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

Q60611 (SATB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. 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:
DNA-binding protein SATB1
Alternative name(s):
Special AT-rich sequence-binding protein 1
Gene names
Name:Satb1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length764 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for the switching of fetal globin species, and beta- and gamma-globin genes regulation during erythroid differentiation. Plays a role in chromatin organization and nuclear architecture during apoptosis By similarity. Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma. Binds to DNA at special AT-rich sequences, the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or scaffold-associated regions. Thought to recognize the sugar-phosphate structure of double-stranded DNA. Transcriptional repressor controlling nuclear and viral gene expression in a phosphorylated and acetylated status-dependent manner, 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. Modulates genes that are essential in the maturation of the immune T-cell CD8SP from thymocytes. Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16

Subunit structure

Interacts with PCAF. Interacts with sumoylated PML and HDAC1 Tat via the PDZ-like dimerization domain. Interacts also with DYNLT3 and POLR2J2. Binds to EP300 By similarity. Homodimer. Part of the nuclear protein complex gamma-globin promoter and enhancer binding factor (gamma-PE) composed at least by SATB1 and HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment to DNA and promotes transcription repression. Interacts (via DNA-binding domains) with CUX1; leading to inhibit the attachment to DNA. Ref.6 Ref.8 Ref.16

Subcellular location

Nucleus. NucleusPML body. Note: Organized into a cage-like network anchoring loops of heterochromatin and tethering specialized DNA sequences. When sumoylated, localized in promyelocytic leukemia nuclear bodies (PML NBs) By similarity. Ref.10 Ref.11

Tissue specificity

Mainly expressed in thymus, spleen, and lymph nodes with a lower level observed in the brain. Ref.12

Post-translational modification

Sumoylated By similarity. Sumoylation promotes cleavage by caspases By similarity.

Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated form interacts with HDAC1, but unphosphorylated form interacts with PCAF. DNA binding properties are activated by phosphorylation and inactivated by acetylation. In opposition, gene expression is down-regulated by phosphorylation but up-regulated by acetylation By similarity.

Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell apoptosis in thymus and during B-cell stimulation. The cleaved forms can not dimerize and lose transcription regulation function because of impaired DNA and chromatin association. Ref.6

Disruption phenotype

Mice are small in size, have disproportionately small thymi and spleens, and die at 3 weeks of age. Multiple defects in T-cell development are observed, including interrupted thymocytes differentiation and abnormal T-cell transcriptome. Ref.9 Ref.12

Sequence similarities

Belongs to the CUT homeobox family.

Contains 2 CUT DNA-binding domains.

Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityChromosomal rearrangement
   DomainHomeobox
Repeat
   LigandDNA-binding
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, alpha-beta T cell differentiation

Inferred from mutant phenotype Ref.9. Source: MGI

CD8-positive, alpha-beta T cell differentiation

Inferred from mutant phenotype Ref.9Ref.12. Source: MGI

T cell activation

Inferred from mutant phenotype Ref.9. Source: MGI

activated T cell proliferation

Inferred from mutant phenotype Ref.12. Source: MGI

chromatin organization

Inferred from direct assay Ref.10. Source: MGI

chromatin remodeling

Inferred from mutant phenotype PubMed 21930775. Source: MGI

epidermis development

Inferred from mutant phenotype PubMed 21930775. Source: MGI

histone methylation

Inferred from direct assay Ref.10. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.11. Source: MGI

reflex

Inferred from mutant phenotype Ref.9. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay Ref.10. Source: MGI

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from electronic annotation. Source: UniProtKB-SubCell

chromatin

Inferred from direct assay Ref.11. Source: MGI

nuclear heterochromatin

Inferred from direct assay Ref.10. Source: MGI

nuclear matrix

Inferred from direct assay Ref.11. Source: MGI

   Molecular_functionDNA binding

Inferred from direct assay Ref.10Ref.11Ref.1. Source: MGI

chromatin binding

Inferred from direct assay PubMed 21930775. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.10. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 764764DNA-binding protein SATB1
PRO_0000202399

