Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8VI24 (SATB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 105. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA-binding protein SATB2
Alternative name(s):
Special AT-rich sequence-binding protein 2
Gene names
Name:Satb2
Synonyms:Kiaa1034
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length733 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to DNA, at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcription factor controlling nuclear gene expression, by binding to matrix attachment regions (MARs) of DNA and inducing a local chromatin-loop remodeling. Acts as a docking site for several chromatin remodeling enzymes and also by recruiting corepressors (HDACs) or coactivators (HATs) directly to promoters and enhancers. Required for the initiation of the upper-layer neurons (UL1) specific genetic program and for the inactivation of deep-layer neurons (DL) and UL2 specific genes, probably by modulating Bcl11b expression. Repressor of Ctip2 and regulatory determinant of corticocortical connections in the developing cerebral cortex. May play an important role in palate formation. Acts as a molecular node in a transcriptional network regulating skeletal development and osteoblast differentiation. Ref.3 Ref.4 Ref.5

Subunit structure

Interacts with PIAS1 By similarity. Interacts with ATF4 and RUNX2; resulting in enhanced DNA binding and transactivation by these transcription factors. Ref.3

Subcellular location

Nucleus matrix By similarity.

Tissue specificity

Expressed in cortical neurons that extend axons across the corpus callosum. Also expressed in branchial arches and in cells of the osteoblast lineage, but not in chondrocytes and osteoclasts. Ref.3 Ref.4

Developmental stage

Expression first detected at 10.5 dpc in the maxillary component of the first pharyngeal arch and the lateral aspect of the frontonasal process in the regions that will subsequently fuse to form the primary palate. At 11 - 11.5 dpc, the expression pattern demarcates the region of the medial aspect of the maxillary process within the primitive oral cavity, which will form the palate shelf. By 12.5 dpc, symmetrical expression is seen in the medial edges of the developing palate shelves and this continues until 13.5 dpc when the strongest expression is in the mesenchyme underlying the medial edge epithelia. By the time of palatal shelf fusion at 14.5 dpc the expression is dramatically down-regulated. No expression detected elsewhere in the embryo at any stage examined. Ref.1

Post-translational modification

Sumoylated by PIAS1. Sumoylation promotes nuclear localization, but represses transcription factor activity By similarity.

Disruption phenotype

Malformations in 2 of the major axonal tracts interconnecting the cortical hemispheres: the corpus callosum (c.c) and the anterior commissure (a.c). Misrouted afferent and efferent cortical axon connections. Impaired migration of upper-layer neurons. Ectopic expression of Ctip2. Craniofacial abnormalities and defects in osteoblast differentiation and function. Ref.3 Ref.4 Ref.5

Sequence similarities

Belongs to the CUT homeobox family.

Contains 2 CUT DNA-binding domains.

Contains 1 homeobox DNA-binding domain.

Sequence caution

The sequence BAC98080.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainHomeobox
Repeat
   LigandDNA-binding
   Molecular functionChromatin regulator
Developmental protein
Repressor
   PTMIsopeptide bond
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from mutant phenotype Ref.3. Source: MGI

cellular response to organic substance

Inferred from direct assay PubMed 18794345. Source: MGI

chromatin remodeling

Inferred from direct assay Ref.5. Source: MGI

embryonic pattern specification

Inferred from mutant phenotype Ref.3. Source: MGI

embryonic skeletal system morphogenesis

Inferred from mutant phenotype Ref.3PubMed 16960803. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.3. Source: MGI

neuron migration

Inferred from mutant phenotype PubMed 18288204. Source: MGI

osteoblast development

Inferred from mutant phenotype Ref.3. Source: MGI

palate development

Inferred from mutant phenotype Ref.3PubMed 16960803. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.3. Source: MGI

regulation of gene expression

Inferred from mutant phenotype Ref.5. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

histone deacetylase complex

Inferred from direct assay Ref.5. Source: MGI

nuclear chromatin

Inferred by curator PubMed 15733084. Source: MGI

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 15733084. Source: MGI

transcription factor complex

Inferred from direct assay Ref.3. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay PubMed 15733084Ref.5. Source: MGI

chromatin binding

Inferred from direct assay Ref.3. Source: MGI

protein binding

Inferred from physical interaction Ref.3. Source: MGI

sequence-specific DNA binding

Inferred from genetic interaction Ref.3. Source: MGI

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8VI24-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q8VI24-2)

The sequence of this isoform differs from the canonical sequence as follows:
     58-116: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 733733DNA-binding protein SATB2
PRO_0000202401

Regions

DNA binding350 – 43788CUT 1
DNA binding473 – 56088CUT 2
DNA binding615 – 67460Homeobox

Amino acid modifications

Cross-link233Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link350Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence58 – 11659Missing in isoform 2.
VSP_008967

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 1, 2002. Version 1.
Checksum: 153CFD1CC3491F25

FASTA73382,559
        10         20         30         40         50         60 
MERRSESPCL RDSPDRRSGS PDVKGPPPVK VARLEQNGSP MGARGRPNGA VAKAVGGLMI 

        70         80         90        100        110        120 
PVFCVVEQLD GSLEYDNREE HAEFVLVRKD VLFSQLVETA LLALGYSHSS AAQAQGIIKL 

       130        140        150        160        170        180 
GRWNPLPLSY VTDAPDATVA DMLQDVYHVV TLKIQLQSCS KLEDLPAEQW NHATVRNALK 

       190        200        210        220        230        240 
ELLKEMNQST LAKECPLSQS MISSIVNSTY YANVSATKCQ EFGRWYKKYK KIKVERVERE 

       250        260        270        280        290        300 
NLSDYCVLGQ RPMHLPNMNQ LASLGKTNEQ SPHSQIHHST PIRNQVPALQ PIMSPGLLSP 

       310        320        330        340        350        360 
QLSPQLVRQQ IAMAHLINQQ IAVSRLLAHQ HPQAINQQFL NHPPIPRAVK PEPTNSSVEV 

       370        380        390        400        410        420 
SPDIYQQVRD ELKRASVSQA VFARVAFNRT QGLLSEILRK EEDPRTASQS LLVNLRAMQN 

       430        440        450        460        470        480 
FLNLPEVERD RIYQDERERS MNPNVSMVSS ASSSPSSSRT PQAKTSTPTT DLPIKVDGAN 

       490        500        510        520        530        540 
VNITAAIYDE IQQEMKRAKV SQALFAKVAA NKSQGWLCEL LRWKENPSPE NRTLWENLCT 

       550        560        570        580        590        600 
IRRFLNLPQH ERDVIYEEES RHHHSERMQH VVQLPPEPVQ VLHRQQSQPT KESSPPREEA 

       610        620        630        640        650        660 
PPPPPPTEDS CAKKPRSRTK ISLEALGILQ SFIHDVGLYP DQEAIHTLSA QLDLPKHTII 

       670        680        690        700        710        720 
KFFQNQRYHV KHHGKLKEHL GSAVDVAEYK DEELLTESEE NDSEEGSEEM YKVEAEEENA 

       730 
DKSKAAPAET DQR 

« Hide

Isoform 2 [UniParc].

Checksum: 199D04A796B2FB77
Show »

FASTA67476,039

References

« Hide 'large scale' references
[1]"Identification of SATB2 as the cleft palate gene on 2q32-q33."
FitzPatrick D.R., Carr I.M., McLaren L., Leek J.P., Wightman P., Williamson K., Gautier P., McGill N., Hayward C., Firth H., Markham A.F., Fantes J.A., Bonthron D.T.
Hum. Mol. Genet. 12:2491-2501(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), DEVELOPMENTAL STAGE.
[2]"Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Embryonic tail.
[3]"SATB2 is a multifunctional determinant of craniofacial patterning and osteoblast differentiation."
Dobreva G., Chahrour M., Dautzenberg M., Chirivella L., Kanzler B., Farinas I., Karsenty G., Grosschedl R.
Cell 125:971-986(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH ATF4 AND RUNX2, TISSUE SPECIFICITY.
[4]"Satb2 regulates callosal projection neuron identity in the developing cerebral cortex."
Alcamo E.A., Chirivella L., Dautzenberg M., Dobreva G., Farinas I., Grosschedl R., McConnell S.K.
Neuron 57:364-377(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[5]"Satb2 is a postmitotic determinant for upper-layer neuron specification in the neocortex."
Britanova O., de Juan Romero C., Cheung A., Kwan K.Y., Schwark M., Gyorgy A., Vogel T., Akopov S., Mitkovski M., Agoston D., Sestan N., Molnar Z., Tarabykin V.
Neuron 57:378-392(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF319623 mRNA. Translation: AAL37172.1.
AK129270 mRNA. Translation: BAC98080.1. Different initiation.
CCDSCCDS14965.1. [Q8VI24-1]
RefSeqNP_631885.1. NM_139146.2. [Q8VI24-1]
UniGeneMm.145599.

3D structure databases

ProteinModelPortalQ8VI24.
SMRQ8VI24. Positions 57-157, 165-231, 350-437, 473-560, 615-674.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid229351. 6 interactions.
DIPDIP-60021N.
IntActQ8VI24. 1 interaction.

PTM databases

PhosphoSiteQ8VI24.

Proteomic databases

MaxQBQ8VI24.
PaxDbQ8VI24.
PRIDEQ8VI24.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000042857; ENSMUSP00000046067; ENSMUSG00000038331. [Q8VI24-2]
ENSMUST00000114415; ENSMUSP00000110057; ENSMUSG00000038331. [Q8VI24-1]
GeneID212712.
KEGGmmu:212712.
UCSCuc007bas.1. mouse. [Q8VI24-1]
uc011wlc.1. mouse. [Q8VI24-2]

Organism-specific databases

CTD23314.
MGIMGI:2679336. Satb2.
RougeSearch...

Phylogenomic databases

eggNOGNOG313826.
GeneTreeENSGT00390000008096.
HOGENOMHOG000004805.
HOVERGENHBG054240.
InParanoidQ8VI24.
OMAPPAEDSC.
OrthoDBEOG7FBRH5.
PhylomeDBQ8VI24.
TreeFamTF332714.

Gene expression databases

ArrayExpressQ8VI24.
BgeeQ8VI24.
CleanExMM_SATB2.
GenevestigatorQ8VI24.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
1.10.260.40. 2 hits.
InterProIPR003350. Hmoeo_CUT.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamPF02376. CUT. 2 hits.
PF00046. Homeobox. 1 hit.
[Graphical view]
SMARTSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 2 hits.
PROSITEPS51042. CUT. 2 hits.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio373676.
PROQ8VI24.
SOURCESearch...

Entry information

Entry nameSATB2_MOUSE
AccessionPrimary (citable) accession number: Q8VI24
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: March 1, 2002
Last modified: July 9, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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