SOX9_RAT
ID SOX9_RAT Reviewed; 507 AA.
AC F1LYL9;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2013, sequence version 2.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Transcription factor SOX-9 {ECO:0000305};
GN Name=Sox9 {ECO:0000312|RGD:620474};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
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).
CC -!- FUNCTION: Transcription factor that plays a key role in chondrocytes
CC differentiation and skeletal development (By similarity). Specifically
CC binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-
CC 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:26150426). 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:26150426}.
CC -!- SUBUNIT: Homodimer; homodimerization is required for activity.
CC Interacts (via C-terminus) with ZNF219; forming a complex that binds to
CC the COL2A1 promoter and activates COL2A1 expression (By similarity).
CC Interacts with DDRGK1. Interacts with EP300/p300 (By similarity).
CC Interacts with beta-catenin (CTNNB1); inhibiting CTNNB1 activity by
CC competing with the binding sites of TCF/LEF within CTNNB1 (By
CC similarity). {ECO:0000250|UniProtKB:P48436,
CC ECO:0000250|UniProtKB:Q04887}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q04887,
CC ECO:0000255|PROSITE-ProRule:PRU00267}.
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:0000250|UniProtKB:P48436}.
CC -!- DOMAIN: The 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000250|UniProtKB:P48436}.
CC -!- DOMAIN: The PQA region (for proline, glutamine and alanine-rich) helps
CC stabilize SOX9 and facilitates transactivation. It lacks intrinsic
CC transactivation capability. {ECO:0000250|UniProtKB:P48436}.
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: 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 -!- PTM: Ubiquitinated; ubiquitination leads to proteasomal degradation and
CC is negatively regulated by DDRGK1. {ECO:0000250|UniProtKB:Q04887}.
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DR EMBL; AABR07030718; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473948; EDM06505.1; -; Genomic_DNA.
DR RefSeq; NP_536328.1; NM_080403.1.
DR AlphaFoldDB; F1LYL9; -.
DR SMR; F1LYL9; -.
DR STRING; 10116.ENSRNOP00000003511; -.
DR PaxDb; F1LYL9; -.
DR Ensembl; ENSRNOT00000003511; ENSRNOP00000003511; ENSRNOG00000002607.
DR GeneID; 140586; -.
DR KEGG; rno:140586; -.
DR CTD; 6662; -.
DR RGD; 620474; Sox9.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000158269; -.
DR HOGENOM; CLU_031800_0_0_1; -.
DR InParanoid; F1LYL9; -.
DR OMA; QSSNSYY; -.
DR OrthoDB; 782373at2759; -.
DR Reactome; R-RNO-3769402; Deactivation of the beta-catenin transactivating complex.
DR PRO; PR:F1LYL9; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Proteomes; UP000234681; Chromosome 10.
DR Bgee; ENSRNOG00000002607; Expressed in colon and 16 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; ISO:RGD.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
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; IMP:RGD.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:UniProtKB.
DR GO; GO:0097157; F:pre-mRNA intronic binding; ISO:RGD.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:RGD.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; ISO:RGD.
DR GO; GO:0097065; P:anterior head development; ISO:RGD.
DR GO; GO:0003180; P:aortic valve morphogenesis; ISO:RGD.
DR GO; GO:0060018; P:astrocyte fate commitment; ISO:RGD.
DR GO; GO:0030282; P:bone mineralization; IEA:Ensembl.
DR GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; ISO:RGD.
DR GO; GO:0060532; P:bronchus cartilage development; ISO:RGD.
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; IEP:RGD.
DR GO; GO:0030154; P:cell differentiation; ISO:RGD.
DR GO; GO:0045165; P:cell fate commitment; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; ISS:UniProtKB.
DR GO; GO:0071300; P:cellular response to retinoic acid; ISO:RGD.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:UniProtKB.
DR GO; GO:0007417; P:central nervous system development; ISO:RGD.
DR GO; GO:0002063; P:chondrocyte development; ISO:RGD.
DR GO; GO:0002062; P:chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0003413; P:chondrocyte differentiation involved in endochondral bone morphogenesis; ISS:UniProtKB.
DR GO; GO:0003415; P:chondrocyte hypertrophy; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; ISS:UniProtKB.
DR GO; GO:0007010; P:cytoskeleton organization; ISO:RGD.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; ISS:UniProtKB.
DR GO; GO:0060350; P:endochondral bone morphogenesis; ISO:RGD.
DR GO; GO:0031018; P:endocrine pancreas development; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0085029; P:extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0007507; P:heart development; ISO:RGD.
DR GO; GO:0003170; P:heart valve development; ISS:UniProtKB.
DR GO; GO:0003188; P:heart valve formation; ISO:RGD.
DR GO; GO:0003179; P:heart valve morphogenesis; ISS:UniProtKB.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0032808; P:lacrimal gland development; ISO:RGD.
DR GO; GO:0060174; P:limb bud formation; ISO:RGD.
DR GO; GO:0060487; P:lung epithelial cell differentiation; ISO:RGD.
DR GO; GO:0061145; P:lung smooth muscle development; ISO:RGD.
DR GO; GO:0019100; P:male germ-line sex determination; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; ISS:UniProtKB.
DR GO; GO:0030238; P:male sex determination; ISO:RGD.
DR GO; GO:0030879; P:mammary gland development; ISO:RGD.
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:0072170; P:metanephric tubule development; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:1904864; P:negative regulation of beta-catenin-TCF complex assembly; ISO:RGD.
DR GO; GO:0070168; P:negative regulation of biomineral tissue development; ISS:UniProtKB.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISO:RGD.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:RGD.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; ISO:RGD.
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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; ISO:RGD.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; ISS:UniProtKB.
DR GO; GO:0030279; P:negative regulation of ossification; ISS:UniProtKB.
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; ISO:RGD.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0014032; P:neural crest cell development; ISO:RGD.
DR GO; GO:0048665; P:neuron fate specification; IEA:Ensembl.
DR GO; GO:0007219; P:Notch signaling pathway; ISO:RGD.
DR GO; GO:0030903; P:notochord development; ISO:RGD.
DR GO; GO:0006334; P:nucleosome assembly; ISS:UniProtKB.
DR GO; GO:0048709; P:oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0001503; P:ossification; ISO:RGD.
DR GO; GO:0071599; P:otic vesicle development; ISO:RGD.
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; ISS:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISS:UniProtKB.
DR GO; GO:2000138; P:positive regulation of cell proliferation involved in heart morphogenesis; ISO:RGD.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; ISO:RGD.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; ISS:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; ISS:UniProtKB.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; ISO:RGD.
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; ISS: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; ISS: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; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030850; P:prostate gland development; ISO:RGD.
DR GO; GO:0060512; P:prostate gland morphogenesis; ISO:RGD.
DR GO; GO:0043491; P:protein kinase B signaling; ISS:UniProtKB.
DR GO; GO:0034504; P:protein localization to nucleus; ISO:RGD.
DR GO; GO:0006468; P:protein phosphorylation; IEA:Ensembl.
DR GO; GO:0065003; P:protein-containing complex assembly; ISS:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0061046; P:regulation of branching involved in lung morphogenesis; ISO:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0010564; P:regulation of cell cycle process; ISS:UniProtKB.
DR GO; GO:0045595; P:regulation of cell differentiation; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0010468; P:regulation of gene expression; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:RGD.
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; IEP:UniProtKB.
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; ISS: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; ISO:RGD.
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:0072189; P:ureter development; ISO:RGD.
DR GO; GO:0072197; P:ureter morphogenesis; ISO:RGD.
DR GO; GO:0072193; P:ureter smooth muscle cell differentiation; ISO:RGD.
DR GO; GO:0072190; P:ureter urothelium development; ISO:RGD.
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 Acetylation; Activator; Differentiation; DNA-binding; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..507
FT /note="Transcription factor SOX-9"
FT /id="PRO_0000450217"
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:0000250|UniProtKB:P48436"
FT REGION 63..103
FT /note="PQA"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 160..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..307
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 335..429
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..507
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 477..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 275..284
FT /note="9aaTAD 1"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 290..298
FT /note="9aaTAD 2"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 458..466
FT /note="9aaTAD 3"
FT /evidence="ECO:0000250|UniProtKB:P48436"
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..367
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..507
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 396
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q04887"
SQ SEQUENCE 507 AA; 56124 MW; 0EF0A9E4733D48AB 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
PKTDVQAGKV DLKREGRPLA EGGRQPPIDF RDVDIGELSS DVISNIETFD VNEFDQYLPP
NGHPGVPATH GQVSYTGSYG ISSTAPTPAT AGHVWMSKQQ APPPPPQQPP QAPQAPQAPP
QQQAPPQPQQ APQQQQAHTL TTLSSEPGQS QRTHIKTEQL SPSHYSEQQQ HSPQQISYSP
FNLPHYNPSY PTITRSQYDY TDHQNSGSYY SHAAGQGSGL YSTFTYMNPA QRPMYTPIAD
TSGVPSIPQT HSPQHWEQPV YTQLTRP
