ID   BRSK1_HUMAN             Reviewed;         778 AA.
AC   Q8TDC3; F1DG44; Q5J5B5; Q8NDD0; Q8NDR4; Q8TDC2; Q96AV4; Q96JL4;
DT   29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   11-NOV-2015, entry version 135.
DE   RecName: Full=Serine/threonine-protein kinase BRSK1;
DE            EC=2.7.11.1;
DE   AltName: Full=Brain-selective kinase 1;
DE            EC=2.7.11.26;
DE   AltName: Full=Brain-specific serine/threonine-protein kinase 1;
DE            Short=BR serine/threonine-protein kinase 1;
DE   AltName: Full=Serine/threonine-protein kinase SAD-B;
DE   AltName: Full=Synapses of Amphids Defective homolog 1;
DE            Short=SAD1 homolog;
DE            Short=hSAD1;
GN   Name=BRSK1; Synonyms=KIAA1811, SAD1, SADB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ENZYME REGULATION,
RP   PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF THR-189.
RX   PubMed=14976552; DOI=10.1038/sj.emboj.7600110;
RA   Lizcano J.M., Goeransson O., Toth R., Deak M., Morrice N.A.,
RA   Boudeau J., Hawley S.A., Udd L., Maekelae T.P., Hardie D.G.,
RA   Alessi D.R.;
RT   "LKB1 is a master kinase that activates 13 kinases of the AMPK
RT   subfamily, including MARK/PAR-1.";
RL   EMBO J. 23:833-843(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR
RP   LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-59.
RC   TISSUE=Testis;
RX   PubMed=15150265; DOI=10.1074/jbc.M404728200;
RA   Lu R., Niida H., Nakanishi M.;
RT   "Human SAD1 kinase is involved in UV-induced DNA damage checkpoint
RT   function.";
RL   J. Biol. Chem. 279:31164-31170(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX   PubMed=16630837; DOI=10.1016/j.neuron.2006.03.018;
RA   Inoue E., Mochida S., Takagi H., Higa S., Deguchi-Tawarada M.,
RA   Takao-Rikitsu E., Inoue M., Yao I., Takeuchi K., Kitajima I.,
RA   Setou M., Ohtsuka T., Takai Y.;
RT   "SAD: a presynaptic kinase associated with synaptic vesicles and the
RT   active zone cytomatrix that regulates neurotransmitter release.";
RL   Neuron 50:261-275(2006).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX   PubMed=19648910; DOI=10.1038/ncb1921;
RA   Alvarado-Kristensson M., Rodriguez M.J., Silio V., Valpuesta J.M.,
RA   Carrera A.C.;
RT   "SADB phosphorylation of gamma-tubulin regulates centrosome
RT   duplication.";
RL   Nat. Cell Biol. 11:1081-1092(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Brain;
RA   She X.Y., Yu L., Guo J.H.;
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA   Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA   Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA   Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA   Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA   Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA   Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA   Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA   Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA   Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA   Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA   Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA   Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA   Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA   Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 35-778.
RC   TISSUE=Brain;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 64-778.
RC   TISSUE=Brain;
RX   PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA   Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XX.
RT   The complete sequences of 100 new cDNA clones from brain which code
RT   for large proteins in vitro.";
RL   DNA Res. 8:85-95(2001).
RN   [9]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 287-778.
RC   TISSUE=Lymph;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [10]
RP   PHOSPHORYLATION AT THR-189, AND MUTAGENESIS OF GLY-327.
RX   PubMed=18339622; DOI=10.1074/jbc.M710381200;
RA   Bright N.J., Carling D., Thornton C.;
RT   "Investigating the regulation of brain-specific kinases 1 and 2 by
RT   phosphorylation.";
RL   J. Biol. Chem. 283:14946-14954(2008).
RN   [11]
RP   PHOSPHORYLATION.
RX   PubMed=19958286; DOI=10.1042/BJ20091372;
RA   Fogarty S., Hawley S.A., Green K.A., Saner N., Mustard K.J.,
RA   Hardie D.G.;
RT   "Calmodulin-dependent protein kinase kinase-beta activates AMPK
RT   without forming a stable complex: synergistic effects of Ca2+ and
RT   AMP.";
RL   Biochem. J. 426:109-118(2010).
RN   [12]
RP   FUNCTION.
RX   PubMed=20026642; DOI=10.1242/jcs.058230;
RA   Muller M., Lutter D., Puschel A.W.;
RT   "Persistence of the cell-cycle checkpoint kinase Wee1 in SadA- and
RT   SadB-deficient neurons disrupts neuronal polarity.";
RL   J. Cell Sci. 123:286-294(2010).
RN   [13]
RP   CATALYTIC ACTIVITY, AND FUNCTION IN MAPT PHOSPHORYLATION.
RX   PubMed=21985311; DOI=10.1111/j.1471-4159.2011.07523.x;
RA   Yoshida H., Goedert M.;
RT   "Phosphorylation of microtubule-associated protein tau by AMPK-related
RT   kinases.";
RL   J. Neurochem. 120:165-176(2012).
RN   [14]
RP   VARIANTS [LARGE SCALE ANALYSIS] TRP-303; ILE-319; GLU-391; ASN-531;
RP   SER-749 AND ALA-764.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Serine/threonine-protein kinase that plays a key role in
CC       polarization of neurons and centrosome duplication. Phosphorylates
CC       CDC25B, CDC25C, MAPT/TAU, RIMS1, TUBG1, TUBG2 and WEE1. Following
CC       phosphorylation and activation by STK11/LKB1, acts as a key
CC       regulator of polarization of cortical neurons, probably by
CC       mediating phosphorylation of microtubule-associated proteins such
CC       as MAPT/TAU at 'Thr-529' and 'Ser-579'. Also regulates neuron
CC       polarization by mediating phosphorylation of WEE1 at 'Ser-642' in
CC       post-mitotic neurons, leading to down-regulate WEE1 activity in
CC       polarized neurons. In neurons, localizes to synaptic vesicles and
CC       plays a role in neurotransmitter release, possibly by
CC       phosphorylating RIMS1. Also acts as a positive regulator of
CC       centrosome duplication by mediating phosphorylation of gamma-
CC       tubulin (TUBG1 and TUBG2) at 'Ser-131', leading to translocation
CC       of gamma-tubulin and its associated proteins to the centrosome.
CC       Involved in the UV-induced DNA damage checkpoint response,
CC       probably by inhibiting CDK1 activity through phosphorylation and
CC       activation of WEE1, and inhibition of CDC25B and CDC25C.
CC       {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:15150265,
CC       ECO:0000269|PubMed:20026642, ECO:0000269|PubMed:21985311}.
CC   -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.
CC       {ECO:0000269|PubMed:21985311}.
CC   -!- CATALYTIC ACTIVITY: ATP + [tau protein] = ADP + [tau protein]
CC       phosphate. {ECO:0000269|PubMed:21985311}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ENZYME REGULATION: Activated by phosphorylation on Thr-189 by
CC       STK11/LKB1. {ECO:0000269|PubMed:14976552}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15150265}.
CC       Nucleus {ECO:0000269|PubMed:15150265}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome {ECO:0000250}. Cell
CC       junction, synapse {ECO:0000250}. Note=Localizes to synaptic
CC       vesicles in neurons (By similarity). Nuclear in the absence of DNA
CC       damage. Translocated to the nucleus in response to UV- or MMS-
CC       induced DNA damage. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1; Synonyms=SADB-Long, L;
CC         IsoId=Q8TDC3-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TDC3-2; Sequence=VSP_008158;
CC       Name=3; Synonyms=SADB-short, S;
CC         IsoId=Q8TDC3-3; Sequence=VSP_041742;
CC   -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in brain
CC       and testis. Protein levels remain constant throughout the cell
CC       cycle. {ECO:0000269|PubMed:15150265}.
CC   -!- PTM: Phosphorylated at Thr-189 by STK11/LKB1 in complex with
CC       STE20-related adapter-alpha (STRADA) pseudo kinase and CAB39. Not
CC       phosphorylated at Thr-189 by CaMKK2. In contrast, it is
CC       phosphorylated and activated by CaMKK1. May be inactivated via
CC       dephosphorylation of Thr-189 by PP2C.
CC       {ECO:0000269|PubMed:14976552, ECO:0000269|PubMed:18339622,
CC       ECO:0000269|PubMed:19958286}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. CAMK
CC       Ser/Thr protein kinase family. SNF1 subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 1 UBA domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00212}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH16681.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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DR   EMBL; AY458602; AAS10354.1; -; mRNA.
DR   EMBL; AY505124; AAS86442.1; -; mRNA.
DR   EMBL; HQ830199; ADX95745.1; -; mRNA.
DR   EMBL; AF479826; AAL87697.1; -; mRNA.
DR   EMBL; AF479827; AAL87698.1; -; mRNA.
DR   EMBL; AC008974; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL831945; CAD38595.1; -; mRNA.
DR   EMBL; AL834275; CAD38950.2; -; mRNA.
DR   EMBL; AB058714; BAB47440.1; -; mRNA.
DR   EMBL; BC016681; AAH16681.1; ALT_INIT; mRNA.
DR   CCDS; CCDS12921.1; -. [Q8TDC3-1]
DR   RefSeq; NP_115806.1; NM_032430.1. [Q8TDC3-1]
DR   UniGene; Hs.182081; -.
DR   ProteinModelPortal; Q8TDC3; -.
DR   SMR; Q8TDC3; 2-355.
DR   BioGrid; 124084; 4.
DR   IntAct; Q8TDC3; 2.
DR   MINT; MINT-1651556; -.
DR   STRING; 9606.ENSP00000310649; -.
DR   BindingDB; Q8TDC3; -.
DR   ChEMBL; CHEMBL5650; -.
DR   GuidetoPHARMACOLOGY; 1946; -.
DR   PhosphoSite; Q8TDC3; -.
DR   BioMuta; BRSK1; -.
DR   DMDM; 347595639; -.
DR   PaxDb; Q8TDC3; -.
DR   PRIDE; Q8TDC3; -.
DR   Ensembl; ENST00000309383; ENSP00000310649; ENSG00000160469. [Q8TDC3-1]
DR   Ensembl; ENST00000585418; ENSP00000467357; ENSG00000160469. [Q8TDC3-3]
DR   Ensembl; ENST00000590333; ENSP00000468190; ENSG00000160469. [Q8TDC3-2]
DR   GeneID; 84446; -.
DR   KEGG; hsa:84446; -.
DR   UCSC; uc002qkf.3; human. [Q8TDC3-2]
DR   UCSC; uc002qkg.3; human. [Q8TDC3-1]
DR   UCSC; uc021vbs.1; human. [Q8TDC3-3]
DR   CTD; 84446; -.
DR   GeneCards; BRSK1; -.
DR   H-InvDB; HIX0015461; -.
DR   HGNC; HGNC:18994; BRSK1.
DR   HPA; HPA021212; -.
DR   HPA; HPA061719; -.
DR   MIM; 609235; gene.
DR   neXtProt; NX_Q8TDC3; -.
DR   PharmGKB; PA134888976; -.
DR   eggNOG; KOG0588; Eukaryota.
DR   eggNOG; ENOG410XNQ0; LUCA.
DR   GeneTree; ENSGT00810000125454; -.
DR   HOVERGEN; HBG007240; -.
DR   InParanoid; Q8TDC3; -.
DR   KO; K08796; -.
DR   OMA; QHSQSYP; -.
DR   OrthoDB; EOG7XSTDH; -.
DR   PhylomeDB; Q8TDC3; -.
DR   TreeFam; TF313967; -.
DR   SignaLink; Q8TDC3; -.
DR   ChiTaRS; BRSK1; human.
DR   GeneWiki; BRSK1; -.
DR   GenomeRNAi; 84446; -.
DR   NextBio; 74213; -.
DR   PRO; PR:Q8TDC3; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   Bgee; Q8TDC3; -.
DR   CleanEx; HS_BRSK1; -.
DR   ExpressionAtlas; Q8TDC3; baseline and differential.
DR   Genevisible; Q8TDC3; HS.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0008021; C:synaptic vesicle; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IC:UniProtKB.
DR   GO; GO:0043015; F:gamma-tubulin binding; ISS:UniProtKB.
DR   GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0050321; F:tau-protein kinase activity; IDA:UniProtKB.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0051298; P:centrosome duplication; ISS:UniProtKB.
DR   GO; GO:0030010; P:establishment of cell polarity; ISS:UniProtKB.
DR   GO; GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR   GO; GO:0007269; P:neurotransmitter secretion; ISS:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0009411; P:response to UV; IDA:UniProtKB.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR002290; Ser/Thr_dual-sp_kinase.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR015940; UBA.
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.
DR   PROSITE; PS50030; UBA; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell cycle; Cell junction;
KW   Complete proteome; Cytoplasm; Cytoskeleton; DNA damage; Kinase;
KW   Magnesium; Metal-binding; Neurogenesis; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Polymorphism; Reference proteome;
KW   Serine/threonine-protein kinase; Synapse; Transferase.
FT   CHAIN         1    778       Serine/threonine-protein kinase BRSK1.
FT                                /FTId=PRO_0000085669.
FT   DOMAIN       34    285       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   DOMAIN      314    356       UBA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00212}.
FT   NP_BIND      40     48       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   COMPBIAS    492    540       Pro-rich.
FT   ACT_SITE    156    156       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10027}.
