POM1_SCHPO
ID POM1_SCHPO Reviewed; 1087 AA.
AC Q09690;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=DYRK-family kinase pom1;
DE EC=2.7.12.1 {ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772};
GN Name=pom1 {ECO:0000303|PubMed:9573052}; ORFNames=SPAC2F7.03c;
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.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9573052; DOI=10.1101/gad.12.9.1356;
RA Baehler J., Pringle J.R.;
RT "Pom1p, a fission yeast protein kinase that provides positional information
RT for both polarized growth and cytokinesis.";
RL Genes Dev. 12:1356-1370(1998).
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11230130; DOI=10.1093/emboj/20.5.1064;
RA Baehler J., Nurse P.;
RT "Fission yeast Pom1p kinase activity is cell cycle regulated and essential
RT for cellular symmetry during growth and division.";
RL EMBO J. 20:1064-1073(2001).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11950884; DOI=10.1242/jcs.115.8.1651;
RA Niccoli T., Nurse P.;
RT "Different mechanisms of cell polarisation in vegetative and shmooing
RT growth in fission yeast.";
RL J. Cell Sci. 115:1651-1662(2002).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=14663827; DOI=10.1002/yea.1054;
RA Niccoli T., Arellano M., Nurse P.;
RT "Role of Tea1p, Tea3p and Pom1p in the determination of cell ends in
RT Schizosaccharomyces pombe.";
RL Yeast 20:1349-1358(2003).
RN [6]
RP FUNCTION.
RX PubMed=17140794; DOI=10.1016/j.cub.2006.11.024;
RA Padte N.N., Martin S.G., Howard M., Chang F.;
RT "The cell-end factor pom1p inhibits mid1p in specification of the cell
RT division plane in fission yeast.";
RL Curr. Biol. 16:2480-2487(2006).
RN [7]
RP FUNCTION.
RX PubMed=16988828; DOI=10.1007/s00294-006-0099-5;
RA La Carbona S., Le Goff X.;
RT "Spatial regulation of cytokinesis by the Kin1 and Pom1 kinases in fission
RT yeast.";
RL Curr. Genet. 50:377-391(2006).
RN [8]
RP FUNCTION.
RX PubMed=17077120; DOI=10.1242/jcs.03261;
RA Celton-Morizur S., Racine V., Sibarita J.B., Paoletti A.;
RT "Pom1 kinase links division plane position to cell polarity by regulating
RT Mid1p cortical distribution.";
RL J. Cell Sci. 119:4710-4718(2006).
RN [9]
RP FUNCTION.
RX PubMed=17543869; DOI=10.1016/j.devcel.2007.03.015;
RA Huang Y., Chew T.G., Ge W., Balasubramanian M.K.;
RT "Polarity determinants Tea1p, Tea4p, and Pom1p inhibit division-septum
RT assembly at cell ends in fission yeast.";
RL Dev. Cell 12:987-996(2007).
RN [10]
RP FUNCTION, AND INTERACTION WITH RGA4.
RX PubMed=18328707; DOI=10.1016/j.cub.2008.02.005;
RA Tatebe H., Nakano K., Maximo R., Shiozaki K.;
RT "Pom1 DYRK regulates localization of the Rga4 GAP to ensure bipolar
RT activation of Cdc42 in fission yeast.";
RL Curr. Biol. 18:322-330(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND IDENTIFICATION BY
RP 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 [12]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=19474792; DOI=10.1038/nature08054;
RA Martin S.G., Berthelot-Grosjean M.;
RT "Polar gradients of the DYRK-family kinase Pom1 couple cell length with the
RT cell cycle.";
RL Nature 459:852-856(2009).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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).
RN [14]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND INTERACTION WITH TEA4.
RX PubMed=21703453; DOI=10.1016/j.cell.2011.05.014;
RA Hachet O., Berthelot-Grosjean M., Kokkoris K., Vincenzetti V.,
RA Moosbrugger J., Martin S.G.;
RT "A phosphorylation cycle shapes gradients of the DYRK family kinase Pom1 at
RT the plasma membrane.";
RL Cell 145:1116-1128(2011).
RN [15]
RP SUBCELLULAR LOCATION.
RX PubMed=22342545; DOI=10.1016/j.devcel.2012.01.001;
RA Saunders T.E., Pan K.Z., Angel A., Guan Y., Shah J.V., Howard M., Chang F.;
RT "Noise reduction in the intracellular pom1p gradient by a dynamic
RT clustering mechanism.";
RL Dev. Cell 22:558-572(2012).
RN [16]
RP FUNCTION.
RX PubMed=22684255; DOI=10.1038/ncb2514;
RA Grallert A., Connolly Y., Smith D.L., Simanis V., Hagan I.M.;
RT "The S. pombe cytokinesis NDR kinase Sid2 activates Fin1 NIMA kinase to
RT control mitotic commitment through Pom1/Wee1.";
RL Nat. Cell Biol. 14:738-745(2012).
RN [17]
RP FUNCTION.
RX PubMed=24047646; DOI=10.4161/cc.26462;
RA Wood E., Nurse P.;
RT "Pom1 and cell size homeostasis in fission yeast.";
RL Cell Cycle 12:3228-3236(2013).
RN [18]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24316795; DOI=10.4161/cc.27411;
RA Bhatia P., Hachet O., Hersch M., Rincon S.A., Berthelot-Grosjean M.,
RA Dalessi S., Basterra L., Bergmann S., Paoletti A., Martin S.G.;
RT "Distinct levels in Pom1 gradients limit Cdr2 activity and localization to
RT time and position division.";
RL Cell Cycle 13:538-552(2014).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=24508166; DOI=10.1016/j.cub.2014.01.009;
RA Deng L., Baldissard S., Kettenbach A.N., Gerber S.A., Moseley J.B.;
RT "Dueling kinases regulate cell size at division through the SAD kinase
RT Cdr2.";
RL Curr. Biol. 24:428-433(2014).
RN [20]
RP FUNCTION.
RX PubMed=24982431; DOI=10.1083/jcb.201311097;
RA Rincon S.A., Bhatia P., Bicho C., Guzman-Vendrell M., Fraisier V.,
RA Borek W.E., Alves F.L., Dingli F., Loew D., Rappsilber J., Sawin K.E.,
RA Martin S.G., Paoletti A.;
RT "Pom1 regulates the assembly of Cdr2-Mid1 cortical nodes for robust spatial
RT control of cytokinesis.";
RL J. Cell Biol. 206:61-77(2014).
RN [21]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=25720772; DOI=10.1074/mcp.m114.045245;
RA Kettenbach A.N., Deng L., Wu Y., Baldissard S., Adamo M.E., Gerber S.A.,
RA Moseley J.B.;
RT "Quantitative phosphoproteomics reveals pathways for coordination of cell
RT growth and division by the conserved fission yeast kinase pom1.";
RL Mol. Cell. Proteomics 14:1275-1287(2015).
RN [22]
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=26150232; DOI=10.15252/msb.20145996;
RA Hersch M., Hachet O., Dalessi S., Ullal P., Bhatia P., Bergmann S.,
RA Martin S.G.;
RT "Pom1 gradient buffering through intermolecular auto-phosphorylation.";
RL Mol. Syst. Biol. 11:818-818(2015).
CC -!- FUNCTION: Polarity factor involved in localization of polarized growth
CC and cytokinesis (PubMed:11230130, PubMed:11950884, PubMed:14663827,
CC PubMed:17077120). Forms an intracellular gradient that serves to
CC measure cell length and control mitotic entry (PubMed:19474792,
CC PubMed:19474789, PubMed:21703453, PubMed:24047646). Controls the timing
CC of mitotic commitment by regulating the inhibitory impact of cdr1/cdr2
CC on wee1 activity (PubMed:19474792, PubMed:22684255, PubMed:24316795).
CC Directly phosphorylates the tail of cdr2 which inhibits cdr2 activation
CC by ssp1 (PubMed:19474792, PubMed:24508166). Cdr2 phosphorylation by
CC pom1 also modulates cdr2 association with membranes and inhibits cdr2
CC interaction with mid1, reducing its clustering ability, possibly via
CC the down-regulation of cdr2 kinase activity (PubMed:24982431). Acts as
CC a negative regulator of mid1 distribution, excluding mid1 from non-
CC growing ends, which prevents division-septum assembly at the cell ends
CC (PubMed:17140794, PubMed:17077120, PubMed:17543869). The pom1 polar
CC gradient also mediates mitotic entry by regulating cdk1
CC (PubMed:19474789). Plays an essential role in proper localization and
CC phosphorylation of a GAP for cdc42, rga4, which ensures bipolar
CC localization of GTP-bound, active cdc42 involved in F-actin formation
CC (PubMed:18328707). Phosphorylates multiple other substrates that
CC function in polarized cell growth, including tea4, mod5, pal1, the Rho
CC GAP rga7, and the Arf GEF syt22 (PubMed:25720772).
