ID   WIS1_SCHPO              Reviewed;         605 AA.
AC   P33886;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   04-NOV-2026, entry version 191.
DE   RecName: Full=Protein kinase wis1;
DE            EC=2.7.12.2;
DE   AltName: Full=Protein kinase sty2;
GN   Name=wis1; Synonyms=spc2, sty2; ORFNames=SPBC409.07c;
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].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=1756736; DOI=10.1002/j.1460-2075.1991.tb05007.x;
RA   Warbrick E., Fantes P.A.;
RT   "The wis1 protein kinase is a dosage-dependent regulator of mitosis in
RT   Schizosaccharomyces pombe.";
RL   EMBO J. 10:4291-4299(1991).
RN   [2]
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   [3]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-168 AND SER-253, AND
RP   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: Dosage-dependent regulator of mitosis with serine/ threonine
CC       protein kinase activity. May play a role in the integration of
CC       nutritional sensing with the control over entry into mitosis. It may
CC       interact with cdc25, wee1 and win1. May activate sty1.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP +
CC         H(+); 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=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060, Rhea:RHEA-
CC         COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:61977, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] +
CC         ADP + H(+); Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC         COMP:20101, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:61978, ChEBI:CHEBI:456216; EC=2.7.12.2;
CC   -!- PTM: Dephosphorylated by pyp1 and pyp2.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. STE Ser/Thr
CC       protein kinase family. MAP kinase kinase subfamily. {ECO:0000305}.
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DR   EMBL; X62631; CAA44499.1; -; Genomic_DNA.
DR   EMBL; CU329671; CAB52609.1; -; Genomic_DNA.
DR   PIR; S18648; S18648.
DR   RefSeq; NP_595457.1; NM_001021367.3.
DR   AlphaFoldDB; P33886; -.
DR   SMR; P33886; -.
DR   BioGRID; 277570; 43.
DR   FunCoup; P33886; 292.
DR   IntAct; P33886; 2.
DR   STRING; 284812.P33886; -.
DR   iPTMnet; P33886; -.
DR   PaxDb; 284812-P33886; -.
DR   GeneID; 2541055; -.
DR   KEGG; spo:2541055; -.
DR   PomBase; SPBC409.07c; wis1.
DR   VEuPathDB; FungiDB:SPBC409.07c; -.
DR   eggNOG; KOG0581; Eukaryota.
DR   HOGENOM; CLU_000288_79_1_1; -.
DR   InParanoid; P33886; -.
DR   OMA; AICDGDP; -.
DR   PhylomeDB; P33886; -.
DR   BRENDA; 2.7.12.2; 5613.
DR   Reactome; R-SPO-168638; NOD1/2 Signaling Pathway.
DR   Reactome; R-SPO-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-SPO-2871796; FCERI mediated MAPK activation.
DR   Reactome; R-SPO-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-SPO-6811555; PI5P Regulates TP53 Acetylation.
DR   PRO; PR:P33886; -.
DR   Proteomes; UP000002485; Chromosome II.
DR   GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR   GO; GO:0005829; C:cytosol; IDA:PomBase.
DR   GO; GO:1990315; C:Mcs4 RR-MAPKKK complex; IDA:PomBase.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0004708; F:MAP kinase kinase activity; IDA:PomBase.
DR   GO; GO:0004672; F:protein kinase activity; IDA:PomBase.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR   GO; GO:0071474; P:cellular hyperosmotic response; IBA:GO_Central.
DR   GO; GO:0071470; P:cellular response to osmotic stress; IMP:PomBase.
DR   GO; GO:0000165; P:MAPK cascade; IBA:GO_Central.
DR   GO; GO:0038066; P:p38MAPK cascade; IDA:PomBase.
DR   GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR   GO; GO:0090055; P:positive regulation of silent mating-type cassette heterochromatin formation; EXP:PomBase.
DR   CDD; cd06622; PKc_PBS2_like; 1.
DR   FunFam; 3.30.200.20:FF:000341; MAP kinase kinase PBS2; 1.
DR   Gene3D; 3.30.200.20; Phosphorylase Kinase, domain 1; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR48013; DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN KINASE KINASE 5-RELATED; 1.
DR   PANTHER; PTHR48013:SF25; MAP KINASE KINASE PBS2; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cell cycle; Cell division; Kinase; Mitosis;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..605
FT                   /note="Protein kinase wis1"
FT                   /id="PRO_0000086817"
FT   DOMAIN          320..579
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..141
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..263
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..73
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        90..105
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..115
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..200
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        244..256
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        441
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         326..334
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         349
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18257517"
FT   MOD_RES         469
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         473
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   605 AA;  64762 MW;  3EB97AF74190AD93 CRC64;
     MSSPNNQPLS CSLRQLSISP TAPPGDVGTP GSLLSLSSSS SSNTDSSGSS LGSLSLNSNS
     SGSDNDSKVS SPSREIPSDP PLPRAVPTVR LGRSTSSRSR NSLNLDMKDP SEKPRRSLPT
     AAGQNNIGSP PTPPGPFPGG LSTDIQEKLK AFHASRSKSM PEVVNKISSP TTPIVGMGQR
     GSYPLPNSQL AGRLSNSPVK SPNMPESGLA KSLAAARNPL LNRPTSFNRQ TRIRRAPPGK
     LDLSNSNPTS PVSPSSMASR RGLNIPPTLK QAVSETPFST FSDILDAKSG TLNFKNKAVL
     NSEGVNFSSG SSFRINMSEI IKLEELGKGN YGVVYKALHQ PTGVTMALKE IRLSLEEATF
     NQIIMELDIL HKAVSPYIVD FYGAFFVEGS VFICMEYMDA GSMDKLYAGG IKDEGVLART
     AYAVVQGLKT LKEEHNIIHR DVKPTNVLVN SNGQVKLCDF GVSGNLVASI SKTNIGCQSY
     MAPERIRVGG PTNGVLTYTV QADVWSLGLT ILEMALGAYP YPPESYTSIF AQLSAICDGD
     PPSLPDSFSP EARDFVNKCL NKNPSLRPDY HELANHPWLL KYQNADVDMA SWAKGALKEK
     GEKRS
//