Q60611 (SATB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA-binding protein SATB1

Alternative name(s):
Special AT-rich sequence-binding protein 1

Gene names

Name:

Satb1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	764 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Nucleus › PML 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 process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Chromosomal rearrangement
Domain	Homeobox Repeat
Ligand	DNA-binding
Molecular function	Chromatin regulator Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	CD4-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 activated T cell proliferation Inferred from mutant phenotype Ref.12. 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 transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	PML body Inferred from electronic annotation. Source: UniProtKB-SubCell nuclear heterochromatin Inferred from direct assay Ref.10. Source: MGI nuclear matrix Inferred from direct assay Ref.11. Source: MGI
Molecular_function	DNA 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 764	764	DNA-binding protein SATB1		PRO_0000202399
Regions
	DNA binding	361 – 448	88	CUT 1
	DNA binding	484 – 571	88	CUT 2
	DNA binding	646 – 705	60	Homeobox
	Region	90 – 204	115	PDZ-like dimerization domain
	Region	224 – 278	55	Nuclear matrix targeting sequence (NMTS) By similarity
	Region	400 – 410	11	Matrix attachment region (MAR) DNA-binding By similarity
	Motif	20 – 40	21	Nuclear localization signal By similarity
	Motif	139 – 143	5	Protein interaction By similarity
	Motif	224 – 278	55	Nuclear matrix targeting sequence (NMTS)
	Compositional bias	591 – 607	17	Poly-Gln
	Compositional bias	608 – 617	10	Poly-Pro
Sites
	Binding site	390	1	Matrix attachment region (MAR) DNA By similarity
	Binding site	425	1	Matrix attachment region (MAR) DNA By similarity
	Site	254 – 255	2	Cleavage; by caspases
Amino acid modifications
	Modified residue	136	1	N6-acetyllysine By similarity
	Modified residue	185	1	Phosphoserine By similarity
	Cross-link	745		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Experimental info
	Sequence conflict	155	1	D → N in AAA17372. Ref.1
	Sequence conflict	515	1	L → P in AAA17372. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q60611 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 330ECCDBA8683B78	FASTA	764	85,880
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00119007.
PIR	A56208.
RefSeq	NP_001157102.1. NM_001163630.1. NP_001157103.1. NM_001163631.1. NP_001157104.1. NM_001163632.1. NP_033148.2. NM_009122.2.
UniGene	Mm.311655.
3D structure databases
ProteinModelPortal	Q60611.
SMR	Q60611. Positions 71-171, 179-250, 370-452, 486-573, 647-705.
ModBase	Search...
PTM databases
PhosphoSite	Q60611.
Proteomic databases
PaxDb	Q60611.
PRIDE	Q60611.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000133574; ENSMUSP00000120536; ENSMUSG00000023927. ENSMUST00000144331; ENSMUSP00000116006; ENSMUSG00000023927. ENSMUST00000152830; ENSMUSP00000119842; ENSMUSG00000023927. ENSMUST00000169480; ENSMUSP00000128841; ENSMUSG00000023927. ENSMUST00000176669; ENSMUSP00000134957; ENSMUSG00000023927.
GeneID	20230.
KEGG	mmu:20230.
Organism-specific databases
CTD	6304.
MGI	MGI:105084. Satb1.
Phylogenomic databases
eggNOG	NOG313826.
GeneTree	ENSGT00390000008096.
HOGENOM	HOG000004805.
HOVERGEN	HBG054240.
InParanoid	Q91XB1.
Gene expression databases
ArrayExpress	Q60611.
Bgee	Q60611.
CleanEx	MM_SATB1.
Genevestigator	Q60611.
GermOnline	ENSMUSG00000023927. Mus musculus.
Family and domain databases
Gene3D	1.10.10.60. 1 hit. 1.10.260.40. 2 hits.
InterPro	IPR003350. Hmoeo_CUT. IPR001356. Homeodomain. IPR009057. Homeodomain-like. IPR010982. Lambda_DNA-bd_dom. [Graphical view]
Pfam	PF02376. CUT. 2 hits. PF00046. Homeobox. 1 hit. [Graphical view]
SMART	SM00389. HOX. 1 hit. [Graphical view]
SUPFAM	SSF46689. Homeodomain_like. 1 hit. SSF47413. Lambda_like_DNA. 2 hits.
PROSITE	PS51042. CUT. 2 hits. PS00027. HOMEOBOX_1. False negative. PS50071. HOMEOBOX_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SATB1. mouse.
NextBio	297861.
SOURCE	Search...

Entry information

Entry name

SATB1_MOUSE

Accession

Primary (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 3, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program