CC {ECO:0000269|PubMed:11230130, ECO:0000269|PubMed:11950884,
CC ECO:0000269|PubMed:14663827, ECO:0000269|PubMed:16988828,
CC ECO:0000269|PubMed:17077120, ECO:0000269|PubMed:17140794,
CC ECO:0000269|PubMed:17543869, ECO:0000269|PubMed:18328707,
CC ECO:0000269|PubMed:19474789, ECO:0000269|PubMed:19474792,
CC ECO:0000269|PubMed:21703453, ECO:0000269|PubMed:22684255,
CC ECO:0000269|PubMed:24047646, ECO:0000269|PubMed:24316795,
CC ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:24982431,
CC ECO:0000269|PubMed:25720772, ECO:0000269|PubMed:9573052}.
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166,
CC ECO:0000269|PubMed:25720772};
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=2.7.12.1; Evidence={ECO:0000269|PubMed:19474792,
CC ECO:0000269|PubMed:24508166, ECO:0000269|PubMed:25720772};
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=2.7.12.1;
CC Evidence={ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:24508166,
CC ECO:0000269|PubMed:25720772};
CC -!- SUBUNIT: Interacts with rga4 (PubMed:18328707). Interacts with tea4;
CC this interaction triggers pom1 plasma membrane association
CC (PubMed:21703453). {ECO:0000269|PubMed:18328707,
CC ECO:0000269|PubMed:21703453}.
CC -!- INTERACTION:
CC Q09690; P87050: cdr2; NbExp=2; IntAct=EBI-4319163, EBI-4319869;
CC Q09690; O60132: tea4; NbExp=5; IntAct=EBI-4319163, EBI-1099982;
CC -!- SUBCELLULAR LOCATION: Cell tip {ECO:0000269|PubMed:11230130,
CC ECO:0000269|PubMed:11950884, ECO:0000269|PubMed:14663827}. Cell septum
CC {ECO:0000269|PubMed:14663827}. Cell membrane
CC {ECO:0000269|PubMed:21703453}; Peripheral membrane protein
CC {ECO:0000269|PubMed:21703453}. Note=Forms an intracellular gradient
CC that serves to measure cell length and control mitotic entry
CC (PubMed:19474792, PubMed:19474789, PubMed:21703453, PubMed:22342545,
CC PubMed:26150232). Localized to the septum at the time of cytokinesis
CC (PubMed:14663827). Tea4 recruits pom1 to the cell cortex from where it
CC then moves laterally at the plasma membrane, which it binds through a
CC basic region exhibiting direct lipid interaction (PubMed:21703453).
CC Pom1 autophosphorylates in this region to lower lipid affinity and
CC promote membrane release (PubMed:21703453). Tea4 triggers pom1 plasma
CC membrane association by promoting its dephosphorylation through the
CC protein phosphatase dis2 (PubMed:21703453).
CC {ECO:0000269|PubMed:14663827, ECO:0000269|PubMed:19474789,
CC ECO:0000269|PubMed:19474792, ECO:0000269|PubMed:21703453,
CC ECO:0000269|PubMed:22342545, ECO:0000269|PubMed:26150232}.
CC -!- PTM: Autophosphorylates at the cell cortex to lower lipid affinity and
CC promote membrane release (PubMed:21703453, PubMed:26150232).
CC Dephosphorylation by dis2, regulated by tea4, triggers membrane
CC association (PubMed:21703453). {ECO:0000269|PubMed:21703453,
CC ECO:0000269|PubMed:26150232}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. MNB/DYRK subfamily. {ECO:0000305}.
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DR EMBL; CU329670; CAA90490.1; -; Genomic_DNA.
DR PIR; S58147; S58147.
DR RefSeq; NP_592974.1; NM_001018374.2.
DR AlphaFoldDB; Q09690; -.
DR SMR; Q09690; -.
DR BioGRID; 278379; 202.
DR DIP; DIP-59764N; -.
DR ELM; Q09690; -.
DR IntAct; Q09690; 3.
DR STRING; 4896.SPAC2F7.03c.1; -.
DR iPTMnet; Q09690; -.
DR MaxQB; Q09690; -.
DR PaxDb; Q09690; -.
DR PRIDE; Q09690; -.
DR EnsemblFungi; SPAC2F7.03c.1; SPAC2F7.03c.1:pep; SPAC2F7.03c.
DR GeneID; 2541889; -.
DR KEGG; spo:SPAC2F7.03c; -.
DR PomBase; SPAC2F7.03c; pom1.
DR VEuPathDB; FungiDB:SPAC2F7.03c; -.
DR eggNOG; KOG0667; Eukaryota.
DR HOGENOM; CLU_009940_0_0_1; -.
DR InParanoid; Q09690; -.
DR OMA; MQQFINW; -.
DR PhylomeDB; Q09690; -.
DR Reactome; R-SPO-6804756; Regulation of TP53 Activity through Phosphorylation.
