MAST1_HUMAN
ID MAST1_HUMAN Reviewed; 1570 AA.
AC Q9Y2H9; O00114; Q8N6X0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Microtubule-associated serine/threonine-protein kinase 1;
DE EC=2.7.11.1;
DE AltName: Full=Syntrophin-associated serine/threonine-protein kinase;
GN Name=MAST1 {ECO:0000312|HGNC:HGNC:19034};
GN Synonyms=KIAA0973 {ECO:0000312|EMBL:BAA76817.1}, SAST;
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] {ECO:0000305, ECO:0000312|EMBL:BAA76817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain {ECO:0000312|EMBL:BAA76817.1};
RX PubMed=10231032; DOI=10.1093/dnares/6.1.63;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:63-70(1999).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAB51171.1}
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 [3] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 390-1570.
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, TISSUE SPECIFICITY, INVOLVEMENT IN MCCCHCM, VARIANTS MCCCHCM
RP GLU-195 DEL; LYS-277 DEL; LEU-279 DEL AND SER-517, AND VARIANTS LEU-93;
RP VAL-98; SER-517; THR-915 AND ARG-1177.
RX PubMed=30449657; DOI=10.1016/j.neuron.2018.10.044;
RA Tripathy R., Leca I., van Dijk T., Weiss J., van Bon B.W., Sergaki M.C.,
RA Gstrein T., Breuss M., Tian G., Bahi-Buisson N., Paciorkowski A.R.,
RA Pagnamenta A.T., Wenninger-Weinzierl A., Martinez-Reza M.F., Landler L.,
RA Lise S., Taylor J.C., Terrone G., Vitiello G., Del Giudice E.,
RA Brunetti-Pierri N., D'Amico A., Reymond A., Voisin N., Bernstein J.A.,
RA Farrelly E., Kini U., Leonard T.A., Valence S., Burglen L., Armstrong L.,
RA Hiatt S.M., Cooper G.M., Aldinger K.A., Dobyns W.B., Mirzaa G.,
RA Pierson T.M., Baas F., Chelly J., Cowan N.J., Keays D.A.;
RT "Mutations in MAST1 cause mega-corpus-callosum syndrome with cerebellar
RT hypoplasia and cortical malformations.";
RL Neuron 100:1354-1368(2018).
RN [5]
RP VARIANTS [LARGE SCALE ANALYSIS] THR-269; TYR-1240 AND SER-1292.
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: Microtubule-associated protein essential for correct brain
CC development (PubMed:30449657). Appears to link the dystrophin/utrophin
CC network with microtubule filaments via the syntrophins. Phosphorylation
CC of DMD or UTRN may modulate their affinities for associated proteins
CC (By similarity). {ECO:0000250|UniProtKB:Q9R1L5,
CC ECO:0000269|PubMed:30449657}.
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 Evidence={ECO:0000250|UniProtKB:Q9BXM7};
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; Evidence={ECO:0000250|UniProtKB:Q9BXM7};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q9BXM7};
CC -!- SUBUNIT: Interacts with the microtubules. Part of a low affinity
CC complex that associates with, but is distinct from, the postsynaptic
CC density. Interacts with SNTB2. {ECO:0000250|UniProtKB:Q9R1L5}.
CC -!- INTERACTION:
CC Q9Y2H9; P00533: EGFR; NbExp=3; IntAct=EBI-3385920, EBI-297353;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1L5};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9R1L5}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9R1L5}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q9R1L5}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q9R1L5}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q9R1L5}. Note=Also localized in the soma of
CC neurons. Observed as punctate clusters in the processes of interneurons
CC and along the cell body periphery. Colocalizes with syntrophins at the
CC cell membrane. {ECO:0000250|UniProtKB:Q9R1L5}.
CC -!- TISSUE SPECIFICITY: Expressed in fetal brain.
CC {ECO:0000269|PubMed:30449657}.
