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Protein

Transcription factor SOX-9

Gene

SOX9

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcription factor that selectively activates enhancer through its interaction with a DNA-binding partner factor. Activates enhancer of COL2A1 through its binding with DNA sequence 5'-ATTCAT-3'. In response to bone morphogenetic protein stimulus, phosphorylation is induced and then sumoylation, allowing cooperation with SNAI2 to trigger neural crest delamination. Functions at the level of mesenchymal cell condensation by inducing cartilage development in limbs and by changing the aggregation properties of limb mesenchymal cells. Regulates the cell fate decision to follow the cartilage differentiation pathway.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi105 – 17369HMG boxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-GGA-3769402. Deactivation of the beta-catenin transactivating complex.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor SOX-9
Gene namesi
Name:SOX9
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 18

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nuclear transcription factor complex Source: Ensembl
  • nucleoplasm Source: Ensembl
  • nucleus Source: AgBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611K → R: Decreases cooperating with SNAI2 to trigger neural crest delamination; when associated with R-254 and R-376. 1 Publication
Mutagenesisi64 – 641S → A: Abolishes sumoylation; when associated with A-181. Abolishes phosphorylation; when associated with A-181. Reduces ability to associate with UBE2I; when associated with A-181. Prevents trunk neural crest delamination; when associated with A-181. Prevents cooperating with SNAI2 to trigger neural crest delamination; when associated with A-181. Abolishes interaction with SNAI2; when associated with A-181. 1 Publication
Mutagenesisi64 – 641S → D: Sumoylation; when associated with D-181. Initiates trunk neural crest delamination; when associated with D-181. Allows cooperating with SNAI2 to trigger neural crest delamination; when associated with D-181. Allows interaction with SNAI2; when associated with D-181. 1 Publication
Mutagenesisi181 – 1811S → A: Abolishes sumoylation; when associated with A-64. Abolishes phosphorylation; when associated with A-64. Reduces ability to associate with UBE2I; when associated with A-64. Prevents trunk neural crest delamination; when associated with A-64. Prevents cooperating with SNAI2 to trigger neural crest delamination; when associated with A-64. Abolishes interaction with SNAI2; when associated with A-64. 1 Publication
Mutagenesisi181 – 1811S → D: Sumoylation; when associated with D-64. Initiates trunk neural crest delamination; when associated with D-64. Allows cooperating with SNAI2 to trigger neural crest delamination; when associated with D-64. Allows interaction with SNAI2; when associated with D-64. 1 Publication
Mutagenesisi254 – 2541K → R: Decreases cooperating with SNAI2 to trigger neural crest delamination; when associated with R-61 and R-376. 1 Publication
Mutagenesisi376 – 3761K → R: Decreases cooperating with SNAI2 to trigger neural crest delamination; when associated with R-61 and R-254. 1 Publication
Mutagenesisi376 – 3761K → R: Not sumoylated. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 494494Transcription factor SOX-9PRO_0000048745Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphoserine1 Publication
Modified residuei181 – 1811Phosphoserine1 Publication
Cross-linki376 – 376Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Phosphorylated at Ser-181 in the developing neural tube. Phosphorylation at either Ser-64 or Ser-181 is required for sumoylation, but phosphorylation is not dependent on sumoylation. Sumoylation is enhanced by PKA. Phosphorylation is required for interaction with SNAI2 to trigger neural crest delamination and for an efficient trunk neural crest delamination, whereas sumoylation plays a less significant role. Phosphorylation and sumoylation are induced by BMP signaling pathway.1 Publication
Sumoylated at Lys-376; phosphorylation at either Ser-64 or Ser-181 is required for sumoylation. Sumoylation is induced by BMP signaling pathway.1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP48434.

PTM databases

iPTMnetiP48434.

Expressioni

Developmental stagei

Found in chondrogenic regions in the branchial arches, somites and limb buds at E22. At E28 detected in the limbs, developing scapula, prevertebrae and ribs. Found in condensing mesenchyme of the forelimb at E25. Expressed in the condensing mesenchyme at the distal tips of the developing hindlimbs at E26.1 Publication

Inductioni

By BMP2 during chondrogenesis.1 Publication

Gene expression databases

ExpressionAtlasiP48434. baseline and differential.

Interactioni

Subunit structurei

Interacts with SNAI2; triggers neural crest delamination in a phosphorylation dependent manner. Interacts with UBE2I.1 Publication

GO - Molecular functioni

  • ubiquitin-like protein conjugating enzyme binding Source: AgBase

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037718.

Structurei

3D structure databases

ProteinModelPortaliP48434.
SMRiP48434. Positions 105-179.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi214 – 2196Poly-Ser
Compositional biasi342 – 36019Gln/Pro-richAdd
BLAST
Compositional biasi395 – 4028Poly-Gln

Sequence similaritiesi

Contains 1 HMG box DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0527. Eukaryota.
ENOG410XT0K. LUCA.
GeneTreeiENSGT00760000118988.
HOGENOMiHOG000108876.
HOVERGENiHBG002061.
InParanoidiP48434.
KOiK18435.
OMAiTITRSQY.
OrthoDBiEOG7Q2N5K.
PhylomeDBiP48434.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
IPR029548. SOX-9.
IPR022151. Sox_N.
[Graphical view]
PANTHERiPTHR10270:SF212. PTHR10270:SF212. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
PF12444. Sox_N. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P48434-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNLLDPFMKM TEEQDKCISD APSPTMSDDS AGSPCPSGSG SDTENTRPQE
60 70 80 90 100
NTFPKGDPDL KKESDEDKFP VCIREAVSQV LKGYDWTLVP MPVRVNGSSK
110 120 130 140 150
NKPHVKRPMN AFMVWAQAAR RKLADQYPHL HNAELSKTLG KLWRLLNESE
160 170 180 190 200
KRPFVEEAER LRVQHKKDHP DYKYQPRRRK SVKNGQSEQE EGSEQTHISP
210 220 230 240 250
NAIFKALQAD SPQSSSSISE VHSPGEHSGQ SQGPPTPPTT PKTDAQQPGK
260 270 280 290 300
QDLKREGRPL AEGGRQPPHI DFRDVDIGEL SSDVISNIET FDVNEFDQYL
310 320 330 340 350
PPNGHPGVPA THGQVTTYSG TYGISSSASS PAGAGHAWMA KQQPQPPQPP
360 370 380 390 400
AQPPAQHTLP ALSGEQGPAQ QRPHIKTEQL SPSHYSEQQQ HSPQQQQQQQ
410 420 430 440 450
QQLGYGSFNL QHYGSSYPPI TRSQYDYTEH QNSGSYYSHA AGQSGGLYST
460 470 480 490
FTYMNPTQRP MYTPIADTSG VPSIPQTHSP QHWEQPVYTQ LTRP
Length:494
Mass (Da):54,848
Last modified:July 9, 2014 - v3
Checksum:iA3926313CA954E32
GO

Sequence cautioni

The sequence AAB09663.1 differs from that shown. Reason: Frameshift at several positions. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti17 – 204CISD → GLSG in AAB09663 (PubMed:10340758).Curated
Sequence conflicti181 – 1811S → T in AAB09663 (PubMed:10340758).Curated
Sequence conflicti385 – 3851Y → N in AAB09663 (PubMed:10340758).Curated
Sequence conflicti415 – 4151S → F in AAB09663 (PubMed:10340758).Curated
Sequence conflicti424 – 4241Q → E in AAB09663 (PubMed:10340758).Curated
Sequence conflicti446 – 4461G → S in AAB09663 (PubMed:10340758).Curated
Sequence conflicti473 – 4731S → T in AAB09663 (PubMed:10340758).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12533 mRNA. Translation: AAB09663.1. Frameshift.
AB012236 mRNA. Translation: BAA25296.1.
AADN03007462 Genomic DNA. No translation available.
RefSeqiNP_989612.1. NM_204281.1.
UniGeneiGga.890.

Genome annotation databases

EnsembliENSGALT00000038513; ENSGALP00000037718; ENSGALG00000004386.
GeneIDi374148.
KEGGigga:374148.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12533 mRNA. Translation: AAB09663.1. Frameshift.
AB012236 mRNA. Translation: BAA25296.1.
AADN03007462 Genomic DNA. No translation available.
RefSeqiNP_989612.1. NM_204281.1.
UniGeneiGga.890.

3D structure databases

ProteinModelPortaliP48434.
SMRiP48434. Positions 105-179.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000037718.

PTM databases

iPTMnetiP48434.

Proteomic databases

PaxDbiP48434.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000038513; ENSGALP00000037718; ENSGALG00000004386.
GeneIDi374148.
KEGGigga:374148.

Organism-specific databases

CTDi6662.

Phylogenomic databases

eggNOGiKOG0527. Eukaryota.
ENOG410XT0K. LUCA.
GeneTreeiENSGT00760000118988.
HOGENOMiHOG000108876.
HOVERGENiHBG002061.
InParanoidiP48434.
KOiK18435.
OMAiTITRSQY.
OrthoDBiEOG7Q2N5K.
PhylomeDBiP48434.

Enzyme and pathway databases

ReactomeiR-GGA-3769402. Deactivation of the beta-catenin transactivating complex.

Miscellaneous databases

PROiP48434.

Gene expression databases

ExpressionAtlasiP48434. baseline and differential.

Family and domain databases

Gene3Di1.10.30.10. 1 hit.
InterProiIPR009071. HMG_box_dom.
IPR029548. SOX-9.
IPR022151. Sox_N.
[Graphical view]
PANTHERiPTHR10270:SF212. PTHR10270:SF212. 1 hit.
PfamiPF00505. HMG_box. 1 hit.
PF12444. Sox_N. 1 hit.
[Graphical view]
SMARTiSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMiSSF47095. SSF47095. 1 hit.
PROSITEiPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Regulation and role of Sox9 in cartilage formation."
    Healy C., Uwanogho D., Sharpe P.T.
    Dev. Dyn. 215:69-78(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CARTILAGE DEVELOPMENT, DEVELOPMENTAL STAGE, INDUCTION.
  2. "Mechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9."
    Kamachi Y., Cheah K.S., Kondoh H.
    Mol. Cell. Biol. 19:107-120(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN TRANSCRIPTION REGULATION.
  3. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowl.
  4. "Phosphorylation of Sox9 is required for neural crest delamination and is regulated downstream of BMP and canonical Wnt signaling."
    Liu J.A., Wu M.H., Yan C.H., Chau B.K., So H., Ng A., Chan A., Cheah K.S., Briscoe J., Cheung M.
    Proc. Natl. Acad. Sci. U.S.A. 110:2882-2887(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN NEURAL CREST DELAMINATION, INTERACTION WITH SNAI2 AND UBE2I, SUBCELLULAR LOCATION, SUMOYLATIOON AT LYS-376, PHOSPHORYLATION AT SER-64 AND SER-181, MUTAGENESIS OF LYS-61; SER-64; SER-181; LYS-254 AND LYS-376.

Entry informationi

Entry nameiSOX9_CHICK
AccessioniPrimary (citable) accession number: P48434
Secondary accession number(s): F1P307, O73668
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: July 9, 2014
Last modified: June 8, 2016
This is version 100 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.