SID2_SCHPO
ID SID2_SCHPO Reviewed; 607 AA.
AC Q09898;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Serine/threonine-protein kinase sid2;
DE EC=2.7.11.1;
GN Name=sid2; ORFNames=SPAC24B11.11c;
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 [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 [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=10459013; DOI=10.1083/jcb.146.4.777;
RA Sparks C.A., Morphew M., McCollum D.;
RT "Sid2p, a spindle pole body kinase that regulates the onset of
RT cytokinesis.";
RL J. Cell Biol. 146:777-790(1999).
RN [3]
RP INTERACTION WITH MOB1.
RX PubMed=10769201; DOI=10.1242/jcs.113.10.1695;
RA Salimova E., Sohrmann M., Fournier N., Simanis V.;
RT "The S. pombe orthologue of the S. cerevisiae mob1 gene is essential and
RT functions in signalling the onset of septum formation.";
RL J. Cell Sci. 113:1695-1704(2000).
RN [4]
RP INTERACTION WITH CDC11.
RX PubMed=15062098; DOI=10.1016/j.cub.2004.03.036;
RA Morrell J.L., Tomlin G.C., Rajagopalan S., Venkatram S., Feoktistova A.S.,
RA Tasto J.J., Mehta S., Jennings J.L., Link A., Balasubramanian M.K.,
RA Gould K.L.;
RT "Sid4p-Cdc11p assembles the septation initiation network and its regulators
RT at the S. pombe SPB.";
RL Curr. Biol. 14:579-584(2004).
RN [5]
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-56; SER-60; SER-65; SER-86
RP AND SER-402, 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).
CC -!- FUNCTION: Part of a signaling pathway. Required for initiation of
CC medial ring constriction and septation. {ECO:0000269|PubMed:10459013}.
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 mob1 and cdc11. {ECO:0000269|PubMed:10769201,
CC ECO:0000269|PubMed:15062098}.
CC -!- INTERACTION:
CC Q09898; O94360: mob1; NbExp=3; IntAct=EBI-1563447, EBI-1563433;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Cytoplasm.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
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DR EMBL; CU329670; CAA91776.1; -; Genomic_DNA.
DR PIR; S62556; S62556.
DR RefSeq; NP_592848.1; NM_001018249.2.
DR AlphaFoldDB; Q09898; -.
DR SMR; Q09898; -.
DR BioGRID; 278096; 64.
DR IntAct; Q09898; 1.
DR STRING; 4896.SPAC24B11.11c.1; -.
DR iPTMnet; Q09898; -.
DR MaxQB; Q09898; -.
DR PaxDb; Q09898; -.
DR PRIDE; Q09898; -.
DR EnsemblFungi; SPAC24B11.11c.1; SPAC24B11.11c.1:pep; SPAC24B11.11c.
DR GeneID; 2541599; -.
DR KEGG; spo:SPAC24B11.11c; -.
DR PomBase; SPAC24B11.11c; sid2.
DR VEuPathDB; FungiDB:SPAC24B11.11c; -.
DR eggNOG; KOG0605; Eukaryota.
DR HOGENOM; CLU_000288_67_4_1; -.
DR InParanoid; Q09898; -.
DR OMA; KPQYEDP; -.
DR PhylomeDB; Q09898; -.
DR PRO; PR:Q09898; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0110085; C:mitotic actomyosin contractile ring; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
DR GO; GO:0034973; C:Sid2-Mob1 complex; IPI:PomBase.
DR GO; GO:0005816; C:spindle pole body; IBA:GO_Central.
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; IDA:PomBase.
DR GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR GO; GO:0061163; P:endoplasmic reticulum polarization; IMP:PomBase.
DR GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR GO; GO:0044878; P:mitotic cytokinesis checkpoint signaling; IMP:PomBase.
DR GO; GO:2000250; P:negative regulation of actin cytoskeleton reorganization; IMP:PomBase.
DR GO; GO:0032091; P:negative regulation of protein binding; IMP:PomBase.
DR GO; GO:0140325; P:negative regulation of protein localization to medial cortex; EXP:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0010971; P:positive regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1903473; P:positive regulation of mitotic actomyosin contractile ring contraction; IMP:PomBase.
DR GO; GO:1902846; P:positive regulation of mitotic spindle elongation; IMP:PomBase.
DR GO; GO:1902854; P:positive regulation of nuclear migration during mitotic telophase; IMP:PomBase.
DR GO; GO:1905758; P:positive regulation of primary cell septum biogenesis; IMP:PomBase.
DR GO; GO:0031028; P:septation initiation signaling; IMP:PomBase.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR017892; Pkinase_C.
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 Pfam; PF00433; Pkinase_C; 1.
DR SMART; SM00133; S_TK_X; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 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; Cytoskeleton; Kinase;
KW Mitosis; Nucleotide-binding; Phosphoprotein; Reference proteome; Septation;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..607
FT /note="Serine/threonine-protein kinase sid2"
FT /id="PRO_0000086654"
FT DOMAIN 208..508
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 509..589
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 93..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 331
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 214..222
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 65
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 219
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 402
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 607 AA; 70492 MW; D92E5263C7341F1D CRC64;
MNRVNDMSPV EGDLGLQLSS EADKKFDAYM KRHGLFEPGN LSNNDKERNL EDQFNSMKLS
PVASSKENYP DNHMHSKHIS KLPIASPIPR GLDRSGELSY KDNNHWSDRS STGSPRWENG
SMNLSVEEME KVVQPKVKRM ATICQMFFLD HYFEQLHYLY TRKQRARLFE EQLLKEPDSR
RDELVKRYNG RERVYLRKRR TRISHGDFQT ITQVGQGGYG SVWLARKRDT KEIVALKIMN
KSVLHKMDEI RHVLTERDIL TTANSEWLVR LLYAFQDTSN IYLAMEFVPG GDFRTLLSNS
GVLRDHHAKF YATEMFLAID ALHQLGYIHR DLKPENFLVG ASGHIKLTDF GLSSGIISKK
KIESMKIRLQ EVNNVVVPER SMRERRQVFR TLLSQDPVYA HSVVGSPDYM APEVLRGENY
NHSVDYWSLG CIMYECLSGF PPFSGSNVNE TWSNLKNWRK CFQRPHYDDP RDLEFNWRDD
AWDFVCHCIT DPKDRFCSLK QVMQHPYFSK IDWKNVRTAY RPPFVPDLNS EIDAGYFDDF
TNENDMSKYK EVHEKQAAIA NMVNTFNKPK RNAFIGFTFR HQKNSHPTSS SSALSSPLSA
PSFGTLL