CC -!- DISEASE: Mega-corpus-callosum syndrome with cerebellar hypoplasia and
CC cortical malformations (MCCCHCM) [MIM:618273]: An autosomal dominant
CC neurodevelopmental disorder with onset in infancy. MCCCHCM is
CC characterized by global developmental delay, impaired intellectual
CC development, poor or absent speech, unsteady gait, ataxia, inability to
CC walk, and variable brain abnormalities. Seizures and autistic features
CC are observed in some patients. Brain imaging findings include an
CC enlarged corpus callosum in the absence of megalencephaly, cerebellar
CC hypoplasia, ventricular dilation, gyral abnormalities, and cortical
CC malformations. {ECO:0000269|PubMed:30449657}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB51171.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAH27985.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA76817.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB023190; BAA76817.1; ALT_INIT; mRNA.
DR EMBL; AC020934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AD000092; AAB51171.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BC027985; AAH27985.2; ALT_INIT; mRNA.
DR CCDS; CCDS32921.1; -.
DR PIR; T45070; T45070.
DR RefSeq; NP_055790.1; NM_014975.2.
DR PDB; 2M9X; NMR; -; A=187-287.
DR PDB; 3PS4; X-ray; 1.85 A; A/B/C/D=965-1057.
DR PDBsum; 2M9X; -.
DR PDBsum; 3PS4; -.
DR AlphaFoldDB; Q9Y2H9; -.
DR SMR; Q9Y2H9; -.
DR BioGRID; 116632; 53.
DR IntAct; Q9Y2H9; 211.
DR STRING; 9606.ENSP00000251472; -.
DR BindingDB; Q9Y2H9; -.
DR ChEMBL; CHEMBL1163128; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q9Y2H9; -.
DR GlyConnect; 2057; 4 N-Linked glycans (1 site).
DR GlyGen; Q9Y2H9; 2 sites, 8 N-linked glycans (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y2H9; -.
DR PhosphoSitePlus; Q9Y2H9; -.
DR BioMuta; MAST1; -.
DR DMDM; 60390226; -.
DR EPD; Q9Y2H9; -.
DR jPOST; Q9Y2H9; -.
DR MassIVE; Q9Y2H9; -.
DR MaxQB; Q9Y2H9; -.
DR PaxDb; Q9Y2H9; -.
DR PeptideAtlas; Q9Y2H9; -.
DR PRIDE; Q9Y2H9; -.
DR ProteomicsDB; 85788; -.
DR Antibodypedia; 26218; 102 antibodies from 24 providers.
DR DNASU; 22983; -.
DR Ensembl; ENST00000251472.9; ENSP00000251472.3; ENSG00000105613.10.
DR GeneID; 22983; -.
DR KEGG; hsa:22983; -.
DR MANE-Select; ENST00000251472.9; ENSP00000251472.3; NM_014975.3; NP_055790.1.
DR UCSC; uc002mvm.4; human.
DR CTD; 22983; -.
DR DisGeNET; 22983; -.
DR GeneCards; MAST1; -.
DR HGNC; HGNC:19034; MAST1.
DR HPA; ENSG00000105613; Group enriched (brain, pituitary gland, retina).
DR MalaCards; MAST1; -.
DR MIM; 612256; gene.
DR MIM; 618273; phenotype.
DR neXtProt; NX_Q9Y2H9; -.
DR OpenTargets; ENSG00000105613; -.
DR PharmGKB; PA134946727; -.
DR VEuPathDB; HostDB:ENSG00000105613; -.
DR eggNOG; KOG0605; Eukaryota.
DR eggNOG; KOG0606; Eukaryota.
DR GeneTree; ENSGT00940000157700; -.
DR HOGENOM; CLU_000288_9_0_1; -.
DR InParanoid; Q9Y2H9; -.
DR OMA; GMREKSW; -.
DR OrthoDB; 323328at2759; -.
DR PhylomeDB; Q9Y2H9; -.
DR TreeFam; TF313149; -.
DR PathwayCommons; Q9Y2H9; -.
DR SignaLink; Q9Y2H9; -.
DR SIGNOR; Q9Y2H9; -.
DR BioGRID-ORCS; 22983; 16 hits in 1106 CRISPR screens.
DR ChiTaRS; MAST1; human.
DR EvolutionaryTrace; Q9Y2H9; -.
DR GeneWiki; MAST1; -.
DR GenomeRNAi; 22983; -.
DR Pharos; Q9Y2H9; Tchem.
