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 03-AUG-2022, entry version 190.
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; 4896.SPAC31G5.09c.1; -.
DR iPTMnet; P27638; -.
DR MaxQB; P27638; -.
DR PaxDb; P27638; -.
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-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-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:0006468; P:protein phosphorylation; IEA:InterPro.
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 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
