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Q01826

- SATB1_HUMAN

UniProt

Q01826 - SATB1_HUMAN

Protein

DNA-binding protein SATB1

Gene

SATB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    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.By similarity18 Publications

    Sites

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

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi361 – 44888CUT 1PROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi484 – 57188CUT 2PROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi645 – 70460HomeoboxPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. double-stranded DNA binding Source: ProtInc
    3. protein binding Source: IntAct
    4. sequence-specific DNA binding Source: InterPro
    5. sequence-specific DNA binding transcription factor activity Source: Ensembl

    GO - Biological processi

    1. activated T cell proliferation Source: Ensembl
    2. apoptotic process Source: Reactome
    3. CD4-positive, alpha-beta T cell differentiation Source: Ensembl
    4. CD8-positive, alpha-beta T cell differentiation Source: Ensembl
    5. cellular component disassembly involved in execution phase of apoptosis Source: Reactome
    6. chromatin organization Source: ProtInc
    7. chromatin remodeling Source: Ensembl
    8. epidermis development Source: Ensembl
    9. histone methylation Source: Ensembl
    10. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    11. reflex Source: Ensembl
    12. transcription, DNA-templated Source: UniProtKB-KW
    13. viral process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Repressor

    Keywords - Biological processi

    Host-virus interaction, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_107. 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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:10541. SATB1.

    Subcellular locationi

    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).

    GO - Cellular componenti

    1. nuclear heterochromatin Source: Ensembl
    2. nuclear matrix Source: UniProtKB-SubCell
    3. nucleoplasm Source: Reactome
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi29 – 291K → A: Loss of nuclear localization, cytoplasmic. 1 Publication
    Mutagenesisi32 – 321R → A: Loss of nuclear localization, cytoplasmic. 1 Publication
    Mutagenesisi34 – 341E → A: Normal nuclear localization. 1 Publication
    Mutagenesisi36 – 361N → A: Normal nuclear localization. 1 Publication
    Mutagenesisi136 – 1361K → A, Q or R: No acetylation. 2 Publications
    Mutagenesisi185 – 1851S → A: No phosphorylation. 1 Publication
    Mutagenesisi254 – 2541D → A: CASP6-resistant. 1 Publication
    Mutagenesisi373 – 3731S → A: Slightly reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi380 – 3801R → N: Reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi384 – 3841K → N: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi395 – 3951R → N: Reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi402 – 4021Q → A: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi403 – 4031G → A: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi406 – 4061S → A: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi410 – 4101R → N: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi411 – 4111K → R: Normal sumoylation. 1 Publication
    Mutagenesisi416 – 4161K → N: Impaired MAR-DNA-binding. 1 Publication
    Mutagenesisi427 – 4271R → N: Reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi442 – 4421R → N: Reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi451 – 4511S → A: Slightly reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi475 – 4751K → N: Reduced MAR-DNA-binding. 1 Publication
    Mutagenesisi486 – 4861K → R: Normal sumoylation. 1 Publication
    Mutagenesisi646 – 6461R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-648. 1 Publication
    Mutagenesisi648 – 6481R → A: Reduced interaction with matrix attachment region (MAR) DNA; when associated with A-646. 1 Publication
    Mutagenesisi693 – 6953FQN → AAA: Reduced interaction with matrix attachment region (MAR) DNA.
    Mutagenesisi720 – 7201K → R: Normal sumoylation. 1 Publication
    Mutagenesisi744 – 7441K → R: Loss of sumoylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA34951.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 763763DNA-binding protein SATB1PRO_0000202398Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei136 – 1361N6-acetyllysine1 Publication
    Modified residuei185 – 1851Phosphoserine1 Publication
    Cross-linki744 – 744Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

    Post-translational modificationi

    Sumoylated. Sumoylation promotes cleavage by caspases.2 Publications
    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.1 Publication
    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.

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ01826.
    PaxDbiQ01826.
    PRIDEiQ01826.

    PTM databases

    PhosphoSiteiQ01826.

    Miscellaneous databases

    PMAP-CutDBQ01826.

    Expressioni

    Tissue specificityi

    Expressed predominantly in thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ01826.
    BgeeiQ01826.
    CleanExiHS_SATB1.
    GenevestigatoriQ01826.

    Organism-specific databases

    HPAiCAB023814.

    Interactioni

    Subunit structurei

    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.By similarity13 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP6P552122EBI-743747,EBI-718729
    SUMO1P631652EBI-743747,EBI-80140

    Protein-protein interaction databases

    BioGridi112211. 28 interactions.
    DIPiDIP-48757N.
    IntActiQ01826. 9 interactions.
    MINTiMINT-1478608.
    STRINGi9606.ENSP00000341024.

    Structurei

    Secondary structure

    1
    763
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi72 – 8312
    Beta strandi92 – 10211
    Helixi107 – 1093
    Helixi110 – 1178
    Helixi122 – 1276
    Beta strandi129 – 1346
    Helixi142 – 1443
    Helixi153 – 1575
    Turni158 – 1636
    Beta strandi164 – 1696
    Helixi181 – 1833
    Helixi186 – 19611
    Turni197 – 1993
    Helixi202 – 2087
    Beta strandi209 – 2113
    Helixi213 – 2219
    Helixi230 – 24516
    Helixi375 – 38612
    Helixi390 – 3989
    Helixi402 – 41110
    Helixi415 – 4173
    Helixi420 – 43314
    Helixi437 – 45216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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[»]
    ProteinModelPortaliQ01826.
    SMRiQ01826. Positions 71-171, 179-250, 370-452, 486-573, 646-704.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ01826.

    Family & Domainsi

    Region

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

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi20 – 4021Nuclear localization signal1 PublicationAdd
    BLAST
    Motifi139 – 1435Protein interaction

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi591 – 60717Poly-GlnAdd
    BLAST
    Compositional biasi609 – 6146Poly-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.
    HOGENOMiHOG000004805.
    HOVERGENiHBG054240.
    OMAiSMNINAS.
    OrthoDBiEOG7FBRH5.
    PhylomeDBiQ01826.
    TreeFamiTF332714.

    Family and domain databases

    Gene3Di1.10.10.60. 1 hit.
    1.10.260.40. 2 hits.
    InterProiIPR003350. Hmoeo_CUT.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q01826-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA    50
    KMQGVPLKHS GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL 100
    VRKDMLFNQL IEMALLSLGY SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD 150
    ATVADMLQDV YHVVTLKIQL HSCPKLEDLP PEQWSHTTVR NALKDLLKDM 200
    NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY KHFKKTKDMM 250
    VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL 300
    PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP 350
    PPVSRSMNKP LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR 400
    TQGLLSEILR KEEDPKTASQ SLLVNLRAMQ NFLQLPEAER DRIYQDERER 450
    SLNAASAMGP APLISTPPSR PPQVKTATIA TERNGKPENN TMNINASIYD 500
    EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP ENRTLWENLS 550
    MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ 600
    QQQQQQQAPP PPQPQQQPQT GPRLPPRQPT VASPAESDEE NRQKTRPRTK 650
    ISVEALGILQ SFIQDVGLYP DEEAIQTLSA QLDLPKYTII KFFQNQRYYL 700
    KHHGKLKDNS GLEVDVAEYK EEELLKDLEE SVQDKNTNTL FSVKLEEELS 750
    VEGNTDINTD LKD 763
    Length:763
    Mass (Da):85,957
    Last modified:October 1, 1993 - v1
    Checksum:iD4FE09B09FB7683B
    GO
    Isoform 2 (identifier: Q01826-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:795
    Mass (Da):89,127
    Checksum:i4883C06CCD96D9FF
    GO

    Sequence cautioni

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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei592 – 5921I → IQSPSPTTLGKGESRGVFLP GLPTPAPWLGAAP in isoform 2. 1 PublicationVSP_038296

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS2631.1. [Q01826-1]
    CCDS56242.1. [Q01826-2]
    PIRiA43314.
    RefSeqiNP_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]
    UniGeneiHs.517717.

