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P48436 (SOX9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor SOX-9
Gene names
Name:SOX9
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length509 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays an important role in the normal skeletal development. May regulate the expression of other genes involved in chondrogenesis by acting as a transcription factor for these genes.

Subcellular location

Nucleus Potential.

Involvement in disease

Campomelic dysplasia (CMD1) [MIM:114290]: Rare, often lethal, dominantly inherited, congenital osteochondrodysplasia, associated with male-to-female autosomal sex reversal in two-thirds of the affected karyotypic males. A disease of the newborn characterized by congenital bowing and angulation of long bones, unusually small scapulae, deformed pelvis and spine and a missing pair of ribs. Craniofacial defects such as cleft palate, micrognathia, flat face and hypertelorism are common. Various defects of the ear are often evident, affecting the cochlea, malleus incus, stapes and tympanum. Most patients die soon after birth due to respiratory distress which has been attributed to hypoplasia of the tracheobronchial cartilage and small thoracic cage.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17

46,XX sex reversal 2 (SRXX2) [MIM:278850]: A condition in which male gonads develop in a genetic female (female to male sex reversal).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.6

Sequence similarities

Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseDisease mutation
   LigandDNA-binding
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from sequence or structural similarity PubMed 21512138. Source: UniProtKB

Sertoli cell development

Inferred from electronic annotation. Source: Ensembl

Sertoli cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

astrocyte fate commitment

Inferred from electronic annotation. Source: Ensembl

branching involved in ureteric bud morphogenesis

Inferred from electronic annotation. Source: Ensembl

cAMP-mediated signaling

Inferred from direct assay PubMed 10805756. Source: UniProtKB

cartilage condensation

Inferred from sequence or structural similarity. Source: UniProtKB

cartilage development

Inferred from sequence or structural similarity. Source: UniProtKB

cell fate specification

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to epidermal growth factor stimulus

Inferred from sequence or structural similarity PubMed 21512138. Source: UniProtKB

cellular response to heparin

Inferred from sequence or structural similarity PubMed 21512138. Source: UniProtKB

cellular response to interleukin-1

Inferred from expression pattern PubMed 20079164. Source: UniProtKB

cellular response to mechanical stimulus

Inferred from sequence or structural similarity PubMed 21512138. Source: UniProtKB

cellular response to retinoic acid

Inferred from expression pattern PubMed 12420222. Source: UniProtKB

cellular response to transforming growth factor beta stimulus

Inferred from direct assay PubMed 21401405. Source: UniProtKB

chondrocyte differentiation involved in endochondral bone morphogenesis

Inferred from mutant phenotype PubMed 20676705. Source: UniProtKB

chondrocyte hypertrophy

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin remodeling

Inferred from direct assay PubMed 20484372. Source: UniProtKB

cochlea morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

endocardial cushion morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

endocrine pancreas development

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Inferred from sequence or structural similarity PubMed 21512138. Source: UniProtKB

epithelial cell proliferation involved in prostatic bud elongation

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular matrix organization

Inferred from electronic annotation. Source: Ensembl

hair follicle development

Inferred from sequence or structural similarity. Source: UniProtKB

heart valve development

Inferred from sequence or structural similarity. Source: UniProtKB

heart valve formation

Inferred from electronic annotation. Source: Ensembl

heart valve morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

intestinal epithelial structure maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

intrahepatic bile duct development

Inferred from electronic annotation. Source: Ensembl

limb bud formation

Inferred from electronic annotation. Source: Ensembl

male germ-line sex determination

Inferred from sequence or structural similarity. Source: UniProtKB

male gonad development

Inferred from mutant phenotype PubMed 8640233. Source: UniProtKB

mammary gland development

Inferred from electronic annotation. Source: Ensembl

metanephric nephron tubule formation

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of a branching epithelium

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 21367821. Source: UniProtKB

negative regulation of biomineral tissue development

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of bone mineralization

Inferred from electronic annotation. Source: Ensembl

negative regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of chondrocyte differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of immune system process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of myoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of ossification

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of photoreceptor cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 20651055. Source: UniProtKB

neural crest cell development

Inferred from electronic annotation. Source: Ensembl

notochord development

Inferred from electronic annotation. Source: Ensembl

nucleosome assembly

Inferred from direct assay PubMed 20484372. Source: UniProtKB

oligodendrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

ossification

Inferred from electronic annotation. Source: Ensembl

otic vesicle formation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of branching involved in ureteric bud morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cartilage development

Inferred from direct assay PubMed 21401405. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 20651055. Source: UniProtKB

positive regulation of cell proliferation involved in heart morphogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of chondrocyte differentiation

