Transcription factor SOX-2 - Mus musculus (Mouse)

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P48432 (SOX2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 97. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Transcription factor SOX-2

Gene names

Name:	Sox2
Synonyms:	Sox-2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	319 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor that forms a trimeric complex with OCT4 on DNA and controls the expression of a number of genes involved in embryonic development such as YES1, FGF4, UTF1 and ZFP206. Critical for early embryogenesis and for embryonic stem cell pluripotency. May function as a switch in neuronal development. Keeps neural cells undifferentiated by counteracting the activity of proneural proteins and suppresses neuronal differentiation By similarity. Ref.4
Subunit structure	Interacts with ZSCAN10. Interacts with SOX3 and FGFR1. Ref.6 Ref.7
Subcellular location	Nucleus Ref.4.
Tissue specificity	Expressed in the brain and retina. A very low level expression is seen in the stomach and lung. Expressed in developing urogenital ridge.
Post-translational modification	Sumoylation inhibits binding on DNA and negatively regulates the FGF4 transactivation.
Biotechnological use	POU5F1/OCT4, SOX2, MYC/c-Myc and KLF4 are the four Yamanaka factors. When combined, these factors are sufficient to reprogram differentiated cells to an embryonic-like state designated iPS (induced pluripotent stem) cells. iPS cells exhibit the morphology and growth properties of ES cells and express ES cell marker genes. Ref.5
Sequence similarities	Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Activator Developmental protein
PTM	Isopeptide bond Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	adenohypophysis development Inferred from mutant phenotype. Source: MGI cell fate specification Inferred from mutant phenotype. Source: MGI cerebral cortex development Inferred from mutant phenotype. Source: MGI detection of mechanical stimulus involved in equilibrioception Inferred from mutant phenotype. Source: MGI detection of mechanical stimulus involved in sensory perception of sound Inferred from mutant phenotype. Source: MGI diencephalon morphogenesis Inferred from mutant phenotype. Source: MGI epithelial tube branching involved in lung morphogenesis Inferred from direct assay. Source: MGI forebrain neuron differentiation Inferred from mutant phenotype. Source: MGI inner ear morphogenesis Inferred from mutant phenotype. Source: MGI lens induction in camera-type eye Inferred from genetic interaction. Source: MGI lung alveolus development Inferred from direct assay. Source: MGI male genitalia development Inferred from mutant phenotype. Source: MGI negative regulation of canonical Wnt receptor signaling pathway Inferred from direct assay. Source: UniProtKB negative regulation of neuron differentiation Inferred from direct assay. Source: MGI negative regulation of osteoblast differentiation Inferred from direct assay. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: MGI neuron fate commitment Inferred from mutant phenotype. Source: MGI olfactory placode formation Inferred from genetic interaction. Source: MGI pigment biosynthetic process Inferred from mutant phenotype. Source: MGI positive regulation of Notch signaling pathway Inferred from direct assay. Source: MGI positive regulation of epithelial cell differentiation Inferred from direct assay. Source: MGI positive regulation of neuroblast proliferation Inferred from mutant phenotype. Source: MGI positive regulation of neuron differentiation Inferred from mutant phenotype. Source: MGI positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.4. Source: MGI response to retinoic acid Inferred from direct assay. Source: MGI retina morphogenesis in camera-type eye Inferred from mutant phenotype. Source: MGI stem cell maintenance Inferred from mutant phenotype. Source: MGI tongue development Inferred from mutant phenotype. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: MGI soluble fraction Inferred from direct assay. Source: MGI transcription factor complex Inferred from direct assay. Source: MGI
Molecular function	chromatin binding Inferred from direct assay. Source: MGI sequence-specific DNA binding Inferred from direct assay. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from direct assay Ref.4. Source: MGI transcription factor binding Inferred from physical interaction. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Sin3a	Q60520	3	EBI-2313612,EBI-349034

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 319

319

Transcription factor SOX-2

PRO_0000048716

Regions

DNA binding

43 – 111

HMG box

Compositional bias

19 – 25

Poly-Gly

Amino acid modifications

Cross-link

247

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.4

Experimental info

Mutagenesis

247

K → R: Absence of sumoylation. Increased FGF4 activation. No effect on nuclear localization. Ref.4

Sequence conflict

153 – 155

GGL → AGV in CAA63847. Ref.3

Sequence conflict

203

V → D in CAA63847. Ref.3

Sequence conflict

310 – 311

KY → IN in CAA63847. Ref.3

Secondary structure

319

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P48432 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: C40DE49E524C49F1
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FASTA

319

34,454

        10         20         30         40         50         60 
MYNMMETELK PPGPQQASGG GGGGGNATAA ATGGNQKNSP DRVKRPMNAF MVWSRGQRRK 

        70         80         90        100        110        120 
MAQENPKMHN SEISKRLGAE WKLLSETEKR PFIDEAKRLR ALHMKEHPDY KYRPRRKTKT 

       130        140        150        160        170        180 
LMKKDKYTLP GGLLAPGGNS MASGVGVGAG LGGGLNQRMD SYAHMNGWSN GSYSMMQEQL 

       190        200        210        220        230        240 
GYPQHPGLNA HGAAQMQPMH RYVVSALQYN SMTSSQTYMN GSPTYSMSYS QQGTPGMALG 

       250        260        270        280        290        300 
SMGSVVKSEA SSSPPVVTSS SHSRAPCQAG DLRDMISMYL PGAEVPEPAA PSRLHMAQHY 

       310 
QSGPVPGTAK YGTLPLSHM

« Hide

References

[1]	"Developmental-specific activity of the FGF-4 enhancer requires the synergistic action of Sox2 and Oct-3." Yuan H., Corbi N., Basilico C., Dailey L. Genes Dev. 9:2635-2645(1995) [PubMed: 7590241] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Yuan H., Corbi N., Basilico C., Dailey L. Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"A comparison of the properties of Sox-3 with Sry and two related genes, Sox-1 and Sox-2." Collignon J., Sockanathan S., Hacker A., Cohen-Tannoudji M., Norris D., Rastan S., Stevanovic M., Goodfellow P.N., Lovell-Badge R. Development 122:509-520(1996) [PubMed: 8625802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 129.
[4]	"Inhibition of DNA binding of Sox2 by the SUMO conjugation." Tsuruzoe S., Ishihara K., Uchimura Y., Watanabe S., Sekita Y., Aoto T., Saitoh H., Yuasa Y., Niwa H., Kawasuji M., Baba H., Nakao M. Biochem. Biophys. Res. Commun. 351:920-926(2006) [PubMed: 17097055] [Abstract] Cited for: SUMOYLATION AT LYS-247, MUTAGENESIS OF LYS-247, SUBCELLULAR LOCATION, FUNCTION.
[5]	"Induction of pluripotent stem cells from mouse embryonic and adult fibroblast cultures by defined factors." Takahashi K., Yamanaka S. Cell 126:663-676(2006) [PubMed: 16904174] [Abstract] Cited for: BIOTECHNOLOGY.
[6]	"SOX3 activity during pharyngeal segmentation is required for craniofacial morphogenesis." Rizzoti K., Lovell-Badge R. Development 134:3437-3448(2007) [PubMed: 17728342] [Abstract] Cited for: INTERACTION WITH SOX3 AND FGFR1.
[7]	"Zfp206, Oct4, and Sox2 are integrated components of a transcriptional regulatory network in embryonic stem cells." Yu H.B., Kunarso G., Hong F.H., Stanton L.W. J. Biol. Chem. 284:31327-31335(2009) [PubMed: 19740739] [Abstract] Cited for: INTERACTION WITH ZSCAN10.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U31967 mRNA. Translation: AAC31791.1.
X94127 Genomic DNA. Translation: CAA63847.1.

IPI

IPI00319017.

PIR

S10949.

RefSeq

NP_035573.3. NM_011443.3.

UniGene

Mm.65396.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1GT0	X-ray	2.60	D	41-120	[»]

ProteinModelPortal

P48432.

SMR

P48432. Positions 41-119.

ModBase

Search...

Protein-protein interaction databases

IntAct

P48432. 4 interactions.

STRING

P48432.

PTM databases

PhosphoSite

P48432.

Proteomic databases

PRIDE

P48432.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

20674.

KEGG

mmu:20674.

Organism-specific databases

CTD

6657.

MGI

MGI:98364. Sox2.

Phylogenomic databases

eggNOG

roNOG07798.

HOGENOM

HBG446398.

HOVERGEN

HBG105663.

InParanoid

P48432.

OrthoDB

EOG4MPHQV.

Gene expression databases

ArrayExpress

P48432.

Bgee

P48432.

CleanEx

MM_SOX2.

Genevestigator

P48432.

GermOnline

ENSMUSG00000074637. Mus musculus.

Family and domain databases

InterPro

IPR000910. HMG_HMG1/HMG2.
IPR009071. HMG_superfamily.
IPR022097. TF_SOX.
[Graphical view]

Gene3D

G3DSA:1.10.30.10. HMG-box. 1 hit.

K09267.

Pfam

PF00505. HMG_box. 1 hit.
PF12336. SOXp. 1 hit.
[Graphical view]

SMART

SM00398. HMG. 1 hit.
[Graphical view]

SUPFAM

SSF47095. HMG-box. 1 hit.

PROSITE

PS50118. HMG_BOX_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

SOURCE

Search...

Entry information

Entry name

SOX2_MOUSE

Accession

Primary (citable) accession number: P48432

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	July 15, 1999
Last modified:	January 25, 2012
This is version 97 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents