ID   LMTK2_HUMAN             Reviewed;        1503 AA.
AC   Q8IWU2; A4D272; Q75MG7; Q9UPS3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   17-APR-2007, sequence version 2.
DT   27-MAR-2024, entry version 172.
DE   RecName: Full=Serine/threonine-protein kinase LMTK2;
DE            EC=2.7.11.1;
DE   AltName: Full=Apoptosis-associated tyrosine kinase 2;
DE   AltName: Full=Brain-enriched kinase;
DE            Short=hBREK;
DE   AltName: Full=CDK5/p35-regulated kinase;
DE            Short=CPRK;
DE   AltName: Full=Kinase/phosphatase/inhibitor 2;
DE   AltName: Full=Lemur tyrosine kinase 2;
DE   AltName: Full=Serine/threonine-protein kinase KPI-2;
GN   Name=LMTK2; Synonyms=AATYK2, BREK, KIAA1079, KPI2, LMR2;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INTERACTION WITH PPP1C
RP   AND INH2.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=12393858; DOI=10.1074/jbc.m209335200;
RA   Wang H., Brautigan D.L.;
RT   "A novel transmembrane Ser/Thr kinase complexes with protein phosphatase-1
RT   and inhibitor-2.";
RL   J. Biol. Chem. 277:49605-49612(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT MET-780.
RC   TISSUE=Brain;
RX   PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA   Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA   Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XIV. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 6:197-205(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA   Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.-C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [6]
RP   CHARACTERIZATION.
RX   PubMed=15005709; DOI=10.1111/j.1356-9597.2004.00714.x;
RA   Kawa S., Fujimoto J., Tezuka T., Nakazawa T., Yamamoto T.;
RT   "Involvement of BREK, a serine/threonine kinase enriched in brain, in NGF
RT   signalling.";
RL   Genes Cells 9:219-232(2004).
RN   [7]
RP   PHOSPHORYLATION.
RX   PubMed=16887929; DOI=10.1074/mcp.m600188-mcp200;
RA   Wang H., Brautigan D.L.;
RT   "Peptide microarray analysis of substrate specificity of the transmembrane
RT   Ser/Thr kinase KPI-2 reveals reactivity with cystic fibrosis transmembrane
RT   conductance regulator and phosphorylase.";
RL   Mol. Cell. Proteomics 5:2124-2130(2006).
RN   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Leukemic T-cell;
RX   PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA   Rodionov V., Han D.K.;
RT   "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT   reveals system-wide modulation of protein-protein interactions.";
RL   Sci. Signal. 2:RA46-RA46(2009).
RN   [9]
RP   TOPOLOGY, AND SUBCELLULAR LOCATION.
RX   PubMed=23114966; DOI=10.1152/ajpcell.00288.2012;
RA   Nixon A., Jia Y., White C., Bradbury N.A.;
RT   "Determination of the membrane topology of lemur tyrosine kinase 2 (LMTK2)
RT   by fluorescence protease protection.";
RL   Am. J. Physiol. 304:C164-169(2013).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-886; SER-1107 AND SER-1450,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   VARIANTS [LARGE SCALE ANALYSIS] HIS-484; ILE-595; MET-624; THR-693;
RP   MET-780; PHE-849; THR-862; ARG-916; ASN-1061; ASN-1220; GLY-1341 AND
RP   ASN-1401.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA   Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA   Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA   Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA   Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA   Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA   Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA   Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA   Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA   Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA   Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA   Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
CC   -!- FUNCTION: Phosphorylates PPP1C, phosphorylase b and CFTR.
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 PPP1C and inhibitor-2.
CC       {ECO:0000269|PubMed:12393858}.
CC   -!- INTERACTION:
CC       Q8IWU2; P36873: PPP1CC; NbExp=5; IntAct=EBI-2008933, EBI-356283;
CC       Q8IWU2; P41236: PPP1R2; NbExp=4; IntAct=EBI-2008933, EBI-1056517;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:23114966}; Multi-
CC       pass membrane protein {ECO:0000269|PubMed:23114966}.
CC   -!- TISSUE SPECIFICITY: Mainly expressed in skeletal muscle, and weakly in
CC       brain and pancreas. {ECO:0000269|PubMed:12393858}.
CC   -!- PTM: Autophosphorylated. Phosphorylated (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA83031.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=LMTK2 entry;
CC       URL="https://en.wikipedia.org/wiki/LMTK2";
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DR   EMBL; AY130988; AAN08717.1; -; mRNA.
DR   EMBL; AB029002; BAA83031.2; ALT_INIT; mRNA.
DR   EMBL; AC073101; AAS07515.1; -; Genomic_DNA.
DR   EMBL; CH471091; EAW76721.1; -; Genomic_DNA.
DR   EMBL; AC091654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH236956; EAL23894.1; -; Genomic_DNA.
DR   CCDS; CCDS5654.1; -.
DR   RefSeq; NP_055731.2; NM_014916.3.
DR   AlphaFoldDB; Q8IWU2; -.
DR   SMR; Q8IWU2; -.
DR   BioGRID; 116524; 102.
DR   IntAct; Q8IWU2; 82.
DR   MINT; Q8IWU2; -.
DR   STRING; 9606.ENSP00000297293; -.
DR   iPTMnet; Q8IWU2; -.
DR   PhosphoSitePlus; Q8IWU2; -.
DR   SwissPalm; Q8IWU2; -.
DR   BioMuta; LMTK2; -.
DR   CPTAC; non-CPTAC-6030; -.
DR   CPTAC; non-CPTAC-6031; -.
DR   EPD; Q8IWU2; -.
DR   jPOST; Q8IWU2; -.
DR   MassIVE; Q8IWU2; -.
DR   MaxQB; Q8IWU2; -.
DR   PaxDb; 9606-ENSP00000297293; -.
DR   PeptideAtlas; Q8IWU2; -.
DR   ProteomicsDB; 70894; -.
DR   Pumba; Q8IWU2; -.
DR   Antibodypedia; 2093; 276 antibodies from 33 providers.
DR   DNASU; 22853; -.
DR   Ensembl; ENST00000297293.6; ENSP00000297293.5; ENSG00000164715.6.
DR   GeneID; 22853; -.
DR   KEGG; hsa:22853; -.
DR   MANE-Select; ENST00000297293.6; ENSP00000297293.5; NM_014916.4; NP_055731.2.
DR   UCSC; uc003upd.3; human.
DR   AGR; HGNC:17880; -.
DR   CTD; 22853; -.
DR   DisGeNET; 22853; -.
DR   GeneCards; LMTK2; -.
DR   HGNC; HGNC:17880; LMTK2.
DR   HPA; ENSG00000164715; Low tissue specificity.
DR   MIM; 610989; gene.
DR   neXtProt; NX_Q8IWU2; -.
DR   OpenTargets; ENSG00000164715; -.
DR   PharmGKB; PA134884391; -.
DR   VEuPathDB; HostDB:ENSG00000164715; -.
DR   eggNOG; ENOG502QSD2; Eukaryota.
DR   GeneTree; ENSGT00940000158475; -.
DR   HOGENOM; CLU_004618_0_0_1; -.
DR   InParanoid; Q8IWU2; -.
DR   OMA; SHKSVSC; -.
DR   OrthoDB; 2910608at2759; -.
DR   PhylomeDB; Q8IWU2; -.
DR   TreeFam; TF332280; -.
DR   PathwayCommons; Q8IWU2; -.
DR   SignaLink; Q8IWU2; -.
DR   SIGNOR; Q8IWU2; -.
DR   BioGRID-ORCS; 22853; 9 hits in 1190 CRISPR screens.
DR   ChiTaRS; LMTK2; human.
DR   GeneWiki; LMTK2; -.