DR PRO; PR:Q9Y2H9; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y2H9; protein.
DR Bgee; ENSG00000105613; Expressed in right hemisphere of cerebellum and 109 other tissues.
DR ExpressionAtlas; Q9Y2H9; baseline and differential.
DR Genevisible; Q9Y2H9; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR GO; GO:0000287; F:magnesium ion binding; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IMP:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; ISS:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0006468; P:protein phosphorylation; ISS:UniProtKB.
DR CDD; cd05609; STKc_MAST; 1.
DR Gene3D; 1.20.1480.20; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR015022; MA_Ser/Thr_Kinase_dom.
DR InterPro; IPR037711; MAST.
DR InterPro; IPR028777; MAST1.
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:SF150; PTHR24356:SF150; 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; SSF140482; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF56112; SSF56112; 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.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Disease variant; Intellectual disability; Kinase; Magnesium;
KW Membrane; Metal-binding; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..1570
FT /note="Microtubule-associated serine/threonine-protein
FT kinase 1"
FT /id="PRO_0000086309"
FT DOMAIN 374..647
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 648..719
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT DOMAIN 967..1055
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 23..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 340..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 717..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 929..965
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1065..1184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1305..1570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 32..46
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..760
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..823
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 934..965
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1078..1094
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1097..1177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1221..1239
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1278..1293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 497
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-
FT ProRule:PRU10027"
FT BINDING 380..388
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 403
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9BXM7,
FT ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 90
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 351
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 687
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 893
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R1L5"
FT MOD_RES 952
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT MOD_RES 1413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q810W7"
FT VARIANT 93
FT /note="S -> L (in a patient with neurodevelopmental
FT abnormalities; de novo variant; unknown pathological
FT significance; dbSNP:rs878853165)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081872"
FT VARIANT 98
FT /note="G -> V (in a patient with neurodevelopmental
FT abnormalities; de novo variant; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081873"
FT VARIANT 195
FT /note="Missing (in MCCCHCM; unknown pathological
FT significance; dbSNP:rs1568408280)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081874"
FT VARIANT 269
FT /note="A -> T (in a metastatic melanoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040768"
FT VARIANT 277
FT /note="Missing (in MCCCHCM; dbSNP:rs1568409494)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081875"
FT VARIANT 279
FT /note="Missing (in MCCCHCM; expression of this variant in
FT transgenic mice results in thicker corpus callosum,
FT hypoplastic cortex and hypoplastic cerebellum)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081876"
FT VARIANT 517
FT /note="G -> S (in MCCCHCM; dbSNP:rs1568413207)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081877"
FT VARIANT 915
FT /note="A -> T (in a patient with neurodevelopmental
FT abnormalities; de novo variant; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081878"
FT VARIANT 1048
FT /note="A -> S (in dbSNP:rs35052801)"
FT /id="VAR_051644"
FT VARIANT 1177
FT /note="P -> R (in a patient with neurodevelopmental
FT abnormalities; de novo variant; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:30449657"
FT /id="VAR_081879"
FT VARIANT 1240
FT /note="H -> Y (in an ovarian serous carcinoma sample;
FT somatic mutation; dbSNP:rs1411105125)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040769"
FT VARIANT 1292
FT /note="P -> S (in dbSNP:rs35071862)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_040770"
FT HELIX 189..202
FT /evidence="ECO:0007829|PDB:2M9X"
FT HELIX 216..237
FT /evidence="ECO:0007829|PDB:2M9X"
FT HELIX 242..261
FT /evidence="ECO:0007829|PDB:2M9X"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:2M9X"
FT STRAND 968..971
FT /evidence="ECO:0007829|PDB:3PS4"
FT STRAND 973..975
FT /evidence="ECO:0007829|PDB:3PS4"
FT STRAND 978..987
FT /evidence="ECO:0007829|PDB:3PS4"
FT STRAND 994..1003
FT /evidence="ECO:0007829|PDB:3PS4"
FT HELIX 1008..1012
FT /evidence="ECO:0007829|PDB:3PS4"
FT STRAND 1019..1023
FT /evidence="ECO:0007829|PDB:3PS4"
FT HELIX 1033..1042
FT /evidence="ECO:0007829|PDB:3PS4"
FT TURN 1043..1045
FT /evidence="ECO:0007829|PDB:3PS4"
FT STRAND 1046..1052
FT /evidence="ECO:0007829|PDB:3PS4"
SQ SEQUENCE 1570 AA; 170677 MW; 189D24AE07B62A1E CRC64;
MSDSLWTALS NFSMPSFPGG SMFRRTKSCR TSNRKSLILT STSPTLPRPH SPLPGHLGSS
PLDSPRNFSP NTPAHFSFAS SRRADGRRWS LASLPSSGYG TNTPSSTVSS SCSSQERLHQ
LPYQPTVDEL HFLSKHFGST ESITDEDGGR RSPAVRPRSR SLSPGRSPSS YDNEIVMMNH
VYKERFPKAT AQMEEKLRDF TRAYEPDSVL PLADGVLSFI HHQIIELARD CLTKSRDGLI
TTVYFYELQE NLEKLLQDAY ERSESLEVAF VTQLVKKLLI IISRPARLLE CLEFNPEEFY
HLLEAAEGHA KEGHLVKTDI PRYIIRQLGL TRDPFPDVVH LEEQDSGGSN TPEQDDLSEG
RSSKAKKPPG ENDFDTIKLI SNGAYGAVYL VRHRDTRQRF AMKKINKQNL ILRNQIQQAF
VERDILTFAE NPFVVGMFCS FETRRHLCMV MEYVEGGDCA TLLKNIGALP VEMARMYFAE
TVLALEYLHN YGIVHRDLKP DNLLITSMGH IKLTDFGLSK MGLMSLTTNL YEGHIEKDAR
EFLDKQVCGT PEYIAPEVIL RQGYGKPVDW WAMGIILYEF LVGCVPFFGD TPEELFGQVI
SDDILWPEGD EALPTEAQLL ISSLLQTNPL VRLGAGGAFE VKQHSFFRDL DWTGLLRQKA
EFIPHLESED DTSYFDTRSD RYHHVNSYDE DDTTEEEPVE IRQFSSCSPR FSKVYSSMEQ
LSQHEPKTPV AAAGSSKREP STKGPEEKVA GKREGLGGLT LREKTWRGGS PEIKRFSASE
ASFLEGEASP PLGARRRFSA LLEPSRFSAP QEDEDEARLR RPPRPSSDPA GSLDARAPKE
ETQGEGTSSA GDSEATDRPR PGDLCPPSKD GDASGPRATN DLVLRRARHQ QMSGDVAVEK
RPSRTGGKVI KSASATALSV MIPAVDPHGS SPLASPMSPR SLSSNPSSRD SSPSRDYSPA
VSGLRSPITI QRSGKKYGFT LRAIRVYMGD TDVYSVHHIV WHVEEGGPAQ EAGLCAGDLI
THVNGEPVHG MVHPEVVELI LKSGNKVAVT TTPFENTSIR IGPARRSSYK AKMARRNKRP
SAKEGQESKK RSSLFRKITK QSNLLHTSRS LSSLNRSLSS SDSLPGSPTH GLPARSPTHS
YRSTPDSAYL GASSQSSSPA SSTPNSPASS ASHHIRPSTL HGLSPKLHRQ YRSARCKSAG
NIPLSPLAHT PSPTQASPPP LPGHTVGSSH TTQSFPAKLH SSPPVVRPRP KSAEPPRSPL
LKRVQSAEKL GASLSADKKG ALRKHSLEVG HPDFRKDFHG ELALHSLAES DGETPPVEGL
GAPRQVAVRR LGRQESPLSL GADPLLPEGA SRPPVSSKEK ESPGGAEACT PPRATTPGGR
TLERDVGCTR HQSVQTEDGT GGMARAVAKA ALSPVQEHET GRRSSSGEAG TPLVPIVVEP
ARPGAKAVVP QPLGADSKGL QEPAPLAPSV PEAPRGRERW VLEVVEERTT LSGPRSKPAS
PKLSPEPQTP SLAPAKCSAP SSAVTPVPPA SLLGSGTKPQ VGLTSRCPAE AVPPAGLTKK
GVSSPAPPGP
