GSK3_SCHPO
ID GSK3_SCHPO Reviewed; 387 AA.
AC Q10452; O94456;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein kinase gsk3;
DE EC=2.7.11.1;
DE AltName: Full=Protein kinase skp1;
GN Name=gsk3; Synonyms=skp1; ORFNames=SPAC1687.15;
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], FUNCTION, INTERACTION WITH CDC14,
RP MUTAGENESIS OF LYS-61; TYR-192 AND SER-335, AND PHOSPHORYLATION AT TYR-192
RP AND SER-335.
RX PubMed=8524294; DOI=10.1128/mcb.16.1.179;
RA Plyte S.E., Feoktistova A., Burke J.D., Woodgett J.R., Gould K.L.;
RT "Schizosaccharomyces pombe skp1+ encodes a protein kinase related to
RT mammalian glycogen synthase kinase 3 and complements a cdc14 cytokinesis
RT mutant.";
RL Mol. Cell. Biol. 16:179-191(1996).
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 FUNCTION.
RX PubMed=12773390; DOI=10.1093/emboj/cdg266;
RA Goshima G., Iwasaki O., Obuse C., Yanagida M.;
RT "The role of Ppe1/PP6 phosphatase for equal chromosome segregation in
RT fission yeast kinetochore.";
RL EMBO J. 22:2752-2763(2003).
RN [4]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-191 AND TYR-192, 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: Interacts with cdc14 which is thought to play a role in the
CC initiation and completion of mitosis. Involved in the positive
CC regulation of mis12. {ECO:0000269|PubMed:12773390,
CC ECO:0000269|PubMed:8524294}.
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=2.7.11.1;
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=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus
CC {ECO:0000269|PubMed:16823372}.
CC -!- PTM: Autophosphorylated on tyrosine residues.
CC {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:8524294}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. GSK-3 subfamily. {ECO:0000305}.
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DR EMBL; L29449; AAB51081.1; -; Genomic_DNA.
DR EMBL; CU329670; CAA22609.1; -; Genomic_DNA.
DR PIR; T37758; T37758.
DR PIR; T45138; T45138.
DR RefSeq; NP_593134.1; NM_001018530.2.
DR AlphaFoldDB; Q10452; -.
DR SMR; Q10452; -.
DR BioGRID; 279106; 386.
DR STRING; 4896.SPAC1687.15.1; -.
DR iPTMnet; Q10452; -.
DR MaxQB; Q10452; -.
DR PaxDb; Q10452; -.
DR PRIDE; Q10452; -.
DR EnsemblFungi; SPAC1687.15.1; SPAC1687.15.1:pep; SPAC1687.15.
DR GeneID; 2542652; -.
DR KEGG; spo:SPAC1687.15; -.
DR PomBase; SPAC1687.15; gsk3.
DR VEuPathDB; FungiDB:SPAC1687.15; -.
DR eggNOG; KOG0658; Eukaryota.
DR HOGENOM; CLU_000288_181_20_1; -.
DR InParanoid; Q10452; -.
DR OMA; EMQYTQC; -.
DR PhylomeDB; Q10452; -.
DR BRENDA; 2.7.11.26; 5613.
DR Reactome; R-SPO-3371453; Regulation of HSF1-mediated heat shock response.
DR PRO; PR:Q10452; -.
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:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IDA:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:PomBase.
DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IDA:UniProtKB.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IDA:PomBase.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IGI:UniProtKB.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR GO; GO:0032933; P:SREBP signaling pathway; IMP:PomBase.
DR CDD; cd14137; STKc_GSK3; 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 InterPro; IPR039192; STKc_GSK3.
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; Cytoplasm; Kinase; Mitosis;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..387
FT /note="Protein kinase gsk3"
FT /id="PRO_0000085985"
FT DOMAIN 32..316
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT ACT_SITE 157
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 38..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 61
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 191
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 192
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:18257517,
FT ECO:0000269|PubMed:8524294"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8524294"
FT MUTAGEN 61
FT /note="K->A: Abolishes protein kinase activity."
FT /evidence="ECO:0000269|PubMed:8524294"
FT MUTAGEN 192
FT /note="Y->E: Delays formation of F-actin contractile ring."
FT /evidence="ECO:0000269|PubMed:8524294"
FT MUTAGEN 192
FT /note="Y->F: Loss of tyrosine phosphorylation."
FT /evidence="ECO:0000269|PubMed:8524294"
FT MUTAGEN 335
FT /note="S->A: Delays cytokinesis. Chromatin condenses."
FT /evidence="ECO:0000269|PubMed:8524294"
FT CONFLICT 349..387
FT /note="ELSIRPDLNQKLIPSHARDALPVKLDDFVPIPIHRARID -> GTIHSS
FT (in Ref. 1; AAB51081)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 387 AA; 44165 MW; FDF2EEF81DC60CDD CRC64;
MNHGTKIPVD PFRIIKETAR DGSTGEVKQL SYTSSKVVGS GSFGVVMQVH LIESDSKAAI
KRVLQDKRFK NRELQIMRIM KHPNIVDLIA YYYTTGDNSD EVYLNLVLEF MPETIYRASR
LYTRQKLSMP MLEVKLYIYQ LLRSLAYIHA SGICHRDIKP QNLLLDPENG ILKLCDFGSA
KILVAGEPNV SYICSRYYRA PELIFGATDY THAIDIWSTG CVMAELMLGH PLFPGESGID
QLVEIIKILG TPSREQIKTM NPNYMEHRFP QIRPQPLSRV FSRSVPLDAL DLLSKMLQYT
PTDRLTAAEA MCHPFFDELR DPNTKLHNSR NPDASPRHLP ELFNFSPFEL SIRPDLNQKL
IPSHARDALP VKLDDFVPIP IHRARID
