ID   NPR1_YEAST              Reviewed;         790 AA.
AC   P22211; D6W103;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   27-MAR-2024, entry version 201.
DE   RecName: Full=Nitrogen permease reactivator protein;
DE            EC=2.7.11.1;
DE   AltName: Full=Serine/threonine-protein kinase NPR1;
GN   Name=NPR1; OrderedLocusNames=YNL183C; ORFNames=N1631;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Sigma 1278B;
RX   PubMed=2125693; DOI=10.1007/bf00633845;
RA   Vandenbol M., Jauniaux J.-C., Grenson M.;
RT   "The Saccharomyces cerevisiae NPR1 gene required for the activity of
RT   ammonia-sensitive amino acid permeases encodes a protein kinase
RT   homologue.";
RL   Mol. Gen. Genet. 222:393-399(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169873;
RA   Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA   Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA   Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA   Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA   Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA   Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA   Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA   Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA   Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA   Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA   Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA   Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA   Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA   Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA   Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA   Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA   Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT   evolutionary implications.";
RL   Nature 387:93-98(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   PROTEIN SEQUENCE OF 45-60; 63-120; 123-147; 255-269; 273-296; 315-362 AND
RP   368-403, PHOSPHORYLATION AT SER-47; SER-85; SER-90; SER-100; SER-111;
RP   SER-116; SER-125; SER-137; SER-141; SER-257; SER-259; SER-260; SER-288;
RP   SER-292; SER-317; SER-320; SER-328; SER-336; SER-353; SER-356; SER-357 AND
RP   SER-385, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-47;
RP   SER-257 AND SER-357.
RX   PubMed=18980262; DOI=10.1002/rcm.3790;
RA   Gander S., Bonenfant D., Altermatt P., Martin D.E., Hauri S., Moes S.,
RA   Hall M.N., Jenoe P.;
RT   "Identification of the rapamycin-sensitive phosphorylation sites within the
RT   Ser/Thr-rich domain of the yeast Npr1 protein kinase.";
RL   Rapid Commun. Mass Spectrom. 22:3743-3753(2008).
RN   [5]
RP   FUNCTION.
RX   PubMed=6343084; DOI=10.1111/j.1432-1033.1983.tb07439.x;
RA   Grenson M.;
RT   "Study of the positive control of the general amino-acid permease and other
RT   ammonia-sensitive uptake systems by the product of the NPR1 gene in the
RT   yeast Saccharomyces cerevisiae.";
RL   Eur. J. Biochem. 133:141-144(1983).
RN   [6]
RP   FUNCTION.
RX   PubMed=9843498; DOI=10.1093/emboj/17.23.6924;
RA   Schmidt A., Beck T., Koller A., Kunz J., Hall M.N.;
RT   "The TOR nutrient signalling pathway phosphorylates NPR1 and inhibits
RT   turnover of the tryptophan permease.";
RL   EMBO J. 17:6924-6931(1998).
RN   [7]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11500493; DOI=10.1074/jbc.m102944200;
RA   De Craene J.-O., Soetens O., Andre B.;
RT   "The Npr1 kinase controls biosynthetic and endocytic sorting of the yeast
RT   Gap1 permease.";
RL   J. Biol. Chem. 276:43939-43948(2001).
RN   [8]
RP   INTERACTION WITH TIP41.
RX   PubMed=11741537; DOI=10.1016/s1097-2765(01)00386-0;
RA   Jacinto E., Guo B., Arndt K.T., Schmelzle T., Hall M.N.;
RT   "TIP41 interacts with TAP42 and negatively regulates the TOR signaling
RT   pathway.";
RL   Mol. Cell 8:1017-1026(2001).
RN   [9]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [10]
RP   FUNCTION.
RX   PubMed=15247235; DOI=10.1074/jbc.m407372200;
RA   Crespo J.L., Helliwell S.B., Wiederkehr C., Demougin P., Fowler B.,
RA   Primig M., Hall M.N.;
RT   "NPR1 kinase and RSP5-BUL1/2 ubiquitin ligase control GLN3-dependent
RT   transcription in Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 279:37512-37517(2004).
RN   [11]
RP   FUNCTION.
RX   PubMed=16864574; DOI=10.1074/jbc.m605551200;
RA   Feller A., Boeckstaens M., Marini A.-M., Dubois E.;
RT   "Transduction of the nitrogen signal activating Gln3-mediated transcription
RT   is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in
RT   Saccharomyces cerevisiae.";
RL   J. Biol. Chem. 281:28546-28554(2006).
RN   [12]
RP   FUNCTION.
RX   PubMed=16864577; DOI=10.1074/jbc.m604171200;
RA   Tate J.J., Rai R., Cooper T.G.;
RT   "Ammonia-specific regulation of Gln3 localization in Saccharomyces
RT   cerevisiae by protein kinase Npr1.";
RL   J. Biol. Chem. 281:28460-28469(2006).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125 AND SER-357, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ADR376;
RX   PubMed=17330950; DOI=10.1021/pr060559j;
RA   Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA   Elias J.E., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of alpha-factor-arrested
RT   Saccharomyces cerevisiae.";
RL   J. Proteome Res. 6:1190-1197(2007).
RN   [14]
RP   FUNCTION.
RX   PubMed=17493133; DOI=10.1111/j.1365-2958.2007.05681.x;
RA   Boeckstaens M., Andre B., Marini A.M.;
RT   "The yeast ammonium transport protein Mep2 and its positive regulator, the
RT   Npr1 kinase, play an important role in normal and pseudohyphal growth on
RT   various nitrogen media through retrieval of excreted ammonium.";
RL   Mol. Microbiol. 64:534-546(2007).
RN   [15]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA   Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT   "A multidimensional chromatography technology for in-depth phosphoproteome
RT   analysis.";
RL   Mol. Cell. Proteomics 7:1389-1396(2008).
RN   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-137; SER-141 AND
RP   TYR-334, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19779198; DOI=10.1126/science.1172867;
RA   Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT   "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT   into evolution.";
RL   Science 325:1682-1686(2009).
CC   -!- FUNCTION: Nutrient-regulated protein kinase that promotes the activity
CC       of at least 6 distinct transport systems for nitrogenous nutrients
CC       under conditions of nitrogen catabolite derepression. Under poor
CC       nitrogen growth conditions, required for post-Golgi sorting of the
CC       general amino acid permease GAP1 and the three known ammonia permeases,
CC       MEP1/2/3, to the plasma membrane. Contributes also to the stability and
CC       the retention of GAP1 at the plasma membrane. Inversely, promotes the
CC       degradation of tryptophan permease TAT2 under the same conditions.
CC       Activity is regulated by the TOR signaling pathway via phosphatase
CC       SIT4. Although thought to be involved in regulation of GLN3-dependent
CC       transcription by nitrogen catabolite repression, this seems to be an
CC       indirect effect from the reduced uptake of the nitrogen-repressing
CC       compound. {ECO:0000269|PubMed:11500493, ECO:0000269|PubMed:15247235,
CC       ECO:0000269|PubMed:16864574, ECO:0000269|PubMed:16864577,
CC       ECO:0000269|PubMed:17493133, ECO:0000269|PubMed:6343084,
CC       ECO:0000269|PubMed:9843498}.
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   -!- ACTIVITY REGULATION: Dephosphorylation by SIT4 activates NPR1 kinase
CC       activity.
CC   -!- SUBUNIT: Interacts with TIP41. {ECO:0000269|PubMed:11741537}.
CC   -!- INTERACTION:
CC       P22211; P15442: GCN2; NbExp=2; IntAct=EBI-12207, EBI-330;
CC       P22211; P06782: SNF1; NbExp=2; IntAct=EBI-12207, EBI-17516;
CC       P22211; P35169: TOR1; NbExp=2; IntAct=EBI-12207, EBI-19374;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11500493}.
CC       Note=Appears to be more concentrated in punctate structures reminiscent
CC       of the Golgi or of an endosomal compartment.
CC   -!- PTM: Hyperphosphorylated in nitrogen-rich growth medium. Nitrogen
CC       limitation (or rapamycin treatment) leads to substantial, though not
CC       complete dephosphorylation. Autophosphorylation plays only a minor role
CC       and seems not to be regulated by the quality of the nitrogen source.
CC       {ECO:0000269|PubMed:18980262}.
CC   -!- MISCELLANEOUS: Present with 284 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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; X56084; CAA39564.1; -; Genomic_DNA.
DR   EMBL; Z71459; CAA96076.1; -; Genomic_DNA.
DR   EMBL; BK006947; DAA10369.1; -; Genomic_DNA.
DR   PIR; S63138; S63138.
DR   RefSeq; NP_014216.1; NM_001183021.1.
DR   AlphaFoldDB; P22211; -.
DR   SMR; P22211; -.
DR   BioGRID; 35649; 175.
DR   DIP; DIP-4327N; -.
DR   IntAct; P22211; 54.
DR   MINT; P22211; -.
DR   STRING; 4932.YNL183C; -.
DR   GlyGen; P22211; 12 sites, 1 O-linked glycan (12 sites).
DR   iPTMnet; P22211; -.
DR   MaxQB; P22211; -.
DR   PaxDb; 4932-YNL183C; -.
DR   PeptideAtlas; P22211; -.
DR   EnsemblFungi; YNL183C_mRNA; YNL183C; YNL183C.
DR   GeneID; 855538; -.
DR   KEGG; sce:YNL183C; -.
DR   AGR; SGD:S000005127; -.
DR   SGD; S000005127; NPR1.
DR   VEuPathDB; FungiDB:YNL183C; -.
DR   eggNOG; KOG0590; Eukaryota.
DR   GeneTree; ENSGT00940000176633; -.
DR   HOGENOM; CLU_000288_82_4_1; -.
DR   InParanoid; P22211; -.
DR   OMA; LQVMEYC; -.
DR   OrthoDB; 5318028at2759; -.
DR   BioCyc; YEAST:G3O-33194-MONOMER; -.
DR   BRENDA; 2.7.11.1; 984.
DR   BioGRID-ORCS; 855538; 1 hit in 13 CRISPR screens.
DR   PRO; PR:P22211; -.
DR   Proteomes; UP000002311; Chromosome XIV.
DR   RNAct; P22211; Protein.
DR   GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR   GO; GO:0005829; C:cytosol; HDA:SGD.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:SGD.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:SGD.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0045806; P:negative regulation of endocytosis; IMP:SGD.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0090153; P:regulation of sphingolipid biosynthetic process; IMP:SGD.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 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   PANTHER; PTHR24343:SF113; NITROGEN PERMEASE REACTIVATOR PROTEIN; 1.
DR   PANTHER; PTHR24343; SERINE/THREONINE KINASE; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 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; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Serine/threonine-protein kinase; Transferase.
FT   CHAIN           1..790
FT                   /note="Nitrogen permease reactivator protein"
FT                   /id="PRO_0000086445"
FT   DOMAIN          438..742
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..188
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          234..258
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          276..357
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          666..704
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          766..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..356
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        676..690
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        561
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         444..452
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         467
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         47
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         90
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         100
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         111
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         116
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         125
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262,
FT                   ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198"
FT   MOD_RES         137
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         141
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262,
FT                   ECO:0007744|PubMed:19779198"
FT   MOD_RES         257
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         259
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         260
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         288
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         317
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         320
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         328
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         334
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:19779198"
FT   MOD_RES         336
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         353
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         356
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MOD_RES         357
FT                   /note="Phosphoserine; by autocatalysis"
FT                   /evidence="ECO:0000269|PubMed:18980262,
FT                   ECO:0007744|PubMed:17330950"
FT   MOD_RES         385
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MUTAGEN         47
FT                   /note="S->A: Abolishes autophosphorylation; when associated
FT                   with A-257 and A-357."
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MUTAGEN         257
FT                   /note="S->A: Abolishes autophosphorylation; when associated
FT                   with A-47 and A-357."
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MUTAGEN         257
FT                   /note="S->D: Abolishes autophosphorylation."
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   MUTAGEN         357
FT                   /note="S->A: Abolishes autophosphorylation; when associated
FT                   with A-47 and A-257."
FT                   /evidence="ECO:0000269|PubMed:18980262"
FT   CONFLICT        154
FT                   /note="T -> A (in Ref. 1; CAA39564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        277
FT                   /note="S -> P (in Ref. 1; CAA39564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   790 AA;  85990 MW;  0ECFA33376740733 CRC64;
     MSSLTRLLQE KRKNETSNSS PRTSADTLTT TPESQSLDLH SRNKSSSHIG SVSNSSSSDR
     NRANVPVPGS VTTVTQIYSE EDSSSTAGSS LDDRNQFSSS FLNANFAHTA SFYGTSAQSR
     DRFGSLINDQ GTAGLSSHGG SFAAQNRITS RLSTTSHTSG RAIPSLSSSI PYSVPNSNKD
     NNSSNSNSSS LSSSWLETYA GGMPNNISAI DSNVISSPKV DSVEPRFVIS KQKLQKASMD
     SNNANATQSR SISRSGSFSS QLGNFFFSKN SKESSNSNSA GMSFSANSNG PSPNIKNPNV
     TNGSTPIPKP IRARQSSIYS ASRQPTGSYT DNFYGSPSSV HDHLPPSQSV PRSQHSSIGD
     LKRFFKKSSN SNLSSNSNNV IPNGSPLSSG IAVPSHSHSS SHFAAGNNSY STSYNGNGDT
     IYSHSHGGSG IPFSKRYIKT GADLGAGAGG SVKLAQRISD NKIFAVKEFR TKFENESKRD
     YVKKITSEYC IGTTLNHPNI IETIEIVYEN DRILQVMEYC EYDLFAIVMS NKMSYEEICC
     CFKQILTGVQ YLHSIGLAHR DLKLDNCVIN EKGIVKLIDF GAAVVFSYPF SKNLVEASGI
     VGSDPYLAPE VCIFAKYDPR PVDIWSSAII FACMILKKFP WKIPKLRDNS FKLFCSGRDC
     DSLSSLVTRT PDPPSYDESH STEKKKPESS SNNVSDPNNV NIGPQRLLHS LPEETQHIVG
     RMIDLAPACR GNIEEIMEDP WIRSIDMCHL VEDGLSFKVV RGEDHHHTQV DQSEAHIAGL
     EKKKKKQNNQ
//