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Q01826 (SATB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length763 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Crucial silencing factor contributing to the initiation of X inactivation mediated by Xist RNA that occurs during embryogenesis and in lymphoma By similarity. 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 (e.g. PML at the MHC-I locus) 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. 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. Interacts with the unique region (UR) of cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide a unique chromatin context which seems preferentially targeted by the HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1-mediated repression of IL2 and IL2RA (interleukin) in T-cells by binding to the same domain than HDAC1. Delineates specific epigenetic modifications at target gene loci, directly up-regulating metastasis-associated genes while down-regulating tumor-suppressor genes. Reprograms chromatin organization and the transcription profiles of breast tumors to promote growth and metastasis. Ref.1 Ref.7 Ref.8 Ref.9 Ref.11 Ref.13 Ref.15 Ref.16 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25 Ref.28 Ref.30 Ref.31 Ref.32 Ref.33

Subunit structure

Interacts with CUX1 (via DNA-binding domains); the interaction inhibits the attachment of both proteins to DNA 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 PCAF. Interacts with sumoylated PML, HDAC1 and HIV-1 Tat via the PDZ-like dimerization domain. Interacts also with DYNLT3 and POLR2J2. Binds to EP300. Ref.9 Ref.11 Ref.12 Ref.14 Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.29 Ref.32

Subcellular location

Nucleus matrix. 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). Ref.1 Ref.10 Ref.15 Ref.17 Ref.19 Ref.20 Ref.27

Tissue specificity

Expressed predominantly in thymus. Ref.1

Post-translational modification

Sumoylated. Sumoylation promotes cleavage by caspases. Ref.18 Ref.27

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. Ref.23

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.10 Ref.11 Ref.22 Ref.27

Sequence similarities

Belongs to the CUT homeobox family.

Contains 2 CUT DNA-binding domains.

Contains 1 homeobox DNA-binding domain.

Sequence caution

The sequence BAD92998.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DomainHomeobox
Repeat
   LigandDNA-binding
   Molecular functionChromatin regulator
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processCD4-positive, alpha-beta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

CD8-positive, alpha-beta T cell differentiation

Inferred from electronic annotation. Source: Ensembl

activated T cell proliferation

Inferred from electronic annotation. Source: Ensembl

apoptotic process

Traceable author statement. Source: Reactome

cellular component disassembly involved in execution phase of apoptosis

Traceable author statement. Source: Reactome

chromatin organization

Traceable author statement Ref.1. Source: ProtInc

chromatin remodeling

Inferred from electronic annotation. Source: Ensembl

epidermis development

Inferred from electronic annotation. Source: Ensembl

histone methylation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.19. Source: MGI

reflex

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentPML body

Inferred from direct assay Ref.27. Source: UniProtKB

nuclear heterochromatin

Inferred from electronic annotation. Source: Ensembl

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.27. Source: UniProtKB

   Molecular_functionchromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Traceable author statement Ref.1. Source: ProtInc

protein binding

Inferred from physical interaction Ref.27. Source: IntAct

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CASP6P552122EBI-743747,EBI-718729
SUMO1P631652EBI-743747,EBI-80140

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q01826-1)

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: Q01826-2)

The sequence of this isoform differs from the canonical sequence as follows:
     592-592: I → IQSPSPTTLGKGESRGVFLPGLPTPAPWLGAAP

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 763763DNA-binding protein SATB1
PRO_0000202398

Regions

DNA binding361 – 44888CUT 1
DNA binding484 – 57188CUT 2
DNA binding645 – 70460Homeobox
Region90 – 204115PDZ-like dimerization domain
Region224 – 27855Nuclear matrix targeting sequence (NMTS)
Region400 – 41011Matrix attachment region (MAR) DNA-binding
Motif20 – 4021Nuclear localization signal Ref.17
Motif139 – 1435Protein interaction
Compositional bias591 – 60717Poly-Gln
Compositional bias609 – 6146Poly-Pro

Sites

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

Amino acid modifications

Modified residue1361N6-acetyllysine Ref.23
Modified residue1851Phosphoserine Ref.23
Cross-link744Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.27

Natural variations

Alternative sequence5921I → IQSPSPTTLGKGESRGVFLP GLPTPAPWLGAAP in isoform 2.
VSP_038296

Experimental info

Mutagenesis291K → A: Loss of nuclear localization, cytoplasmic. Ref.17
Mutagenesis321R → A: Loss of nuclear localization, cytoplasmic. Ref.17
Mutagenesis341E → A: Normal nuclear localization. Ref.17
Mutagenesis361N → A: Normal nuclear localization. Ref.17
Mutagenesis1361K → A, Q or R: No acetylation. Ref.23 Ref.32
Mutagenesis1851S → A: No phosphorylation. Ref.23
Mutagenesis2541D → A: CASP6-resistant. Ref.11
Mutagenesis3731S → A: Slightly reduced MAR-DNA-binding. Ref.34
Mutagenesis3801R → N: Reduced MAR-DNA-binding. Ref.34
Mutagenesis3841K → N: Impaired MAR-DNA-binding. Ref.34
Mutagenesis3951R → N: Reduced MAR-DNA-binding. Ref.34
Mutagenesis4021Q → A: Impaired MAR-DNA-binding. Ref.35
Mutagenesis4031G → A: Impaired MAR-DNA-binding. Ref.35
Mutagenesis4061S → A: Impaired MAR-DNA-binding. Ref.34
Mutagenesis4101R → N: Impaired MAR-DNA-binding. Ref.34
Mutagenesis4111K → R: Normal sumoylation. Ref.27
Mutagenesis4161K → N: Impaired MAR-DNA-binding. Ref.34
Mutagenesis4271R → N: Reduced MAR-DNA-binding. Ref.34
Mutagenesis4421R → N: Reduced MAR-DNA-binding. Ref.34
Mutagenesis4511S → A: Slightly reduced MAR-DNA-binding. Ref.34
Mutagenesis4751K → N: Reduced MAR-DNA-binding. Ref.34
Mutagenesis4861K → R: Normal sumoylation. Ref.27
Mutagenesis6461R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648. Ref.7
Mutagenesis6481R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646. Ref.7
Mutagenesis693 – 6953FQN → AAA: Reduced interaction with matrix attachment region (MAR) DNA. Ref.7
Mutagenesis7201K → R: Normal sumoylation. Ref.27
Mutagenesis7441K → R: Loss of sumoylation. Ref.27

Secondary structure

.......................................... 763
Helix Strand Turn

Details...

Sequences

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

Last modified October 1, 1993. Version 1.
Checksum: D4FE09B09FB7683B

FASTA76385,957
        10         20         30         40         50         60 
MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA 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 APLISTPPSR PPQVKTATIA 

       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 
QQQQQQQAPP PPQPQQQPQT GPRLPPRQPT VASPAESDEE NRQKTRPRTK ISVEALGILQ 

       670        680        690        700        710        720 
SFIQDVGLYP DEEAIQTLSA QLDLPKYTII KFFQNQRYYL KHHGKLKDNS GLEVDVAEYK 

       730        740        750        760 
EEELLKDLEE SVQDKNTNTL FSVKLEEELS VEGNTDINTD LKD 

« Hide

Isoform 2 [UniParc].

Checksum: 4883C06CCD96D9FF
Show »

