位置:首页 > 蛋白库 > WEE1_SCHPO
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024