DR PRO; PR:Q09690; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0051285; C:cell cortex of cell tip; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0030428; C:cell septum; IEA:UniProtKB-SubCell.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IBA:GO_Central.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; EXP:PomBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:PomBase.
DR GO; GO:0120105; C:mitotic actomyosin contractile ring, intermediate layer; IDA:PomBase.
DR GO; GO:0030427; C:site of polarized growth; IDA:PomBase.
DR GO; GO:0005524; F:ATP binding; ISM:PomBase.
DR GO; GO:1901981; F:phosphatidylinositol phosphate binding; IDA: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:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:RHEA.
DR GO; GO:0051519; P:activation of bipolar cell growth; IMP:PomBase.
DR GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:PomBase.
DR GO; GO:0031569; P:mitotic G2 cell size control checkpoint signaling; IMP:PomBase.
DR GO; GO:1903138; P:negative regulation of cell wall integrity MAPK cascade; IMP:PomBase.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IMP:PomBase.
DR GO; GO:1903067; P:negative regulation of protein localization to cell tip; IMP:PomBase.
DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; IDA:PomBase.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0018107; P:peptidyl-threonine phosphorylation; IBA:GO_Central.
DR GO; GO:1903617; P:positive regulation of mitotic cytokinesis, site selection; IMP:PomBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; NAS:PomBase.
DR GO; GO:2000769; P:regulation of establishment or maintenance of cell polarity regulating cell shape; IMP:PomBase.
DR Gene3D; 3.30.10.30; -; 1.
DR InterPro; IPR042521; DYRK.
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 membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Transferase.
FT CHAIN 1..1087
FT /note="DYRK-family kinase pom1"
FT /id="PRO_0000086579"
FT DOMAIN 699..995
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 57..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 120..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 238..308
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..578
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1017..1056
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..308
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..379
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..444
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..525
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..578
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1056
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 825
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 705..713
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 728
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1087 AA; 121146 MW; 3277E7CA840F8BE2 CRC64;
MGYLQSQKAV SLGDENTDAL FKLHTSNRKS ANMFGIKSEL LNPSELSAVG SYSNDICPNR
QSSSSTAADT SPSTNASNTN ISFPEQEHKD ELFMNVEPKG VGSSMDNHAI TIHHSTGNGL
LRSSFDHDYR QKNSPRNSIH RLSNISIGNN PIDFESSQQN NPSSLNTSSH HRTSSISNSK
SFGTSLSYYN RSSKPSDWNQ QNNGGHLSGV ISITQDVSSV PLQSSVFSSG NHAYHASMAP
KRSGSWRHTN FHSTSHPRAA SIGNKSGIPP VPTIPPNIGH STDHQHPKAN ISGSLTKSSS
ESKNLSTIQS PLKTSNSFFK ELSPHSQITL SNVKNNHSHV GSQTKSHSFA TPSVFDNNKP
VSSDNHNNTT TSSQVHPDSR NPDPKAAPKA VSQKTNVDGH RNHEAKHGNT VQNESKSQKS
SNKEGRSSRG GFFSRLSFSR SSSRMKKGSK AKHEDAPDVP AIPHAYIADS STKSSYRNGK
KTPTRTKSRM QQFINWFKPS KERSSNGNSD SASPPPVPRL SITRSQVSRE PEKPEEIPSV
PPLPSNFKDK GHVPQQRSVS YTPKRSSDTS ESLQPSLSFA SSNVLSEPFD RKVADLAMKA
INSKRINKLL DDAKVMQSLL DRACIITPVR NTEVQLINTA PLTEYEQDEI NNYDNIYFTG
LRNVDKRRSA DENTSSNFGF DDERGDYKVV LGDHIAYRYE VVDFLGKGSF GQVLRCIDYE
TGKLVALKII RNKKRFHMQA LVETKILQKI REWDPLDEYC MVQYTDHFYF RDHLCVATEL
LGKNLYELIK SNGFKGLPIV VIKSITRQLI QCLTLLNEKH VIHCDLKPEN ILLCHPFKSQ
VKVIDFGSSC FEGECVYTYI QSRFYRSPEV ILGMGYGTPI DVWSLGCIIA EMYTGFPLFP
GENEQEQLAC IMEIFGPPDH SLIDKCSRKK VFFDSSGKPR PFVSSKGVSR RPFSKSLHQV
LQCKDVSFLS FISDCLKWDP DERMTPQQAA QHDFLTGKQD VRRPNTAPAR QKFARPPNIE
TAPIPRPLPN LPMEYNDHTL PSPKEPSNQA SNLVRSSDKF PNLLTNLDYS IISDNGFLRK
PVEKSRP
