WIS1_SCHPO
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 03-AUG-2022, entry version 174.
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=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=2.7.12.2;
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=2.7.12.2;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, 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_001021367.2.
DR AlphaFoldDB; P33886; -.
DR SMR; P33886; -.
DR BioGRID; 277570; 42.
DR IntAct; P33886; 2.
DR STRING; 4896.SPBC409.07c.1; -.
DR iPTMnet; P33886; -.
DR MaxQB; P33886; -.
DR PaxDb; P33886; -.
DR PRIDE; P33886; -.
DR EnsemblFungi; SPBC409.07c.1; SPBC409.07c.1:pep; SPBC409.07c.
DR GeneID; 2541055; -.
DR KEGG; spo:SPBC409.07c; -.
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; SVFICME; -.
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-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; HDA:PomBase.
DR GO; GO:1990315; C:Mcs4 RR-MAPKKK complex; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0034599; P:cellular response to oxidative 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 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 Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 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..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..104
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..262
FT /note="Polar residues"
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
