SOX9_CHICK
ID SOX9_CHICK Reviewed; 494 AA.
AC P48434; F1P307; O73668;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 09-JUL-2014, sequence version 3.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Transcription factor SOX-9 {ECO:0000305};
GN Name=SOX9 {ECO:0000303|PubMed:10340758};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CARTILAGE DEVELOPMENT,
RP DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=10340758;
RX DOI=10.1002/(sici)1097-0177(199905)215:1<69::aid-dvdy8>3.0.co;2-n;
RA Healy C., Uwanogho D., Sharpe P.T.;
RT "Regulation and role of Sox9 in cartilage formation.";
RL Dev. Dyn. 215:69-78(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION IN TRANSCRIPTION REGULATION.
RX PubMed=9858536; DOI=10.1128/mcb.19.1.107;
RA Kamachi Y., Cheah K.S., Kondoh H.;
RT "Mechanism of regulatory target selection by the SOX high-mobility-group
RT domain proteins as revealed by comparison of SOX1/2/3 and SOX9.";
RL Mol. Cell. Biol. 19:107-120(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [4]
RP FUNCTION IN NEURAL CREST DELAMINATION, INTERACTION WITH SNAI2 AND UBE2I,
RP SUBCELLULAR LOCATION, SUMOYLATION AT LYS-376, PHOSPHORYLATION AT SER-64 AND
RP SER-181, AND MUTAGENESIS OF LYS-61; SER-64; SER-181; LYS-254 AND LYS-376.
RX PubMed=23382206; DOI=10.1073/pnas.1211747110;
RA Liu J.A., Wu M.H., Yan C.H., Chau B.K., So H., Ng A., Chan A., Cheah K.S.,
RA Briscoe J., Cheung M.;
RT "Phosphorylation of Sox9 is required for neural crest delamination and is
RT regulated downstream of BMP and canonical Wnt signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:2882-2887(2013).
CC -!- FUNCTION: Transcription factor that plays a key role in chondrocytes
CC differentiation and skeletal development (PubMed:10340758,
CC PubMed:9858536). Specifically binds the 5'-ACAAAG-3' DNA motif present
CC in enhancers and super-enhancers and promotes expression of genes
CC important for chondrogenesis, including COL2A1 (PubMed:10340758,
CC PubMed:9858536). Plays a central role in successive steps of
CC chondrocyte differentiation. Absolutely required for precartilaginous
CC condensation, the first step in chondrogenesis during which skeletal
CC progenitors differentiate into prechondrocytes (By similarity).
CC Together with SOX5 and SOX6, required for overt chondrogenesis when
CC condensed prechondrocytes differentiate into early stage chondrocytes,
CC the second step in chondrogenesis (By similarity). Later, required to
CC direct hypertrophic maturation and block osteoblast differentiation of
CC growth plate chondrocytes: maintains chondrocyte columnar
CC proliferation, delays prehypertrophy and then prevents osteoblastic
CC differentiation of chondrocytes (By similarity). Also required for
CC chondrocyte hypertrophy, both indirectly, by keeping the lineage fate
CC of chondrocytes, and directly, by remaining present in upper
CC hypertrophic cells (By similarity). Low lipid levels are the main
CC nutritional determinant for chondrogenic commitment of skeletal
CC progenitor cells: when lipids levels are low, FOXO transcription
CC factors promote expression of SOX9, which induces chondrogenic
CC commitment and suppresses fatty acid oxidation (By similarity). In
CC addition to cartilage development, also acts as a regulator of
CC proliferation and differentiation in epithelial stem/progenitor cells
CC (By similarity). In response to bone morphogenetic protein stimulus,
CC phosphorylation is induced and then sumoylation, allowing cooperation
CC with SNAI2 to trigger neural crest delamination (PubMed:23382206).
CC {ECO:0000250|UniProtKB:Q04887, ECO:0000269|PubMed:10340758,
CC ECO:0000269|PubMed:23382206, ECO:0000269|PubMed:9858536}.
