CDR2_SCHPO
ID CDR2_SCHPO Reviewed; 775 AA.
AC P87050;
DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Mitosis inducer protein kinase cdr2;
DE EC=2.7.11.1;
GN Name=cdr2; ORFNames=SPAC57A10.02;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9843577; DOI=10.1091/mbc.9.12.3399;
RA Breeding C.S., Hudson J., Balasubramanian M.K., Hemmingsen S.M.,
RA Young P.G., Gould K.L.;
RT "The cdr2(+) gene encodes a regulator of G2/M progression and cytokinesis
RT in Schizosaccharomyces pombe.";
RL Mol. Biol. Cell 9:3399-3415(1998).
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, AND AUTOPHOSPHORYLATION.
RX PubMed=9843572; DOI=10.1091/mbc.9.12.3321;
RA Kanoh J., Russell P.;
RT "The protein kinase Cdr2, related to Nim1/Cdr1 mitotic inducer, regulates
RT the onset of mitosis in fission yeast.";
RL Mol. Biol. Cell 9:3321-3334(1998).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-311; SER-476;
RP SER-587 AND SER-632, AND 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).
RN [5]
RP SUBCELLULAR LOCATION, FUNCTION, AND INTERACTION WITH BLT1 AND MID1.
RX PubMed=19474789; DOI=10.1038/nature08074;
RA Moseley J.B., Mayeux A., Paoletti A., Nurse P.;
RT "A spatial gradient coordinates cell size and mitotic entry in fission
RT yeast.";
RL Nature 459:857-860(2009).
CC -!- FUNCTION: Acts as a mitotic inducer. In G2 it negatively regulates
CC wee1, a mitotic inhibitor. Also has a role in cytokinesis where it
CC required for proper septum formation. {ECO:0000269|PubMed:19474789,
CC ECO:0000269|PubMed:9843572, ECO:0000269|PubMed:9843577}.
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 -!- SUBUNIT: Interacts with blt1 and mid1. {ECO:0000269|PubMed:19474789}.
CC -!- INTERACTION:
CC P87050; Q09690: pom1; NbExp=2; IntAct=EBI-4319869, EBI-4319163;
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:18257517}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK Ser/Thr
CC protein kinase family. NIM1 subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAB08165.1; -; Genomic_DNA.
DR EMBL; AF092508; AAC72832.1; -; Genomic_DNA.
DR PIR; T38929; T38929.
DR RefSeq; NP_593307.1; NM_001018737.2.
DR AlphaFoldDB; P87050; -.
DR SMR; P87050; -.
DR BioGRID; 278087; 67.
DR DIP; DIP-59761N; -.
DR IntAct; P87050; 3.
DR STRING; 4896.SPAC57A10.02.1; -.
DR iPTMnet; P87050; -.
DR MaxQB; P87050; -.
DR PaxDb; P87050; -.
DR PRIDE; P87050; -.
DR EnsemblFungi; SPAC57A10.02.1; SPAC57A10.02.1:pep; SPAC57A10.02.
DR GeneID; 2541590; -.
DR KEGG; spo:SPAC57A10.02; -.
DR PomBase; SPAC57A10.02; cdr2.
DR VEuPathDB; FungiDB:SPAC57A10.02; -.
DR eggNOG; KOG0588; Eukaryota.
DR HOGENOM; CLU_019531_0_0_1; -.
DR InParanoid; P87050; -.
DR OMA; QAQHLLY; -.
DR PhylomeDB; P87050; -.
DR BRENDA; 2.7.11.1; 5613.
DR PRO; PR:P87050; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0110115; C:Cdr2 medial cortical node complex; IDA:PomBase.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0071341; C:medial cortical node; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IGI:PomBase.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0031569; P:mitotic G2 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:0120047; P:positive regulation of protein localization to medial cortical node; IMP:PomBase.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR Gene3D; 3.30.310.220; -; 1.
DR InterPro; IPR031850; Fungal_KA1_dom.
DR InterPro; IPR043024; KA1_sf_fungal.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF16797; Fungal_KA1; 1.
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 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..775
FT /note="Mitosis inducer protein kinase cdr2"
FT /id="PRO_0000085845"
FT DOMAIN 10..262
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 549..620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 549..593
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..618
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 133
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 16..24
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 39
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 587
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 775 AA; 85972 MW; 2EE2EECABC8A4FAC CRC64;
MSTISEVGPW ELGLSLGSGG PNSSRLAKHR ETGQLAVVKP IVGWSELTSS QQARIEGELV
LLRLIEHPNV LQLIDVISAQ EQLFVVVEYM PGGELFDCML RKGSFTEQDT AKFLWQILCG
LEYCHKLHIC HRDLKPENLY LDAHGSIKIG EFGMASIQQP GKLLQTSCGS PHYASPEIIM
GRSYDGCASD IWSCGIIFFA LLTGKLPFDD DNIRSLLLKV CQGQFEMPSN ISPQAQHLLY
RMLDVDSSTR ITMEQIREHP FLSCFVHPNI SIPIISAPIQ PIDPLIVQHL SLVFRCSDDP
MPLYEKLASQ SPLVEKTLYT LLSRHLHPPS SAAVDRNRAV VDDLLGTAAS NGQQMDEEEI
EQAINIPTLA PYPISYAAES VPRPATSASP FLTPVTTSGT FNYSFNATNP QSILQRPATT
SSAVPQLPKS VTPGLAYPHD SSMLSSNYRP PSALSPRNFN VSINDPEVQL SRRATSLDMS
NDFRMNENDP SIVGNLAASN FPTGMGPPRK RVTSRMSEHT GNRVVSFPRG SAFNPRVTRF
NVGNEQFSNN IDNNNYNQPY ANATMNNSRR LRTPSGERSM RADLSQSPAS YDSLNVPKHR
RRQSLFSPSS TKKKLSGSPF QPKRSFLRRL FSSEPSCKCV YASLVASELE HEILEVLRRW
QLLGIGIADI IYDSVSASIS ARIKRQNSLN LKPVRFRISV LAEFFGSQAV FVLESGSSTT
FDHLATEFQL IFEDKGFLDN LELSYFQASA SRPVSRMSVS SSPFAVFRQR QSVQS
