ID SATB2_HUMAN Reviewed; 733 AA. AC Q9UPW6; A8K5Z8; Q3ZB87; Q4V763; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 24-JAN-2024, entry version 203. DE RecName: Full=DNA-binding protein SATB2; DE AltName: Full=Special AT-rich sequence-binding protein 2; GN Name=SATB2; Synonyms=KIAA1034; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=10470851; DOI=10.1093/dnares/6.3.197; RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIV. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 6:197-205(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). 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 FUNCTION, INTERACTION WITH PIAS1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, RP MUTAGENESIS OF LYS-233 AND LYS-350, AND SUMOYLATION. RX PubMed=14701874; DOI=10.1101/gad.1153003; RA Dobreva G., Dambacher J., Grosschedl R.; RT "SUMO modification of a novel MAR-binding protein, SATB2, modulates RT immunoglobulin mu gene expression."; RL Genes Dev. 17:3048-3061(2003). RN [7] RP INVOLVEMENT IN CPI, AND CHROMOSOMAL TRANSLOCATIONS. RX PubMed=12915443; DOI=10.1093/hmg/ddg248; RA FitzPatrick D.R., Carr I.M., McLaren L., Leek J.P., Wightman P., RA Williamson K., Gautier P., McGill N., Hayward C., Firth H., Markham A.F., RA Fantes J.A., Bonthron D.T.; RT "Identification of SATB2 as the cleft palate gene on 2q32-q33."; RL Hum. Mol. Genet. 12:2491-2501(2003). RN [8] RP INVOLVEMENT IN CPI. RX PubMed=17377962; DOI=10.1002/humu.20515; RA Leoyklang P., Suphapeetiporn K., Siriwan P., Desudchit T., RA Chaowanapanja P., Gahl W.A., Shotelersuk V.; RT "Heterozygous nonsense mutation SATB2 associated with cleft palate, RT osteoporosis, and cognitive defects."; RL Hum. Mutat. 28:732-738(2007). RN [9] RP CHROMOSOMAL TRANSLOCATION. RX PubMed=19170718; DOI=10.1111/j.1399-0004.2008.01145.x; RA Tegay D.H., Chan K.K., Leung L., Wang C., Burkett S., Stone G., Stanyon R., RA Toriello H.V., Hatchwell E.; RT "Toriello-Carey syndrome in a patient with a de novo balanced translocation RT [46,XY,t(2;14)(q33;q22)] interrupting SATB2."; RL Clin. Genet. 75:259-264(2009). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-39; SER-454; THR-467 RP AND SER-594, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [11] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25218447; DOI=10.1038/nsmb.2890; RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., RA Vertegaal A.C.; RT "Uncovering global SUMOylation signaling networks in a site-specific RT manner."; RL Nat. Struct. Mol. Biol. 21:927-936(2014). RN [12] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033; RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., RA Vertegaal A.C.; RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."; RL Cell Rep. 10:1778-1791(2015). RN [13] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-350, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25755297; DOI=10.1074/mcp.o114.044792; RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., RA Vertegaal A.C.; RT "System-wide analysis of SUMOylation dynamics in response to replication RT stress reveals novel small ubiquitin-like modified target proteins and RT acceptor lysines relevant for genome stability."; RL Mol. Cell. Proteomics 14:1419-1434(2015). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-24; LYS-30; LYS-161; LYS-350; RP LYS-475 AND LYS-724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [15] RP STRUCTURE BY NMR OF 615-674. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the homeodomain of KIAA1034 protein."; RL Submitted (FEB-2009) to the PDB data bank. RN [16] RP STRUCTURE BY NMR OF 350-437. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the first CUT domain of KIAA1034 protein."; RL Submitted (FEB-2009) to the PDB data bank. RN [17] RP STRUCTURE BY NMR OF 473-560. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the second CUT domain of human SATB2."