WEE1_SCHPO
ID WEE1_SCHPO Reviewed; 877 AA.
AC P07527; Q9UU00;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1988, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Mitosis inhibitor protein kinase wee1;
DE EC=2.7.10.2;
DE AltName: Full=P107 protein kinase homolog;
GN Name=wee1; ORFNames=SPCC18B5.03;
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=3032459; DOI=10.1016/0092-8674(87)90458-2;
RA Russell P., Nurse P.;
RT "Negative regulation of mitosis by wee1+, a gene encoding a protein kinase
RT homolog.";
RL Cell 49:559-567(1987).
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 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 406-625, AND SUBCELLULAR
RP LOCATION.
RC STRAIN=ATCC 38364 / 968;
RX PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
RA Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
RA Hiraoka Y.;
RT "Large-scale screening of intracellular protein localization in living
RT fission yeast cells by the use of a GFP-fusion genomic DNA library.";
RL Genes Cells 5:169-190(2000).
RN [4]
RP FUNCTION.
RX PubMed=1825699; DOI=10.1038/349808a0;
RA Featherstone C., Russell P.;
RT "Fission yeast p107wee1 mitotic inhibitor is a tyrosine/serine kinase.";
RL Nature 349:808-811(1991).
CC -!- FUNCTION: Protein kinase that acts both on serines and on tyrosines. It
CC acts as a dosage-dependent negative regulator of entry into mitosis (G2
CC to M transition). Phosphorylates and inhibits cdc2.
CC {ECO:0000269|PubMed:1825699}.
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=2.7.10.2;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 magnesium ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Negatively regulated by phosphorylation in the M-
CC phase.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889}.
CC -!- PTM: Phosphorylated in the C-terminal by NIM1/CDR1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. WEE1 subfamily. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; M16508; AAA35354.1; -; Genomic_DNA.
DR EMBL; CU329672; CAB52150.1; -; Genomic_DNA.
DR EMBL; AB027900; BAA87204.1; -; Genomic_DNA.
DR PIR; A25962; A25962.
DR RefSeq; NP_587933.1; NM_001022924.2.
DR AlphaFoldDB; P07527; -.
DR SMR; P07527; -.
DR BioGRID; 275695; 92.
DR DIP; DIP-16N; -.
DR STRING; 4896.SPCC18B5.03.1; -.
DR iPTMnet; P07527; -.
DR SwissPalm; P07527; -.
DR PaxDb; P07527; -.
DR PRIDE; P07527; -.
DR EnsemblFungi; SPCC18B5.03.1; SPCC18B5.03.1:pep; SPCC18B5.03.
DR GeneID; 2539123; -.
DR KEGG; spo:SPCC18B5.03; -.
DR PomBase; SPCC18B5.03; wee1.
DR VEuPathDB; FungiDB:SPCC18B5.03; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_346520_0_0_1; -.
DR InParanoid; P07527; -.
DR OMA; QVELCEN; -.
DR Reactome; R-SPO-156711; Polo-like kinase mediated events.
DR PRO; PR:P07527; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0110115; C:Cdr2 medial cortical node complex; EXP:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IBA:GO_Central.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:PomBase.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IGI:PomBase.
DR GO; GO:0031569; P:mitotic G2 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0110031; P:negative regulation of G2/MI transition of meiotic 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; Magnesium; Metal-binding;
KW Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Transferase; Tyrosine-protein kinase.
FT CHAIN 1..877
FT /note="Mitosis inhibitor protein kinase wee1"
FT /id="PRO_0000086815"
FT DOMAIN 566..843
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 775..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..76
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 410..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..806
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 693
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 572..580
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 596
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 698
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 711
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT MUTAGEN 596
FT /note="K->L: Inactivates enzyme."
SQ SEQUENCE 877 AA; 96261 MW; C8B5113D66C39D10 CRC64;
MSSSSNTSSH RSYGLRRSQR SMNLNRATLL APPTPSSLYD ANNSTSSTSS QKPNTSFTSL
FGPRKQTTSS PSFSHAAPLH PLSPPSFTHS QPQIQAQPVP RRPSLFDRPN LVSRSSSRLG
DSPSLSPVAQ VANPIHHTAP SPSDVRAFPI HKNASTGVKR SFFSSSMSNG AMSPPSHSPS
PFLQSSQHIP PSTPAQKLRK KNNFDSFRIS NSHISPFASG SFSPFATSSP NFLSTSTPAP
PNSNNANPST LFSSIPSSRH TTSNHFPSNS AQSSLFSPTA RPLTARKLGF ASSQTKSAVS
NNHSRNSSKD ASFMMKSFIP SNRSHPQTQQ NESSLFSDNS MVNSSSNSFS LFPNATLPNP
PSSELLTTPF QQIKPPSQVF MSTGLLSKQH RPRKNINFTP LPPSTPSKPS TFVRPHSSST
DSPPSPSTPS NTQTDSYFIQ RENTPTNHNS IPTIQLEKSS MDFLRFDPPP SAVKTSHNYG
LPFLSNQRCP ATPTRNPFAF ENTVSIHMDG RQPSPIKSRN NNQMSFAMEE EADVSQPSSS
SFTLSFPSAL TSSKVSSSTS HLLTRFRNVT LLGSGEFSEV FQVEDPVEKT LKYAVKKLKV
KFSGPKERNR LLQEVSIQRA LKGHDHIVEL MDSWEHGGFL YMQVELCENG SLDRFLEEQG
QLSRLDEFRV WKILVEVALG LQFIHHKNYV HLDLKPANVM ITFEGTLKIG DFGMASVWPV
PRGMEREGDC EYIAPEVLAN HLYDKPADIF SLGITVFEAA ANIVLPDNGQ SWQKLRSGDL
SDAPRLSSTD NGSSLTSSSR ETPANSIIGQ GGLDRVVEWM LSPEPRNRPT IDQILATDEV
CWVEMRRKAG AIIYEGIHGS SSNPQGDQMM EDWQVNV