FT   BINDING      63     63       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   MOD_RES     189    189       Phosphothreonine; by LKB1.
FT                                {ECO:0000269|PubMed:14976552,
FT                                ECO:0000269|PubMed:18339622}.
FT   MOD_RES     399    399       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     443    443       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     447    447       Phosphoserine.
FT                                {ECO:0000269|PubMed:19958286}.
FT   MOD_RES     450    450       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     508    508       Phosphoserine.
FT                                {ECO:0000269|PubMed:19958286}.
FT   MOD_RES     529    529       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     535    535       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     563    563       Phosphoserine.
FT                                {ECO:0000269|PubMed:19958286}.
FT   MOD_RES     583    583       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:Q5RJI5}.
FT   MOD_RES     586    586       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:B2DD29}.
FT   MOD_RES     587    587       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:B2DD29}.
FT   MOD_RES     601    601       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:B2DD29}.
FT   VAR_SEQ       1     26       MSSGAKEGGGGSPAYHLPHPHPHPPQ -> MVAGLTLGKGP
FT                                ESPDGDVSVPERKDEVAGGGGEEEEAEERGR (in
FT                                isoform 2). {ECO:0000303|PubMed:14976552,
FT                                ECO:0000303|Ref.5}.
FT                                /FTId=VSP_008158.
FT   VAR_SEQ     344    778       Missing (in isoform 3).
FT                                {ECO:0000303|PubMed:19648910}.
FT                                /FTId=VSP_041742.
FT   VARIANT     303    303       R -> W (in a gastric adenocarcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040394.
FT   VARIANT     319    319       V -> I (in a lung large cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040395.
FT   VARIANT     391    391       G -> E (in a metastatic melanoma sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040396.
FT   VARIANT     531    531       T -> N (in dbSNP:rs55892637).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040397.
FT   VARIANT     749    749       G -> S (in dbSNP:rs12978445).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040398.
FT   VARIANT     764    764       P -> A (in dbSNP:rs55796422).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_040399.
FT   MUTAGEN      59     59       K->A: Loss of kinase activity.
FT                                {ECO:0000269|PubMed:15150265}.
FT   MUTAGEN     189    189       T->A: Prevents phosphorylation and
FT                                activation by STK11/LKB1 complex.
FT                                {ECO:0000269|PubMed:14976552}.
FT   MUTAGEN     327    327       G->A: Abolishes activation of kinase
FT                                activity. {ECO:0000269|PubMed:18339622}.
FT   CONFLICT    762    762       G -> A (in Ref. 9; AAH16681).
FT                                {ECO:0000305}.
SQ   SEQUENCE   778 AA;  85087 MW;  8D1818D4E54398BB CRC64;
     MSSGAKEGGG GSPAYHLPHP HPHPPQHAQY VGPYRLEKTL GKGQTGLVKL GVHCITGQKV
     AIKIVNREKL SESVLMKVER EIAILKLIEH PHVLKLHDVY ENKKYLYLVL EHVSGGELFD
     YLVKKGRLTP KEARKFFRQI VSALDFCHSY SICHRDLKPE NLLLDEKNNI RIADFGMASL
     QVGDSLLETS CGSPHYACPE VIKGEKYDGR RADMWSCGVI LFALLVGALP FDDDNLRQLL
     EKVKRGVFHM PHFIPPDCQS LLRGMIEVEP EKRLSLEQIQ KHPWYLGGKH EPDPCLEPAP
     GRRVAMRSLP SNGELDPDVL ESMASLGCFR DRERLHRELR SEEENQEKMI YYLLLDRKER
     YPSCEDQDLP PRNDVDPPRK RVDSPMLSRH GKRRPERKSM EVLSITDAGG GGSPVPTRRA
     LEMAQHSQRS RSVSGASTGL SSSPLSSPRS PVFSFSPEPG AGDEARGGGS PTSKTQTLPS
     RGPRGGGAGE QPPPPSARST PLPGPPGSPR SSGGTPLHSP LHTPRASPTG TPGTTPPPSP
     GGGVGGAAWR SRLNSIRNSF LGSPRFHRRK MQVPTAEEMS SLTPESSPEL AKRSWFGNFI
     SLDKEEQIFL VLKDKPLSSI KADIVHAFLS IPSLSHSVLS QTSFRAEYKA SGGPSVFQKP
     VRFQVDISSS EGPEPSPRRD GSGGGGIYSV TFTLISGPSR RFKRVVETIQ AQLLSTHDQP
     SVQALADEKN GAQTRPAGAP PRSLQPPPGR PDPELSSSPR RGPPKDKKLL ATNGTPLP
//