Inferred from direct assay PubMed 21401405. Source: UniProtKB

positive regulation of epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 21512138. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from expression pattern PubMed 20103652. Source: UniProtKB

positive regulation of kidney development

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of male gonad development

Inferred from direct assay PubMed 21412441. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal stem cell differentiation

Inferred from direct assay PubMed 21401405. Source: UniProtKB

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein catabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20530484PubMed 8640233. Source: UniProtKB

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10805756. Source: UniProtKB

prostate gland development

Inferred from expression pattern PubMed 20103652. Source: UniProtKB

protein complex assembly

Inferred from direct assay PubMed 20530484. Source: UniProtKB

protein kinase B signaling

Inferred from electronic annotation. Source: Ensembl

regulation of apoptotic process

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

regulation of cell cycle process

Inferred from mutant phenotype PubMed 12420222. Source: UniProtKB

regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell proliferation involved in tissue homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

renal vesicle induction

Inferred from sequence or structural similarity. Source: UniProtKB

retina development in camera-type eye

Inferred from sequence or structural similarity. Source: UniProtKB

retinal rod cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system development

Inferred from mutant phenotype PubMed 8640233. Source: UniProtKB

somatic stem cell maintenance

Inferred from sequence or structural similarity. Source: UniProtKB

spermatogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

tissue homeostasis

Inferred from sequence or structural similarity. Source: UniProtKB

transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20484372PubMed 21412441. Source: GOC

ureter morphogenesis

Inferred from electronic annotation. Source: Ensembl

ureter urothelium development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentnucleus

Inferred from direct assay PubMed 10805756PubMed 12420222PubMed 18512230PubMed 8640233. Source: UniProtKB

protein complex

Inferred from direct assay PubMed 20530484. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription

Inferred from direct assay PubMed 20484372PubMed 20530484PubMed 21367821. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 20484372PubMed 21412441. Source: UniProtKB

chromatin binding

Inferred from direct assay PubMed 20484372. Source: UniProtKB

core promoter sequence-specific DNA binding

Inferred from direct assay PubMed 20530484. Source: UniProtKB

enhancer binding

Inferred from direct assay PubMed 10805756. Source: UniProtKB

enhancer sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase A catalytic subunit binding

Inferred from physical interaction PubMed 10805756. Source: UniProtKB

protein kinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 10805756. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 509509Transcription factor SOX-9
PRO_0000048739

Regions

DNA binding105 – 17369HMG box
Compositional bias339 – 37840Gln/Pro-rich
Compositional bias342 – 3465Poly-Pro

Natural variations

Natural variant761A → E in CMD1; dimerization and the resulting capacity to activate promoters via dimeric binding sites is lost; other features of the protein function remain unaltered. Ref.15
VAR_063642
Natural variant1081P → L in CMD1. Ref.9
VAR_003735
Natural variant1121F → L in CMD1; loss of DNA binding. Ref.8 Ref.11
VAR_003736
Natural variant1121F → S in CMD1. Ref.10
VAR_003737
Natural variant1131M → T in CMD1. Ref.16
VAR_063643
Natural variant1131M → V in CMD1; residual DNA binding and transactivation of regulated genes. Ref.17
VAR_063644
Natural variant1191A → V in CMD1; almost no loss of DNA binding. Ref.8 Ref.11
VAR_003738
Natural variant1431W → R in CMD1. Ref.9
VAR_003739
Natural variant1521R → P in CMD1. Ref.9
VAR_003740
Natural variant1541F → L in CMD1; 5% of wild-type DNA binding activity; transcriptional activation is only reduced to 26% of wild-type activity. Ref.14
VAR_008529
Natural variant1581A → T in CMD1; 17% of wild-type DNA binding activity; shows a 2-fold reduction in nuclear import efficiency; transcriptional activation is only reduced to 62% of wild-type activity. Ref.14
VAR_008530
Natural variant1651H → Q in CMD1; residual DNA binding and transactivation of regulated genes. Ref.17
VAR_063645
Natural variant1651H → Y in CMD1; loss of DNA binding. Ref.11 Ref.13
Corresponds to variant rs28940282 [ dbSNP | Ensembl ].
VAR_008531
Natural variant1701P → L in CMD1. Ref.16
VAR_063646
Natural variant1701P → R in CMD1. Ref.9 Ref.11
VAR_003741
Natural variant1731K → E in CMD1. Ref.12
VAR_063647
Natural variant354 – 3563Missing in CMD1.
VAR_003742

Secondary structure

....... 509
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P48436 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 9289CFBB8D6631A2

FASTA50956,137
        10         20         30         40         50         60 
MNLLDPFMKM TDEQEKGLSG APSPTMSEDS AGSPCPSGSG SDTENTRPQE NTFPKGEPDL 

        70         80         90        100        110        120 
KKESEEDKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK NKPHVKRPMN AFMVWAQAAR 

       130        140        150        160        170        180 
RKLADQYPHL HNAELSKTLG KLWRLLNESE KRPFVEEAER LRVQHKKDHP DYKYQPRRRK 

       190        200        210        220        230        240 
SVKNGQAEAE EATEQTHISP NAIFKALQAD SPHSSSGMSE VHSPGEHSGQ SQGPPTPPTT 

       250        260        270        280        290        300 
PKTDVQPGKA DLKREGRPLP EGGRQPPIDF RDVDIGELSS DVISNIETFD VNEFDQYLPP 

       310        320        330        340        350        360 
NGHPGVPATH GQVTYTGSYG ISSTAATPAS AGHVWMSKQQ APPPPPQQPP QAPPAPQAPP 

       370        380        390        400        410        420 
QPQAAPPQQP AAPPQQPQAH TLTTLSSEPG QSQRTHIKTE QLSPSHYSEQ QQHSPQQIAY 

       430        440        450        460        470        480 
SPFNLPHYSP SYPPITRSQY DYTDHQNSSS YYSHAAGQGT GLYSTFTYMN PAQRPMYTPI 

       490        500 
ADTSGVPSIP QTHSPQHWEQ PVYTQLTRP 

« Hide

References

« Hide 'large scale' references
[1]"Campomelic dysplasia and autosomal sex reversal caused by mutations in an SRY-related gene."
Foster J.W., Dominguez-Steglich M.A., Guioli S., Kowk G., Weller P.A., Stevanovic M., Weissenbach J., Mansour S., Young I.D., Goodfellow P.N., Schafer A.J.
Nature 372:525-530(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[2]"Autosomal sex reversal and campomelic dysplasia are caused by mutations in and around the SRY-related gene SOX9."
Wagner T., Wirth J., Meyer J., Zabel B., Held M., Zimmer J., Pasantes J., Bricarelli F.D., Keutel J., Hustert E., Wolf U., Tommerup N., Schempp W., Scherer G.
Cell 79:1111-1120(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye and PNS.
[6]"A SOX9 duplication and familial 46,XX developmental testicular disorder."
Cox J.J., Willatt L., Homfray T., Woods C.G.
N. Engl. J. Med. 364:91-93(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN SRXX2.
[7]"Mutations in SRY and SOX9: testis-determining genes."
Cameron F.J., Sinclair A.H.
Hum. Mutat. 9:388-395(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON VARIANTS.
[8]"Mutations in SOX9, the gene responsible for Campomelic dysplasia and autosomal sex reversal."
Kwok C., Weller P.A., Guioli S., Foster J.W., Mansour S., Zuffardi O., Punnett H.H., Dominguez-Steglich M.A., Brook J.D., Young I.D., Goodfellow P.N., Schafer A.J.
Am. J. Hum. Genet. 57:1028-1036(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 LEU-112 AND VAL-119.
[9]"Mutational analysis of the SOX9 gene in campomelic dysplasia and autosomal sex reversal: lack of genotype/phenotype correlations."
Meyer J., Suedbeck P., Held M., Wagner T., Schmitz M.L., Bricarelli F.D., Eggermont E., Friedrich U., Haas O.A., Kobelt A., Leroy J.G., van Maldergem L., Michel E., Mitulla B., Pfeiffer R.A., Schinzel A., Schmidt H., Scherer G.
Hum. Mol. Genet. 6:91-98(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 LEU-108; ARG-143; PRO-152 AND ARG-170.
[10]"Novel missense mutation in the HMG box of SOX9 gene in a Japanese XY male resulted in campomelic dysplasia and severe defect in masculinization."
Goji K., Nishijima E., Tsugawa C., Nishio H., Pokharel R.K., Matsuo M.
Hum. Mutat. Suppl. 1:S114-S116(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1 SER-112.
[11]"Functional and structural studies of wild type SOX9 and mutations causing campomelic dysplasia."
McDowall S., Argentaro A., Ranganathan S., Weller P., Mertin S., Mansour S., Tolmie J., Harley V.
J. Biol. Chem. 274:24023-24030(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 LEU-112; VAL-119; TYR-165 AND ARG-170, 3D-STRUCTURE MODELING.
[12]"Acampomelic campomelic dysplasia with SOX9 mutation."
Thong M.-K., Scherer G., Kozlowski K., Haan E., Morris L.
Am. J. Med. Genet. 93:421-425(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1 GLU-173.
[13]"Acampomelic campomelic syndrome."
Moog U., Jansen N.J., Scherer G., Schrander-Stumpel C.T.
Am. J. Med. Genet. 104:239-245(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1 TYR-165.
[14]"Compound effects of point mutations causing campomelic dysplasia/autosomal sex reversal upon SOX9 structure, nuclear transport, DNA binding, and transcriptional activation."
Preiss S., Argentaro A., Clayton A., John A., Jans D.A., Ogata T., Nagai T., Barroso I., Schafer A.J., Harley V.R.
J. Biol. Chem. 276:27864-27872(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 LEU-154 AND THR-158, CHARACTERIZATION OF VARIANTS CMD1 LEU-154 AND THR-158.
[15]"Loss of DNA-dependent dimerization of the transcription factor SOX9 as a cause for campomelic dysplasia."
Sock E., Pagon R.A., Keymolen K., Lissens W., Wegner M., Scherer G.
Hum. Mol. Genet. 12:1439-1447(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1 GLU-76.
[16]"Mutation analysis of SOX9 and single copy number variant analysis of the upstream region in eight patients with campomelic dysplasia and acampomelic campomelic dysplasia."
Wada Y., Nishimura G., Nagai T., Sawai H., Yoshikata M., Miyagawa S., Hanita T., Sato S., Hasegawa T., Ishikawa S., Ogata T.
Am. J. Med. Genet. A 149:2882-2885(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 THR-113 AND LEU-170.
[17]"Heterozygous SOX9 mutations allowing for residual DNA-binding and transcriptional activation lead to the acampomelic variant of campomelic dysplasia."
Staffler A., Hammel M., Wahlbuhl M., Bidlingmaier C., Flemmer A.W., Pagel P., Nicolai T., Wegner M., Holzinger A.
Hum. Mutat. 31:E1436-E1444(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMD1 VAL-113 AND GLN-165, CHARACTERIZATION OF VARIANTS CMD1 VAL-113 AND GLN-165.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z46629 mRNA. Translation: CAA86598.1.
S74506, S74504, S74505 Genomic DNA. Translation: AAB32870.1.
BT006875 mRNA. Translation: AAP35521.1.
CH471099 Genomic DNA. Translation: EAW89102.1.
BC007951 mRNA. Translation: AAH07951.1.
BC056420 mRNA. Translation: AAH56420.1.
PIRA55204.
RefSeqNP_000337.1. NM_000346.3.
UniGeneHs.647409.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1S9Mmodel-A101-177[»]
1SX9model-A101-177[»]
4EUWX-ray2.77A98-181[»]
ProteinModelPortalP48436.
SMRP48436. Positions 103-174.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112545. 15 interactions.
IntActP48436. 1 interaction.
STRING9606.ENSP00000245479.

PTM databases

PhosphoSiteP48436.

Polymorphism databases

DMDM1351096.

Proteomic databases

PaxDbP48436.
PRIDEP48436.

Protocols and materials databases

DNASU6662.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000245479; ENSP00000245479; ENSG00000125398.
GeneID6662.
KEGGhsa:6662.
UCSCuc002jiw.3. human.

Organism-specific databases

CTD6662.
GeneCardsGC17P070117.
HGNCHGNC:11204. SOX9.
HPACAB022456.
HPA001758.
MIM114290. phenotype.
278850. phenotype.
608160. gene.
neXtProtNX_P48436.
Orphanet2138. 46,XX ovotesticular disorder of sex development.
393. 46,XX testicular disorder of sex development.
140. Campomelic dysplasia.
PharmGKBPA36041.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG295709.
HOGENOMHOG000108876.
HOVERGENHBG002061.
InParanoidP48436.
KOK09270.
OMAPTQRPMY.
OrthoDBEOG7Q2N5K.
PhylomeDBP48436.

Enzyme and pathway databases

SignaLinkP48436.

Gene expression databases

BgeeP48436.
CleanExHS_SOX9.
GenevestigatorP48436.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
InterProIPR009071. HMG_box_dom.
IPR022151. Sox_N.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
PF12444. Sox_N. 1 hit.
[Graphical view]
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. SSF47095. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiSOX9.
GenomeRNAi6662.
NextBio25973.
PROP48436.
SOURCESearch...

Entry information

Entry nameSOX9_HUMAN
AccessionPrimary (citable) accession number: P48436
Secondary accession number(s): Q53Y80
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM