MIK1_SCHPO
ID MIK1_SCHPO Reviewed; 581 AA.
AC P30290;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1993, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Mitosis inhibitor protein kinase mik1;
DE EC=2.7.11.1;
GN Name=mik1; ORFNames=SPBC660.14;
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=1706223; DOI=10.1016/0092-8674(91)90266-2;
RA Lundgren K., Walworth N., Booher R., Dembski M., Kirschner M., Beach D.;
RT "mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of
RT cdc2.";
RL Cell 64:1111-1122(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).
CC -!- FUNCTION: Protein kinase that acts both on serines and on tyrosines. It
CC acts as a negative regulator of entry into mitosis (G2 to M
CC transition). Phosphorylates and inhibits cdc2.
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 -!- 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; M60834; AAA91278.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA22534.1; -; Genomic_DNA.
DR PIR; A37913; A37913.
DR RefSeq; NP_595093.1; NM_001021000.2.
DR AlphaFoldDB; P30290; -.
DR SMR; P30290; -.
DR BioGRID; 277402; 61.
DR STRING; 4896.SPBC660.14.1; -.
DR iPTMnet; P30290; -.
DR PaxDb; P30290; -.
DR PRIDE; P30290; -.
DR EnsemblFungi; SPBC660.14.1; SPBC660.14.1:pep; SPBC660.14.
DR GeneID; 2540885; -.
DR KEGG; spo:SPBC660.14; -.
DR PomBase; SPBC660.14; mik1.
DR VEuPathDB; FungiDB:SPBC660.14; -.
DR eggNOG; KOG0601; Eukaryota.
DR HOGENOM; CLU_468646_0_0_1; -.
DR InParanoid; P30290; -.
DR OMA; QPHTPCK; -.
DR PhylomeDB; P30290; -.
DR PRO; PR:P30290; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
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:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IGI:PomBase.
DR GO; GO:0110031; P:negative regulation of G2/MI transition of meiotic cell cycle; IMP:PomBase.
DR GO; GO:0023052; P:signaling; NAS:PomBase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
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; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Kinase; Magnesium; Metal-binding;
KW Mitosis; Nucleotide-binding; Reference proteome;
KW Serine/threonine-protein kinase; Transferase; Tyrosine-protein kinase.
FT CHAIN 1..581
FT /note="Mitosis inhibitor protein kinase mik1"
FT /id="PRO_0000086327"
FT DOMAIN 289..561
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 43..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 148..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 417
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 295..303
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 422
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 435
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
SQ SEQUENCE 581 AA; 65934 MW; 371E0CEDB2CA1CE3 CRC64;
MDSSTTIPIT PTRTPCFFNI SSSFNEHSPL NFYDEPIYNF SSGHEENQSH KSSKLTFFKP
SNTKRSPHTP MQNNAKAIRL STTVRHGIFK NSDLDGCSKP FAFSSGLKLS KKIVDASTPI
DLKRKRAVTS LSTGLLSKRE KWSLWEGNLT NPRSEQPHTP CKKGTKIKLK PPQSPLSPTT
SLLARKCKHI DLDTFSRLDH PNSDSSDETF EMEELPSLSY GSEDLLEFCE TPCKSQPIFL
SSSHVNNWDE KDVPSSLSWT PTSPIFLNIN SADDYEEEED WTSDLRIRFQ QVKPIHESDF
SFVYHVSSIN PPTETVYVVK MLKKNAAKFT GKERHLQEVS ILQRLQACPF VVNLVNVWSY
NDNIFLQLDY CENGDLSLFL SELGLLQVMD PFRVWKMLFQ LTQALNFIHL LEFVHLDVKP
SNVLITRDGN LKLGDFGLAT SLPVSSMVDL EGDRVYIAPE ILASHNYGKP ADVYSLGLSM
IEAATNVVLP ENGVEWQRLR SGDYSNLPNL KDLLLSKEKV QINKVRCAES LQCLLQRMTH
PYVDCRPTTQ DLLAMPEMIF ISEHSQKAAI IYEDHNSWLE T
