ID   MAST3_HUMAN             Reviewed;        1309 AA.
AC   O60307; Q7LDZ8; Q9UPI0;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 2.
DT   27-MAR-2024, entry version 192.
DE   RecName: Full=Microtubule-associated serine/threonine-protein kinase 3;
DE            EC=2.7.11.1;
GN   Name=MAST3; Synonyms=KIAA0561;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., 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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-1309.
RC   TISSUE=Brain;
RX   PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA   Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA   Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. IX. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 5:31-39(1998).
RN   [3]
RP   INTERACTION WITH PTEN.
RX   PubMed=15951562; DOI=10.1074/jbc.m504761200;
RA   Valiente M., Andres-Pons A., Gomar B., Torres J., Gil A., Tapparel C.,
RA   Antonarakis S.E., Pulido R.;
RT   "Binding of PTEN to specific PDZ domains contributes to PTEN protein
RT   stability and phosphorylation by microtubule-associated serine/threonine
RT   kinases.";
RL   J. Biol. Chem. 280:28936-28943(2005).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1223, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-146; SER-680 AND SER-1223,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; SER-782; SER-792 AND
RP   SER-793, AND 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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-85; SER-146; SER-754;
RP   SER-782 AND SER-793, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   [9]
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   [10]
RP   STRUCTURE BY NMR OF 181-281.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of putative domain of human KIAA0561 protein.";
RL   Submitted (MAR-2005) to the PDB data bank.
RN   [11]
RP   VARIANT [LARGE SCALE ANALYSIS] SER-883.
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).
RN   [12]
RP   VARIANTS DEE108 PRO-406; SER-510; SER-515; PRO-516 AND LEU-551, INVOLVEMENT
RP   IN DEE108, AND VARIANT LEU-655.
RX   PubMed=34185323; DOI=10.1002/ana.26147;
RG   Undiagnosed Diseases Network (UDN);
RA   Spinelli E., Christensen K.R., Bryant E., Schneider A., Rakotomamonjy J.,
RA   Muir A.M., Giannelli J., Littlejohn R.O., Roeder E.R., Schmidt B.,
RA   Wilson W.G., Marco E.J., Iwama K., Kumada S., Pisano T., Barba C.,
RA   Vetro A., Brilstra E.H., van Jaarsveld R.H., Matsumoto N.,
RA   Goldberg-Stern H., Carney P.W., Andrews P.I., El Achkar C.M., Berkovic S.,
RA   Rodan L.H., McWalter K., Guerrini R., Scheffer I.E., Mefford H.C.,
RA   Mandelstam S., Laux L., Millichap J.J., Guemez-Gamboa A., Nairn A.C.,
RA   Carvill G.L.;
RT   "Pathogenic MAST3 Variants in the STK Domain Are Associated with
RT   Epilepsy.";
RL   Ann. Neurol. 90:274-284(2021).
RN   [13]
RP   VARIANTS DEE108 PHE-101; LEU-104; SER-515 AND PRO-516, AND INVOLVEMENT IN
RP   DEE108.
RX   PubMed=35095415; DOI=10.3389/fnmol.2021.775479;
RA   Shu L., Xiao N., Qin J., Tian Q., Zhang Y., Li H., Liu J., Li Q., Gu W.,
RA   Wang P., Wang H., Mao X.;
RT   "The Role of Microtubule Associated Serine/Threonine Kinase 3 Variants in
RT   Neurodevelopmental Diseases: Genotype-Phenotype Association.";
RL   Front. Mol. Neurosci. 14:775479-775479(2021).
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SUBUNIT: Interacts with PTEN. {ECO:0000269|PubMed:15951562}.
CC   -!- INTERACTION:
CC       O60307; P60484: PTEN; NbExp=3; IntAct=EBI-311420, EBI-696162;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q3U214}.
CC   -!- DISEASE: Developmental and epileptic encephalopathy 108 (DEE108)
CC       [MIM:620115]: A form of epileptic encephalopathy, a heterogeneous group
CC       of early-onset epilepsies characterized by refractory seizures,
CC       neurodevelopmental impairment, and poor prognosis. Development is
CC       normal prior to seizure onset, after which cognitive and motor delays
CC       become apparent. DEE108 is an autosomal dominant form characterized by
CC       the onset of multiple types of seizures in the first 2 years of life.