DR   GenomeRNAi; 22853; -.
DR   Pharos; Q8IWU2; Tbio.
DR   PRO; PR:Q8IWU2; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8IWU2; Protein.
DR   Bgee; ENSG00000164715; Expressed in middle temporal gyrus and 187 other cell types or tissues.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR   GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR   GO; GO:0070853; F:myosin VI binding; IPI:UniProtKB.
DR   GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; IDA:UniProtKB.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR   GO; GO:0045022; P:early endosome to late endosome transport; IMP:UniProtKB.
DR   GO; GO:0032456; P:endocytic recycling; IMP:UniProtKB.
DR   GO; GO:0018105; P:peptidyl-serine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0018107; P:peptidyl-threonine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0006468; P:protein phosphorylation; IDA:UniProtKB.
DR   GO; GO:0001881; P:receptor recycling; IMP:UniProtKB.
DR   GO; GO:0033572; P:transferrin transport; IMP:UniProtKB.
DR   CDD; cd05086; PTKc_Aatyk2; 1.
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; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR24417; SERINE/THREONINE-PROTEIN KINASE LMTK1; 1.
DR   PANTHER; PTHR24417:SF8; SERINE_THREONINE-PROTEIN KINASE LMTK2; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   PRINTS; PR00109; TYRKINASE.
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; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; Q8IWU2; HS.
PE   1: Evidence at protein level;
KW   ATP-binding; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW   Reference proteome; Serine/threonine-protein kinase; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..1503
FT                   /note="Serine/threonine-protein kinase LMTK2"
FT                   /id="PRO_0000259458"
FT   TOPO_DOM        1..10
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        11..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        32..42
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        43..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        64..1503
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          137..407
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   REGION          597..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          804..840
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          875..898
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..999
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1013..1202
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1276..1317
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1372..1469
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        804..821
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1089..1106
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1183..1202
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1279..1295
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1296..1317
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1427..1469
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10028"
FT   BINDING         143..151
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         805
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         806
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         886
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1107
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1305
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         1307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         1308
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         1310
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         1450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1496
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   MOD_RES         1497
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3TYD6"
FT   VARIANT         30
FT                   /note="P -> A (in dbSNP:rs3735252)"
FT                   /id="VAR_028940"
FT   VARIANT         484
FT                   /note="D -> H (in a lung large cell carcinoma sample;
FT                   somatic mutation; dbSNP:rs147940573)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041727"
FT   VARIANT         595
FT                   /note="V -> I (in dbSNP:rs34461195)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041728"
FT   VARIANT         624
FT                   /note="V -> M (in dbSNP:rs34628253)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041729"
FT   VARIANT         693
FT                   /note="I -> T (in dbSNP:rs56204700)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041730"
FT   VARIANT         780
FT                   /note="L -> M (in dbSNP:rs11765552)"
FT                   /evidence="ECO:0000269|PubMed:10470851,
FT                   ECO:0000269|PubMed:17344846"
FT                   /id="VAR_028941"
FT   VARIANT         849
FT                   /note="V -> F (in dbSNP:rs56196840)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041731"
FT   VARIANT         862
FT                   /note="A -> T (in dbSNP:rs34005293)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041732"
FT   VARIANT         916
FT                   /note="S -> R (in dbSNP:rs55867257)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041733"
FT   VARIANT         1061
FT                   /note="D -> N (in dbSNP:rs3801295)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_028942"
FT   VARIANT         1220
FT                   /note="D -> N (in dbSNP:rs35912712)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041734"
FT   VARIANT         1341
FT                   /note="A -> G (in dbSNP:rs56343792)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041735"
FT   VARIANT         1401
FT                   /note="S -> N (in dbSNP:rs45488394)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_041736"
FT   CONFLICT        910
FT                   /note="S -> I (in Ref. 1; AAN08717)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1444..1454
FT                   /note="QTSKYFSPPPP -> PSTLPAFPSHT (in Ref. 2; BAA83031)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1455..1503
FT                   /note="Missing (in Ref. 2; BAA83031)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1503 AA;  164900 MW;  52665B054F04D17A CRC64;
     MPGPPALRRR LLLLLLVLLI AGSAGAAPLP QTGAGEAPPA AEVSSSFVIL CVCSLIILIV
     LIANCVSCCK DPEIDFKEFE DNFDDEIDFT PPAEDTPSVQ SPAEVFTLSV PNISLPAPSQ
     FQPSVEGLKS QVARHSLNYI QEIGNGWFGK VLLGEIYTGT SVARVIVKEL KASANPKEQD
     TFLKNGEPYY ILQHPNILQC VGQCVEAIPY LLVFEFCDLG DLKAYLRSEQ EHMRGDSQTM
     LLQRMACEVA AGLAAMHKLH FLHSDLALRN CFLTSDLNVK VGDYGIGFSR YKEDYIETDD
     KKVFPLRWTA PELVTSFQDR LLTADQTKYS NIWSLGVTLW ELFDNAAQPY SNLSNLDVLN
     QVIRERDTKL PKPQLEQPYS DRWYEVLQFC WLSPEKRPAA EDVHRLLTYL RLQSQRDSEV
     DFEQQWNALK PNTNSRDSSN NAAFPILDHF ARDRLGREME EVLTVTETSQ GLSFEYVWEA
     AKHDHFDERS RGHLDEGLSY TSIFYPVEVF ESSLSDPGPG KQDDSGQDVP LRVPGVVPVF
     DAHNLSVGSD YYIQLEEKSG SNLELDYPPA LLTTDMDNPE RTGPELSQLT ALRSVELEES
     STDEDFFQSS TDPKDSSLPG DLHVTSGPES PFNNIFNDVD KSEDLPSHQK IFDLMELNGV
     QADFKPATLS SSLDNPKESV ITGHFEKEKP RKIFDSEPLC LSDNLMHQDN FDPLNVQELS
     ENFLFLQEKN LLKGSLSSKE HINDLQTELK NAGFTEAMLE TSCRNSLDTE LQFAENKPGL
     SLLQENVSTK GDDTDVMLTG DTLSTSLQSS PEVQVPPTSF ETEETPRRVP PDSLPTQGET
     QPTCLDVIVP EDCLHQDISP DAVTVPVEIL STDARTHSLD NRSQDSPGES EETLRLTESD
     SVLADDILAS RVSVGSSLPE LGQELHNKPF SEDHHSHRRL EKNLEAVETL NQLNSKDAAK
     EAGLVSALSS DSTSQDSLLE DSLSAPFPAS EPSLETPDSL ESVDVHEALL DSLGSHTPQK
     LVPPDKPADS GYETENLESP EWTLHPAPEG TADSEPATTG DGGHSGLPPN PVIVISDAGD
     GHRGTEVTPE TFTAGSQGSY RDSAYFSDND SEPEKRSEEV PGTSPSALVL VQEQPLPEPV
     LPEQSPAAQD SCLEARKSQP DESCLSALHN SSDLELRATP EPAQTGVPQQ VHPTEDEASS
     PWSVLNAELS SGDDFETQDD RPCTLASTGT NTNELLAYTN SALDKSLSSH SEGPKLKEPD
     IEGKYLGKLG VSGMLDLSED GMDADEEDEN SDDSDEDLRA FNLHSLSSES EDETEHPVPI
     ILSNEDGRHL RSLLKPTAAN APDPLPEDWK KEKKAVTFFD DVTVYLFDQE TPTKELGPCG
     GEACGPDLSG PAPASGSPYL SRCINSESST DEEGGGFEWD DDFSPDPFMS KTTSNLLSSK
     PSLQTSKYFS PPPPARSTEQ SWPHSAPYSR FSISPANIAS FSLTHLTDSD IEQGGSSEDG
     EKD
//