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   27-MAR-2024, entry version 196.
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; Schizosaccharomycetaceae;
OC   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 AP-
RT   1-like transcription factor and a protein kinase related to the mammalian
RT   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 expressed
RT   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., 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   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.13.10.6427-6434.1993;
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, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; 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   -!- INTERACTION:
CC       P27638; P10506: byr1; NbExp=2; IntAct=EBI-2104356, EBI-2042633;
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 the
CC       enzyme. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC       protein kinase family. MAP kinase subfamily. {ECO:0000305}.
CC   -!- CAUTION: Was originally thought to confer resistance to staurosporine.
CC       {ECO:0000305|PubMed:1899230}.
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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   AlphaFoldDB; P27638; -.
DR   SMR; P27638; -.
DR   BioGRID; 278934; 19.
DR   IntAct; P27638; 3.
DR   STRING; 284812.P27638; -.
DR   iPTMnet; P27638; -.
DR   MaxQB; P27638; -.
DR   PaxDb; 4896-SPAC31G5-09c-1; -.
DR   EnsemblFungi; SPAC31G5.09c.1; SPAC31G5.09c.1:pep; SPAC31G5.09c.
DR   GeneID; 2542474; -.
DR   KEGG; spo:SPAC31G5.09c; -.
DR   PomBase; SPAC31G5.09c; spk1.
DR   VEuPathDB; FungiDB:SPAC31G5.09c; -.
DR   eggNOG; KOG0660; Eukaryota.
DR   HOGENOM; CLU_000288_181_1_1; -.
DR   InParanoid; P27638; -.
DR   OMA; PYVAAYH; -.
DR   PhylomeDB; P27638; -.
DR   BRENDA; 2.7.11.24; 5613.
DR   Reactome; R-SPO-110056; MAPK3 (ERK1) activation.
DR   Reactome; R-SPO-111995; phospho-PLA2 pathway.
DR   Reactome; R-SPO-112409; RAF-independent MAPK1/3 activation.
DR   Reactome; R-SPO-112411; MAPK1 (ERK2) activation.
DR   Reactome; R-SPO-170968; Frs2-mediated activation.
DR   Reactome; R-SPO-198753; ERK/MAPK targets.
DR   Reactome; R-SPO-202670; ERKs are inactivated.
DR   Reactome; R-SPO-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR   Reactome; R-SPO-375165; NCAM signaling for neurite out-growth.
DR   Reactome; R-SPO-437239; Recycling pathway of L1.
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-5668599; RHO GTPases Activate NADPH Oxidases.
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-5675221; Negative regulation of MAPK pathway.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   Reactome; R-SPO-881907; Gastrin-CREB signalling pathway via PKC and MAPK.
DR   Reactome; R-SPO-9634635; Estrogen-stimulated signaling through PRKCZ.
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:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; 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; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd07849; STKc_ERK1_2_like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
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   PANTHER; PTHR24055; MITOGEN-ACTIVATED PROTEIN KINASE; 1.
DR   PANTHER; PTHR24055:SF590; MITOGEN-ACTIVATED PROTEIN KINASE KSS1; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   PRINTS; PR01773; P38MAPKINASE.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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   1: Evidence at protein level;
KW   ATP-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..372
FT                   /note="Mitogen-activated protein kinase spk1"
FT                   /id="PRO_0000186340"
FT   DOMAIN          39..327
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..29
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           199..201
FT                   /note="TXY"
FT   ACT_SITE        163
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         45..53
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         68
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         199
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         201
FT                   /note="Phosphotyrosine"
FT                   /evidence="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
//