SATB1_MOUSE
ID SATB1_MOUSE Reviewed; 764 AA.
AC Q60611; Q91XB1;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=DNA-binding protein SATB1;
DE AltName: Full=Special AT-rich sequence-binding protein 1;
GN Name=Satb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=8114718; DOI=10.1128/mcb.14.3.1852-1860.1994;
RA Nakagomi K., Kohwi Y., Dickinson L.A., Kohwi-Shigematsu T.;
RT "A novel DNA-binding motif in the nuclear matrix attachment DNA-binding
RT protein SATB1.";
RL Mol. Cell. Biol. 14:1852-1860(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus, and Visual cortex;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J.,
RA Wiemann S., Schick M., Korn B.;
RT "Cloning of mouse full open reading frames in Gateway(R) system entry
RT vector (pDONR201).";
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Salivary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 255-259, FUNCTION, DIMERIZATION, AND CLEAVAGE BY CASP6.
RX PubMed=11463840; DOI=10.1128/mcb.21.16.5591-5604.2001;
RA Galande S., Dickinson L.A., Mian I.S., Sikorska M., Kohwi-Shigematsu T.;
RT "SATB1 cleavage by caspase 6 disrupts PDZ domain-mediated dimerization,
RT causing detachment from chromatin early in T-cell apoptosis.";
RL Mol. Cell. Biol. 21:5591-5604(2001).
RN [7]
RP FUNCTION.
RX PubMed=9271405; DOI=10.1128/mcb.17.9.5275;
RA Liu J., Bramblett D., Zhu Q., Lozano M., Kobayashi R., Ross S.R.,
RA Dudley J.P.;
RT "The matrix attachment region-binding protein SATB1 participates in
RT negative regulation of tissue-specific gene expression.";
RL Mol. Cell. Biol. 17:5275-5287(1997).
RN [8]
RP INTERACTION WITH CUX1.
RX PubMed=10373541; DOI=10.1128/mcb.19.7.4918;
RA Liu J., Barnett A., Neufeld E.J., Dudley J.P.;
RT "Homeoproteins CDP and SATB1 interact: potential for tissue-specific
RT regulation.";
RL Mol. Cell. Biol. 19:4918-4926(1999).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=10716941;
RA Alvarez J.D., Yasui D.H., Niida H., Joh T., Loh D.Y., Kohwi-Shigematsu T.;
RT "The MAR-binding protein SATB1 orchestrates temporal and spatial expression
RT of multiple genes during T-cell development.";
RL Genes Dev. 14:521-535(2000).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12692553; DOI=10.1038/ng1146;
RA Cai S., Han H.-J., Kohwi-Shigematsu T.;
RT "Tissue-specific nuclear architecture and gene expression regulated by
RT SATB1.";
RL Nat. Genet. 34:42-51(2003).
RN [11]
RP SUBCELLULAR LOCATION, AND NUCLEAR MATRIX TARGETING SEQUENCE.
RX PubMed=15851481; DOI=10.1074/jbc.m414076200;
RA Seo J., Lozano M.M., Dudley J.P.;
RT "Nuclear matrix binding regulates SATB1-mediated transcriptional
RT repression.";
RL J. Biol. Chem. 280:24600-24609(2005).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=15814699; DOI=10.4049/jimmunol.174.8.4745;
RA Nie H., Maika S.D., Tucker P.W., Gottlieb P.D.;
RT "A role for SATB1, a nuclear matrix association region-binding protein, in
RT the development of CD8SP thymocytes and peripheral T lymphocytes.";
RL J. Immunol. 174:4745-4752(2005).
RN [13]
RP FUNCTION.
RX PubMed=17057718; DOI=10.1038/ng1913;
RA Cai S., Lee C.C., Kohwi-Shigematsu T.;
RT "SATB1 packages densely looped, transcriptionally active chromatin for
RT coordinated expression of cytokine genes.";
RL Nat. Genet. 38:1278-1288(2006).
RN [14]
RP FUNCTION.
RX PubMed=18722016; DOI=10.1016/j.molimm.2008.07.007;
RA Nie H., Yao X., Maika S.D., Tucker P.W.;
RT "SATB1 is required for CD8 coreceptor reversal.";
RL Mol. Immunol. 46:207-211(2008).
RN [15]
RP FUNCTION.
RX PubMed=19386260; DOI=10.1016/j.devcel.2009.03.006;
RA Agrelo R., Souabni A., Novatchkova M., Haslinger C., Leeb M.,
RA Komnenovic V., Kishimoto H., Gresh L., Kohwi-Shigematsu T., Kenner L.,
RA Wutz A.;
RT "SATB1 defines the developmental context for gene silencing by Xist in
RT lymphoma and embryonic cells.";
RL Dev. Cell 16:507-516(2009).
RN [16]
RP FUNCTION, AND INTERACTION WITH CTBP1.
RX PubMed=19103759; DOI=10.1128/mcb.00822-08;
RA Purbey P.K., Singh S., Notani D., Kumar P.P., Limaye A.S., Galande S.;
RT "Acetylation-dependent interaction of SATB1 and CtBP1 mediates
RT transcriptional repression by SATB1.";
RL Mol. Cell. Biol. 29:1321-1337(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-638, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [18]
RP FUNCTION, TISSUE SPECIFICITY, INDUCTION BY DIFFERENTIATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=26305964; DOI=10.1073/pnas.1513780112;
RA Wang F., Tidei J.J., Polich E.D., Gao Y., Zhao H., Perrone-Bizzozero N.I.,
RA Guo W., Zhao X.;
RT "Positive feedback between RNA-binding protein HuD and transcription factor
RT SATB1 promotes neurogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:E4995-E5004(2015).
CC -!- FUNCTION: Required for the switching of fetal globin species, and
CC beta- and gamma-globin genes regulation during erythroid
CC differentiation. Plays a role in chromatin organization and nuclear
CC architecture during apoptosis (By similarity). Crucial silencing factor
CC contributing to the initiation of X inactivation mediated by Xist RNA
CC that occurs during embryogenesis and in lymphoma. Binds to DNA at
CC special AT-rich sequences, the consensus SATB1-binding sequence (CSBS),
CC at nuclear matrix- or scaffold-associated regions. Thought to recognize
CC the sugar-phosphate structure of double-stranded DNA. Transcriptional
CC repressor controlling nuclear and viral gene expression in a
CC phosphorylated and acetylated status-dependent manner, by binding to
CC matrix attachment regions (MARs) of DNA and inducing a local chromatin-
CC loop remodeling. Acts as a docking site for several chromatin
CC remodeling enzymes and also by recruiting corepressors (HDACs) or
CC coactivators (HATs) directly to promoters and enhancers. Modulates
CC genes that are essential in the maturation of the immune T-cell CD8SP
CC from thymocytes. Promotes neuronal differentiation of neural
CC stem/progenitor cells in the adult subventricular zone, possibly by
CC positively regulating the expression of NEUROD1 (PubMed:26305964).
CC {ECO:0000250, ECO:0000269|PubMed:10716941, ECO:0000269|PubMed:11463840,
CC ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:15814699,
CC ECO:0000269|PubMed:17057718, ECO:0000269|PubMed:18722016,
CC ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19386260,
CC ECO:0000269|PubMed:26305964, ECO:0000269|PubMed:9271405}.
CC -!- SUBUNIT: Interacts with PCAF. Interacts with sumoylated PML and HDAC1
CC Tat via the ULD domain. Interacts also with DYNLT3 and POLR2J2. Binds
CC to EP300 (By similarity). Homodimer. Part of the nuclear protein
CC complex gamma-globin promoter and enhancer binding factor (gamma-PE)
CC composed at least of SATB1 and HOXB2. Interaction with CtBP1 when not
CC acetylated stabalizes attachment to DNA and promotes transcription
CC repression. Interacts with CUX1 (via DNA-binding domains); the
CC interaction inhibits the attachment of both proteins to DNA.
CC {ECO:0000250, ECO:0000269|PubMed:10373541,
CC ECO:0000269|PubMed:19103759}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Nucleus, PML body. Note=Organized into a
CC cage-like network anchoring loops of heterochromatin and tethering
CC specialized DNA sequences. When sumoylated, localized in promyelocytic
CC leukemia nuclear bodies (PML NBs) (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the subventricular zone, rostral
CC migratory stream and in the olfactory bulb (at protein level)
CC (PubMed:26305964). Mainly expressed in thymus, spleen, and lymph nodes
CC with a lower level observed in the brain (PubMed:15814699).
CC {ECO:0000269|PubMed:15814699, ECO:0000269|PubMed:26305964}.
CC -!- INDUCTION: Up-regulated during adult neuronal stem cell
CC differentiation. {ECO:0000269|PubMed:26305964}.
CC -!- PTM: Sumoylated. Sumoylation promotes cleavage by caspases.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylated by PKC. Acetylated by PCAF. Phosphorylated form
CC interacts with HDAC1, but unphosphorylated form interacts with PCAF.
CC DNA binding properties are activated by phosphorylation and inactivated
CC by acetylation. In opposition, gene expression is down-regulated by
CC phosphorylation but up-regulated by acetylation (By similarity).
CC {ECO:0000250}.
CC -!- PTM: Cleaved at Asp-254 by caspase-3 and caspase-6 during T-cell
CC apoptosis in thymus and during B-cell stimulation. The cleaved forms
CC cannot dimerize and lose transcription regulation function because of
CC impaired DNA and chromatin association. {ECO:0000269|PubMed:11463840}.
CC -!- DISRUPTION PHENOTYPE: Mice are small in size, have disproportionately
CC small thymi and spleens, and die at 3 weeks of age. Multiple defects in
CC T-cell development are observed, including interrupted thymocytes
CC differentiation and abnormal T-cell transcriptome. RNAi-mediated
CC knockdown in neural stem/progenitor cells in the adult subventricular
CC zone impairs early neuronal differentiation (PubMed:26305964).
CC {ECO:0000269|PubMed:10716941, ECO:0000269|PubMed:15814699,
CC ECO:0000269|PubMed:26305964}.
CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}.
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DR EMBL; U05252; AAA17372.1; -; mRNA.
DR EMBL; AK088563; BAC40427.1; -; mRNA.
DR EMBL; AK158518; BAE34542.1; -; mRNA.
DR EMBL; CT010371; CAJ18578.1; -; mRNA.
DR EMBL; BC011132; AAH11132.1; -; mRNA.
DR EMBL; CH466559; EDL23652.1; -; Genomic_DNA.
DR CCDS; CCDS28876.1; -.
DR PIR; A56208; A56208.
DR RefSeq; NP_001157102.1; NM_001163630.1.
DR RefSeq; NP_001157103.1; NM_001163631.1.
DR RefSeq; NP_001157104.1; NM_001163632.1.
DR RefSeq; NP_033148.2; NM_009122.2.
DR RefSeq; XP_017172852.1; XM_017317363.1.
DR RefSeq; XP_017172853.1; XM_017317364.1.
DR PDB; 4Q2J; X-ray; 2.60 A; A/B/C/D=71-246.
DR PDBsum; 4Q2J; -.
DR AlphaFoldDB; Q60611; -.
DR BMRB; Q60611; -.
DR SMR; Q60611; -.
DR BioGRID; 203077; 7.
DR IntAct; Q60611; 1.
DR MINT; Q60611; -.
DR STRING; 10090.ENSMUSP00000116006; -.
DR iPTMnet; Q60611; -.
DR PhosphoSitePlus; Q60611; -.
DR EPD; Q60611; -.
DR jPOST; Q60611; -.
DR MaxQB; Q60611; -.
DR PaxDb; Q60611; -.
DR PRIDE; Q60611; -.
DR ProteomicsDB; 256706; -.
DR Antibodypedia; 11251; 520 antibodies from 44 providers.
DR DNASU; 20230; -.
DR Ensembl; ENSMUST00000129667; ENSMUSP00000116020; ENSMUSG00000023927.
DR Ensembl; ENSMUST00000133574; ENSMUSP00000120536; ENSMUSG00000023927.
DR Ensembl; ENSMUST00000144331; ENSMUSP00000116006; ENSMUSG00000023927.
DR Ensembl; ENSMUST00000152830; ENSMUSP00000119842; ENSMUSG00000023927.
DR Ensembl; ENSMUST00000169480; ENSMUSP00000128841; ENSMUSG00000023927.
DR Ensembl; ENSMUST00000176669; ENSMUSP00000134957; ENSMUSG00000023927.
DR GeneID; 20230; -.
DR KEGG; mmu:20230; -.
DR UCSC; uc008czd.2; mouse.
DR CTD; 6304; -.
DR MGI; MGI:105084; Satb1.
DR VEuPathDB; HostDB:ENSMUSG00000023927; -.
DR eggNOG; KOG3755; Eukaryota.
DR GeneTree; ENSGT00390000008096; -.
DR HOGENOM; CLU_012559_1_0_1; -.
DR InParanoid; Q60611; -.
DR OMA; DVADYKD; -.
DR OrthoDB; 204499at2759; -.
DR PhylomeDB; Q60611; -.
DR TreeFam; TF332714; -.
DR Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
DR Reactome; R-MMU-4551638; SUMOylation of chromatin organization proteins.
DR BioGRID-ORCS; 20230; 4 hits in 77 CRISPR screens.
DR ChiTaRS; Satb1; mouse.
DR PRO; PR:Q60611; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q60611; protein.
DR Bgee; ENSMUSG00000023927; Expressed in thymus and 291 other tissues.
DR ExpressionAtlas; Q60611; baseline and differential.
DR Genevisible; Q60611; MM.
DR GO; GO:0000785; C:chromatin; IDA:MGI.
DR GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0016363; C:nuclear matrix; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0016605; C:PML body; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:ARUK-UCL.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0050798; P:activated T cell proliferation; IMP:MGI.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0043374; P:CD8-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0006325; P:chromatin organization; IDA:MGI.
DR GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR GO; GO:0008544; P:epidermis development; IMP:MGI.
DR GO; GO:0016571; P:histone methylation; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0060004; P:reflex; IMP:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
DR GO; GO:0042110; P:T cell activation; IMP:MGI.
DR CDD; cd00086; homeodomain; 1.
DR CDD; cd11585; SATB1_N; 1.
DR Gene3D; 1.10.260.40; -; 2.
DR Gene3D; 1.10.260.70; -; 1.
DR Gene3D; 3.10.20.710; -; 1.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR032355; CUTL.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR039673; SATB1/SATB2.
DR InterPro; IPR038216; SATB_CUTL_sf.
DR InterPro; IPR038224; SATB_ULD_sf.
DR InterPro; IPR032392; ULD.
DR PANTHER; PTHR15116; PTHR15116; 1.
DR Pfam; PF02376; CUT; 2.
DR Pfam; PF16557; CUTL; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16534; ULD; 1.
DR SMART; SM01109; CUT; 2.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 2.
DR PROSITE; PS51042; CUT; 2.
DR PROSITE; PS51983; CUTL; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51982; ULD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromatin regulator; Chromosomal rearrangement;
KW Direct protein sequencing; DNA-binding; Homeobox; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..764
FT /note="DNA-binding protein SATB1"
FT /id="PRO_0000202399"
FT DOMAIN 71..172
FT /note="ULD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01326"
FT DOMAIN 175..248
FT /note="CUTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01327"
FT DNA_BIND 361..448
FT /note="CUT 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 484..571
FT /note="CUT 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374"
FT DNA_BIND 646..705
FT /note="Homeobox"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT REGION 1..56
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..278
FT /note="Nuclear matrix targeting sequence (NMTS)"
FT /evidence="ECO:0000250"
FT REGION 266..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 450..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 591..650
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 20..40
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000250"
FT MOTIF 139..143
FT /note="Protein interaction"
FT /evidence="ECO:0000250"
FT MOTIF 224..278
FT /note="Nuclear matrix targeting sequence (NMTS)"
FT COMPBIAS 266..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..626
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 390
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_part="matrix attachment region (MAR) of DNA"
FT /evidence="ECO:0000250"
FT BINDING 400..410
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_part="matrix attachment region (MAR) of DNA"
FT /evidence="ECO:0000250"
FT BINDING 425
FT /ligand="DNA"
FT /ligand_id="ChEBI:CHEBI:16991"
FT /ligand_part="matrix attachment region (MAR) of DNA"
FT /evidence="ECO:0000250"
FT SITE 254..255
FT /note="Cleavage; by caspases"
FT MOD_RES 136
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q01826"
FT MOD_RES 185
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q01826"
FT MOD_RES 638
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 51
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q01826"
FT CROSSLNK 745
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250"
FT CONFLICT 155
FT /note="D -> N (in Ref. 1; AAA17372)"
FT /evidence="ECO:0000305"
FT CONFLICT 515
FT /note="L -> P (in Ref. 1; AAA17372)"
FT /evidence="ECO:0000305"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:4Q2J"
FT STRAND 95..102
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 123..126
FT /evidence="ECO:0007829|PDB:4Q2J"
FT STRAND 129..134
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 142..145
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 153..157
FT /evidence="ECO:0007829|PDB:4Q2J"
FT TURN 158..163
FT /evidence="ECO:0007829|PDB:4Q2J"
FT STRAND 164..169
FT /evidence="ECO:0007829|PDB:4Q2J"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 186..197
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 202..208
FT /evidence="ECO:0007829|PDB:4Q2J"
FT STRAND 209..211
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:4Q2J"
FT HELIX 230..242
FT /evidence="ECO:0007829|PDB:4Q2J"
SQ SEQUENCE 764 AA; 85880 MW; 330ECCDBA8683B78 CRC64;
MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGG KMQGVPLKHS
GHLMKTNLRK GTMLPVFCVV EHYENAIEYD CKEEHAEFVL VRKDMLFNQL IEMALLSLGY
SHSSAAQAKG LIQVGKWNPV PLSYVTDAPD ATVADMLQDV YHVVTLKIQL HSCPKLEDLP
PEQWSHTTVR NALKDLLKDM NQSSLAKECP LSQSMISSIV NSTYYANVSA AKCQEFGRWY
KHFKKTKDMM VEMDSLSELS QQGANHVNFG QQPVPGNTAE QPPSPAQLSH GSQPSVRTPL
PNLHPGLVST PISPQLVNQQ LVMAQLLNQQ YAVNRLLAQQ SLNQQYLNHP PPVSRSMNKP
LEQQVSTNTE VSSEIYQWVR DELKRAGISQ AVFARVAFNR TQGLLSEILR KEEDPKTASQ
SLLVNLRAMQ NFLQLPEAER DRIYQDERER SLNAASAMGP APLLSTPPSR PPQVKTATLA
TERNGKPENN TMNINASIYD EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP
ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ
QQQQQQQPPP PPPQPQPQPQ AGPRLPPRQP TVASSAESDE ENRQKTRPRT KISVEALGIL
QSFIQDVGLY PDEEAIQTLS AQLDLPKYTI IKFFQNQRYY LKHHGKLKDN SGLEVDVAEY
KDEELLKDLE ESVQDKNANT LFSVKLEEEL SVEGSTDVNA DLKD
