SOX6_MOUSE
ID SOX6_MOUSE Reviewed; 827 AA.
AC P40645; Q62250; Q9QWS5;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Transcription factor SOX-6 {ECO:0000305};
DE AltName: Full=SOX-LZ {ECO:0000303|PubMed:10996314};
GN Name=Sox6 {ECO:0000303|PubMed:7567444, ECO:0000312|MGI:MGI:98368};
GN Synonyms=Sox-6;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=7567444; DOI=10.1093/nar/23.17.3365;
RA Connor F., Wright E., Denny P., Koopman P., Ashworth A.;
RT "The Sry-related HMG box-containing gene Sox6 is expressed in the adult
RT testis and developing nervous system of the mouse.";
RL Nucleic Acids Res. 23:3365-3372(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=7791783; DOI=10.1128/mcb.15.7.3759;
RA Takamatsu N., Kanda H., Tsuchiya I., Yamada S., Ito M., Kabeno S.,
RA Shiba T., Yamashita S.;
RT "A gene that is related to SRY and is expressed in the testes encodes a
RT leucine zipper-containing protein.";
RL Mol. Cell. Biol. 15:3759-3766(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 519-827, AND FUNCTION.
RX PubMed=9755172; DOI=10.1093/emboj/17.19.5718;
RA Lefebvre V., Li P., de Crombrugghe B.;
RT "A new long form of Sox5 (L-Sox5), Sox6 and Sox9 are coexpressed in
RT chondrogenesis and cooperatively activate the type II collagen gene.";
RL EMBO J. 17:5718-5733(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 631-684.
RC STRAIN=Parkes; TISSUE=Brain, and Testis;
RX PubMed=1614875; DOI=10.1093/nar/20.11.2887;
RA Denny P., Swift S., Brand N., Dabhade N., Barton P., Ashworth A.;
RT "A conserved family of genes related to the testis determining gene, SRY.";
RL Nucleic Acids Res. 20:2887-2887(1992).
RN [5]
RP PROTEIN SEQUENCE OF 660-666, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP POSSIBLE INTERACTION WITH CENPK.
RX PubMed=10996314; DOI=10.1016/s0014-5793(00)01987-6;
RA Yamashita A., Ito M., Takamatsu N., Shiba T.;
RT "Characterization of Solt, a novel SoxLZ/Sox6 binding protein expressed in
RT adult mouse testis.";
RL FEBS Lett. 481:147-151(2000).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11702786; DOI=10.1016/s1534-5807(01)00003-x;
RA Smits P., Li P., Mandel J., Zhang Z., Deng J.M., Behringer R.R.,
RA de Crombrugghe B., Lefebvre V.;
RT "The transcription factors L-Sox5 and Sox6 are essential for cartilage
RT formation.";
RL Dev. Cell 1:277-290(2001).
RN [8]
RP INDUCTION.
RX PubMed=12414734; DOI=10.1101/gad.1017802;
RA Akiyama H., Chaboissier M.C., Martin J.F., Schedl A., de Crombrugghe B.;
RT "The transcription factor Sox9 has essential roles in successive steps of
RT the chondrocyte differentiation pathway and is required for expression of
RT Sox5 and Sox6.";
RL Genes Dev. 16:2813-2828(2002).
RN [9]
RP INTERACTION WITH DAZAP2.
RX PubMed=14530442; DOI=10.1093/nar/gkg807;
RA Cohen-Barak O., Yi Z., Hagiwara N., Monzen K., Komuro I., Brilliant M.H.;
RT "Sox6 regulation of cardiac myocyte development.";
RL Nucleic Acids Res. 31:5941-5948(2003).
RN [10]
RP FUNCTION.