CC       {ECO:0000269|PubMed:34185323, ECO:0000269|PubMed:35095415}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC       protein kinase family. {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1, Met-171 or Met-172 is the
CC       initiator. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC62830.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AC005793; AAC62830.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AC007192; AAD22670.1; -; Genomic_DNA.
DR   EMBL; AC093054; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB011133; BAA25487.1; -; mRNA.
DR   CCDS; CCDS46014.1; -.
DR   RefSeq; NP_055831.1; NM_015016.1.
DR   PDB; 1V9V; NMR; -; A=181-281.
DR   PDB; 3KHF; X-ray; 1.20 A; A/B=948-1040.
DR   PDBsum; 1V9V; -.
DR   PDBsum; 3KHF; -.
DR   AlphaFoldDB; O60307; -.
DR   BMRB; O60307; -.
DR   SMR; O60307; -.
DR   BioGRID; 116670; 123.
DR   IntAct; O60307; 43.
DR   STRING; 9606.ENSP00000262811; -.
DR   BindingDB; O60307; -.
DR   ChEMBL; CHEMBL2417352; -.
DR   GuidetoPHARMACOLOGY; 1512; -.
DR   GlyGen; O60307; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; O60307; -.
DR   PhosphoSitePlus; O60307; -.
DR   BioMuta; MAST3; -.
DR   CPTAC; non-CPTAC-5671; -.
DR   EPD; O60307; -.
DR   jPOST; O60307; -.
DR   MassIVE; O60307; -.
DR   MaxQB; O60307; -.
DR   PaxDb; 9606-ENSP00000262811; -.
DR   PeptideAtlas; O60307; -.
DR   ProteomicsDB; 49334; -.
DR   Pumba; O60307; -.
DR   Antibodypedia; 27914; 202 antibodies from 32 providers.
DR   DNASU; 23031; -.
DR   Ensembl; ENST00000262811.10; ENSP00000262811.4; ENSG00000099308.13.
DR   GeneID; 23031; -.
DR   KEGG; hsa:23031; -.
DR   UCSC; uc002nhz.5; human.
DR   AGR; HGNC:19036; -.
DR   CTD; 23031; -.
DR   DisGeNET; 23031; -.
DR   GeneCards; MAST3; -.
DR   HGNC; HGNC:19036; MAST3.
DR   HPA; ENSG00000099308; Tissue enhanced (brain).
DR   MalaCards; MAST3; -.
DR   MIM; 612258; gene.
DR   MIM; 620115; phenotype.
DR   neXtProt; NX_O60307; -.
DR   OpenTargets; ENSG00000099308; -.
DR   PharmGKB; PA134877725; -.
DR   VEuPathDB; HostDB:ENSG00000099308; -.
DR   eggNOG; KOG0606; Eukaryota.
DR   GeneTree; ENSGT00940000157166; -.
DR   HOGENOM; CLU_000288_9_0_1; -.
DR   InParanoid; O60307; -.
DR   OMA; ARICWPQ; -.
DR   OrthoDB; 2915765at2759; -.
DR   PhylomeDB; O60307; -.
DR   TreeFam; TF313149; -.
DR   PathwayCommons; O60307; -.
DR   SignaLink; O60307; -.
DR   SIGNOR; O60307; -.
DR   BioGRID-ORCS; 23031; 28 hits in 1184 CRISPR screens.
DR   ChiTaRS; MAST3; human.
DR   EvolutionaryTrace; O60307; -.
DR   GenomeRNAi; 23031; -.
DR   Pharos; O60307; Tchem.
DR   PRO; PR:O60307; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O60307; Protein.
DR   Bgee; ENSG00000099308; Expressed in frontal pole and 177 other cell types or tissues.
DR   ExpressionAtlas; O60307; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR   GO; GO:0004674; F:protein serine/threonine kinase activity; IBA:GO_Central.
DR   GO; GO:0007010; P:cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0035556; P:intracellular signal transduction; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd05609; STKc_MAST; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.20.1480.20; MAST3 pre-PK domain-like; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000961; AGC-kinase_C.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR037711; MAST.
DR   InterPro; IPR015022; MAST_pre-PK_dom.
DR   InterPro; IPR023142; MAST_pre-PK_dom_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   PANTHER; PTHR24356:SF140; MICROTUBULE-ASSOCIATED SERINE_THREONINE-PROTEIN KINASE 3; 1.
DR   PANTHER; PTHR24356; SERINE/THREONINE-PROTEIN KINASE; 1.
DR   Pfam; PF08926; DUF1908; 1.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00069; Pkinase; 1.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF140482; MAST3 pre-PK domain-like; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
DR   Genevisible; O60307; HS.
PE   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Cytoplasm; Disease variant; Epilepsy;
KW   Intellectual disability; Kinase; Magnesium; Nucleotide-binding;
KW   Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW   Transferase.
FT   CHAIN           1..1309
FT                   /note="Microtubule-associated serine/threonine-protein
FT                   kinase 3"
FT                   /id="PRO_0000086314"
FT   DOMAIN          367..640
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   DOMAIN          641..712
FT                   /note="AGC-kinase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT   DOMAIN          950..1038
FT                   /note="PDZ"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          88..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          136..162
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          337..360
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          756..895
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          908..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1046..1245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        32..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..113
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        756..787
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        811..825
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        828..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        857..872
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..941
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1052..1068
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1134..1153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1186..1213
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1219..1245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        490
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT                   ECO:0000255|PROSITE-ProRule:PRU10027"
FT   BINDING         373..381
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   BINDING         396
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         85
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         146
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         680
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19369195"
FT   MOD_RES         710
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U214"
FT   MOD_RES         728
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U214"
FT   MOD_RES         754
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         774
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         782
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         792
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332"
FT   MOD_RES         793
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1223
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19369195"
FT   MOD_RES         1273
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q3U214"
FT   VARIANT         101
FT                   /note="S -> F (in DEE108; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:35095415"
FT                   /id="VAR_087834"
FT   VARIANT         104
FT                   /note="S -> L (in DEE108)"
FT                   /evidence="ECO:0000269|PubMed:35095415"