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Binds to DNA, at nuclear matrix- or scaffold-associated CC regions. Thought to recognize the sugar-phosphate structure of double- CC stranded DNA. Transcription factor controlling nuclear gene expression, CC by binding to matrix attachment regions (MARs) of DNA and inducing a CC local chromatin-loop remodeling. Acts as a docking site for several CC chromatin remodeling enzymes and also by recruiting corepressors CC (HDACs) or coactivators (HATs) directly to promoters and enhancers. CC Required for the initiation of the upper-layer neurons (UL1) specific CC genetic program and for the inactivation of deep-layer neurons (DL) and CC UL2 specific genes, probably by modulating BCL11B expression. Repressor CC of Ctip2 and regulatory determinant of corticocortical connections in CC the developing cerebral cortex. May play an important role in palate CC formation. Acts as a molecular node in a transcriptional network CC regulating skeletal development and osteoblast differentiation. CC {ECO:0000269|PubMed:14701874}. CC -!- SUBUNIT: Interacts with ATF4 and RUNX2; resulting in enhanced DNA CC binding and transactivation by these transcription factors (By CC similarity). Interacts with PIAS1. {ECO:0000250, CC ECO:0000269|PubMed:14701874}. CC -!- INTERACTION: CC Q9UPW6; Q9H1A7: POLR2J3; NbExp=3; IntAct=EBI-8298169, EBI-12818681; CC Q9UPW6; Q8TBN0: RAB3IL1; NbExp=3; IntAct=EBI-8298169, EBI-743796; CC Q9UPW6; Q9H3D4-2: TP63; NbExp=5; IntAct=EBI-8298169, EBI-6481107; CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000255|PROSITE- CC ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00374, CC ECO:0000269|PubMed:14701874}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UPW6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UPW6-2; Sequence=VSP_054416; CC -!- TISSUE SPECIFICITY: High expression in adult brain, moderate expression CC in fetal brain, and weak expression in adult liver, kidney, and spinal CC cord and in select brain regions, including amygdala, corpus callosum, CC caudate nucleus, and hippocampus. {ECO:0000269|PubMed:14701874}. CC -!- PTM: Sumoylated by PIAS1. Sumoylation promotes nuclear localization, CC but represses transcription factor activity. CC {ECO:0000269|PubMed:14701874}. CC -!- DISEASE: Note=Chromosomal aberrations involving SATB2 are found in CC isolated cleft palate. Translocation t(2;7); translocation t(2;11). CC {ECO:0000269|PubMed:12915443}. CC -!- DISEASE: Cleft palate isolated (CPI) [MIM:119540]: A congenital fissure CC of the soft and/or hard palate, due to faulty fusion. Isolated cleft CC palate is not associated with cleft lips. Some patients may manifest CC other craniofacial dysmorphic features, intellectual disability, and CC osteoporosis. {ECO:0000269|PubMed:12915443, CC ECO:0000269|PubMed:17377962}. Note=The disease may be caused by CC variants affecting the gene represented in this entry. CC -!- DISEASE: Note=A chromosomal aberration involving SATB2 is found in a CC patient with classical features of Toriello-Carey syndrome. CC Translocation t(2;14)(q33;q22). {ECO:0000269|PubMed:19170718}. CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA82986.1; Type=Erroneous initiation; Evidence={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; AB028957; BAA82986.1; ALT_INIT; mRNA. DR EMBL; AK291463; BAF84152.1; -; mRNA. DR EMBL; AC016746; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC017096; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471063; EAW70180.1; -; Genomic_DNA. DR EMBL; BC098136; AAH98136.1; -; mRNA. DR EMBL; BC099723; AAH99723.1; -; mRNA. DR EMBL; BC103492; AAI03493.1; -; mRNA. DR EMBL; BC103500; AAI03501.1; -; mRNA. DR CCDS; CCDS2327.1; -. [Q9UPW6-1] DR RefSeq; NP_001165980.1; NM_001172509.1. [Q9UPW6-1] DR RefSeq; NP_001165988.1; NM_001172517.1. [Q9UPW6-1] DR RefSeq; NP_056080.1; NM_015265.3. [Q9UPW6-1] DR RefSeq; XP_006712435.1; XM_006712372.2. DR RefSeq; XP_011509142.1; XM_011510840.2. DR PDB; 1WI3; NMR; -; A=615-672. DR PDB; 1WIZ; NMR; -; A=350-437. DR PDB; 2CSF; NMR; -; A=473-560. DR PDBsum; 1WI3; -. DR