TBX3_HUMAN
ID TBX3_HUMAN Reviewed; 743 AA.
AC O15119; Q8TB20; Q9UKF8;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 12-FEB-2003, sequence version 4.
DT 03-AUG-2022, entry version 208.
DE RecName: Full=T-box transcription factor TBX3;
DE Short=T-box protein 3;
GN Name=TBX3;
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] (ISOFORM I), AND FUNCTION.
RC TISSUE=Mammary carcinoma;
RX PubMed=10468588; DOI=10.1073/pnas.96.18.10212;
RA He M.-L., Wen L., Campbell C.E., Wu J.Y., Rao Y.;
RT "Transcription repression by Xenopus ET and its human ortholog TBX3, a gene
RT involved in ulnar-mammary syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:10212-10217(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-488 (ISOFORM I).
RC TISSUE=Kidney;
RX PubMed=9207801; DOI=10.1038/ng0797-311;
RA Bamshad M., Lin R.C., Law D.J., Watkins W.S., Krakowiak P.A., Moore M.E.,
RA Franceschini P., Lala R., Holmes L.B., Gebuhr T.C., Schinzel A.,
RA Bruneau B.G., Seidman J.G., Seidman C.E., Jorde L.B.;
RT "Mutations in human TBX3 alter limb, apocrine and genital development in
RT ulnar-mammary syndrome.";
RL Nat. Genet. 16:311-315(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 592-743, ALTERNATIVE SPLICING, AND VARIANTS
RP UMS PRO-143 AND SER-149.
RX PubMed=10330342; DOI=10.1086/302417;
RA Bamshad M., Le T., Watkins W.S., Dixon M.E., Kramer B.E., Roeder A.D.,
RA Carey J.C., Root S., Schinzel A., Van Maldergem L., Gardner R.J.M.,
RA Lin R.C., Seidman C.E., Seidman J.G., Wallerstein R., Moran E., Sutphen R.,
RA Campbell C.E., Jorde L.B.;
RT "The spectrum of mutations in TBX3: genotype/phenotype relationship in
RT ulnar-mammary syndrome.";
RL Am. J. Hum. Genet. 64:1550-1562(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM III).
RC TISSUE=Adrenal gland;
RA Song H., Gao G., Peng Y., Ren S., Chen Z., Han Z.;
RT "A novel gene expressed in human adrenal gland.";
RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM II).
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 [6]
RP FUNCTION, AND MUTAGENESIS OF LEU-143 AND TYR-149.
RX PubMed=12000749; DOI=10.1074/jbc.m200403200;
RA Lingbeek M.E., Jacobs J.J., van Lohuizen M.;
RT "The T-box repressors TBX2 and TBX3 specifically regulate the tumor
RT suppressor gene p14ARF via a variant T-site in the initiator.";
RL J. Biol. Chem. 277:26120-26127(2002).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-432 AND SER-438, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371; SER-707; SER-738;
RP SER-740 AND SER-742, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [9]
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 [10]
RP FUNCTION, AND INTERACTION WITH PML.
RX PubMed=22002537; DOI=10.1038/emboj.2011.370;
RA Martin N., Benhamed M., Nacerddine K., Demarque M.D., van Lohuizen M.,
RA Dejean A., Bischof O.;
RT "Physical and functional interaction between PML and TBX2 in the
RT establishment of cellular senescence.";
RL EMBO J. 31:95-109(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438; SER-456; SER-707 AND
RP SER-738, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND IDENTIFICATION BY
RP 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 [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 101-311.
RX PubMed=12005433; DOI=10.1016/s0969-2126(02)00722-0;
RA Coll M., Seidman J.G., Muller C.W.;
RT "Structure of the DNA-bound T-box domain of human TBX3, a transcription
RT factor responsible for ulnar-mammary syndrome.";
RL Structure 10:343-356(2002).
CC -!- FUNCTION: Transcriptional repressor involved in developmental processes
CC (PubMed:10468588). Binds to the palindromic T site 5'-
CC TTCACACCTAGGTGTGAA-3' DNA sequence, or a half-site, which are present
CC in the regulatory region of several genes (PubMed:12000749). Probably
CC plays a role in limb pattern formation (PubMed:10468588). Required for
CC mammary placode induction, and maintenance of the mammary buds during
CC development (By similarity). Involved in branching morphogenesis in
CC both developing lungs and adult mammary glands, via negative modulation
CC of target genes; acting redundantly with TBX2 (By similarity).
CC Required, together with TBX2, to maintain cell proliferation in the
CC embryonic lung mesenchyme; perhaps acting downstream of SHH, BMP and
CC TGFbeta signaling (By similarity). Involved in modulating early inner
CC ear development, acting independently of, and also redundantly with,
CC TBX2 in different subregions of the developing ear (By similarity).
