SATB2_HUMAN
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 03-AUG-2022, entry version 195.
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};
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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. [Q9UPW6-1]
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; 127.
DR DIP; DIP-60551N; -.
DR ELM; Q9UPW6; -.
DR IntAct; Q9UPW6; 93.
DR MINT; Q9UPW6; -.
DR STRING; 9606.ENSP00000401112; -.
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; Q9UPW6; -.
DR PeptideAtlas; Q9UPW6; -.
DR PRIDE; Q9UPW6; -.
DR ProteomicsDB; 61903; -.
DR ProteomicsDB; 85463; -. [Q9UPW6-1]
DR Antibodypedia; 19915; 321 antibodies from 41 providers.
DR DNASU; 23314; -.
DR Ensembl; ENST00000260926.9; ENSP00000260926.5; ENSG00000119042.17. [Q9UPW6-1]
DR Ensembl; ENST00000417098.6; ENSP00000401112.1; ENSG00000119042.17. [Q9UPW6-1]
DR Ensembl; ENST00000428695.5; ENSP00000388581.1; ENSG00000119042.17. [Q9UPW6-2]
DR Ensembl; ENST00000457245.5; ENSP00000405420.1; ENSG00000119042.17. [Q9UPW6-1]
DR Ensembl; ENST00000614512.4; ENSP00000483287.1; ENSG00000119042.17. [Q9UPW6-2]
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 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; KXGLLSE; -.
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 1103 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 147 other tissues.
DR ExpressionAtlas; Q9UPW6; baseline and differential.
DR Genevisible; Q9UPW6; HS.
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; 1.10.260.40; -; 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; 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
