LMTK2_HUMAN
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 03-AUG-2022, entry version 163.
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=3; 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; 51.
DR IntAct; Q8IWU2; 31.
DR MINT; Q8IWU2; -.
DR STRING; 9606.ENSP00000297293; -.
DR iPTMnet; Q8IWU2; -.
DR PhosphoSitePlus; Q8IWU2; -.
DR SwissPalm; Q8IWU2; -.
DR BioMuta; LMTK2; -.
DR EPD; Q8IWU2; -.
DR jPOST; Q8IWU2; -.
DR MassIVE; Q8IWU2; -.
DR MaxQB; Q8IWU2; -.
DR PaxDb; Q8IWU2; -.
DR PeptideAtlas; Q8IWU2; -.
DR PRIDE; Q8IWU2; -.
DR ProteomicsDB; 70894; -.
DR Antibodypedia; 2093; 246 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 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; EQSWPHV; -.
DR OrthoDB; 53680at2759; -.
DR PhylomeDB; Q8IWU2; -.
DR TreeFam; TF332280; -.
DR PathwayCommons; Q8IWU2; -.
DR SignaLink; Q8IWU2; -.
DR SIGNOR; Q8IWU2; -.
DR BioGRID-ORCS; 22853; 8 hits in 1110 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 185 other tissues.
DR Genevisible; Q8IWU2; HS.
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:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0043235; C:receptor complex; IBA:GO_Central.
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: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:0007409; P:axonogenesis; IBA:GO_Central.
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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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 Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
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
