Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q60611

- SATB1_MOUSE

UniProt

Q60611 - SATB1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

DNA-binding protein SATB1

Gene

Satb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity9 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei254 – 2552Cleavage; by caspases
Binding sitei390 – 3901Matrix attachment region (MAR) DNABy similarity
Binding sitei425 – 4251Matrix attachment region (MAR) DNABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi361 – 44888CUT 1PROSITE-ProRule annotationAdd
BLAST
DNA bindingi484 – 57188CUT 2PROSITE-ProRule annotationAdd
BLAST
DNA bindingi646 – 70560HomeoboxPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. chromatin binding Source: MGI
  2. DNA binding Source: MGI
  3. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. activated T cell proliferation Source: MGI
  2. CD4-positive, alpha-beta T cell differentiation Source: MGI
  3. CD8-positive, alpha-beta T cell differentiation Source: MGI
  4. chromatin organization Source: MGI
  5. chromatin remodeling Source: MGI
  6. epidermis development Source: MGI
  7. histone methylation Source: MGI
  8. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  9. reflex Source: MGI
  10. regulation of transcription, DNA-templated Source: MGI
  11. T cell activation Source: MGI
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_224460. Apoptotic cleavage of cellular proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-binding protein SATB1
Alternative name(s):
Special AT-rich sequence-binding protein 1
Gene namesi
Name:Satb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:105084. Satb1.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. chromatin Source: MGI
  2. nuclear heterochromatin Source: MGI
  3. nuclear matrix Source: MGI
  4. PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Disruption phenotypei

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.2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 764764DNA-binding protein SATB1PRO_0000202399Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei136 – 1361N6-acetyllysineBy similarity
Modified residuei185 – 1851PhosphoserineBy similarity
Cross-linki745 – 745Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Sumoylated. 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.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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ60611.
PaxDbiQ60611.
PRIDEiQ60611.

PTM databases

PhosphoSiteiQ60611.

Expressioni

Tissue specificityi

Mainly expressed in thymus, spleen, and lymph nodes with a lower level observed in the brain.1 Publication

Gene expression databases

BgeeiQ60611.
CleanExiMM_SATB1.
ExpressionAtlasiQ60611. baseline and differential.
GenevestigatoriQ60611.

Interactioni

Subunit structurei

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 of SATB1 and HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment to DNA and promotes transcription repression. Interacts with CUX1 (via DNA-binding domains); the interaction inhibits the attachment of both proteins to DNA.By similarity2 Publications

Protein-protein interaction databases

BioGridi203077. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ60611.
SMRiQ60611. Positions 71-171, 179-250, 370-452, 486-573, 647-705.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 204115PDZ-like dimerization domainAdd
BLAST
Regioni224 – 27855Nuclear matrix targeting sequence (NMTS)By similarityAdd
BLAST
Regioni400 – 41011Matrix attachment region (MAR) DNA-bindingBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 4021Nuclear localization signalBy similarityAdd
BLAST
Motifi139 – 1435Protein interactionBy similarity
Motifi224 – 27855Nuclear matrix targeting sequence (NMTS)Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi591 – 60717Poly-GlnAdd
BLAST
Compositional biasi608 – 61710Poly-Pro

Sequence similaritiesi

Belongs to the CUT homeobox family.Curated
Contains 2 CUT DNA-binding domains.PROSITE-ProRule annotation
Contains 1 homeobox DNA-binding domain.PROSITE-ProRule annotation

Keywords - Domaini

Homeobox, Repeat

Phylogenomic databases

eggNOGiNOG313826.
GeneTreeiENSGT00390000008096.
HOGENOMiHOG000004805.
HOVERGENiHBG054240.
InParanoidiQ60611.
OrthoDBiEOG7FBRH5.
PhylomeDBiQ60611.
TreeFamiTF332714.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
1.10.260.40. 2 hits.
InterProiIPR003350. CUT_dom.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view]
PfamiPF02376. CUT. 2 hits.
PF00046. Homeobox. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 2 hits.
PROSITEiPS51042. CUT. 2 hits.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q60611-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGG
60 70 80 90 100
KMQGVPLKHS GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL
110 120 130 140 150
VRKDMLFNQL IEMALLSLGY SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD
160 170 180 190 200
ATVADMLQDV YHVVTLKIQL HSCPKLEDLP PEQWSHTTVR NALKDLLKDM
210 220 230 240 250
NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY KHFKKTKDMM
260 270 280 290 300
VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL
310 320 330 340 350
PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP
360 370 380 390 400
PPVSRSMNKP LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR
410 420 430 440 450
TQGLLSEILR KEEDPKTASQ SLLVNLRAMQ NFLQLPEAER DRIYQDERER
460 470 480 490 500
SLNAASAMGP APLLSTPPSR PPQVKTATLA TERNGKPENN TMNINASIYD
510 520 530 540 550
EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP ENRTLWENLS
560 570 580 590 600
MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ
610 620 630 640 650
QQQQQQQPPP PPPQPQPQPQ AGPRLPPRQP TVASSAESDE ENRQKTRPRT
660 670 680 690 700
KISVEALGIL QSFIQDVGLY PDEEAIQTLS AQLDLPKYTI IKFFQNQRYY
710 720 730 740 750
LKHHGKLKDN SGLEVDVAEY KDEELLKDLE ESVQDKNANT LFSVKLEEEL
760
SVEGSTDVNA DLKD
Length:764
Mass (Da):85,880
Last modified:July 27, 2011 - v2
Checksum:i330ECCDBA8683B78
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti155 – 1551D → N in AAA17372. (PubMed:8114718)Curated
Sequence conflicti515 – 5151L → P in AAA17372. (PubMed:8114718)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS28876.1.
PIRiA56208.
RefSeqiNP_001157102.1. NM_001163630.1.
NP_001157103.1. NM_001163631.1.
NP_001157104.1. NM_001163632.1.
NP_033148.2. NM_009122.2.
UniGeneiMm.311655.

Genome annotation databases

EnsembliENSMUST00000129667; ENSMUSP00000116020; ENSMUSG00000023927.
ENSMUST00000133574; ENSMUSP00000120536; ENSMUSG00000023927.
ENSMUST00000144331; ENSMUSP00000116006; ENSMUSG00000023927.
ENSMUST00000152830; ENSMUSP00000119842; ENSMUSG00000023927.
ENSMUST00000169480; ENSMUSP00000128841; ENSMUSG00000023927.
ENSMUST00000176669; ENSMUSP00000134957; ENSMUSG00000023927.
GeneIDi20230.
KEGGimmu:20230.
UCSCiuc008czd.2. mouse.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS28876.1.
PIRi A56208.
RefSeqi NP_001157102.1. NM_001163630.1.
NP_001157103.1. NM_001163631.1.
NP_001157104.1. NM_001163632.1.
NP_033148.2. NM_009122.2.
UniGenei Mm.311655.

3D structure databases

ProteinModelPortali Q60611.
SMRi Q60611. Positions 71-171, 179-250, 370-452, 486-573, 647-705.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203077. 1 interaction.

PTM databases

PhosphoSitei Q60611.

Proteomic databases

MaxQBi Q60611.
PaxDbi Q60611.
PRIDEi Q60611.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000129667 ; ENSMUSP00000116020 ; ENSMUSG00000023927 .
ENSMUST00000133574 ; ENSMUSP00000120536 ; ENSMUSG00000023927 .
ENSMUST00000144331 ; ENSMUSP00000116006 ; ENSMUSG00000023927 .
ENSMUST00000152830 ; ENSMUSP00000119842 ; ENSMUSG00000023927 .
ENSMUST00000169480 ; ENSMUSP00000128841 ; ENSMUSG00000023927 .
ENSMUST00000176669 ; ENSMUSP00000134957 ; ENSMUSG00000023927 .
GeneIDi 20230.
KEGGi mmu:20230.
UCSCi uc008czd.2. mouse.

Organism-specific databases

CTDi 6304.
MGIi MGI:105084. Satb1.

Phylogenomic databases

eggNOGi NOG313826.
GeneTreei ENSGT00390000008096.
HOGENOMi HOG000004805.
HOVERGENi HBG054240.
InParanoidi Q60611.
OrthoDBi EOG7FBRH5.
PhylomeDBi Q60611.
TreeFami TF332714.

Enzyme and pathway databases

Reactomei REACT_224460. Apoptotic cleavage of cellular proteins.

Miscellaneous databases

ChiTaRSi SATB1. mouse.
NextBioi 297861.
PROi Q60611.
SOURCEi Search...

Gene expression databases

Bgeei Q60611.
CleanExi MM_SATB1.
ExpressionAtlasi Q60611. baseline and differential.
Genevestigatori Q60611.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
1.10.260.40. 2 hits.
InterProi IPR003350. CUT_dom.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR010982. Lambda_DNA-bd_dom.
[Graphical view ]
Pfami PF02376. CUT. 2 hits.
PF00046. Homeobox. 1 hit.
[Graphical view ]
SMARTi SM00389. HOX. 1 hit.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
SSF47413. SSF47413. 2 hits.
PROSITEi PS51042. CUT. 2 hits.
PS50071. HOMEOBOX_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiSATB1_MOUSE
AccessioniPrimary (citable) accession number: Q60611
Secondary accession number(s): Q91XB1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3