CC -!- SUBUNIT: Interacts with SNAI2; triggers neural crest delamination in a
CC phosphorylation dependent manner. Interacts with UBE2I.
CC {ECO:0000269|PubMed:23382206}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:23382206}.
CC -!- DEVELOPMENTAL STAGE: Found in chondrogenic regions in the branchial
CC arches, somites and limb buds at E22. At E28 detected in the limbs,
CC developing scapula, prevertebrae and ribs. Found in condensing
CC mesenchyme of the forelimb at E25. Expressed in the condensing
CC mesenchyme at the distal tips of the developing hindlimbs at E26.
CC {ECO:0000269|PubMed:10340758}.
CC -!- INDUCTION: By BMP2 during chondrogenesis.
CC {ECO:0000269|PubMed:10340758}.
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 -!- PTM: Phosphorylated at Ser-181 in the developing neural tube.
CC Phosphorylation at either Ser-64 or Ser-181 is required for
CC sumoylation, but phosphorylation is not dependent on sumoylation.
CC Sumoylation is enhanced by PKA. Phosphorylation is required for
CC interaction with SNAI2 to trigger neural crest delamination and for an
CC efficient trunk neural crest delamination, whereas sumoylation plays a
CC less significant role. Phosphorylation and sumoylation are induced by
CC BMP signaling pathway. {ECO:0000269|PubMed:23382206}.
CC -!- PTM: Sumoylated at Lys-376; phosphorylation at either Ser-64 or Ser-181
CC is required for sumoylation. Sumoylation is induced by BMP signaling
CC pathway. {ECO:0000269|PubMed:23382206}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB09663.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U12533; AAB09663.1; ALT_FRAME; mRNA.
DR EMBL; AB012236; BAA25296.1; -; mRNA.
DR EMBL; AADN03007462; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_989612.1; NM_204281.1.
DR AlphaFoldDB; P48434; -.
DR SMR; P48434; -.
DR STRING; 9031.ENSGALP00000037718; -.
DR iPTMnet; P48434; -.
DR PaxDb; P48434; -.
DR Ensembl; ENSGALT00000038513; ENSGALP00000037718; ENSGALG00000004386.
DR GeneID; 374148; -.
DR KEGG; gga:374148; -.
DR CTD; 6662; -.
DR VEuPathDB; HostDB:geneid_374148; -.
DR eggNOG; KOG0527; Eukaryota.
DR GeneTree; ENSGT00940000158269; -.
DR HOGENOM; CLU_031800_0_0_1; -.
DR InParanoid; P48434; -.
DR OMA; QSSNSYY; -.
DR OrthoDB; 782373at2759; -.
DR PhylomeDB; P48434; -.
DR Reactome; R-GGA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-GGA-8878166; Transcriptional regulation by RUNX2.
DR PRO; PR:P48434; -.
DR Proteomes; UP000000539; Chromosome 18.
DR Bgee; ENSGALG00000004386; Expressed in cerebellum and 10 other tissues.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:AgBase.
DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl.
DR GO; GO:0008013; F:beta-catenin binding; IEA:Ensembl.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0097157; F:pre-mRNA intronic binding; IEA:Ensembl.
DR GO; GO:0034236; F:protein kinase A catalytic subunit binding; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:AgBase.
DR GO; GO:0097065; P:anterior head development; IEA:Ensembl.
DR GO; GO:0003180; P:aortic valve morphogenesis; IEA:Ensembl.
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; IEP:UniProtKB.
DR GO; GO:0060532; P:bronchus cartilage development; IEA:Ensembl.
DR GO; GO:0019933; P:cAMP-mediated signaling; IEA:Ensembl.
DR GO; GO:0060070; P:canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0001502; P:cartilage condensation; IDA: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; IDA:UniProtKB.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071504; P:cellular response to heparin; IEA:Ensembl.
DR GO; GO:0071347; P:cellular response to interleukin-1; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0002062; P:chondrocyte differentiation; IDA:UniProtKB.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0048566; P:embryonic digestive tract development; IMP:AgBase.