Regions

DNA binding361 – 44888CUT 1
DNA binding484 – 57188CUT 2
DNA binding646 – 70560Homeobox
Region90 – 204115PDZ-like dimerization domain
Region224 – 27855Nuclear matrix targeting sequence (NMTS) By similarity
Region400 – 41011Matrix attachment region (MAR) DNA-binding By similarity
Motif20 – 4021Nuclear localization signal By similarity
Motif139 – 1435Protein interaction By similarity
Motif224 – 27855Nuclear matrix targeting sequence (NMTS)
Compositional bias591 – 60717Poly-Gln
Compositional bias608 – 61710Poly-Pro

Sites

Binding site3901Matrix attachment region (MAR) DNA By similarity
Binding site4251Matrix attachment region (MAR) DNA By similarity
Site254 – 2552Cleavage; by caspases

Amino acid modifications

Modified residue1361N6-acetyllysine By similarity
Modified residue1851Phosphoserine By similarity
Cross-link745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict1551D → N in AAA17372. Ref.1
Sequence conflict5151L → P in AAA17372. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q60611 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 330ECCDBA8683B78

FASTA76485,880
        10         20         30         40         50         60 
MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGG KMQGVPLKHS 

        70         80         90        100        110        120 
GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL VRKDMLFNQL IEMALLSLGY 

       130        140        150        160        170        180 
SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD ATVADMLQDV YHVVTLKIQL HSCPKLEDLP 

       190        200        210        220        230        240 
PEQWSHTTVR NALKDLLKDM NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY 

       250        260        270        280        290        300 
KHFKKTKDMM VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL 

       310        320        330        340        350        360 
PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP PPVSRSMNKP 

       370        380        390        400        410        420 
LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR TQGLLSEILR KEEDPKTASQ 

       430        440        450        460        470        480 
SLLVNLRAMQ NFLQLPEAER DRIYQDERER SLNAASAMGP APLLSTPPSR PPQVKTATLA 

       490        500        510        520        530        540 
TERNGKPENN TMNINASIYD EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP 

       550        560        570        580        590        600 
ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ 

       610        620        630        640        650        660 
QQQQQQQPPP PPPQPQPQPQ AGPRLPPRQP TVASSAESDE ENRQKTRPRT KISVEALGIL 

       670        680        690        700        710        720 
QSFIQDVGLY PDEEAIQTLS AQLDLPKYTI IKFFQNQRYY LKHHGKLKDN SGLEVDVAEY 

       730        740        750        760 
KDEELLKDLE ESVQDKNANT LFSVKLEEEL SVEGSTDVNA DLKD 

« Hide

References

« Hide 'large scale' references
[1]"A novel DNA-binding motif in the nuclear matrix attachment DNA-binding protein SATB1."
Nakagomi K., Kohwi Y., Dickinson L.A., Kohwi-Shigematsu T.
Mol. Cell. Biol. 14:1852-1860(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Thymus.
[2]"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 and NOD.
Tissue: Thymus and Visual cortex.
[3]"Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., 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].
Strain: FVB/N.
Tissue: Salivary gland.
[6]"SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization, causing detachment from chromatin early in T-cell apoptosis."
Galande S., Dickinson L.A., Mian I.S., Sikorska M., Kohwi-Shigematsu T.
Mol. Cell. Biol. 21:5591-5604(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 255-259, FUNCTION, DIMERIZATION, CLEAVAGE BY CASP6.
[7]"The matrix attachment region-binding protein SATB1 participates in negative regulation of tissue-specific gene expression."
Liu J., Bramblett D., Zhu Q., Lozano M., Kobayashi R., Ross S.R., Dudley J.P.
Mol. Cell. Biol. 17:5275-5287(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Homeoproteins CDP and SATB1 interact: potential for tissue-specific regulation."
Liu J., Barnett A., Neufeld E.J., Dudley J.P.
Mol. Cell. Biol. 19:4918-4926(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CUX1.
[9]"The MAR-binding protein SATB1 orchestrates temporal and spatial expression of multiple genes during T-cell development."
Alvarez J.D., Yasui D.H., Niida H., Joh T., Loh D.Y., Kohwi-Shigematsu T.
Genes Dev. 14:521-535(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[10]"Tissue-specific nuclear architecture and gene expression regulated by SATB1."
Cai S., Han H.-J., Kohwi-Shigematsu T.
Nat. Genet. 34:42-51(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Nuclear matrix binding regulates SATB1-mediated transcriptional repression."
Seo J., Lozano M.M., Dudley J.P.
J. Biol. Chem. 280:24600-24609(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR MATRIX TARGETING SEQUENCE.
[12]"A role for SATB1, a nuclear matrix association region-binding protein, in the development of CD8SP thymocytes and peripheral T lymphocytes."
Nie H., Maika S.D., Tucker P.W., Gottlieb P.D.
J. Immunol. 174:4745-4752(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
[13]"SATB1 packages densely looped, transcriptionally active chromatin for coordinated expression of cytokine genes."
Cai S., Lee C.C., Kohwi-Shigematsu T.
Nat. Genet. 38:1278-1288(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"SATB1 is required for CD8 coreceptor reversal."
Nie H., Yao X., Maika S.D., Tucker P.W.
Mol. Immunol. 46:207-211(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]"SATB1 defines the developmental context for gene silencing by Xist in lymphoma and embryonic cells."
Agrelo R., Souabni A., Novatchkova M., Haslinger C., Leeb M., Komnenovic V., Kishimoto H., Gresh L., Kohwi-Shigematsu T., Kenner L., Wutz A.
Dev. Cell 16:507-516(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[16]"Acetylation-dependent interaction of SATB1 and CtBP1 mediates transcriptional repression by SATB1."
Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.
Mol. Cell. Biol. 29:1321-1337(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CTBP1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U05252 mRNA. Translation: AAA17372.1.
AK088563 mRNA. Translation: BAC40427.1.
AK158518 mRNA. Translation: BAE34542.1.
CT010371 mRNA. Translation: CAJ18578.1.
BC011132 mRNA. Translation: AAH11132.1.
CH466559 Genomic DNA. Translation: EDL23652.1.
PIRA56208.
RefSeqNP_001157102.1. NM_001163630.1.
NP_001157103.1. NM_001163631.1.
NP_001157104.1. NM_001163632.1.
NP_033148.2. NM_009122.2.
UniGeneMm.311655.

3D structure databases

ProteinModelPortalQ60611.
SMRQ60611. Positions 71-171, 179-250, 370-452, 486-573, 647-705.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203077. 1 interaction.

PTM databases

PhosphoSiteQ60611.

Proteomic databases

PaxDbQ60611.
PRIDEQ60611.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000133574; ENSMUSP00000120536; ENSMUSG00000023927.
ENSMUST00000144331; ENSMUSP00000116006; ENSMUSG00000023927.
ENSMUST00000152830; ENSMUSP00000119842; ENSMUSG00000023927.
ENSMUST00000169480; ENSMUSP00000128841; ENSMUSG00000023927.
ENSMUST00000176669; ENSMUSP00000134957; ENSMUSG00000023927.
GeneID20230.
KEGGmmu:20230.
UCSCuc008czd.2. mouse.

Organism-specific databases

CTD6304.
MGIMGI:105084. Satb1.

Phylogenomic databases

eggNOGNOG313826.
GeneTreeENSGT00390000008096.
HOGENOMHOG000004805.
HOVERGENHBG054240.
InParanoidQ91XB1.
OrthoDBEOG7FBRH5.
PhylomeDBQ60611.
TreeFamTF332714.

Gene expression databases

ArrayExpressQ60611.
BgeeQ60611.
CleanExMM_SATB1.
GenevestigatorQ60611.

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

ChiTaRSSATB1. mouse.
NextBio297861.
PROQ60611.
SOURCESearch...

Entry information

Entry nameSATB1_MOUSE
AccessionPrimary (citable) accession number: Q60611
Secondary accession number(s): Q91XB1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 125 of the entry and version 2 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