RX PubMed=15529345; DOI=10.1002/art.20611;
RA Ikeda T., Kamekura S., Mabuchi A., Kou I., Seki S., Takato T., Nakamura K.,
RA Kawaguchi H., Ikegawa S., Chung U.I.;
RT "The combination of SOX5, SOX6, and SOX9 (the SOX trio) provides signals
RT sufficient for induction of permanent cartilage.";
RL Arthritis Rheum. 50:3561-3573(2004).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14993235; DOI=10.1083/jcb.200312045;
RA Smits P., Dy P., Mitra S., Lefebvre V.;
RT "Sox5 and Sox6 are needed to develop and maintain source, columnar, and
RT hypertrophic chondrocytes in the cartilage growth plate.";
RL J. Cell Biol. 164:747-758(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-119; SER-399; THR-401;
RP SER-439 AND SER-442, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Kidney, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [14]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=26150426; DOI=10.1093/nar/gkv688;
RA Liu C.F., Lefebvre V.;
RT "The transcription factors SOX9 and SOX5/SOX6 cooperate genome-wide through
RT super-enhancers to drive chondrogenesis.";
RL Nucleic Acids Res. 43:8183-8203(2015).
RN [15]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=26525805; DOI=10.1111/jnc.13414;
RA Baroti T., Schillinger A., Wegner M., Stolt C.C.;
RT "Sox13 functionally complements the related Sox5 and Sox6 as important
RT developmental modulators in mouse spinal cord oligodendrocytes.";
RL J. Neurochem. 136:316-328(2016).
RN [16]
RP DEVELOPMENTAL STAGE.
RX PubMed=27923061; DOI=10.1371/journal.pgen.1006474;
RA Brunmeir R., Wu J., Peng X., Kim S.Y., Julien S.G., Zhang Q., Xie W.,
RA Xu F.;
RT "Comparative Transcriptomic and Epigenomic Analyses Reveal New Regulators
RT of Murine Brown Adipogenesis.";
RL PLoS Genet. 12:E1006474-E1006474(2016).
RN [17]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF TRP-161;
RP MET-624; TRP-658 AND SER-765.
RX PubMed=32442410; DOI=10.1016/j.ajhg.2020.04.015;
RG Genomics England Research Consortium;
RA Tolchin D., Yeager J.P., Prasad P., Dorrani N., Russi A.S.,
RA Martinez-Agosto J.A., Haseeb A., Angelozzi M., Santen G.W.E.,
RA Ruivenkamp C., Mercimek-Andrews S., Depienne C., Kuechler A., Mikat B.,
RA Ludecke H.J., Bilan F., Le Guyader G., Gilbert-Dussardier B., Keren B.,
RA Heide S., Haye D., Van Esch H., Keldermans L., Ortiz D., Lancaster E.,
RA Krantz I.D., Krock B.L., Pechter K.B., Arkader A., Medne L., DeChene E.T.,
RA Calpena E., Melistaccio G., Wilkie A.O.M., Suri M., Foulds N., Begtrup A.,
RA Henderson L.B., Forster C., Reed P., McDonald M.T., McConkie-Rosell A.,
RA Thevenon J., Le Tanno P., Coutton C., Tsai A.C.H., Stewart S., Maver A.,
RA Gorazd R., Pichon O., Nizon M., Cogne B., Isidor B., Martin-Coignard D.,
RA Stoeva R., Lefebvre V., Le Caignec C.;
RT "De Novo SOX6 Variants Cause a Neurodevelopmental Syndrome Associated with
RT ADHD, Craniosynostosis, and Osteochondromas.";
RL Am. J. Hum. Genet. 106:830-845(2020).
CC -!- FUNCTION: Transcription factor that plays a key role in several
CC developmental processes, including neurogenesis, chondrocytes
CC differentiation and cartilage formation (Probable). Specifically binds
CC the 5'-AACAAT-3' DNA motif present in enhancers and super-enhancers and
CC promotes expression of genes important for chondrogenesis
CC (PubMed:9755172, PubMed:11702786). Required for overt chondrogenesis
CC when condensed prechondrocytes differentiate into early stage
CC chondrocytes: SOX5 and SOX6 cooperatively bind with SOX9 on active
CC enhancers and super-enhancers associated with cartilage-specific genes,
CC and thereby potentiate SOX9's ability to transactivate
CC (PubMed:11702786, PubMed:15529345, PubMed:26150426). Not involved in
CC precartilaginous condensation, the first step in chondrogenesis, during
CC which skeletal progenitors differentiate into prechondrocytes
CC (PubMed:14993235, PubMed:26150426). Together with SOX5, required to
CC form and maintain a pool of highly proliferating chondroblasts between
CC epiphyses and metaphyses, to form columnar chondroblasts, delay
CC chondrocyte prehypertrophy but promote hypertrophy, and to delay
CC terminal differentiation of chondrocytes on contact with ossification
CC fronts (PubMed:14993235). Binds to the proximal promoter region of the
CC myelin protein MPZ gene, and is thereby involved in the differentiation
CC of oligodendroglia in the developing spinal tube (PubMed:26525805).
CC Binds to the gene promoter of MBP and acts as a transcriptional
CC repressor (PubMed:26525805). {ECO:0000269|PubMed:11702786,
CC ECO:0000269|PubMed:14993235, ECO:0000269|PubMed:15529345,
CC ECO:0000269|PubMed:26150426, ECO:0000269|PubMed:26525805,
CC ECO:0000269|PubMed:32442410, ECO:0000269|PubMed:7567444,
CC ECO:0000269|PubMed:9755172, ECO:0000305|PubMed:32442410}.
CC -!- SUBUNIT: Homodimer (PubMed:32442410). Interacts with DAZAP2
CC (PubMed:14530442). May interact with CENPK (PubMed:10996314).
CC {ECO:0000269|PubMed:10996314, ECO:0000269|PubMed:14530442,
CC ECO:0000269|PubMed:32442410}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:32442410}. Cytoplasm {ECO:0000269|PubMed:32442410}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=P40645-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P40645-2; Sequence=VSP_002198;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC -!- DEVELOPMENTAL STAGE: Expression is transiently increased during brown
CC adipocyte differentiation. {ECO:0000269|PubMed:27923061}.
CC -!- INDUCTION: Expression is dependent on SOX9.
CC {ECO:0000269|PubMed:12414734}.
CC -!- PTM: Sumoylation inhibits the transcriptional activity.
CC {ECO:0000250|UniProtKB:P35712}.
CC -!- DISRUPTION PHENOTYPE: Newborn mice display mild skeletal abnormalities
CC (PubMed:11702786). Knockout mice also display increase in prematurely
CC differentiated oligodendrocyte precursor cells in the motor neuron
CC progenitor domain of the spinal tube at 11.5 dpc (PubMed:26525805). At
CC 18.5 dpc the number and distribution of oligodendroglia are normal,
CC however there is an increased number of differentiating
CC oligodendrocytes (PubMed:26525805). Double knockout of Sox13 and Sox6
CC show an increase in oligodendrocyte precursor cells in the spinal tube
CC at 11.5 dpc, at 18.5 dpc the number and distribution of oligodendroglia
CC are normal but contain an increased number of differentiating cells
CC (PubMed:26525805). Mice lacking both Sox5 and Sox6 develop a severe
CC chondrodysplasia characterized by the virtual absence of cartilage:
CC chondrogenic cells are largely arrested at the stage of chondrogenic
CC mesenchymal condensations (PubMed:11702786). Embryos lacking Sox5
CC (homozygous knockout) and heterozygous for Sox6 live until birth and
CC show severe growth plate chondrocyte defects (PubMed:14993235). Embryos
CC lacking Sox6 (homozygous knockout) and heterozygous for Sox5 live until
CC birth and show severe growth plate chondrocyte defects
CC (PubMed:14993235). {ECO:0000269|PubMed:11702786,
CC ECO:0000269|PubMed:14993235, ECO:0000269|PubMed:26525805}.
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DR EMBL; U32614; AAC52263.1; -; mRNA.
DR EMBL; D61689; BAA09618.1; -; mRNA.
DR EMBL; AJ010605; CAA09270.1; -; mRNA.
DR EMBL; X65659; CAA46610.1; -; mRNA.
DR CCDS; CCDS40098.1; -. [P40645-1]
DR PIR; S22944; S22944.
DR PIR; S59121; S59121.
DR RefSeq; NP_001264255.1; NM_001277326.1. [P40645-1]
DR RefSeq; NP_001264257.1; NM_001277328.1. [P40645-2]
DR RefSeq; NP_035575.1; NM_011445.4. [P40645-1]
DR RefSeq; XP_011240009.1; XM_011241707.2. [P40645-1]
DR RefSeq; XP_011240013.1; XM_011241711.2.
DR AlphaFoldDB; P40645; -.
DR SMR; P40645; -.
DR BioGRID; 203410; 6.
DR IntAct; P40645; 3.
DR STRING; 10090.ENSMUSP00000072583; -.
DR iPTMnet; P40645; -.
DR PhosphoSitePlus; P40645; -.
DR jPOST; P40645; -.
DR MaxQB; P40645; -.
DR PaxDb; P40645; -.
DR PRIDE; P40645; -.
DR ProteomicsDB; 261117; -. [P40645-1]
DR ProteomicsDB; 261118; -. [P40645-2]
DR Antibodypedia; 1097; 299 antibodies from 33 providers.
DR DNASU; 20679; -.
DR Ensembl; ENSMUST00000072804; ENSMUSP00000072583; ENSMUSG00000051910. [P40645-1]
DR Ensembl; ENSMUST00000166207; ENSMUSP00000129027; ENSMUSG00000051910. [P40645-1]
DR GeneID; 20679; -.
DR KEGG; mmu:20679; -.
DR UCSC; uc009jin.2; mouse. [P40645-2]
DR UCSC; uc009jip.2; mouse. [P40645-1]
DR CTD; 55553; -.
DR MGI; MGI:98368; Sox6.
DR VEuPathDB; HostDB:ENSMUSG00000051910; -.
DR eggNOG; KOG0528; Eukaryota.
DR GeneTree; ENSGT00940000156433; -.
DR InParanoid; P40645; -.
DR OMA; GDKAMNG; -.
DR PhylomeDB; P40645; -.
DR TreeFam; TF320471; -.
DR Reactome; R-MMU-3769402; Deactivation of the beta-catenin transactivating complex.
DR BioGRID-ORCS; 20679; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Sox6; mouse.
DR PRO; PR:P40645; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P40645; protein.
DR Bgee; ENSMUSG00000051910; Expressed in triceps brachii and 239 other tissues.
DR ExpressionAtlas; P40645; baseline and differential.
DR Genevisible; P40645; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IC:MGI.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001217; F:DNA-binding transcription repressor activity; IDA:UniProtKB.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IMP:NTNU_SB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IMP:NTNU_SB.
DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:MGI.
DR GO; GO:0048708; P:astrocyte differentiation; ISO:MGI.
DR GO; GO:0007420; P:brain development; ISS:UniProtKB.
DR GO; GO:0055007; P:cardiac muscle cell differentiation; IDA:MGI.
DR GO; GO:0001502; P:cartilage condensation; IMP:UniProtKB.
DR GO; GO:0051216; P:cartilage development; IDA:UniProtKB.
DR GO; GO:0045165; P:cell fate commitment; IGI:MGI.
DR GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISO:MGI.
DR GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
DR GO; GO:0002062; P:chondrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0048821; P:erythrocyte development; IMP:MGI.
DR GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0021778; P:oligodendrocyte cell fate specification; IMP:MGI.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IMP:MGI.
DR GO; GO:0061036; P:positive regulation of cartilage development; ISO:MGI.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:UniProtKB.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0009791; P:post-embryonic development; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0021529; P:spinal cord oligodendrocyte cell differentiation; IMP:UniProtKB.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR027153; SOX-6.
DR PANTHER; PTHR45789:SF1; PTHR45789:SF1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Coiled coil; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..827
FT /note="Transcription factor SOX-6"
FT /id="PRO_0000048730"
FT DNA_BIND 620..688
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..827
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..262
FT /evidence="ECO:0000255"
FT COMPBIAS 21..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 797..812
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 119
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 401
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 439
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 404
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT VAR_SEQ 327..367
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:7791783"
FT /id="VSP_002198"
FT MUTAGEN 161
FT /note="W->C: Decreased localization to the nucleus. No
FT effect on homodimerization. No effect on transcription cis-
FT regulatory region binding. No effect on DNA-binding
FT transcription factor activity."
FT /evidence="ECO:0000269|PubMed:32442410"
FT MUTAGEN 624
FT /note="M->T: Decreased localization to the nucleus. No
FT effect on homodimerization. Decreased transcription cis-
FT regulatory region binding. Loss of DNA-binding
FT transcription factor activity. Acts as a dominant
FT negative."
FT /evidence="ECO:0000269|PubMed:32442410"
FT MUTAGEN 658
FT /note="W->R: Loss of localization to the nucleus. Loss of
FT transcription cis-regulatory region binding. Loss of DNA-
FT binding transcription factor activity. Acts as a dominant
FT negative."
FT /evidence="ECO:0000269|PubMed:32442410"
FT MUTAGEN 765
FT /note="S->L: Increased localization to the nucleus.
FT Decreased transcription cis-regulatory region binding. No
FT effect on DNA-binding transcription factor activity."
FT /evidence="ECO:0000269|PubMed:32442410"
FT CONFLICT 312..313
FT /note="MA -> SS (in Ref. 2; BAA09618)"
FT /evidence="ECO:0000305"
FT CONFLICT 632
FT /note="K -> R (in Ref. 4; CAA46610)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 827 AA; 91803 MW; F777BAB7CFB1E93B CRC64;
MSSKQATSPF ACTADGEEAM TQDLTSREKE EGSDQHPASH LPLHPIMHNK PHSEELPTLV
STIQQDADWD SVLSSQQRME SENNKLCSLY SFRNTSTSPH KPDEGSRERE IMNSVTFGTP
ERRKGSLADV VDTLKQKKLE EMTRTEQEDS SCMEKLLSKD WKEKMERLNT SELLGEIKGT
PESLAEKERQ LSTMITQLIS LREQLLAAHD EQKKLAASQI EKQRQQMDLA RQQQEQIARQ
QQQLLQQQHK INLLQQQIQV QGHMPPLMIP IFPHDQRTLA AAAAAQQGFL FPPGITYKPG
DNYPVQFIPS TMAAAAASGL SPLQLQKGHV SHPQINPRLK GISDRFGRNL DPSEHGGGHS
YNHRQIEQLY AAQLASMQVS PGAKMPSTPQ PPNSAGAVSP TGIKNEKRGT SPVTQVKDET
TAQPLNLSSR PKTAEPVKSP TSPTQNLFPA SKTSPVNLPN KSSIPSPIGG SLGRGSSLDI
LSSLNSPALF GDQDTVMKAI QEARKMREQI QREQQQQPHG VDGKLSSMNN MGLSNCRTEK
ERTRFENLGP QLTGKSSEDG KLGPGVIDLT RPEDAEGSKA MNGSAAKLQQ YYCWPTGGAT
VAEARVYRDA RGRASSEPHI KRPMNAFMVW AKDERRKILQ AFPDMHNSNI SKILGSRWKS
MSNQEKQPYY EEQARLSKIH LEKYPNYKYK PRPKRTCIVD GKKLRIGEYK QLMRSRRQEM
RQFFTVGQQP QMPITTGTGV VYPGAITMAT TTPSPQMTSD CSSTSASPEP SLPVIQSTYG
MKMDGASLAG NDMINGEDEM EAYDDYEDDP KSDYSSENEA PEPVSAN