FASTA79589,127

References

« Hide 'large scale' references
[1]"A tissue-specific MAR/SAR DNA-binding protein with unusual binding site recognition."
Dickinson L.A., Joh T., Kohwi Y., Kohwi-Shigematsu T.
Cell 70:631-645(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Hippocampus.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno F.R.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Brain.
[4]"The DNA sequence, annotation and analysis of human chromosome 3."
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. expand/collapse author list , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1).
Tissue: Lung.
[7]"An atypical homeodomain in SATB1 promotes specific recognition of the key structural element in a matrix attachment region."
Dickinson L.A., Dickinson C.D., Kohwi-Shigematsu T.
J. Biol. Chem. 272:11463-11470(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF ARG-646; ARG-648 AND 693-PHE--ASN-695.
[8]"The genomic sequences bound to special AT-rich sequence-binding protein 1 (SATB1) in vivo in Jurkat T cells are tightly associated with the nuclear matrix at the bases of the chromatin loops."
de Belle I., Cai S., Kohwi-Shigematsu T.
J. Cell Biol. 141:335-348(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[9]"The gammaPE complex contains both SATB1 and HOXB2 and has positive and negative roles in human gamma-globin gene regulation."
Case S.S., Huber P., Lloyd J.A.
DNA Cell Biol. 18:805-817(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE GAMMA-GLOBIN PROMOTER COMPLEX, IDENTIFICATION IN THE ENHANCER BINDING FACTOR COMPLEX.
[10]"The fate of the nuclear matrix-associated-region-binding protein SATB1 during apoptosis."
Gotzmann J., Meissner M., Gerner C.
Cell Death Differ. 7:425-438(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CLEAVAGE BY CASPASES, SUBCELLULAR LOCATION.
[11]"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: FUNCTION, MUTAGENESIS OF ASP-254, SUBUNIT, CLEAVAGE BY CASPASE-6.
[12]"The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with a novel variant of DNA-directed RNA polymerase II, subunit 11."
Durrin L.K., Krontiris T.G.
Genomics 79:809-817(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH POLR2J2.
[13]"SATB1 targets chromatin remodelling to regulate genes over long distances."
Yasui D., Miyano M., Cai S., Varga-Weisz P., Kohwi-Shigematsu T.
Nature 419:641-645(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"SATB1 makes a complex with p300 and represses gp91(phox) promoter activity."
Fujii Y., Kumatori A., Nakamura M.
Microbiol. Immunol. 47:803-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH EP300.
[15]"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.
[16]"SATB1 family protein expressed during early erythroid differentiation modifies globin gene expression."
Wen J., Huang S., Rogers H., Dickinson L.A., Kohwi-Shigematsu T., Noguchi C.T.
Blood 105:3330-3339(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"A nuclear targeting determinant for SATB1, a genome organizer in the T cell lineage."
Nakayama Y., Mian I.S., Kohwi-Shigematsu T., Ogawa T.
Cell Cycle 4:1099-1106(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-29; ARG-32; GLU-34 AND ASN-36, NUCLEAR LOCALIZATION SIGNAL.
[18]"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
Gocke C.B., Yu H., Kang J.
J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION.
[19]"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.
[20]"Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional modulator in a dynein-independent pathway."
Yeh T.-Y., Chuang J.-Z., Sung C.-H.
J. Cell Sci. 118:3431-3443(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DYNLT3, SUBCELLULAR LOCATION.
[21]"Displacement of SATB1-bound histone deacetylase 1 corepressor by the human immunodeficiency virus type 1 transactivator induces expression of interleukin-2 and its receptor in T cells."
Kumar P.P., Purbey P.K., Ravi D.S., Mitra D., Galande S.
Mol. Cell. Biol. 25:1620-1633(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH HIV-1 TAT AND HDAC1.
[22]"The behavior of SATB1, a MAR-binding protein, in response to apoptosis stimulation."
Sun Y., Wang T., Su Y., Yin Y., Xu S., Ma C., Han X.
Cell Biol. Int. 30:244-247(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CLEAVAGE BY CASPASE-3.
[23]"Phosphorylation of SATB1, a global gene regulator, acts as a molecular switch regulating its transcriptional activity in vivo."
Kumar P.P., Purbey P.K., Sinha C.K., Notani D., Limaye A., Jayani R.S., Galande S.
Mol. Cell 22:231-243(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HDAC1 AND PCAF, MUTAGENESIS OF LYS-136 AND SER-185, ACETYLATION AT LYS-136, PHOSPHORYLATION AT SER-185.
[24]"SATB1-binding sequences and Alu-like motifs define a unique chromatin context in the vicinity of human immunodeficiency virus type 1 integration sites."
Kumar P.P., Mehta S., Purbey P.K., Notani D., Jayani R.S., Purohit H.J., Raje D.V., Ravi D.S., Bhonde R.R., Mitra D., Galande S.
J. Virol. 81:5617-5627(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[25]"Functional interaction between PML and SATB1 regulates chromatin-loop architecture and transcription of the MHC class I locus."
Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A., Galande S.
Nat. Cell Biol. 9:45-56(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PML.
[26]"Cellular homeoproteins, SATB1 and CDP, bind to the unique region between the human cytomegalovirus UL127 and major immediate-early genes."
Lee J., Klase Z., Gao X., Caldwell J.S., Stinski M.F., Kashanchi F., Chao S.-H.
Virology 366:117-125(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CYTOMEGALOVIRUS UNIQUE REGION.
[27]"SUMO conjugation to the matrix attachment region-binding protein, special AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic nuclear bodies where it undergoes caspase cleavage."
Tan J.-A.T., Sun Y., Song J., Chen Y., Krontiris T.G., Durrin L.K.
J. Biol. Chem. 283:18124-18134(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-744, MUTAGENESIS OF LYS-411; LYS-486; LYS-720 AND LYS-744, SUBCELLULAR LOCATION, CLEAVAGE BY CASPASE-6.
[28]"SATB1 reprogrammes gene expression to promote breast tumour growth and metastasis."
Han H.-J., Russo J., Kohwi Y., Kohwi-Shigematsu T.
Nature 452:187-193(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ROLE IN BREAST TUMOR GROWTH AND METASTASIS.
[29]"PDZ domain-mediated dimerization and homeodomain-directed specificity are required for high-affinity DNA binding by SATB1."
Purbey P.K., Singh S., Kumar P.P., Mehta S., Ganesh K.N., Mitra D., Galande S.
Nucleic Acids Res. 36:2107-2122(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT, INTERACTION WITH DNA AND NUCLEAR MATRIX.
[30]"SATB1 regulates beta-like globin genes through matrix related nuclear relocation of the cluster."
Gong H., Wang Z., Zhao G.-W., Lv X., Wei G.-H., Wang L., Liu D.-P., Liang C.-C.
Biochem. Biophys. Res. Commun. 383:11-15(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[31]"SATB1 binds an intronic MAR sequence in human PI3kgamma in vitro."
Cai R., Xu W., Dai B., Cai X., Xu R., Lu J.
Mol. Biol. Rep. 37:1461-1465(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[32]"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, MUTAGENESIS OF LYS-136, INTERACTION WITH CTBP1.
[33]"Inter-MAR association contributes to transcriptionally active looping events in human beta-globin gene cluster."
Wang L., Di L.-J., Lv X., Zheng W., Xue Z., Guo Z.-C., Liu D.-P., Liang C.-C.
PLoS ONE 4:E4629-E4629(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[34]"Solution structure and DNA-binding mode of the matrix attachment region-binding domain of the transcription factor SATB1 that regulates the T-cell maturation."
Yamaguchi H., Tateno M., Yamasaki K.
J. Biol. Chem. 281:5319-5327(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 353-490 IN COMPLEX WITH MAR DNA, MUTAGENESIS OF SER-373; ARG-380; LYS-384; ARG-395; SER-406; ARG-410; LYS-416; ARG-427; ARG-442; SER-451 AND LYS-475.
[35]"Structural basis for recognition of the matrix attachment region of DNA by transcription factor SATB1."
Yamasaki K., Akiba T., Yamasaki T., Harata K.
Nucleic Acids Res. 35:5073-5084(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 368-452 IN COMPLEX WITH MAR DNA, MUTAGENESIS OF GLN-402 AND GLY-403.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M97287 mRNA. Translation: AAA60304.1.
AK127242 mRNA. Translation: BAG54463.1.
AB209761 mRNA. Translation: BAD92998.1. Different initiation.
AC139618 Genomic DNA. No translation available.
AC144521 Genomic DNA. No translation available.
CH471055 Genomic DNA. Translation: EAW64291.1.
BC001744 mRNA. Translation: AAH01744.1.
CCDSCCDS2631.1. [Q01826-1]
CCDS56242.1. [Q01826-2]
PIRA43314.
RefSeqNP_001124482.1. NM_001131010.2. [Q01826-1]
NP_001182399.1. NM_001195470.1. [Q01826-2]
NP_002962.1. NM_002971.4. [Q01826-1]
XP_006713343.1. XM_006713280.1. [Q01826-1]
UniGeneHs.517717.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YSENMR-A353-490[»]
2L1PNMR-A179-250[»]
2O49X-ray2.00A368-452[»]
2O4AX-ray1.75A368-452[»]
3NZLX-ray1.20A179-250[»]
3TUOX-ray1.70A/B/C/D71-171[»]
ProteinModelPortalQ01826.
SMRQ01826. Positions 71-171, 179-250, 370-452, 486-573, 646-704.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112211. 28 interactions.
DIPDIP-48757N.
IntActQ01826. 9 interactions.
MINTMINT-1478608.
STRING9606.ENSP00000341024.

PTM databases

PhosphoSiteQ01826.

Polymorphism databases

DMDM417747.

Proteomic databases

MaxQBQ01826.
PaxDbQ01826.
PRIDEQ01826.

Protocols and materials databases

DNASU6304.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000338745; ENSP00000341024; ENSG00000182568. [Q01826-1]
ENST00000417717; ENSP00000399518; ENSG00000182568. [Q01826-2]
ENST00000454909; ENSP00000399708; ENSG00000182568. [Q01826-1]
GeneID6304.
KEGGhsa:6304.
UCSCuc003cbh.3. human. [Q01826-1]
uc003cbi.3. human. [Q01826-2]

Organism-specific databases

CTD6304.
GeneCardsGC03M018364.
HGNCHGNC:10541. SATB1.
HPACAB023814.
MIM602075. gene.
neXtProtNX_Q01826.
PharmGKBPA34951.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313826.
HOGENOMHOG000004805.
HOVERGENHBG054240.
OMASMNINAS.
OrthoDBEOG7FBRH5.
PhylomeDBQ01826.
TreeFamTF332714.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressQ01826.
BgeeQ01826.
CleanExHS_SATB1.
GenevestigatorQ01826.

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. human.
EvolutionaryTraceQ01826.
GeneWikiSATB1.
GenomeRNAi6304.
NextBio24475.
PMAP-CutDBQ01826.
PROQ01826.
SOURCESearch...

Entry information

Entry nameSATB1_HUMAN
AccessionPrimary (citable) accession number: Q01826
Secondary accession number(s): B3KXF1, C9JTR6, Q59EQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: July 9, 2014
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM