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 24-JAN-2024, entry version 193. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 10090-ENSMUSP00000116006; -. DR ProteomicsDB; 256706; -. DR Antibodypedia; 11251; 656 antibodies from 44 providers. DR DNASU; 20230; -. DR Ensembl; ENSMUST00000129667.8; ENSMUSP00000116020.3; ENSMUSG00000023927.16. DR Ensembl; ENSMUST00000133574.8; ENSMUSP00000120536.2; ENSMUSG00000023927.16. DR Ensembl; ENSMUST00000144331.8; ENSMUSP00000116006.2; ENSMUSG00000023927.16. DR Ensembl; ENSMUST00000152830.9; ENSMUSP00000119842.3; ENSMUSG00000023927.16. DR Ensembl; ENSMUST00000169480.8; ENSMUSP00000128841.2; ENSMUSG00000023927.16. DR Ensembl; ENSMUST00000176669.8; ENSMUSP00000134957.2; ENSMUSG00000023927.16. DR GeneID; 20230; -. DR KEGG; mmu:20230; -. DR UCSC; uc008czd.2; mouse. DR AGR; MGI:105084; -. 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 OrthoDB; 2969903at2759; -. 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; 5 hits in 83 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 295 other cell types or tissues. DR ExpressionAtlas; Q60611; baseline and differential. 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:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI. DR GO; GO:0060004; P:reflex; IMP:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IDA:MGI. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0042110; P:T cell activation; IMP:MGI. DR CDD; cd00086; homeodomain; 1. DR CDD; cd11585; SATB1_N; 1. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR Gene3D; 1.10.260.40; lambda repressor-like DNA-binding domains; 2. DR Gene3D; 1.10.260.70; SATB, CULT domain; 1. DR Gene3D; 3.10.20.710; SATB, ubiquitin-like oligomerisation domain; 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; DNA-BINDING PROTEIN SATB FAMILY MEMBER; 1. DR PANTHER; PTHR15116:SF14; DNA-BINDING PROTEIN SATB1; 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; Homeodomain-like; 1. DR SUPFAM; SSF47413; lambda repressor-like DNA-binding domains; 2. DR PROSITE; PS51042; CUT; 2. DR PROSITE; PS51983; CUTL; 1. DR PROSITE; PS50071; HOMEOBOX_2; 1. DR PROSITE; PS51982; ULD; 1. DR Genevisible; Q60611; MM. 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 //