CC Acts as a negative regulator of PML function in cellular senescence
CC (PubMed:22002537). {ECO:0000250|UniProtKB:P70324,
CC ECO:0000269|PubMed:10468588, ECO:0000269|PubMed:12000749,
CC ECO:0000269|PubMed:22002537}.
CC -!- SUBUNIT: Interacts with PML (isoform PML-4).
CC {ECO:0000269|PubMed:22002537}.
CC -!- INTERACTION:
CC O15119; P35219: CA8; NbExp=3; IntAct=EBI-3452216, EBI-718700;
CC O15119; Q8N4W3: CSF3; NbExp=3; IntAct=EBI-3452216, EBI-12843274;
CC O15119; Q99471: PFDN5; NbExp=3; IntAct=EBI-3452216, EBI-357275;
CC O15119; P86480: PRR20D; NbExp=3; IntAct=EBI-3452216, EBI-12754095;
CC O15119; Q08117: TLE5; NbExp=3; IntAct=EBI-3452216, EBI-717810;
CC O15119; Q6NVU6: UFSP1; NbExp=3; IntAct=EBI-3452216, EBI-12068150;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=II;
CC IsoId=O15119-1; Sequence=Displayed;
CC Name=I;
CC IsoId=O15119-2; Sequence=VSP_006384;
CC Name=III;
CC IsoId=O15119-3; Sequence=VSP_006385, VSP_006386;
CC Name=IV;
CC IsoId=O15119-4; Sequence=Not described;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Ulnar-mammary syndrome (UMS) [MIM:181450]: Characterized by
CC ulnar ray defects, obesity, hypogenitalism, delayed puberty, hypoplasia
CC of nipples and apocrine glands. {ECO:0000269|PubMed:10330342}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: [Isoform II]: Contains an interrupted T-box domain.
CC -!- MISCELLANEOUS: [Isoform III]: Contains an interrupted T-box domain.
CC {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform IV]: May be produced by joining exon 1 to exon
CC 7 thereby eliminating the T-box. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TBX3ID42486ch12q24.html";
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DR EMBL; AF170708; AAD50989.2; -; mRNA.
DR EMBL; AF002228; AAC12947.1; -; mRNA.
DR EMBL; AF140240; AAF61816.1; -; mRNA.
DR EMBL; AF216750; AAF61207.1; -; mRNA.
DR EMBL; BC025258; AAH25258.1; -; mRNA.
DR CCDS; CCDS9175.1; -. [O15119-2]
DR CCDS; CCDS9176.1; -. [O15119-1]
DR RefSeq; NP_005987.3; NM_005996.3. [O15119-2]
DR RefSeq; NP_057653.3; NM_016569.3. [O15119-1]
DR PDB; 1H6F; X-ray; 1.70 A; A/B=101-311.
DR PDBsum; 1H6F; -.
DR AlphaFoldDB; O15119; -.
DR SMR; O15119; -.
DR BioGRID; 112788; 63.
DR IntAct; O15119; 20.
DR MINT; O15119; -.
DR STRING; 9606.ENSP00000257566; -.
DR iPTMnet; O15119; -.
DR PhosphoSitePlus; O15119; -.
DR BioMuta; TBX3; -.
DR EPD; O15119; -.
DR jPOST; O15119; -.
DR MassIVE; O15119; -.
DR MaxQB; O15119; -.
DR PaxDb; O15119; -.
DR PeptideAtlas; O15119; -.
DR PRIDE; O15119; -.
DR ProteomicsDB; 48454; -. [O15119-1]
DR ProteomicsDB; 48455; -. [O15119-2]
DR ProteomicsDB; 48456; -. [O15119-3]
DR Antibodypedia; 1789; 474 antibodies from 33 providers.
DR DNASU; 6926; -.
DR Ensembl; ENST00000257566.7; ENSP00000257566.3; ENSG00000135111.16. [O15119-1]
DR Ensembl; ENST00000349155.7; ENSP00000257567.2; ENSG00000135111.16. [O15119-2]
DR GeneID; 6926; -.
DR KEGG; hsa:6926; -.
DR MANE-Select; ENST00000349155.7; ENSP00000257567.2; NM_005996.4; NP_005987.3. [O15119-2]
DR UCSC; uc001tvt.2; human. [O15119-1]
DR CTD; 6926; -.
DR DisGeNET; 6926; -.
DR GeneCards; TBX3; -.
DR HGNC; HGNC:11602; TBX3.
DR HPA; ENSG00000135111; Tissue enhanced (adrenal).
DR MalaCards; TBX3; -.
DR MIM; 181450; phenotype.
DR MIM; 601621; gene.
DR neXtProt; NX_O15119; -.
DR OpenTargets; ENSG00000135111; -.
DR Orphanet; 3138; Ulnar-mammary syndrome.
DR PharmGKB; PA36365; -.
DR VEuPathDB; HostDB:ENSG00000135111; -.
DR eggNOG; KOG3585; Eukaryota.
DR GeneTree; ENSGT00940000158066; -.
DR HOGENOM; CLU_023038_1_0_1; -.
DR InParanoid; O15119; -.
DR OMA; QGIAMSP; -.
DR PhylomeDB; O15119; -.
DR TreeFam; TF106341; -.
DR PathwayCommons; O15119; -.
DR SignaLink; O15119; -.
DR SIGNOR; O15119; -.
DR BioGRID-ORCS; 6926; 34 hits in 1100 CRISPR screens.
DR ChiTaRS; TBX3; human.
DR EvolutionaryTrace; O15119; -.
DR GeneWiki; TBX3; -.
DR GenomeRNAi; 6926; -.
DR Pharos; O15119; Tbio.
DR PRO; PR:O15119; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; O15119; protein.
DR Bgee; ENSG00000135111; Expressed in right adrenal gland cortex and 170 other tissues.
DR ExpressionAtlas; O15119; baseline and differential.
DR Genevisible; O15119; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005929; C:cilium; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; IDA:MGI.
DR GO; GO:0008595; P:anterior/posterior axis specification, embryo; IMP:UniProtKB.
DR GO; GO:0003167; P:atrioventricular bundle cell differentiation; IEA:Ensembl.
DR GO; GO:0036302; P:atrioventricular canal development; ISS:BHF-UCL.
DR GO; GO:1905222; P:atrioventricular canal morphogenesis; ISS:BHF-UCL.
DR GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0003205; P:cardiac chamber development; IBA:GO_Central.
DR GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IMP:BHF-UCL.
DR GO; GO:1905072; P:cardiac jelly development; IMP:BHF-UCL.
DR GO; GO:0060923; P:cardiac muscle cell fate commitment; IEA:Ensembl.
DR GO; GO:0001708; P:cell fate specification; IBA:GO_Central.
DR GO; GO:0090398; P:cellular senescence; IDA:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0042733; P:embryonic digit morphogenesis; IMP:UniProtKB.
DR GO; GO:0035115; P:embryonic forelimb morphogenesis; IMP:UniProtKB.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Ensembl.
DR GO; GO:0003272; P:endocardial cushion formation; IMP:BHF-UCL.
DR GO; GO:0030540; P:female genitalia development; IMP:UniProtKB.
DR GO; GO:0046884; P:follicle-stimulating hormone secretion; IMP:UniProtKB.
DR GO; GO:0035136; P:forelimb morphogenesis; IDA:MGI.
DR GO; GO:0001947; P:heart looping; IBA:GO_Central.
DR GO; GO:0061017; P:hepatoblast differentiation; IEA:Ensembl.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:0021761; P:limbic system development; IEA:Ensembl.
DR GO; GO:0032275; P:luteinizing hormone secretion; IMP:UniProtKB.
DR GO; GO:0030539; P:male genitalia development; IMP:UniProtKB.
DR GO; GO:0030879; P:mammary gland development; IMP:UniProtKB.
DR GO; GO:0060596; P:mammary placode formation; IEA:Ensembl.
DR GO; GO:0048332; P:mesoderm morphogenesis; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
DR GO; GO:2000137; P:negative regulation of cell proliferation involved in heart morphogenesis; IMP:BHF-UCL.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:UniProtKB.
DR GO; GO:2000737; P:negative regulation of stem cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0045787; P:positive regulation of cell cycle; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IDA:UniProtKB.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0061635; P:regulation of protein complex stability; IEA:Ensembl.
DR GO; GO:0031647; P:regulation of protein stability; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
DR GO; GO:0060931; P:sinoatrial node cell development; IDA:BHF-UCL.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0051145; P:smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0010159; P:specification of animal organ position; IEA:Ensembl.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0072105; P:ureteric peristalsis; IEA:Ensembl.
DR GO; GO:0060412; P:ventricular septum morphogenesis; IEA:Ensembl.
DR CDD; cd00182; TBOX; 1.
DR Gene3D; 2.60.40.820; -; 1.
DR InterPro; IPR008967; p53-like_TF_DNA-bd.
DR InterPro; IPR046360; T-box_DNA-bd.
DR InterPro; IPR036960; T-box_sf.
DR InterPro; IPR022582; TBX2/3_TAD.
DR InterPro; IPR001699; TF_T-box.
DR InterPro; IPR018186; TF_T-box_CS.
DR PANTHER; PTHR11267; PTHR11267; 1.
DR Pfam; PF00907; T-box; 1.
DR Pfam; PF12598; TBX; 1.
DR PRINTS; PR00937; TBOX.
DR SMART; SM00425; TBOX; 1.
DR SUPFAM; SSF49417; SSF49417; 1.
DR PROSITE; PS01283; TBOX_1; 1.
DR PROSITE; PS01264; TBOX_2; 1.
DR PROSITE; PS50252; TBOX_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Developmental protein; Disease variant;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..743
FT /note="T-box transcription factor TBX3"
FT /id="PRO_0000184428"
FT DNA_BIND 107..220
FT /note="T-box; first part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT DNA_BIND 241..305
FT /note="T-box; second part"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00201"
FT REGION 301..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..695
FT /note="Transcription repression"
FT REGION 688..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..390
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..434
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 456
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 740
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 742
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 221..240
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000303|PubMed:10468588,
FT ECO:0000303|PubMed:9207801"
FT /id="VSP_006384"
FT VAR_SEQ 490..615
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006385"
FT VAR_SEQ 661..677
FT /note="Missing (in isoform III)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_006386"
FT VARIANT 143
FT /note="L -> P (in UMS)"
FT /evidence="ECO:0000269|PubMed:10330342"
FT /id="VAR_009601"
FT VARIANT 149
FT /note="Y -> S (in UMS)"
FT /evidence="ECO:0000269|PubMed:10330342"
FT /id="VAR_009602"
FT MUTAGEN 143
FT /note="L->P: Reduces binding to T site 5'-
FT TTCACACCTAGGTGTGAA-3' DNA sequence."
FT /evidence="ECO:0000269|PubMed:12000749"
FT MUTAGEN 149
FT /note="Y->S: Reduces binding to T site 5'-
FT TTCACACCTAGGTGTGAA-3' DNA sequence."
FT /evidence="ECO:0000269|PubMed:12000749"
FT CONFLICT 315
FT /note="K -> Q (in Ref. 4; AAF61207)"
FT /evidence="ECO:0000305"
FT CONFLICT 616..628
FT /note="SAAASSSVHRHPF -> LRQPQLRCTAPL (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="V -> A (in Ref. 1; AAD50989)"
FT /evidence="ECO:0000305"
FT CONFLICT 692
FT /note="L -> P (in Ref. 1; AAD50989)"
FT /evidence="ECO:0000305"
FT STRAND 104..107
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 137..142
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 145..166
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 191..193
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 194..197
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 246..255
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 260..265
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 269..272
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 274..276
FT /evidence="ECO:0007829|PDB:1H6F"
FT STRAND 278..283
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 287..296
FT /evidence="ECO:0007829|PDB:1H6F"
FT HELIX 298..303
FT /evidence="ECO:0007829|PDB:1H6F"
SQ SEQUENCE 743 AA; 79389 MW; D5572F9CF871E89F CRC64;
MSLSMRDPVI PGTSMAYHPF LPHRAPDFAM SAVLGHQPPF FPALTLPPNG AAALSLPGAL
AKPIMDQLVG AAETGIPFSS LGPQAHLRPL KTMEPEEEVE DDPKVHLEAK ELWDQFHKRG
TEMVITKSGR RMFPPFKVRC SGLDKKAKYI LLMDIIAADD CRYKFHNSRW MVAGKADPEM
PKRMYIHPDS PATGEQWMSK VVTFHKLKLT NNISDKHGFT LAFPSDHATW QGNYSFGTQT
ILNSMHKYQP RFHIVRANDI LKLPYSTFRT YLFPETEFIA VTAYQNDKIT QLKIDNNPFA
KGFRDTGNGR REKRKQLTLQ SMRVFDERHK KENGTSDESS SEQAAFNCFA QASSPAASTV
GTSNLKDLCP SEGESDAEAE SKEEHGPEAC DAAKISTTTS EEPCRDKGSP AVKAHLFAAE
RPRDSGRLDK ASPDSRHSPA TISSSTRGLG AEERRSPVRE GTAPAKVEEA RALPGKEAFA
PLTVQTDAAA AHLAQGPLPG LGFAPGLAGQ QFFNGHPLFL HPSQFAMGGA FSSMAAAGMG
PLLATVSGAS TGVSGLDSTA MASAAAAQGL SGASAATLPF HLQQHVLASQ GLAMSPFGSL
FPYPYTYMAA AAAASSAAAS SSVHRHPFLN LNTMRPRLRY SPYSIPVPVP DGSSLLTTAL
PSMAAAAGPL DGKVAALAAS PASVAVDSGS ELNSRSSTLS SSSMSLSPKL CAEKEAATSE
LQSIQRLVSG LEAKPDRSRS ASP