PDBsum; 1WIZ; -. DR PDBsum; 2CSF; -. DR AlphaFoldDB; Q9UPW6; -. DR SMR; Q9UPW6; -. DR BioGRID; 116905; 136. DR DIP; DIP-60551N; -. DR ELM; Q9UPW6; -. DR IntAct; Q9UPW6; 95. DR MINT; Q9UPW6; -. DR STRING; 9606.ENSP00000401112; -. DR GlyGen; Q9UPW6; 3 sites, 1 O-linked glycan (3 sites). DR iPTMnet; Q9UPW6; -. DR PhosphoSitePlus; Q9UPW6; -. DR BioMuta; SATB2; -. DR DMDM; 13634020; -. DR EPD; Q9UPW6; -. DR jPOST; Q9UPW6; -. DR MassIVE; Q9UPW6; -. DR MaxQB; Q9UPW6; -. DR PaxDb; 9606-ENSP00000401112; -. DR PeptideAtlas; Q9UPW6; -. DR ProteomicsDB; 61903; -. DR ProteomicsDB; 85463; -. [Q9UPW6-1] DR Pumba; Q9UPW6; -. DR Antibodypedia; 19915; 423 antibodies from 41 providers. DR DNASU; 23314; -. DR Ensembl; ENST00000260926.9; ENSP00000260926.5; ENSG00000119042.18. [Q9UPW6-1] DR Ensembl; ENST00000417098.6; ENSP00000401112.1; ENSG00000119042.18. [Q9UPW6-1] DR Ensembl; ENST00000428695.6; ENSP00000388581.1; ENSG00000119042.18. [Q9UPW6-2] DR Ensembl; ENST00000457245.5; ENSP00000405420.1; ENSG00000119042.18. [Q9UPW6-1] DR Ensembl; ENST00000700191.1; ENSP00000514853.1; ENSG00000119042.18. [Q9UPW6-2] DR Ensembl; ENST00000700193.1; ENSP00000514854.1; ENSG00000119042.18. [Q9UPW6-1] DR GeneID; 23314; -. DR KEGG; hsa:23314; -. DR MANE-Select; ENST00000417098.6; ENSP00000401112.1; NM_001172509.2; NP_001165980.1. DR UCSC; uc002uuy.2; human. [Q9UPW6-1] DR AGR; HGNC:21637; -. DR CTD; 23314; -. DR DisGeNET; 23314; -. DR GeneCards; SATB2; -. DR GeneReviews; SATB2; -. DR HGNC; HGNC:21637; SATB2. DR HPA; ENSG00000119042; Group enriched (brain, intestine). DR MalaCards; SATB2; -. DR MIM; 119540; phenotype. DR MIM; 608148; gene. DR neXtProt; NX_Q9UPW6; -. DR OpenTargets; ENSG00000119042; -. DR Orphanet; 251019; 2q32q33 microdeletion syndrome. DR Orphanet; 251028; SATB2-associated syndrome due to a chromosomal rearrangement. DR Orphanet; 576283; SATB2-associated syndrome due to a pathogenic variant. DR PharmGKB; PA128394624; -. DR VEuPathDB; HostDB:ENSG00000119042; -. DR eggNOG; KOG3755; Eukaryota. DR GeneTree; ENSGT00390000008096; -. DR HOGENOM; CLU_012559_1_0_1; -. DR InParanoid; Q9UPW6; -. DR OMA; YCDLPVG; -. DR OrthoDB; 2969903at2759; -. DR PhylomeDB; Q9UPW6; -. DR TreeFam; TF332714; -. DR PathwayCommons; Q9UPW6; -. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR Reactome; R-HSA-8940973; RUNX2 regulates osteoblast differentiation. DR SignaLink; Q9UPW6; -. DR SIGNOR; Q9UPW6; -. DR BioGRID-ORCS; 23314; 19 hits in 1176 CRISPR screens. DR ChiTaRS; SATB2; human. DR EvolutionaryTrace; Q9UPW6; -. DR GeneWiki; SATB2; -. DR GenomeRNAi; 23314; -. DR Pharos; Q9UPW6; Tbio. DR PRO; PR:Q9UPW6; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9UPW6; Protein. DR Bgee; ENSG00000119042; Expressed in periodontal ligament and 149 other cell types or tissues. DR ExpressionAtlas; Q9UPW6; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0000118; C:histone deacetylase complex; IEA:Ensembl. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005667; C:transcription regulator complex; IEA:Ensembl. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0042826; F:histone deacetylase binding; ISS:ARUK-UCL. 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; IDA:NTNU_SB. DR GO; GO:0051216; P:cartilage development; IEA:Ensembl. DR GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0009880; P:embryonic pattern specification; IEA:Ensembl. DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl. DR GO; GO:0001764; P:neuron migration; IEA:Ensembl. DR GO; GO:0002076; P:osteoblast development; IEA:Ensembl. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0060021; P:roof of mouth development; IEA:Ensembl. 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:SF15; DNA-BINDING PROTEIN SATB2; 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; Q9UPW6; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chromatin regulator; KW Chromosomal rearrangement; Developmental protein; Disease variant; KW DNA-binding; Homeobox; Intellectual disability; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..733 FT /note="DNA-binding protein SATB2" FT /id="PRO_0000202400" FT DOMAIN 57..158 FT /note="ULD" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01326" FT DOMAIN 161..234 FT /note="CUTL" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01327" FT DNA_BIND 350..437 FT /note="CUT 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374" FT DNA_BIND 473..560 FT /note="CUT 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00374" FT DNA_BIND 615..674 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 435..473 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 580..617 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 694..733 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..19 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 439..473 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 595..610 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 694..712 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 713..733 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 20 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 454 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 467 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 594 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 24 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 30 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 161 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 233 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000305" FT CROSSLNK 350 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO); alternate" FT /evidence="ECO:0000305" FT CROSSLNK 350 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2); alternate" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 475 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 724 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 116..233 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_054416" FT VARIANT 263 FT /note="S -> P (in dbSNP:rs12619995)" FT /id="VAR_059320" FT MUTAGEN 233 FT /note="K->R: Reduced sumoylation, impaired nuclear FT localization, but enhanced transcription factor activity." FT /evidence="ECO:0000269|PubMed:14701874" FT MUTAGEN 350 FT /note="K->R: Reduced sumoylation, impaired nuclear FT localization, but enhanced transcription factor activity." FT /evidence="ECO:0000269|PubMed:14701874" FT HELIX 364..375 FT /evidence="ECO:0007829|PDB:1WIZ" FT HELIX 379..387 FT /evidence="ECO:0007829|PDB:1WIZ" FT HELIX 391..399 FT /evidence="ECO:0007829|PDB:1WIZ" FT TURN 404..406 FT /evidence="ECO:0007829|PDB:1WIZ" FT HELIX 409..421 FT /evidence="ECO:0007829|PDB:1WIZ" FT HELIX 426..437 FT /evidence="ECO:0007829|PDB:1WIZ" FT HELIX 486..498 FT /evidence="ECO:0007829|PDB:2CSF" FT HELIX 502..508 FT /evidence="ECO:0007829|PDB:2CSF" FT HELIX 514..523 FT /evidence="ECO:0007829|PDB:2CSF" FT HELIX 532..545 FT /evidence="ECO:0007829|PDB:2CSF" FT HELIX 549..559 FT /evidence="ECO:0007829|PDB:2CSF" FT HELIX 624..636 FT /evidence="ECO:0007829|PDB:1WI3" FT HELIX 642..651 FT /evidence="ECO:0007829|PDB:1WI3" FT HELIX 656..669 FT /evidence="ECO:0007829|PDB:1WI3" SQ SEQUENCE 733 AA; 82555 MW; 1FE1FCBD34F11E9E CRC64; MERRSESPCL RDSPDRRSGS PDVKGPPPVK VARLEQNGSP MGARGRPNGA VAKAVGGLMI PVFCVVEQLD GSLEYDNREE HAEFVLVRKD VLFSQLVETA LLALGYSHSS AAQAQGIIKL GRWNPLPLSY VTDAPDATVA DMLQDVYHVV TLKIQLQSCS KLEDLPAEQW NHATVRNALK ELLKEMNQST LAKECPLSQS MISSIVNSTY YANVSATKCQ EFGRWYKKYK KIKVERVERE NLSDYCVLGQ RPMHLPNMNQ LASLGKTNEQ SPHSQIHHST PIRNQVPALQ PIMSPGLLSP QLSPQLVRQQ IAMAHLINQQ IAVSRLLAHQ HPQAINQQFL NHPPIPRAVK PEPTNSSVEV SPDIYQQVRD ELKRASVSQA VFARVAFNRT QGLLSEILRK EEDPRTASQS LLVNLRAMQN FLNLPEVERD RIYQDERERS MNPNVSMVSS ASSSPSSSRT PQAKTSTPTT DLPIKVDGAN INITAAIYDE IQQEMKRAKV SQALFAKVAA NKSQGWLCEL LRWKENPSPE NRTLWENLCT IRRFLNLPQH ERDVIYEEES RHHHSERMQH VVQLPPEPVQ VLHRQQSQPA KESSPPREEA PPPPPPTEDS CAKKPRSRTK ISLEALGILQ SFIHDVGLYP DQEAIHTLSA QLDLPKHTII KFFQNQRYHV KHHGKLKEHL GSAVDVAEYK DEELLTESEE NDSEEGSEEM YKVEAEEENA DKSKAAPAEI DQR //