    Genome annotation databases

    EnsembliENST00000338745; ENSP00000341024; ENSG00000182568. [Q01826-1]
    ENST00000417717; ENSP00000399518; ENSG00000182568. [Q01826-2]
    ENST00000454909; ENSP00000399708; ENSG00000182568. [Q01826-1]
    GeneIDi6304.
    KEGGihsa:6304.
    UCSCiuc003cbh.3. human. [Q01826-1]
    uc003cbi.3. human. [Q01826-2]

    Polymorphism databases

    DMDMi417747.

    Keywords - Coding sequence diversityi

    Alternative splicing, Chromosomal rearrangement

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS2631.1. [Q01826-1 ]
    CCDS56242.1. [Q01826-2 ]
    PIRi A43314.
    RefSeqi NP_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 ]
    UniGenei Hs.517717.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YSE NMR - A 353-490 [» ]
    2L1P NMR - A 179-250 [» ]
    2O49 X-ray 2.00 A 368-452 [» ]
    2O4A X-ray 1.75 A 368-452 [» ]
    3NZL X-ray 1.20 A 179-250 [» ]
    3TUO X-ray 1.70 A/B/C/D 71-171 [» ]
    ProteinModelPortali Q01826.
    SMRi Q01826. Positions 71-171, 179-250, 370-452, 486-573, 646-704.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112211. 28 interactions.
    DIPi DIP-48757N.
    IntActi Q01826. 9 interactions.
    MINTi MINT-1478608.
    STRINGi 9606.ENSP00000341024.

    PTM databases

    PhosphoSitei Q01826.

    Polymorphism databases

    DMDMi 417747.

    Proteomic databases

    MaxQBi Q01826.
    PaxDbi Q01826.
    PRIDEi Q01826.

    Protocols and materials databases

    DNASUi 6304.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338745 ; ENSP00000341024 ; ENSG00000182568 . [Q01826-1 ]
    ENST00000417717 ; ENSP00000399518 ; ENSG00000182568 . [Q01826-2 ]
    ENST00000454909 ; ENSP00000399708 ; ENSG00000182568 . [Q01826-1 ]
    GeneIDi 6304.
    KEGGi hsa:6304.
    UCSCi uc003cbh.3. human. [Q01826-1 ]
    uc003cbi.3. human. [Q01826-2 ]

    Organism-specific databases

    CTDi 6304.
    GeneCardsi GC03M018364.
    HGNCi HGNC:10541. SATB1.
    HPAi CAB023814.
    MIMi 602075. gene.
    neXtProti NX_Q01826.
    PharmGKBi PA34951.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313826.
    HOGENOMi HOG000004805.
    HOVERGENi HBG054240.
    OMAi SMNINAS.
    OrthoDBi EOG7FBRH5.
    PhylomeDBi Q01826.
    TreeFami TF332714.

    Enzyme and pathway databases

    Reactomei REACT_107. Apoptotic cleavage of cellular proteins.

    Miscellaneous databases

    ChiTaRSi SATB1. human.
    EvolutionaryTracei Q01826.
    GeneWikii SATB1.
    GenomeRNAii 6304.
    NextBioi 24475.
    PMAP-CutDB Q01826.
    PROi Q01826.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q01826.
    Bgeei Q01826.
    CleanExi HS_SATB1.
    Genevestigatori Q01826.

    Family and domain databases

    Gene3Di 1.10.10.60. 1 hit.
    1.10.260.40. 2 hits.
    InterProi IPR003350. Hmoeo_CUT.
    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

    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.
      , 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.
      , 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. 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.

    Entry informationi

    Entry nameiSATB1_HUMAN
    AccessioniPrimary (citable) accession number: Q01826
    Secondary accession number(s): B3KXF1, C9JTR6, Q59EQ0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3