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Q7M6Y2 (SOX11_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transcription factor SOX-11
Gene names
Name:Sox11
Synonyms:Sox-11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length395 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Probably important in the developing nervous system. May also have a role in tissue modeling during development.

Subcellular location

Nucleus Ref.2.

Tissue specificity

Expression prominent in the periventricular cells of the central nervous system, also observed in a wide range of tissues involved in epithelial-mesenchymal interactions.

Developmental stage

Expression detected from 8.5 dpc through to 13.5 dpc, with a considerable increase in expression apparent at 13.5 dpc.

Sequence similarities

Contains 1 HMG box DNA-binding domain.

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   LigandDNA-binding
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcardiac ventricle formation

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

closure of optic fissure

Inferred from mutant phenotype PubMed 18423449. Source: UniProtKB

cornea development in camera-type eye

Inferred from mutant phenotype PubMed 18423449. Source: UniProtKB

embryonic digestive tract morphogenesis

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

embryonic skeletal system morphogenesis

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

eyelid development in camera-type eye

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

glial cell development

Inferred from mutant phenotype PubMed 20147379PubMed 20646169. Source: UniProtKB

glial cell proliferation

Inferred from mutant phenotype PubMed 20147379. Source: UniProtKB

hard palate development

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

kidney development

Inferred from electronic annotation. Source: Compara

lens morphogenesis in camera-type eye

Inferred from mutant phenotype PubMed 18423449. Source: UniProtKB

limb bud formation

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

lung morphogenesis

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

negative regulation of cell death

Inferred from mutant phenotype PubMed 20596238PubMed 20646169. Source: UniProtKB

negative regulation of glial cell proliferation

Inferred from mutant phenotype PubMed 19808959. Source: UniProtKB

negative regulation of lymphocyte proliferation

Inferred from electronic annotation. Source: Compara

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 19808959. Source: UniProtKB

negative regulation of transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

neural crest cell development

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

neural tube formation

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

neuroepithelial cell differentiation

Inferred from mutant phenotype PubMed 20646169. Source: UniProtKB

noradrenergic neuron differentiation

Inferred from mutant phenotype PubMed 20147379. Source: UniProtKB

oligodendrocyte development

Inferred from electronic annotation. Source: Compara

outflow tract morphogenesis

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

positive regulation of BMP signaling pathway

Inferred from mutant phenotype PubMed 18423449. Source: UniProtKB

positive regulation of hippo signaling cascade

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

positive regulation of hormone secretion

Inferred from mutant phenotype PubMed 21527504. Source: UniProtKB

positive regulation of lens epithelial cell proliferation

Inferred from mutant phenotype PubMed 18423449. Source: UniProtKB

positive regulation of neurogenesis

Inferred from direct assay PubMed 19490090. Source: UniProtKB

positive regulation of neuron differentiation

Inferred from direct assay PubMed 19490090. Source: UniProtKB

positive regulation of ossification

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

positive regulation of osteoblast differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of stem cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Compara

skeletal muscle cell differentiation

Inferred from mutant phenotype PubMed 20847309. Source: MGI

soft palate development

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

somite development

Inferred from mutant phenotype PubMed 20596238. Source: UniProtKB

spinal cord development

Inferred from mutant phenotype PubMed 20646169. Source: UniProtKB

sympathetic nervous system development

Inferred from mutant phenotype PubMed 20147379. Source: UniProtKB

ventricular septum morphogenesis

Inferred from mutant phenotype PubMed 15254231. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from direct assay Ref.2PubMed 19490090PubMed 21527504. Source: UniProtKB

   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 18505825. Source: UniProtKB

RNA polymerase II core promoter sequence-specific DNA binding

Inferred from electronic annotation. Source: Compara

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

Inferred from sequence orthology PubMed 9632656. Source: MGI

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 18505825. Source: UniProtKB

enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 19808959PubMed 21527504. Source: UniProtKB

translation factor activity, nucleic acid binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 395395Transcription factor SOX-11
PRO_0000048751

Regions

DNA binding49 – 11769HMG box
Compositional bias188 – 21427Asp/Glu-rich (highly acidic)
Compositional bias297 – 30812Poly-Ser

Amino acid modifications

Modified residue2441Phosphoserine Ref.7

Experimental info

Sequence conflict1031E → G in AAB82425. Ref.1
Sequence conflict1471A → T in AAB82425. Ref.1
Sequence conflict1711A → V in AAB82425. Ref.1
Sequence conflict1771A → G Ref.1
Sequence conflict1771A → G Ref.2
Sequence conflict192 – 1965EDDDE → DEEDD in AAB82425. Ref.1
Sequence conflict2251T → A in AAB82425. Ref.1
Sequence conflict280 – 2812QP → EA in AAB82425. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q7M6Y2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: AFA34270A054C6C5

FASTA39542,629
        10         20         30         40         50         60 
MVQQAESSEA ESNLPRDALD TEEGEFMACS PVALDESDPD WCKTASGHIK RPMNAFMVWS 

        70         80         90        100        110        120 
KIERRKIMEQ SPDMHNAEIS KRLGKRWKML KDSEKIPFIR EAERLRLKHM ADYPDYKYRP 

       130        140        150        160        170        180 
RKKPKTDPAA KPSAGQSPDK SAAGAKAAKG PGKKCAKLKA PAGKAGAGKA AQPGDCAAGK 

       190        200        210        220        230        240 
AAKCVFLDDD DEDDDEDDEL QLRPKPDADD DDDEPAHSHL LPPPTQQQPP QLLRRYSVAK 

       250        260        270        280        290        300 
VPASPTLSSA AESPEGASLY DEVRAGGRLY YSFKNITKQQ PPPAPPALSP ASSRCVSTSS 

       310        320        330        340        350        360 
SSGSSSGSGA EDADDLMFDL SLNFSQGAHS ACEQPLGAGA AGNLSLSLVD KDLDSFSEGS 

       370        380        390 
LGSHFEFPDY CTPELSEMIA GDWLEANFSD LVFTY 

« Hide

References

« Hide 'large scale' references
[1]"Expression of the Sox11 gene in mouse embryos suggests roles in neuronal maturation and epithelio-mesenchymal induction."
Hargrave M., Wright E., Kun J., Emery J., Cooper L., Koopman P.
Dev. Dyn. 210:79-86(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Embryo.
[2]"Interplay of SOX and POU factors in regulation of the nestin gene in neural primordial cells."
Tanaka S., Kamachi Y., Tanouchi A., Hamada H., Jing N., Kondoh H.
Mol. Cell. Biol. 24:8834-8846(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Strain: 129/Ola.
[3]"Screening for mammalian neural genes via fluorescence-activated cell sorter purification of neural precursors from Sox1-gfp knock-in mice."
Aubert J., Stavridis M.P., Tweedie S., O'Reilly M., Vierlinger K., Li M., Ghazal P., Pratt T., Mason J.O., Roy D., Smith A.
Proc. Natl. Acad. Sci. U.S.A. 100:11836-11841(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[4]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Heart and Lung.
[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].
Strain: C57BL/6.
[6]"Seven new members of the Sox gene family expressed during mouse development."
Wright E.M., Snopek B., Koopman P.
Nucleic Acids Res. 21:744-744(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 57-112.
[7]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, MASS SPECTROMETRY.
Tissue: Embryonic brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF009414 mRNA. Translation: AAB82425.1.
AB108675 mRNA. Translation: BAC75670.1.
BK001484 mRNA. Translation: DAA01568.1.
AK165693 mRNA. Translation: BAE38341.1.
AK146514 mRNA. Translation: BAE27226.1.
BC062095 mRNA. Translation: AAH62095.1.
Z18960 mRNA. Translation: CAA79485.1.
IPIIPI00556698.
RefSeqNP_033260.4. NM_009234.6.
UniGeneMm.41702.
Mm.466344.

3D structure databases

ProteinModelPortalQ7M6Y2.
SMRQ7M6Y2. Positions 47-122.
ModBaseSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000078070.

PTM databases

PhosphoSiteQ7M6Y2.

Proteomic databases

PRIDEQ7M6Y2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000079063; ENSMUSP00000078070; ENSMUSG00000063632.
GeneID20666.
KEGGmmu:20666.
UCSCuc007nfn.2. mouse.

Organism-specific databases

CTD6664.
MGIMGI:98359. Sox11.

Phylogenomic databases

eggNOGNOG130659.
GeneTreeENSGT00690000101789.
HOGENOMHOG000231874.
HOVERGENHBG005040.
InParanoidQ7M6Y2.
KOK09268.
OMATEEGEFM.
OrthoDBEOG4QVCCX.

Gene expression databases

BgeeQ7M6Y2.
CleanExMM_SOX11.
GenevestigatorQ7M6Y2.
GermOnlineENSMUSG00000063632. Mus musculus.

Family and domain databases

Gene3D1.10.30.10. 1 hit.
InterProIPR009071. HMG_box_dom.
IPR017386. SOX-12/11/4a.
[Graphical view]
PfamPF00505. HMG_box. 1 hit.
[Graphical view]
PIRSFPIRSF038098. SOX-12/11/4a. 1 hit.
SMARTSM00398. HMG. 1 hit.
[Graphical view]
SUPFAMSSF47095. HMG-box. 1 hit.
PROSITEPS50118. HMG_BOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSOX11. mouse.
NextBio299129.
SOURCESearch...

Entry information

Entry nameSOX11_MOUSE
AccessionPrimary (citable) accession number: Q7M6Y2
Secondary accession number(s): O35178 expand/collapse secondary AC list , O89036, Q04889, Q80XF0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 27, 2006
Last sequence update: December 15, 2003
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families