SOX9_HUMAN
ID SOX9_HUMAN Reviewed; 509 AA.
AC P48436; Q53Y80;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 212.
DE RecName: Full=Transcription factor SOX-9 {ECO:0000305};
GN Name=SOX9 {ECO:0000303|PubMed:7990924, ECO:0000312|HGNC:HGNC:11204};
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], AND INVOLVEMENT IN CMD1.
RC TISSUE=Testis;
RX PubMed=7990924; DOI=10.1038/372525a0;
RA Foster J.W., Dominguez-Steglich M.A., Guioli S., Kowk G., Weller P.A.,
RA Stevanovic M., Weissenbach J., Mansour S., Young I.D., Goodfellow P.N.,
RA Schafer A.J.;
RT "Campomelic dysplasia and autosomal sex reversal caused by mutations in an
RT SRY-related gene.";
RL Nature 372:525-530(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN CMD1, AND VARIANT CMD1
RP 440-TYR--PRO-509 DEL.
RX PubMed=8001137; DOI=10.1016/0092-8674(94)90041-8;
RA Wagner T., Wirth J., Meyer J., Zabel B., Held M., Zimmer J., Pasantes J.,
RA Bricarelli F.D., Keutel J., Hustert E., Wolf U., Tommerup N., Schempp W.,
RA Scherer G.;
RT "Autosomal sex reversal and campomelic dysplasia are caused by mutations in
RT and around the SRY-related gene SOX9.";
RL Cell 79:1111-1120(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye, and PNS;
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, SUBCELLULAR LOCATION, AND DNA-BINDING.
RX PubMed=8640233; DOI=10.1038/ng0696-230;
RA Suedbeck P., Schmitz M.L., Baeuerle P.A., Scherer G.;
RT "Sex reversal by loss of the C-terminal transactivation domain of human
RT SOX9.";
RL Nat. Genet. 13:230-232(1996).
RN [7]
RP INTERACTION WITH EP300.
RX PubMed=12732631; DOI=10.1074/jbc.m303471200;
RA Tsuda M., Takahashi S., Takahashi Y., Asahara H.;
RT "Transcriptional co-activators CREB-binding protein and p300 regulate
RT chondrocyte-specific gene expression via association with Sox9.";
RL J. Biol. Chem. 278:27224-27229(2003).
RN [8]
RP INVOLVEMENT IN SRXX2.
RX PubMed=21208124; DOI=10.1056/nejmc1010311;
RA Cox J.J., Willatt L., Homfray T., Woods C.G.;
RT "A SOX9 duplication and familial 46,XX developmental testicular disorder.";
RL N. Engl. J. Med. 364:91-93(2011).
RN [9]
RP INVOLVEMENT IN SRXY10.
RX PubMed=25604083; DOI=10.1136/jmedgenet-2014-102864;
RA Kim G.J., Sock E., Buchberger A., Just W., Denzer F., Hoepffner W.,
RA German J., Cole T., Mann J., Seguin J.H., Zipf W., Costigan C.,
RA Schmiady H., Rostasy M., Kramer M., Kaltenbach S., Roesler B., Georg I.,
RA Troppmann E., Teichmann A.C., Salfelder A., Widholz S.A., Wieacker P.,
RA Hiort O., Camerino G., Radi O., Wegner M., Arnold H.H., Scherer G.;
RT "Copy number variation of two separate regulatory regions upstream of SOX9
RT causes isolated 46,XY or 46,XX disorder of sex development.";
RL J. Med. Genet. 52:240-247(2015).
RN [10]
RP INTERACTION WITH DDRGK1, AND UBIQUITINATION.
RX PubMed=28263186; DOI=10.1172/jci90193;
RA Egunsola A.T., Bae Y., Jiang M.M., Liu D.S., Chen-Evenson Y., Bertin T.,
RA Chen S., Lu J.T., Nevarez L., Magal N., Raas-Rothschild A., Swindell E.C.,
RA Cohn D.H., Gibbs R.A., Campeau P.M., Shohat M., Lee B.H.;
RT "Loss of DDRGK1 modulates SOX9 ubiquitination in spondyloepimetaphyseal
RT dysplasia.";
RL J. Clin. Invest. 127:1475-1484(2017).
RN [11]
RP REVIEW.
RX PubMed=31382142; DOI=10.1016/j.ceb.2019.07.008;
RA Lefebvre V., Angelozzi M., Haseeb A.;
RT "SOX9 in cartilage development and disease.";
RL Curr. Opin. Cell Biol. 61:39-47(2019).
RN [12]
RP DOMAIN, 9AATAD MOTIFS, AND MUTAGENESIS OF LEU-278; VAL-282; ASP-290;
RP GLU-293; PHE-294; GLN-296; TYR-297 AND LEU-298.
RX PubMed=31194875; DOI=10.1093/nar/gkz523;
RA Haseeb A., Lefebvre V.;
RT "The SOXE transcription factors-SOX8, SOX9 and SOX10-share a bi-partite
RT transactivation mechanism.";
RL Nucleic Acids Res. 47:6917-6931(2019).
RN [13]
RP 9AATAD MOTIF.
RX PubMed=34342803; DOI=10.1007/s12015-021-10225-8;
RA Piskacek M., Otasevic T., Repko M., Knight A.;
RT "The 9aaTAD Activation Domains in the Yamanaka Transcription Factors Oct4,
RT Sox2, Myc, and Klf4.";
RL Stem. Cell. Rev. Rep. 17:1934-1936(2021).
RN [14]
RP REVIEW ON VARIANTS.
RX PubMed=9143916;
RX DOI=10.1002/(sici)1098-1004(1997)9:5<388::aid-humu2>3.0.co;2-0;
RA Cameron F.J., Sinclair A.H.;
RT "Mutations in SRY and SOX9: testis-determining genes.";
RL Hum. Mutat. 9:388-395(1997).
RN [15]
RP VARIANTS CMD1 LEU-112 AND VAL-119.
RX PubMed=7485151;
RA Kwok C., Weller P.A., Guioli S., Foster J.W., Mansour S., Zuffardi O.,
RA Punnett H.H., Dominguez-Steglich M.A., Brook J.D., Young I.D.,
RA Goodfellow P.N., Schafer A.J.;
RT "Mutations in SOX9, the gene responsible for Campomelic dysplasia and
RT autosomal sex reversal.";
RL Am. J. Hum. Genet. 57:1028-1036(1995).
RN [16]
RP VARIANTS CMD1 LEU-108; ARG-143; PRO-152 AND ARG-170.
RX PubMed=9002675; DOI=10.1093/hmg/6.1.91;
RA Meyer J., Suedbeck P., Held M., Wagner T., Schmitz M.L., Bricarelli F.D.,
RA Eggermont E., Friedrich U., Haas O.A., Kobelt A., Leroy J.G.,
RA van Maldergem L., Michel E., Mitulla B., Pfeiffer R.A., Schinzel A.,
RA Schmidt H., Scherer G.;
RT "Mutational analysis of the SOX9 gene in campomelic dysplasia and autosomal
RT sex reversal: lack of genotype/phenotype correlations.";
RL Hum. Mol. Genet. 6:91-98(1997).
RN [17]
RP VARIANT CMD1 SER-112.
RX PubMed=9452059; DOI=10.1002/humu.1380110138;
RA Goji K., Nishijima E., Tsugawa C., Nishio H., Pokharel R.K., Matsuo M.;
RT "Novel missense mutation in the HMG box of SOX9 gene in a Japanese XY male
RT resulted in campomelic dysplasia and severe defect in masculinization.";
RL Hum. Mutat. Suppl. 1:S114-S116(1998).
RN [18]
RP VARIANTS CMD1 LEU-112; VAL-119; TYR-165 AND ARG-170, AND 3D-STRUCTURE
RP MODELING.
RX PubMed=10446171; DOI=10.1074/jbc.274.34.24023;
RA McDowall S., Argentaro A., Ranganathan S., Weller P., Mertin S.,
RA Mansour S., Tolmie J., Harley V.;
RT "Functional and structural studies of wild type SOX9 and mutations causing
RT campomelic dysplasia.";
RL J. Biol. Chem. 274:24023-24030(1999).
RN [19]
RP VARIANT CMD1 GLU-173.
RX PubMed=10951468;
RX DOI=10.1002/1096-8628(20000828)93:5<421::aid-ajmg14>3.0.co;2-5;
RA Thong M.-K., Scherer G., Kozlowski K., Haan E., Morris L.;
RT "Acampomelic campomelic dysplasia with SOX9 mutation.";
RL Am. J. Med. Genet. 93:421-425(2000).
RN [20]
RP VARIANT CMD1 TYR-165.
RX PubMed=11754051; DOI=10.1002/ajmg.10033;
RA Moog U., Jansen N.J., Scherer G., Schrander-Stumpel C.T.;
RT "Acampomelic campomelic syndrome.";
RL Am. J. Med. Genet. 104:239-245(2001).
RN [21]
RP VARIANTS CMD1 LEU-154 AND THR-158, AND CHARACTERIZATION OF VARIANTS CMD1
RP LEU-154 AND THR-158.
RX PubMed=11323423; DOI=10.1074/jbc.m101278200;
RA Preiss S., Argentaro A., Clayton A., John A., Jans D.A., Ogata T.,
RA Nagai T., Barroso I., Schafer A.J., Harley V.R.;
RT "Compound effects of point mutations causing campomelic dysplasia/autosomal
RT sex reversal upon SOX9 structure, nuclear transport, DNA binding, and
RT transcriptional activation.";
RL J. Biol. Chem. 276:27864-27872(2001).
RN [22]
RP VARIANT CMD1 GLU-76.
RX PubMed=12783851; DOI=10.1093/hmg/ddg158;
RA Sock E., Pagon R.A., Keymolen K., Lissens W., Wegner M., Scherer G.;
RT "Loss of DNA-dependent dimerization of the transcription factor SOX9 as a
RT cause for campomelic dysplasia.";
RL Hum. Mol. Genet. 12:1439-1447(2003).
RN [23]
RP VARIANTS CMD1 28-GLU--PRO-509 DEL AND PRO-169.
RX PubMed=19033726; DOI=10.1159/000176299;
RA Massardier J., Roth P., Michel-Calemard L., Rudigoz R.C., Bouvier R.,
RA Dijoud F., Arnould P., Combourieu D., Gaucherand P.;
RT "Campomelic dysplasia: echographic suspicion in the first trimester of
RT pregnancy and final diagnosis of two cases.";
RL Fetal Diagn. Ther. 24:452-457(2008).
RN [24]
RP VARIANTS CMD1 THR-113 AND LEU-170.
RX PubMed=19921652; DOI=10.1002/ajmg.a.33107;
RA Wada Y., Nishimura G., Nagai T., Sawai H., Yoshikata M., Miyagawa S.,
RA Hanita T., Sato S., Hasegawa T., Ishikawa S., Ogata T.;
RT "Mutation analysis of SOX9 and single copy number variant analysis of the
RT upstream region in eight patients with campomelic dysplasia and acampomelic
RT campomelic dysplasia.";
RL Am. J. Med. Genet. A 149:2882-2885(2009).
RN [25]
RP VARIANTS CMD1 VAL-113 AND GLN-165, AND CHARACTERIZATION OF VARIANTS CMD1
RP VAL-113 AND GLN-165.
RX PubMed=20513132; DOI=10.1002/humu.21238;
RA Staffler A., Hammel M., Wahlbuhl M., Bidlingmaier C., Flemmer A.W.,
RA Pagel P., Nicolai T., Wegner M., Holzinger A.;
RT "Heterozygous SOX9 mutations allowing for residual DNA-binding and
RT transcriptional activation lead to the acampomelic variant of campomelic
RT dysplasia.";
RL Hum. Mutat. 31:E1436-E1444(2010).
RN [26]
RP VARIANT CMD1 GLN-169, CHARACTERIZATION OF VARIANT CMD1 GLN-169,
RP CHARACTERIZATION OF VARIANT PRO-169, AND FUNCTION.
RX PubMed=24038782; DOI=10.1002/ajmg.a.36134;
RA Matsushita M., Kitoh H., Kaneko H., Mishima K., Kadono I., Ishiguro N.,
RA Nishimura G.;
RT "A novel SOX9 H169Q mutation in a family with overlapping phenotype of mild
RT campomelic dysplasia and small patella syndrome.";
RL Am. J. Med. Genet. A 161A:2528-2534(2013).
CC -!- FUNCTION: Transcription factor that plays a key role in chondrocytes
CC differentiation and skeletal development (PubMed:24038782).
CC Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and
CC super-enhancers and promotes expression of genes important for
CC chondrogenesis, including cartilage matrix protein-coding genes COL2A1,
CC COL4A2, COL9A1, COL11A2 and ACAN, SOX5 and SOX6 (PubMed:8640233). Also
CC binds to some promoter regions (By similarity). Plays a central role in
CC successive steps of chondrocyte differentiation (By similarity).
CC Absolutely required for precartilaginous condensation, the first step
CC in chondrogenesis during which skeletal progenitors differentiate into
CC prechondrocytes (By similarity). Together with SOX5 and SOX6, required
CC for overt chondrogenesis when condensed prechondrocytes differentiate
CC into early stage chondrocytes, the second step in chondrogenesis (By
CC similarity). Later, required to direct hypertrophic maturation and
CC block osteoblast differentiation of growth plate chondrocytes:
CC maintains chondrocyte columnar proliferation, delays prehypertrophy and
CC then prevents osteoblastic differentiation of chondrocytes by lowering
CC beta-catenin (CTNNB1) signaling and RUNX2 expression (By similarity).
CC Also required for chondrocyte hypertrophy, both indirectly, by keeping
CC the lineage fate of chondrocytes, and directly, by remaining present in
CC upper hypertrophic cells and transactivating COL10A1 along with MEF2C
CC (By similarity). Low lipid levels are the main nutritional determinant
CC for chondrogenic commitment of skeletal progenitor cells: when lipids
CC levels are low, FOXO (FOXO1 and FOXO3) transcription factors promote
CC expression of SOX9, which induces chondrogenic commitment and
CC suppresses fatty acid oxidation (By similarity). Mechanistically,
CC helps, but is not required, to remove epigenetic signatures of
CC transcriptional repression and deposit active promoter and enhancer
CC marks at chondrocyte-specific genes (By similarity). Acts in
CC cooperation with the Hedgehog pathway-dependent GLI (GLI1 and GLI3)
CC transcription factors (By similarity). In addition to cartilage
CC development, also acts as a regulator of proliferation and
CC differentiation in epithelial stem/progenitor cells: involved in the
CC lung epithelium during branching morphogenesis, by balancing
CC proliferation and differentiation and regulating the extracellular
CC matrix (By similarity). Controls epithelial branching during kidney
CC development (By similarity). {ECO:0000250|UniProtKB:Q04887,
CC ECO:0000269|PubMed:24038782, ECO:0000269|PubMed:8640233}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for activity (By
CC similarity). Interacts (via C-terminus) with ZNF219; forming a complex
CC that binds to the COL2A1 promoter and activates COL2A1 expression (By
CC similarity). Interacts with DDRGK1 (PubMed:28263186). Interacts with
CC EP300/p300 (PubMed:12732631). Interacts with beta-catenin (CTNNB1);
CC inhibiting CTNNB1 activity by competing with the binding sites of
CC TCF/LEF within CTNNB1 (By similarity). {ECO:0000250|UniProtKB:Q04887,
CC ECO:0000269|PubMed:12732631, ECO:0000269|PubMed:28263186}.
CC -!- INTERACTION:
CC P48436; Q3U108: Arid5a; Xeno; NbExp=3; IntAct=EBI-3920028, EBI-14022639;
CC P48436; P62157: CALM; Xeno; NbExp=7; IntAct=EBI-3920028, EBI-397403;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:8640233}.
CC -!- DOMAIN: The transactivation domains TAM and TAC (for transactivation
CC domain in the middle and at the C-terminus, respectively) are required
CC to contact transcriptional coactivators and basal transcriptional
CC machinery components and thereby induce gene transactivation.
CC {ECO:0000269|PubMed:31194875, ECO:0000269|PubMed:8640233}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:34342803}.
CC -!- DOMAIN: The PQA region (for proline, glutamine and alanine-rich) helps
CC stabilize SOX9 and facilitates transactivation (PubMed:31194875). It
CC lacks intrinsic transactivation capability (PubMed:31194875).
CC {ECO:0000269|PubMed:31194875}.
CC -!- PTM: Acetylated; acetylation impairs nuclear localization and ability
CC to transactivate expression of target genes. Deacetylated by SIRT1.
CC {ECO:0000250|UniProtKB:Q04887}.
CC -!- PTM: Phosphorylation at Ser-64 and Ser-211 by PKA increases
CC transcriptional activity and may help delay chondrocyte maturation
CC downstream of PTHLH/PTHrP signaling. Phosphorylation at either Ser-64
CC or Ser-211 is required for sumoylation, but phosphorylation is not
CC dependent on sumoylation. Phosphorylated on tyrosine residues; tyrosine
CC dephosphorylation by PTPN11/SHP2 blocks SOX9 phosphorylation by PKA and
CC subsequent SUMOylation. {ECO:0000250|UniProtKB:Q04887}.
CC -!- PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation and
CC is negatively regulated by DDRGK1. {ECO:0000269|PubMed:28263186}.
CC -!- PTM: Sumoylated; phosphorylation at either Ser-64 or Ser-211 is
CC required for sumoylation. Sumoylation is induced by BMP signaling
CC pathway. {ECO:0000250|UniProtKB:Q04887}.
CC -!- DISEASE: Campomelic dysplasia (CMD1) [MIM:114290]: A rare, often
CC lethal, osteochondrodysplasia characterized by congenital bowing and
CC angulation of long bones. Other skeletal defects include unusually
CC small scapula, deformed pelvis and spine, and a missing pair of ribs.
CC Craniofacial and ear defects are common. Most patients die soon after
CC birth due to respiratory distress which has been attributed to
CC hypoplasia of the tracheobronchial cartilage and small thoracic cage.
CC Up to two-thirds of affected XY individuals have genital defects or may
CC develop as phenotypic females. {ECO:0000269|PubMed:10446171,
CC ECO:0000269|PubMed:10951468, ECO:0000269|PubMed:11323423,
CC ECO:0000269|PubMed:11754051, ECO:0000269|PubMed:12783851,
CC ECO:0000269|PubMed:19033726, ECO:0000269|PubMed:19921652,
CC ECO:0000269|PubMed:20513132, ECO:0000269|PubMed:24038782,
CC ECO:0000269|PubMed:7485151, ECO:0000269|PubMed:7990924,
CC ECO:0000269|PubMed:8001137, ECO:0000269|PubMed:9002675,
CC ECO:0000269|PubMed:9452059}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: 46,XX sex reversal 2 (SRXX2) [MIM:278850]: A condition in
CC which male gonads develop in a genetic female (female to male sex
CC reversal). {ECO:0000269|PubMed:21208124}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: 46,XY sex reversal 10 (SRXY10) [MIM:616425]: A disorder of sex
CC development. Affected individuals have a 46,XY karyotype, show gonadal
CC dysgenesis with streak gonads, look like normal females at birth, do
CC not develop secondary sexual characteristics at puberty and do not
CC menstruate. {ECO:0000269|PubMed:25604083}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
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DR EMBL; Z46629; CAA86598.1; -; mRNA.
DR EMBL; S74506; AAB32870.1; -; Genomic_DNA.
DR EMBL; S74504; AAB32870.1; JOINED; Genomic_DNA.
DR EMBL; S74505; AAB32870.1; JOINED; Genomic_DNA.
DR EMBL; BT006875; AAP35521.1; -; mRNA.
DR EMBL; CH471099; EAW89102.1; -; Genomic_DNA.
DR EMBL; BC007951; AAH07951.1; -; mRNA.
DR EMBL; BC056420; AAH56420.1; -; mRNA.
DR CCDS; CCDS11689.1; -.
DR PIR; A55204; A55204.
DR RefSeq; NP_000337.1; NM_000346.3.
DR PDB; 4EUW; X-ray; 2.77 A; A=98-181.
DR PDBsum; 4EUW; -.
DR AlphaFoldDB; P48436; -.
DR SMR; P48436; -.
DR BioGRID; 112545; 82.
DR DIP; DIP-61319N; -.
DR ELM; P48436; -.
DR IntAct; P48436; 54.
DR STRING; 9606.ENSP00000245479; -.
DR ChEMBL; CHEMBL4523231; -.
DR GlyGen; P48436; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P48436; -.
DR PhosphoSitePlus; P48436; -.
DR BioMuta; SOX9; -.
DR DMDM; 1351096; -.
DR EPD; P48436; -.
DR jPOST; P48436; -.
DR MassIVE; P48436; -.
DR MaxQB; P48436; -.
DR PaxDb; P48436; -.
DR PeptideAtlas; P48436; -.
DR PRIDE; P48436; -.
DR ProteomicsDB; 55889; -.
DR Antibodypedia; 915; 926 antibodies from 41 providers.
DR CPTC; P48436; 2 antibodies.
DR DNASU; 6662; -.
DR Ensembl; ENST00000245479.3; ENSP00000245479.2; ENSG00000125398.8.
DR GeneID; 6662; -.
DR KEGG; hsa:6662; -.
DR MANE-Select; ENST00000245479.3; ENSP00000245479.2; NM_000346.4; NP_000337.1.
DR UCSC; uc002jiw.4; human.
DR CTD; 6662; -.
DR DisGeNET; 6662; -.
DR GeneCards; SOX9; -.
DR GeneReviews; SOX9; -.
DR HGNC; HGNC:11204; SOX9.
DR HPA; ENSG00000125398; Tissue enhanced (brain, salivary gland).
DR MalaCards; SOX9; -.
DR MIM; 114290; phenotype.
DR MIM; 278850; phenotype.
DR MIM; 608160; gene.
DR MIM; 616425; phenotype.
DR neXtProt; NX_P48436; -.
DR OpenTargets; ENSG00000125398; -.
DR Orphanet; 2138; 46,XX ovotesticular disorder of sex development.
DR Orphanet; 393; 46,XX testicular disorder of sex development.
DR Orphanet; 242; 46,XY complete gonadal dysgenesis.
DR Orphanet; 251510; 46,XY partial gonadal dysgenesis.
DR Orphanet; 140; Campomelic dysplasia.
DR Orphanet; 718; Isolated Pierre Robin syndrome.
DR PharmGKB; PA36041; -.
DR VEuPathDB; HostDB:ENSG00000125398; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000158269; -.
DR HOGENOM; CLU_031800_0_0_1; -.
DR InParanoid; P48436; -.
DR OMA; QSSNSYY; -.
DR OrthoDB; 1030296at2759; -.
DR PhylomeDB; P48436; -.
DR PathwayCommons; P48436; -.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-8878166; Transcriptional regulation by RUNX2.
DR Reactome; R-HSA-9690406; Transcriptional regulation of testis differentiation.
DR SignaLink; P48436; -.
DR SIGNOR; P48436; -.
DR BioGRID-ORCS; 6662; 117 hits in 1103 CRISPR screens.
DR ChiTaRS; SOX9; human.
DR GeneWiki; SOX9; -.
DR GenomeRNAi; 6662; -.
DR Pharos; P48436; Tbio.
DR PRO; PR:P48436; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P48436; protein.
DR Bgee; ENSG00000125398; Expressed in ventricular zone and 191 other tissues.
DR Genevisible; P48436; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0043425; F:bHLH transcription factor binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
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:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IDA:BHF-UCL.
DR GO; GO:0060018; P:astrocyte fate commitment; IEA:Ensembl.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:0060532; P:bronchus cartilage development; IEA:Ensembl.
DR GO; GO:0019933; P:cAMP-mediated signaling; IDA:UniProtKB.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; ISS:UniProtKB.
DR GO; GO:0051216; P:cartilage development; ISS:UniProtKB.
DR GO; GO:0001708; P:cell fate specification; ISS:UniProtKB.
DR GO; GO:0061323; P:cell proliferation involved in heart morphogenesis; IEA:Ensembl.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0071773; P:cellular response to BMP stimulus; ISS:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0071504; P:cellular response to heparin; ISS:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEP:UniProtKB.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEP:UniProtKB.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IDA:UniProtKB.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; IMP:UniProtKB.
DR GO; GO:0003415; P:chondrocyte hypertrophy; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:UniProtKB.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0060517; P:epithelial cell proliferation involved in prostatic bud elongation; ISS:UniProtKB.
DR GO; GO:0001837; P:epithelial to mesenchymal transition; ISS:UniProtKB.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0002067; P:glandular epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0021780; P:glial cell fate specification; IEA:Ensembl.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; ISS:UniProtKB.
DR GO; GO:0001942; P:hair follicle development; ISS:UniProtKB.
DR GO; GO:0070384; P:Harderian gland development; IEA:Ensembl.
DR GO; GO:0007507; P:heart development; IBA:GO_Central.
DR GO; GO:0003170; P:heart valve development; ISS:UniProtKB.
DR GO; GO:0003188; P:heart valve formation; IEA:Ensembl.
DR GO; GO:0003179; P:heart valve morphogenesis; ISS:UniProtKB.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; ISS:UniProtKB.
DR GO; GO:0035622; P:intrahepatic bile duct development; IEA:Ensembl.
DR GO; GO:0032808; P:lacrimal gland development; IEA:Ensembl.
DR GO; GO:0060174; P:limb bud formation; IEA:Ensembl.
DR GO; GO:0061145; P:lung smooth muscle development; IEA:Ensembl.
DR GO; GO:0019100; P:male germ-line sex determination; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IMP:UniProtKB.
DR GO; GO:0030879; P:mammary gland development; IEA:Ensembl.
DR GO; GO:0097152; P:mesenchymal cell apoptotic process; IEA:Ensembl.
DR GO; GO:0010463; P:mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0072289; P:metanephric nephron tubule formation; ISS:UniProtKB.
DR GO; GO:0061138; P:morphogenesis of a branching epithelium; ISS:UniProtKB.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IBA:GO_Central.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:1904864; P:negative regulation of beta-catenin-TCF complex assembly; IEA:Ensembl.
DR GO; GO:0070168; P:negative regulation of biomineral tissue development; IDA:BHF-UCL.
DR GO; GO:0030502; P:negative regulation of bone mineralization; IEA:Ensembl.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046322; P:negative regulation of fatty acid oxidation; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0002683; P:negative regulation of immune system process; ISS:UniProtKB.
DR GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IDA:BHF-UCL.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0030279; P:negative regulation of ossification; IDA:CACAO.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:CACAO.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
DR GO; GO:0014036; P:neural crest cell fate specification; ISS:UniProtKB.
DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0030903; P:notochord development; IEA:Ensembl.
DR GO; GO:0006334; P:nucleosome assembly; IDA:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IBA:GO_Central.
DR GO; GO:0030916; P:otic vesicle formation; ISS:UniProtKB.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; ISS:UniProtKB.
DR GO; GO:0061036; P:positive regulation of cartilage development; IDA:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; IEA:Ensembl.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IDA:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IDA:CACAO.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEP:UniProtKB.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:0090184; P:positive regulation of kidney development; ISS:UniProtKB.
DR GO; GO:2000020; P:positive regulation of male gonad development; IDA:UniProtKB.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IDA:UniProtKB.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; ISS:UniProtKB.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISS: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; IDA:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0030850; P:prostate gland development; IEP:UniProtKB.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0034504; P:protein localization to nucleus; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0061046; P:regulation of branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0030155; P:regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0010564; P:regulation of cell cycle process; IMP:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:0060784; P:regulation of cell proliferation involved in tissue homeostasis; ISS:UniProtKB.
DR GO; GO:2000794; P:regulation of epithelial cell proliferation involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0072034; P:renal vesicle induction; ISS:UniProtKB.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR GO; GO:0060041; P:retina development in camera-type eye; ISS:UniProtKB.
DR GO; GO:0060221; P:retinal rod cell differentiation; ISS:UniProtKB.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0060008; P:Sertoli cell differentiation; ISS:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:UniProtKB.
DR GO; GO:0001501; P:skeletal system development; IMP:UniProtKB.
DR GO; GO:0035019; P:somatic stem cell population maintenance; ISS:UniProtKB.
DR GO; GO:0007283; P:spermatogenesis; ISS:UniProtKB.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
DR GO; GO:0001894; P:tissue homeostasis; ISS:UniProtKB.
DR GO; GO:0060534; P:trachea cartilage development; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0060509; P:type I pneumocyte differentiation; IEA:Ensembl.
DR GO; GO:0072197; P:ureter morphogenesis; IEA:Ensembl.
DR GO; GO:0072193; P:ureter smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0072190; P:ureter urothelium development; IEA:Ensembl.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR InterPro; IPR029548; SOX-9.
DR InterPro; IPR022151; Sox_N.
DR PANTHER; PTHR45803:SF1; PTHR45803:SF1; 1.
DR Pfam; PF00505; HMG_box; 1.
DR Pfam; PF12444; Sox_N; 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 3D-structure; Acetylation; Activator; Differentiation; Disease variant;
KW DNA-binding; Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..509
FT /note="Transcription factor SOX-9"
FT /id="PRO_0000048739"
FT DNA_BIND 105..173
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 63..103
FT /note="Dimerization (DIM)"
FT /evidence="ECO:0000305|PubMed:31194875"
FT REGION 63..103
FT /note="PQA"
FT /evidence="ECO:0000305|PubMed:31194875"
FT REGION 160..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..307
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000269|PubMed:31194875"
FT REGION 330..415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..509
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000269|PubMed:8640233"
FT REGION 479..509
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..284
FT /note="9aaTAD 1"
FT /evidence="ECO:0000269|PubMed:31194875"
FT MOTIF 290..298
FT /note="9aaTAD 2"
FT /evidence="ECO:0000269|PubMed:31194875"
FT MOTIF 460..468
FT /note="9aaTAD 3"
FT /evidence="ECO:0000269|PubMed:34342803"
FT COMPBIAS 18..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 339..374
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04887"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04887"
FT CROSSLNK 398
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q04887"
FT VARIANT 28..509
FT /note="Missing (in CMD1)"
FT /evidence="ECO:0000269|PubMed:19033726"
FT /id="VAR_078490"
FT VARIANT 76
FT /note="A -> E (in CMD1; dimerization and the resulting
FT capacity to activate promoters via dimeric binding sites is
FT lost; other features of the protein function remain
FT unaltered; dbSNP:rs137853128)"
FT /evidence="ECO:0000269|PubMed:12783851"
FT /id="VAR_063642"
FT VARIANT 108
FT /note="P -> L (in CMD1)"
FT /evidence="ECO:0000269|PubMed:9002675"
FT /id="VAR_003735"
FT VARIANT 112
FT /note="F -> L (in CMD1; loss of DNA binding;
FT dbSNP:rs1407667250)"
FT /evidence="ECO:0000269|PubMed:10446171,
FT ECO:0000269|PubMed:7485151"
FT /id="VAR_003736"
FT VARIANT 112
FT /note="F -> S (in CMD1)"
FT /evidence="ECO:0000269|PubMed:9452059"
FT /id="VAR_003737"
FT VARIANT 113
FT /note="M -> T (in CMD1)"
FT /evidence="ECO:0000269|PubMed:19921652"
FT /id="VAR_063643"
FT VARIANT 113
FT /note="M -> V (in CMD1; residual DNA binding and
FT transactivation of regulated genes)"
FT /evidence="ECO:0000269|PubMed:20513132"
FT /id="VAR_063644"
FT VARIANT 119
FT /note="A -> V (in CMD1; almost no loss of DNA binding)"
FT /evidence="ECO:0000269|PubMed:10446171,
FT ECO:0000269|PubMed:7485151"
FT /id="VAR_003738"
FT VARIANT 143
FT /note="W -> R (in CMD1)"
FT /evidence="ECO:0000269|PubMed:9002675"
FT /id="VAR_003739"
FT VARIANT 152
FT /note="R -> P (in CMD1)"
FT /evidence="ECO:0000269|PubMed:9002675"
FT /id="VAR_003740"
FT VARIANT 154
FT /note="F -> L (in CMD1; 5% of wild-type DNA binding
FT activity; transcriptional activation is only reduced to 26%
FT of wild-type activity; dbSNP:rs137853129)"
FT /evidence="ECO:0000269|PubMed:11323423"
FT /id="VAR_008529"
FT VARIANT 158
FT /note="A -> T (in CMD1; 17% of wild-type DNA binding
FT activity; shows a 2-fold reduction in nuclear import
FT efficiency; transcriptional activation is only reduced to
FT 62% of wild-type activity; dbSNP:rs137853130)"
FT /evidence="ECO:0000269|PubMed:11323423"
FT /id="VAR_008530"
FT VARIANT 165
FT /note="H -> Q (in CMD1; residual DNA binding and
FT transactivation of regulated genes)"
FT /evidence="ECO:0000269|PubMed:20513132"
FT /id="VAR_063645"
FT VARIANT 165
FT /note="H -> Y (in CMD1; loss of DNA binding;
FT dbSNP:rs28940282)"
FT /evidence="ECO:0000269|PubMed:10446171,
FT ECO:0000269|PubMed:11754051"
FT /id="VAR_008531"
FT VARIANT 169
FT /note="H -> P (in CMD1; decreased 75% transactivational
FT activity)"
FT /evidence="ECO:0000269|PubMed:19033726,
FT ECO:0000269|PubMed:24038782"
FT /id="VAR_078491"
FT VARIANT 169
FT /note="H -> Q (in CMD1; mild form overlapping with small
FT patella syndrome; decreased 50% transactivational activity;
FT dbSNP:rs2229989)"
FT /evidence="ECO:0000269|PubMed:24038782"
FT /id="VAR_078492"
FT VARIANT 170
FT /note="P -> L (in CMD1; dbSNP:rs1131691554)"
FT /evidence="ECO:0000269|PubMed:19921652"
FT /id="VAR_063646"
FT VARIANT 170
FT /note="P -> R (in CMD1)"
FT /evidence="ECO:0000269|PubMed:10446171,
FT ECO:0000269|PubMed:9002675"
FT /id="VAR_003741"
FT VARIANT 173
FT /note="K -> E (in CMD1; dbSNP:rs104894647)"
FT /evidence="ECO:0000269|PubMed:10951468"
FT /id="VAR_063647"
FT VARIANT 354..356
FT /note="Missing (in CMD1)"
FT /id="VAR_003742"
FT VARIANT 440..509
FT /note="Missing (in CMD1)"
FT /evidence="ECO:0000269|PubMed:8001137"
FT /id="VAR_083521"
FT MUTAGEN 278
FT /note="L->S: Impaired ability to activate transcription in
FT vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 282
FT /note="V->D: Impaired ability to activate transcription in
FT vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 290
FT /note="D->A: Impaired ability to activate transcription in
FT vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 293
FT /note="E->M,T: Impaired ability to activate transcription
FT in vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 294
FT /note="F->L: Does not affect ability to activate
FT transcription in vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 294
FT /note="F->S,A: Impaired ability to activate transcription
FT in vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 296
FT /note="Q->R: Impaired, but not abolished, ability to
FT activate transcription in vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 297
FT /note="Y->L,S,D,F: Impaired ability to activate
FT transcription in vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT MUTAGEN 298
FT /note="L->D: Impaired ability to activate transcription in
FT vitro."
FT /evidence="ECO:0000269|PubMed:31194875"
FT HELIX 111..126
FT /evidence="ECO:0007829|PDB:4EUW"
FT HELIX 132..143
FT /evidence="ECO:0007829|PDB:4EUW"
FT HELIX 148..168
FT /evidence="ECO:0007829|PDB:4EUW"
SQ SEQUENCE 509 AA; 56137 MW; 9289CFBB8D6631A2 CRC64;
MNLLDPFMKM TDEQEKGLSG APSPTMSEDS AGSPCPSGSG SDTENTRPQE NTFPKGEPDL
KKESEEDKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK NKPHVKRPMN AFMVWAQAAR
RKLADQYPHL HNAELSKTLG KLWRLLNESE KRPFVEEAER LRVQHKKDHP DYKYQPRRRK
SVKNGQAEAE EATEQTHISP NAIFKALQAD SPHSSSGMSE VHSPGEHSGQ SQGPPTPPTT
PKTDVQPGKA DLKREGRPLP EGGRQPPIDF RDVDIGELSS DVISNIETFD VNEFDQYLPP
NGHPGVPATH GQVTYTGSYG ISSTAATPAS AGHVWMSKQQ APPPPPQQPP QAPPAPQAPP
QPQAAPPQQP AAPPQQPQAH TLTTLSSEPG QSQRTHIKTE QLSPSHYSEQ QQHSPQQIAY
SPFNLPHYSP SYPPITRSQY DYTDHQNSSS YYSHAAGQGT GLYSTFTYMN PAQRPMYTPI
ADTSGVPSIP QTHSPQHWEQ PVYTQLTRP
