;
RT   "Fission yeast genes that confer resistance to staurosporine encode an
RT   AP-1-like transcription factor and a protein kinase related to the
RT   mammalian ERK1/MAP2 and budding yeast FUS3 and KSS1 kinases.";
RL   Genes Dev. 5:60-73(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=CD16-1;
RA   Watanabe T., Saito T.T., Nabeshima K., Nojima H.;
RT   "Identification of abundant polyA plus non-coding RNAs that are
RT   expressed in Schizosaccharomyces pombe.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 286-372.
RA   Kawamukai M.;
RT   "S.pombe uroporphrinogen III synthase gene.";
RL   Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   FUNCTION.
RX   PubMed=8413241; DOI=10.1128/MCB.13.10.6427;
RA   Gotoh Y., Nishida E., Shimanuki M., Toda T., Imai Y., Yamamoto M.;
RT   "Schizosaccharomyces pombe Spk1 is a tyrosine-phosphorylated protein
RT   functionally related to Xenopus mitogen-activated protein kinase.";
RL   Mol. Cell. Biol. 13:6427-6434(1993).
CC   -!- FUNCTION: Involved in mating signal transduction pathway.
CC       {ECO:0000269|PubMed:8413241}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC         [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC         COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC         threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC         Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC         EC=2.7.11.24;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Activated by tyrosine and threonine
CC       phosphorylation.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Note=Mainly nuclear.
CC   -!- DOMAIN: The TXY motif contains the threonine and tyrosine residues
CC       whose phosphorylation activates the MAP kinases.
CC   -!- PTM: Dually phosphorylated on Thr-199 and Tyr-201, which activates
CC       the enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC
CC       Ser/Thr protein kinase family. MAP kinase subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to confer resistance to
CC       staurosporine. {ECO:0000305|PubMed:1899230}.
DR   EMBL; D31735; BAA06536.1; -; Genomic_DNA.
DR   EMBL; X57334; CAA40610.1; -; Genomic_DNA.
DR   EMBL; AB084886; BAC54906.1; -; mRNA.
DR   EMBL; AB084887; BAC54907.1; -; mRNA.
DR   EMBL; CU329670; CAB11693.1; -; Genomic_DNA.
DR   EMBL; AB004551; BAA20417.1; -; Genomic_DNA.
DR   PIR; S15663; S15663.
DR   RefSeq; NP_594009.1; NM_001019435.2.
DR   ProteinModelPortal; P27638; -.
DR   SMR; P27638; -.
DR   BioGrid; 278934; 12.
DR   IntAct; P27638; 3.
DR   STRING; 4896.SPAC31G5.09c.1; -.
DR   iPTMnet; P27638; -.
DR   MaxQB; P27638; -.
DR   PaxDb; P27638; -.
DR   PRIDE; P27638; -.
DR   EnsemblFungi; SPAC31G5.09c.1; SPAC31G5.09c.1:pep; SPAC31G5.09c.
DR   GeneID; 2542474; -.
DR   KEGG; spo:SPAC31G5.09c; -.
DR   EuPathDB; FungiDB:SPAC31G5.09c; -.
DR   PomBase; SPAC31G5.09c; spk1.
DR   HOGENOM; HOG000233024; -.
DR   InParanoid; P27638; -.
DR   KO; K04371; -.
DR   OMA; WELPRRY; -.
DR   OrthoDB; EOG092C2FL8; -.
DR   PhylomeDB; P27638; -.
DR   BRENDA; 2.7.11.24; 5613.
DR   Reactome; R-SPO-110056; MAPK3 (ERK1) activation.
DR   Reactome; R-SPO-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-SPO-112411; MAPK1 (ERK2) activation.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-SPO-445144; Signal transduction by L1.
DR   Reactome; R-SPO-450341; Activation of the AP-1 family of transcription factors.
DR   Reactome; R-SPO-5673001; RAF/MAP kinase cascade.
DR   Reactome; R-SPO-5674135; MAP2K and MAPK activation.
DR   Reactome; R-SPO-5674499; Negative feedback regulation of MAPK pathway.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:P27638; -.
DR   Proteomes; UP000002485; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; HDA:PomBase.
DR   GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR   GO; GO:0004707; F:MAP kinase activity; IDA:PomBase.
DR   GO; GO:0071310; P:cellular response to organic substance; IBA:GO_Central.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0071507; P:pheromone response MAPK cascade; IMP:PomBase.
DR   GO; GO:0000750; P:pheromone-dependent signal transduction involved in conjugation with cellular fusion; IMP:PomBase.
DR   GO; GO:0075296; P:positive regulation of ascospore formation; IMP:PomBase.
DR   GO; GO:0034307; P:regulation of ascospore formation; IMP:PomBase.
DR   GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR003527; MAP_kinase_CS.
DR   InterPro; IPR008352; MAPK_p38-like.
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   PRINTS; PR01773; P38MAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS01351; MAPK; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN         1    372       Mitogen-activated protein kinase spk1.
FT                                /FTId=PRO_0000186340.
FT   DOMAIN       39    327       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND      45     53       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOTIF       199    201       TXY.
FT   ACT_SITE    163    163       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      68     68       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     199    199       Phosphothreonine. {ECO:0000250}.
FT   MOD_RES     201    201       Phosphotyrosine. {ECO:0000250}.
SQ   SEQUENCE   372 AA;  42003 MW;  85D980514C9386C7 CRC64;
     MASATSTPTI ADGNSNKESV ATSRSPHTHD LNFELPEEYE MINLIGQGAY GVVCAALHKP
     SGLKVAVKKI HPFNHPVFCL RTLREIKLLR HFRHENIISI LDILPPPSYQ ELEDVYIVQE
     LMETDLYRVI RSQPLSDDHC QYFTYQILRA LKAMHSAGVV HRDLKPSNLL LNANCDLKVA
     DFGLARSTTA QGGNPGFMTE YVATRWYRAP EIMLSFREYS KAIDLWSTGC ILAEMLSARP
     LFPGKDYHSQ ITLILNILGT PTMDDFSRIK SARARKYIKS LPFTPKVSFK ALFPQASPDA
     IDLLEKLLTF NPDKRITAEE ALKHPYVAAY HDASDEPTAS PMPPNLVDLY CNKEDLEIPV
     LKALIFREVN FR
//
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