DR GO; GO:0003203; P:endocardial cushion morphogenesis; IEA:Ensembl.
DR GO; GO:0031018; P:endocrine pancreas development; IEA:Ensembl.
DR GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0060517; P:epithelial cell proliferation involved in prostatic bud elongation; IEA:Ensembl.
DR GO; GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
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: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; IEP:UniProtKB.
DR GO; GO:0003188; P:heart valve formation; IEA:Ensembl.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:AgBase.
DR GO; GO:0060575; P:intestinal epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0008584; P:male gonad development; IEP:UniProtKB.
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; IEA:Ensembl.
DR GO; GO:0002009; P:morphogenesis of an epithelium; IMP:AgBase.
DR GO; GO:1904864; P:negative regulation of beta-catenin-TCF complex assembly; IEA:Ensembl.
DR GO; GO:1903011; P:negative regulation of bone development; IMP:AgBase.
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; IEA:Ensembl.
DR GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:2001054; P:negative regulation of mesenchymal cell apoptotic process; IEA:Ensembl.
DR GO; GO:1902894; P:negative regulation of miRNA transcription; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:UniProtKB.
DR GO; GO:0046533; P:negative regulation of photoreceptor cell differentiation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0036032; P:neural crest cell delamination; IMP:UniProtKB.
DR GO; GO:0014036; P:neural crest cell fate specification; IDA:UniProtKB.
DR GO; GO:0001755; P:neural crest cell migration; IMP:AgBase.
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; IEA:Ensembl.
DR GO; GO:0048709; P:oligodendrocyte differentiation; IBA:GO_Central.
DR GO; GO:0030916; P:otic vesicle formation; IEA:Ensembl.
DR GO; GO:0090190; P:positive regulation of branching involved in ureteric bud morphogenesis; IEA:Ensembl.
DR GO; GO:1902027; P:positive regulation of cartilage condensation; IMP:AgBase.
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; IBA:GO_Central.
DR GO; GO:1902732; P:positive regulation of chondrocyte proliferation; IEA:Ensembl.
DR GO; GO:0032967; P:positive regulation of collagen biosynthetic process; IMP:AgBase.
DR GO; GO:0030858; P:positive regulation of epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IEA:Ensembl.
DR GO; GO:1901203; P:positive regulation of extracellular matrix assembly; IEA:Ensembl.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:2000020; P:positive regulation of male gonad development; IEA:Ensembl.
DR GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:2000741; P:positive regulation of mesenchymal stem cell differentiation; IEA:Ensembl.
DR GO; GO:0090300; P:positive regulation of neural crest formation; IMP:AgBase.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
DR GO; GO:2000648; P:positive regulation of stem cell proliferation; IEA:Ensembl.
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:0061046; P:regulation of branching involved in lung morphogenesis; IEA:Ensembl.
DR GO; GO:0061035; P:regulation of cartilage development; IDA:UniProtKB.
DR GO; GO:0010564; P:regulation of cell cycle process; IEA:Ensembl.
DR GO; GO:0060784; P:regulation of cell proliferation involved in tissue homeostasis; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0070542; P:response to fatty acid; ISS:UniProtKB.
DR GO; GO:0060221; P:retinal rod cell differentiation; IEA:Ensembl.
DR GO; GO:0060009; P:Sertoli cell development; IEA:Ensembl.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0007283; P:spermatogenesis; IEA:Ensembl.
DR GO; GO:0072089; P:stem cell proliferation; IEA:Ensembl.
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:0006351; P:transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0060290; P:transdifferentiation; IMP:AgBase.
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 Activator; Differentiation; DNA-binding; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..494
FT /note="Transcription factor SOX-9"
FT /id="PRO_0000048745"
FT DNA_BIND 105..173
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..66
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 159..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..309
FT /note="Transactivation domain (TAM)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 326..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..494
FT /note="Transactivation domain (TAC)"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT REGION 462..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 277..286
FT /note="9aaTAD 1"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 292..300
FT /note="9aaTAD 2"
FT /evidence="ECO:0000250|UniProtKB:P48436"
FT MOTIF 445..453
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 159..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 248..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23382206"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:23382206"
FT CROSSLNK 376
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT MUTAGEN 61
FT /note="K->R: Decreases cooperating with SNAI2 to trigger
FT neural crest delamination; when associated with R-254 and
FT R-376."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 64
FT /note="S->A: Abolishes sumoylation; when associated with A-
FT 181. Abolishes phosphorylation; when associated with A-181.
FT Reduces ability to associate with UBE2I; when associated
FT with A-181. Prevents trunk neural crest delamination; when
FT associated with A-181. Prevents cooperating with SNAI2 to
FT trigger neural crest delamination; when associated with A-
FT 181. Abolishes interaction with SNAI2; when associated with
FT A-181."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 64
FT /note="S->D: Sumoylation; when associated with D-181.
FT Initiates trunk neural crest delamination; when associated
FT with D-181. Allows cooperating with SNAI2 to trigger neural
FT crest delamination; when associated with D-181. Allows
FT interaction with SNAI2; when associated with D-181."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 181
FT /note="S->A: Abolishes sumoylation; when associated with A-
FT 64. Abolishes phosphorylation; when associated with A-64.
FT Reduces ability to associate with UBE2I; when associated
FT with A-64. Prevents trunk neural crest delamination; when
FT associated with A-64. Prevents cooperating with SNAI2 to
FT trigger neural crest delamination; when associated with A-
FT 64. Abolishes interaction with SNAI2; when associated with
FT A-64."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 181
FT /note="S->D: Sumoylation; when associated with D-64.
FT Initiates trunk neural crest delamination; when associated
FT with D-64. Allows cooperating with SNAI2 to trigger neural
FT crest delamination; when associated with D-64. Allows
FT interaction with SNAI2; when associated with D-64."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 254
FT /note="K->R: Decreases cooperating with SNAI2 to trigger
FT neural crest delamination; when associated with R-61 and R-
FT 376."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 376
FT /note="K->R: Decreases cooperating with SNAI2 to trigger
FT neural crest delamination; when associated with R-61 and R-
FT 254."
FT /evidence="ECO:0000269|PubMed:23382206"
FT MUTAGEN 376
FT /note="K->R: Not sumoylated."
FT /evidence="ECO:0000269|PubMed:23382206"
FT CONFLICT 17..20
FT /note="CISD -> GLSG (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 181
FT /note="S -> T (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="Y -> N (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 415
FT /note="S -> F (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="Q -> E (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="G -> S (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="S -> T (in Ref. 1; AAB09663)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 494 AA; 54848 MW; A3926313CA954E32 CRC64;
MNLLDPFMKM TEEQDKCISD APSPTMSDDS AGSPCPSGSG SDTENTRPQE NTFPKGDPDL
KKESDEDKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK NKPHVKRPMN AFMVWAQAAR
RKLADQYPHL HNAELSKTLG KLWRLLNESE KRPFVEEAER LRVQHKKDHP DYKYQPRRRK
SVKNGQSEQE EGSEQTHISP NAIFKALQAD SPQSSSSISE VHSPGEHSGQ SQGPPTPPTT
PKTDAQQPGK QDLKREGRPL AEGGRQPPHI DFRDVDIGEL SSDVISNIET FDVNEFDQYL
PPNGHPGVPA THGQVTTYSG TYGISSSASS PAGAGHAWMA KQQPQPPQPP AQPPAQHTLP
ALSGEQGPAQ QRPHIKTEQL SPSHYSEQQQ HSPQQQQQQQ QQLGYGSFNL QHYGSSYPPI
TRSQYDYTEH QNSGSYYSHA AGQSGGLYST FTYMNPTQRP MYTPIADTSG VPSIPQTHSP
QHWEQPVYTQ LTRP