FT                   /id="VAR_087835"
FT   VARIANT         203
FT                   /note="R -> Q (in dbSNP:rs35945810)"
FT                   /id="VAR_051646"
FT   VARIANT         406
FT                   /note="R -> P (in DEE108)"
FT                   /evidence="ECO:0000269|PubMed:34185323"
FT                   /id="VAR_087836"
FT   VARIANT         510
FT                   /note="G -> S (in DEE108; dbSNP:rs1478088223)"
FT                   /evidence="ECO:0000269|PubMed:34185323"
FT                   /id="VAR_087837"
FT   VARIANT         515
FT                   /note="G -> S (in DEE108)"
FT                   /evidence="ECO:0000269|PubMed:34185323,
FT                   ECO:0000269|PubMed:35095415"
FT                   /id="VAR_087838"
FT   VARIANT         516
FT                   /note="L -> P (in DEE108)"
FT                   /evidence="ECO:0000269|PubMed:34185323,
FT                   ECO:0000269|PubMed:35095415"
FT                   /id="VAR_087839"
FT   VARIANT         551
FT                   /note="V -> L (in DEE108; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:34185323"
FT                   /id="VAR_087840"
FT   VARIANT         655
FT                   /note="F -> L (found in a patient with autism spectrum
FT                   disorder without history of seizures; uncertain
FT                   significance)"
FT                   /evidence="ECO:0000269|PubMed:34185323"
FT                   /id="VAR_087841"
FT   VARIANT         861
FT                   /note="G -> S (in dbSNP:rs8108738)"
FT                   /id="VAR_051647"
FT   VARIANT         883
FT                   /note="G -> S (in dbSNP:rs369960905)"
FT                   /evidence="ECO:0000269|PubMed:17344846"
FT                   /id="VAR_040786"
FT   HELIX           185..197
FT                   /evidence="ECO:0007829|PDB:1V9V"
FT   TURN            201..203
FT                   /evidence="ECO:0007829|PDB:1V9V"
FT   HELIX           209..230
FT                   /evidence="ECO:0007829|PDB:1V9V"
FT   HELIX           236..255
FT                   /evidence="ECO:0007829|PDB:1V9V"
FT   HELIX           259..276
FT                   /evidence="ECO:0007829|PDB:1V9V"
FT   STRAND          951..954
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   STRAND          962..975
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   STRAND          977..986
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   HELIX           991..995
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   STRAND          1002..1006
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   HELIX           1016..1025
FT                   /evidence="ECO:0007829|PDB:3KHF"
FT   STRAND          1028..1035
FT                   /evidence="ECO:0007829|PDB:3KHF"
SQ   SEQUENCE   1309 AA;  143137 MW;  87E82F2D032ED122 CRC64;
     MDESSLLRRR GLQKELSLPR RGRGCRSGNR KSLVVGTPSP TLSRPLSPLS VPTAGSSPLD
     SPRNFSAASA LNFPFARRAD GRRWSLASLP SSGYGTNTPS STLSSSSSSR ERLHQLPFQP
     TPDELHFLSK HFRSSENVLD EEGGRSPRLR PRSRSLSPGR ATGTFDNEIV MMNHVYRERF
     PKATAQMEGR LQEFLTAYAP GARLALADGV LGFIHHQIVE LARDCLAKSG ENLVTSRYFL
     EMQEKLERLL QDAHERSDSE EVSFIVQLVR KLLIIISRPA RLLECLEFDP EEFYHLLEAA
     EGHAREGQGI KTDLPQYIIG QLGLAKDPLE EMVPLSHLEE EQPPAPESPE SRALVGQSRR
     KPCESDFETI KLISNGAYGA VYLVRHRDTR QRFAIKKINK QNLILRNQIQ QVFVERDILT
     FAENPFVVSM FCSFETRRHL CMVMEYVEGG DCATLLKNMG PLPVDMARLY FAETVLALEY
     LHNYGIVHRD LKPDNLLITS LGHIKLTDFG LSKIGLMSMA TNLYEGHIEK DAREFIDKQV
     CGTPEYIAPE VIFRQGYGKP VDWWAMGVVL YEFLVGCVPF FGDTPEELFG QVVSDEIMWP
     EGDEALPADA QDLITRLLRQ SPLDRLGTGG THEVKQHPFF LALDWAGLLR HKAEFVPQLE
     AEDDTSYFDT RSERYRHLGS EDDETNDEES STEIPQFSSC SHRFSKVYSS SEFLAVQPTP
     TFAERSFSED REEGWERSEV DYGRRLSADI RLRSWTSSGS SCQSSSSQPE RGPSPSLLNT
     ISLDTMPKFA FSSEDEGVGP GPAGPKRPVF ILGEPDPPPA ATPVMPKPSS LSADTAALSH
     ARLRSNSIGA RHSTPRPLDA GRGRRLGGPR DPAPEKSRAS SSGGSGGGSG GRVPKSASVS
     ALSLIITADD GSGGPLMSPL SPRSLSSNPS SRDSSPSRDP SPVCGSLRPP IVIHSSGKKY
     GFSLRAIRVY MGDSDVYTVH HVVWSVEDGS PAQEAGLRAG DLITHINGES VLGLVHMDVV
     ELLLKSGNKI SLRTTALENT SIKVGPARKN VAKGRMARRS KRSRRRETQD RRKSLFKKIS
     KQTSVLHTSR SFSSGLHHSL SSSESLPGSP THSLSPSPTT PCRSPAPDVP ADTTASPPSA
     SPSSSSPASP AAAGHTRPSS LHGLAAKLGP PRPKTGRRKS TSSIPPSPLA CPPISAPPPR
     SPSPLPGHPP APARSPRLRR GQSADKLGTG ERLDGEAGRR TRGPEAELVV MRRLHLSERR
     DSFKKQEAVQ EVSFDEPQEE ATGLPTSVPQ IAVEGEEAVP VALGPTGRD
//