ID SATB1_HUMAN Reviewed; 763 AA. AC Q01826; B3KXF1; C9JTR6; Q59EQ0; DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1993, sequence version 1. DT 27-MAR-2024, entry version 216. DE RecName: Full=DNA-binding protein SATB1 {ECO:0000305}; DE AltName: Full=Special AT-rich sequence-binding protein 1; GN Name=SATB1 {ECO:0000312|HGNC:HGNC:10541}; 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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=1505028; DOI=10.1016/0092-8674(92)90432-c; RA Dickinson L.A., Joh T., Kohwi Y., Kohwi-Shigematsu T.; RT "A tissue-specific MAR/SAR DNA-binding protein with unusual binding site RT recognition."; RL Cell 70:631-645(1992). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hippocampus; 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 MRNA] (ISOFORM 2). RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno F.R.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16641997; DOI=10.1038/nature04728; RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.; RT "The DNA sequence, annotation and analysis of human chromosome 3."; RL Nature 440:1194-1198(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [7] RP FUNCTION, AND MUTAGENESIS OF ARG-646; ARG-648 AND 693-PHE--ASN-695. RX PubMed=9111059; DOI=10.1074/jbc.272.17.11463; RA Dickinson L.A., Dickinson C.D., Kohwi-Shigematsu T.; RT "An atypical homeodomain in SATB1 promotes specific recognition of the key RT structural element in a matrix attachment region."; RL J. Biol. Chem. 272:11463-11470(1997). RN [8] RP FUNCTION. RX PubMed=9548713; DOI=10.1083/jcb.141.2.335; RA de Belle I., Cai S., Kohwi-Shigematsu T.; RT "The genomic sequences bound to special AT-rich sequence-binding protein 1 RT (SATB1) in vivo in Jurkat T cells are tightly associated with the nuclear RT matrix at the bases of the chromatin loops."; RL J. Cell Biol. 141:335-348(1998). RN [9] RP FUNCTION, IDENTIFICATION IN THE GAMMA-GLOBIN PROMOTER COMPLEX, AND RP IDENTIFICATION IN THE ENHANCER BINDING FACTOR COMPLEX. RX PubMed=10595394; DOI=10.1089/104454999314809; RA Case S.S., Huber P., Lloyd J.A.; RT "The gammaPE complex contains both SATB1 and HOXB2 and has positive and RT negative roles in human gamma-globin gene regulation."; RL DNA Cell Biol. 18:805-817(1999). RN [10] RP CLEAVAGE BY CASPASES, AND SUBCELLULAR LOCATION. RX PubMed=10800076; DOI=10.1038/sj.cdd.4400668; RA Gotzmann J., Meissner M., Gerner C.; RT "The fate of the nuclear matrix-associated-region-binding protein SATB1 RT during apoptosis."; RL Cell Death Differ. 7:425-438(2000). RN [11] RP FUNCTION, MUTAGENESIS OF ASP-254, SUBUNIT, AND CLEAVAGE BY CASPASE-6. 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 [12] RP INTERACTION WITH POLR2J2. RX PubMed=12036295; DOI=10.1006/geno.2002.6772; RA Durrin L.K., Krontiris T.G.; RT "The thymocyte-specific MAR binding protein, SATB1, interacts in vitro with RT a novel variant of DNA-directed RNA polymerase II, subunit 11."; RL Genomics 79:809-817(2002). RN [13] RP FUNCTION. RX PubMed=12374985; DOI=10.1038/nature01084; RA Yasui D., Miyano M., Cai S., Varga-Weisz P., Kohwi-Shigematsu T.; RT "SATB1 targets chromatin remodelling to regulate genes over long RT distances."; RL Nature 419:641-645(2002). RN [14] RP INTERACTION WITH EP300. RX PubMed=14605447; DOI=10.1111/j.1348-0421.2003.tb03438.x; RA Fujii Y., Kumatori A., Nakamura M.; RT "SATB1 makes a complex with p300 and represses gp91(phox) promoter RT activity."; RL Microbiol. Immunol. 47:803-811(2003). RN [15] 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 [16] RP FUNCTION. RX PubMed=15618465; DOI=10.1182/blood-2004-08-2988; RA Wen J., Huang S., Rogers H., Dickinson L.A., Kohwi-Shigematsu T., RA Noguchi C.T.; RT "SATB1 family protein expressed during early erythroid differentiation RT modifies globin gene expression."; RL Blood 105:3330-3339(2005). RN [17] RP SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-29; ARG-32; GLU-34 AND ASN-36, AND RP NUCLEAR LOCALIZATION SIGNAL. RX PubMed=15970696; RA Nakayama Y., Mian I.S., Kohwi-Shigematsu T., Ogawa T.; RT "A nuclear targeting determinant for SATB1, a genome organizer in the T RT cell lineage."; RL Cell Cycle 4:1099-1106(2005). RN [18] RP SUMOYLATION. RX PubMed=15561718; DOI=10.1074/jbc.m411718200; RA Gocke C.B., Yu H., Kang J.; RT "Systematic identification and analysis of mammalian small ubiquitin-like RT modifier substrates."; RL J. Biol. Chem. 280:5004-5012(2005). RN [19] 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 [20] RP INTERACTION WITH DYNLT3, AND SUBCELLULAR LOCATION. RX PubMed=16079286; DOI=10.1242/jcs.02472; RA Yeh T.-Y., Chuang J.-Z., Sung C.-H.; RT "Dynein light chain rp3 acts as a nuclear matrix-associated transcriptional RT modulator in a dynein-independent pathway."; RL J. Cell Sci. 118:3431-3443(2005). RN [21] RP FUNCTION, AND INTERACTION WITH HIV-1 TAT (MICROBIAL INFECTION) AND HDAC1. RX PubMed=15713622; DOI=10.1128/mcb.25.5.1620-1633.2005; RA Kumar P.P., Purbey P.K., Ravi D.S., Mitra D., Galande S.; RT "Displacement of SATB1-bound histone deacetylase 1 corepressor by the human RT immunodeficiency virus type 1 transactivator induces expression of RT interleukin-2 and its receptor in T cells."; RL Mol. Cell. Biol. 25:1620-1633(2005). RN [22] RP FUNCTION, AND CLEAVAGE BY CASPASE-3. RX PubMed=16377216; DOI=10.1016/j.cellbi.2005.10.025; RA Sun Y., Wang T., Su Y., Yin Y., Xu S., Ma C., Han X.; RT "The behavior of SATB1, a MAR-binding protein, in response to apoptosis RT stimulation."; RL Cell Biol. Int. 30:244-247(2006). RN [23] RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HDAC1 AND RP PCAF, MUTAGENESIS OF LYS-136 AND SER-185, ACETYLATION AT LYS-136, AND RP PHOSPHORYLATION AT SER-185. RX PubMed=16630892; DOI=10.1016/j.molcel.2006.03.010; RA Kumar P.P., Purbey P.K., Sinha C.K., Notani D., Limaye A., Jayani R.S., RA Galande S.; RT "Phosphorylation of SATB1, a global gene regulator, acts as a molecular RT switch regulating its transcriptional activity in vivo."; RL Mol. Cell 22:231-243(2006). RN [24] RP FUNCTION. RX PubMed=17376900; DOI=10.1128/jvi.01405-06; RA Kumar P.P., Mehta S., Purbey P.K., Notani D., Jayani R.S., Purohit H.J., RA Raje D.V., Ravi D.S., Bhonde R.R., Mitra D., Galande S.; RT "SATB1-binding sequences and Alu-like motifs define a unique chromatin RT context in the vicinity of human immunodeficiency virus type 1 integration RT sites."; RL J. Virol. 81:5617-5627(2007). RN [25] RP FUNCTION, AND INTERACTION WITH PML. RX PubMed=17173041; DOI=10.1038/ncb1516; RA Kumar P.P., Bischof O., Purbey P.K., Notani D., Urlaub H., Dejean A., RA Galande S.; RT "Functional interaction between PML and SATB1 regulates chromatin-loop RT architecture and transcription of the MHC class I locus."; RL Nat. Cell Biol. 9:45-56(2007). RN [26] RP INTERACTION WITH CYTOMEGALOVIRUS UNIQUE REGION. RX PubMed=17512569; DOI=10.1016/j.virol.2007.04.024; RA Lee J., Klase Z., Gao X., Caldwell J.S., Stinski M.F., Kashanchi F., RA Chao S.-H.; RT "Cellular homeoproteins, SATB1 and CDP, bind to the unique region between RT the human cytomegalovirus UL127 and major immediate-early genes."; RL Virology 366:117-125(2007). RN [27] RP SUMOYLATION AT LYS-744, MUTAGENESIS OF LYS-411; LYS-486; LYS-720 AND RP LYS-744, SUBCELLULAR LOCATION, AND CLEAVAGE BY CASPASE-6. RX PubMed=18408014; DOI=10.1074/jbc.m800512200; RA Tan J.-A.T., Sun Y., Song J., Chen Y., Krontiris T.G., Durrin L.K.; RT "SUMO conjugation to the matrix attachment region-binding protein, special RT AT-rich sequence-binding protein-1 (SATB1), targets SATB1 to promyelocytic RT nuclear bodies where it undergoes caspase cleavage."; RL J. Biol. Chem. 283:18124-18134(2008). RN [28] RP FUNCTION, AND ROLE IN BREAST TUMOR GROWTH AND METASTASIS. RX PubMed=18337816; DOI=10.1038/nature06781; RA Han H.-J., Russo J., Kohwi Y., Kohwi-Shigematsu T.; RT "SATB1 reprogrammes gene expression to promote breast tumour growth and RT metastasis."; RL Nature 452:187-193(2008). RN [29] RP SUBUNIT, AND INTERACTION WITH DNA AND NUCLEAR MATRIX. RX PubMed=18187506; DOI=10.1093/nar/gkm1151; RA Purbey P.K., Singh S., Kumar P.P., Mehta S., Ganesh K.N., Mitra D., RA Galande S.; RT "PDZ domain-mediated dimerization and homeodomain-directed specificity are RT required for high-affinity DNA binding by SATB1."; RL Nucleic Acids Res. 36:2107-2122(2008). RN [30] RP FUNCTION. RX PubMed=19332023; DOI=10.1016/j.bbrc.2009.03.122; RA Gong H., Wang Z., Zhao G.-W., Lv X., Wei G.-H., Wang L., Liu D.-P., RA Liang C.-C.; RT "SATB1 regulates beta-like globin genes through matrix related nuclear RT relocation of the cluster."; RL Biochem. Biophys. Res. Commun. 383:11-15(2009). RN [31] RP FUNCTION. RX PubMed=19430959; DOI=10.1007/s11033-009-9538-y; RA Cai R., Xu W., Dai B., Cai X., Xu R., Lu J.; RT "SATB1 binds an intronic MAR sequence in human PI3kgamma in vitro."; RL Mol. Biol. Rep. 37:1461-1465(2010). RN [32] RP FUNCTION, MUTAGENESIS OF LYS-136, 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 [33] RP FUNCTION. RX PubMed=19247486; DOI=10.1371/journal.pone.0004629; RA Wang L., Di L.-J., Lv X., Zheng W., Xue Z., Guo Z.-C., Liu D.-P., RA Liang C.-C.; RT "Inter-MAR association contributes to transcriptionally active looping RT events in human beta-globin gene cluster."; RL PLoS ONE 4:E4629-E4629(2009). RN [34] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-51, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE 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 [35] RP STRUCTURE BY NMR OF 353-490 IN COMPLEX WITH MAR DNA, AND MUTAGENESIS OF RP SER-373; ARG-380; LYS-384; ARG-395; SER-406; ARG-410; LYS-416; ARG-427; RP ARG-442; SER-451 AND LYS-475. RX PubMed=16371359; DOI=10.1074/jbc.m510933200; RA Yamaguchi H., Tateno M., Yamasaki K.; RT "Solution structure and DNA-binding mode of the matrix attachment region- RT binding domain of the transcription factor SATB1 that regulates the T-cell RT maturation."; RL J. Biol. Chem. 281:5319-5327(2006). RN [36] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 368-452 IN COMPLEX WITH MAR DNA, RP AND MUTAGENESIS OF GLN-402 AND GLY-403. RX PubMed=17652321; DOI=10.1093/nar/gkm504; RA Yamasaki K., Akiba T., Yamasaki T., Harata K.; RT "Structural basis for recognition of the matrix attachment region of DNA by RT transcription factor SATB1."; RL Nucleic Acids Res. 35:5073-5084(2007). RN [37] RP VARIANTS DHDBV LEU-181; VAL-323; ARG-402; GLN-407; GLY-407; LYS-413; RP ARG-420; ARG-525; GLN-530; GLY-530; LYS-530; LYS-547; ARG-577; ARG-619 AND RP VAL-682, CHARACTERIZATION OF VARIANTS DHDBV GLY-407; ARG-420; GLN-530; RP LYS-530; LYS-547 AND VAL-682, VARIANTS DEFDA 410-ARG--ASP-763 DEL AND RP 694-GLN--ASP-763 DEL, VARIANTS LEU-366; LEU-519 AND THR-573, RP CHARACTERIZATION OF VARIANTS LEU-366; LEU-519 AND THR-573, CHARACTERIZATION RP OF VARIANTS DEFDA 410-GLN--ASP-763 DEL AND 694-GLN--ASP-763 DEL, RP SUBCELLULAR LOCATION, AND FUNCTION. RX PubMed=33513338; DOI=10.1016/j.ajhg.2021.01.007; RG DDD Study; RA den Hoed J., de Boer E., Voisin N., Dingemans A.J.M., Guex N., Wiel L., RA Nellaker C., Amudhavalli S.M., Banka S., Bena F.S., Ben-Zeev B., RA Bonagura V.R., Bruel A.L., Brunet T., Brunner H.G., Chew H.B., Chrast J., RA Cimbalistiene L., Coon H., Delot E.C., Demurger F., Denomme-Pichon A.S., RA Depienne C., Donnai D., Dyment D.A., Elpeleg O., Faivre L., Gilissen C., RA Granger L., Haber B., Hachiya Y., Abedi Y.H., Hanebeck J., Hehir-Kwa J.Y., RA Horist B., Itai T., Jackson A., Jewell R., Jones K.L., Joss S., Kashii H., RA Kato M., Kattentidt-Mouravieva A.A., Kok F., Kotzaeridou U., RA Krishnamurthy V., Kucinskas V., Kuechler A., Lavillaureix A., Liu P., RA Manwaring L., Matsumoto N., Mazel B., McWalter K., Meiner V., Mikati M.A., RA Miyatake S., Mizuguchi T., Moey L.H., Mohammed S., Mor-Shaked H., RA Mountford H., Newbury-Ecob R., Odent S., Orec L., Osmond M., RA Palculict T.B., Parker M., Petersen A.K., Pfundt R., Preiksaitiene E., RA Radtke K., Ranza E., Rosenfeld J.A., Santiago-Sim T., Schwager C., RA Sinnema M., Snijders Blok L., Spillmann R.C., Stegmann A.P.A., RA Thiffault I., Tran L., Vaknin-Dembinsky A., Vedovato-Dos-Santos J.H., RA Schrier Vergano S.A., Vilain E., Vitobello A., Wagner M., Waheeb A., RA Willing M., Zuccarelli B., Kini U., Newbury D.F., Kleefstra T., Reymond A., RA Fisher S.E., Vissers L.E.L.M.; RT "Mutation-specific pathophysiological mechanisms define different RT neurodevelopmental disorders associated with SATB1 dysfunction."; RL Am. J. Hum. Genet. 108:346-356(2021). CC -!- FUNCTION: Crucial silencing factor contributing to the initiation of X CC inactivation mediated by Xist RNA that occurs during embryogenesis and CC in lymphoma (By similarity). Binds to DNA at special AT-rich sequences, CC the consensus SATB1-binding sequence (CSBS), at nuclear matrix- or CC scaffold-associated regions. Thought to recognize the sugar-phosphate CC structure of double-stranded DNA. Transcriptional repressor controlling CC nuclear and viral gene expression in a phosphorylated and acetylated CC status-dependent manner, by binding to matrix attachment regions (MARs) CC of DNA and inducing a local chromatin-loop remodeling. Acts as a CC docking site for several chromatin remodeling enzymes (e.g. PML at the CC MHC-I locus) 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. Required for the switching of fetal globin species, CC and beta- and gamma-globin genes regulation during erythroid CC differentiation. Plays a role in chromatin organization and nuclear CC architecture during apoptosis. Interacts with the unique region (UR) of CC cytomegalovirus (CMV). Alu-like motifs and SATB1-binding sites provide CC a unique chromatin context which seems preferentially targeted by the CC HIV-1 integration machinery. Moreover, HIV-1 Tat may overcome SATB1- CC mediated repression of IL2 and IL2RA (interleukin) in T-cells by CC binding to the same domain than HDAC1. Delineates specific epigenetic CC modifications at target gene loci, directly up-regulating metastasis- CC associated genes while down-regulating tumor-suppressor genes. CC Reprograms chromatin organization and the transcription profiles of CC breast tumors to promote growth and metastasis. Promotes neuronal CC differentiation of neural stem/progenitor cells in the adult CC subventricular zone, possibly by positively regulating the expression CC of NEUROD1 (By similarity). {ECO:0000250|UniProtKB:Q60611, CC ECO:0000269|PubMed:10595394, ECO:0000269|PubMed:11463840, CC ECO:0000269|PubMed:12374985, ECO:0000269|PubMed:12692553, CC ECO:0000269|PubMed:1505028, ECO:0000269|PubMed:15618465, CC ECO:0000269|PubMed:15713622, ECO:0000269|PubMed:16377216, CC ECO:0000269|PubMed:16630892, ECO:0000269|PubMed:17173041, CC ECO:0000269|PubMed:17376900, ECO:0000269|PubMed:18337816, CC ECO:0000269|PubMed:19103759, ECO:0000269|PubMed:19247486, CC ECO:0000269|PubMed:19332023, ECO:0000269|PubMed:19430959, CC ECO:0000269|PubMed:33513338, ECO:0000269|PubMed:9111059, CC ECO:0000269|PubMed:9548713}. CC -!- SUBUNIT: Interacts with CUX1 (via DNA-binding domains); the interaction CC inhibits the attachment of both proteins to DNA (By similarity). CC Homodimer. Part of the nuclear protein complex gamma-globin promoter CC and enhancer binding factor (gamma-PE) composed at least of SATB1 and CC HOXB2. Interaction with CtBP1 when not acetylated stabalizes attachment CC to DNA and promotes transcription repression. Interacts with PCAF. CC Interacts with sumoylated PML and HDAC1 via the ULD domain. Interacts CC also with DYNLT3 and POLR2J2. Binds to EP300. {ECO:0000250, CC ECO:0000269|PubMed:10595394, ECO:0000269|PubMed:11463840, CC ECO:0000269|PubMed:12036295, ECO:0000269|PubMed:14605447, CC ECO:0000269|PubMed:15713622, ECO:0000269|PubMed:16079286, CC ECO:0000269|PubMed:16371359, ECO:0000269|PubMed:16630892, CC ECO:0000269|PubMed:17173041, ECO:0000269|PubMed:17512569, CC ECO:0000269|PubMed:17652321, ECO:0000269|PubMed:18187506, CC ECO:0000269|PubMed:19103759}. CC -!- SUBUNIT: (Microbial infection) Interacts (via the ULD domain) with HIV- CC 1 Tat. {ECO:0000269|PubMed:15713622}. CC -!- INTERACTION: CC Q01826; P55212: CASP6; NbExp=2; IntAct=EBI-743747, EBI-718729; CC Q01826; P35222: CTNNB1; NbExp=9; IntAct=EBI-743747, EBI-491549; CC Q01826; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-743747, EBI-16439278; CC Q01826; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-743747, EBI-742688; CC Q01826; P63165: SUMO1; NbExp=2; IntAct=EBI-743747, EBI-80140; CC Q01826; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-743747, EBI-10175576; CC -!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:10800076, CC ECO:0000269|PubMed:18408014}. Nucleus, PML body CC {ECO:0000269|PubMed:18408014}. Note=Organized into a cage-like network CC anchoring loops of heterochromatin and tethering specialized DNA CC sequences (PubMed:12692553). When sumoylated, localized in CC promyelocytic leukemia nuclear bodies (PML NBs) (PubMed:18408014). CC {ECO:0000269|PubMed:12692553, ECO:0000269|PubMed:18408014}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q01826-1; Sequence=Displayed; CC Name=2; CC IsoId=Q01826-2; Sequence=VSP_038296; CC -!- TISSUE SPECIFICITY: Expressed predominantly in thymus. CC {ECO:0000269|PubMed:1505028}. CC -!- PTM: Sumoylated. Sumoylation promotes cleavage by caspases. CC {ECO:0000269|PubMed:15561718, ECO:0000269|PubMed:18408014}. 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. CC {ECO:0000269|PubMed:16630892}. 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:15561718, CC ECO:0000269|PubMed:18408014}. CC -!- DISEASE: Den Hoed-de Boer-Voisin syndrome (DHDBV) [MIM:619229]: A CC disorder characterized by global developmental delay, moderately to CC severely impaired intellectual development, poor or absent speech, CC delayed motor skills, and early-onset epilepsy in many patients. Most CC affected individuals have feeding difficulties, poor overall growth, CC dysmorphic facial features, and significant dental anomalies resembling CC amelogenesis imperfecta. More variable features include visual defects, CC behavioral abnormalities, and non-specific involvement of other organ CC systems. DHDBV transmission pattern is consistent with autosomal CC dominant inheritance with incomplete penetrance and variable CC expressivity. {ECO:0000269|PubMed:33513338}. Note=The disease is caused CC by variants affecting the gene represented in this entry. CC -!- DISEASE: Developmental delay with dysmorphic facies and dental CC anomalies (DEFDA) [MIM:619228]: A disorder characterized by mild global CC developmental delay, impaired intellectual development, walking by 2 to CC 3 years, and slow language acquisition.The severity of the disorder CC ranges from moderate cognitive deficits to mild learning difficulties CC or behavioral abnormalities. Most patients have dysmorphic facial CC features, abnormal dentition and non-specific visual defects. DEFDA CC transmission pattern is consistent with autosomal dominant inheritance CC with incomplete penetrance and variable expressivity. CC {ECO:0000269|PubMed:33513338}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the CUT homeobox family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD92998.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/44225/SATB1"; 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; M97287; AAA60304.1; -; mRNA. DR EMBL; AK127242; BAG54463.1; -; mRNA. DR EMBL; AB209761; BAD92998.1; ALT_INIT; mRNA. DR EMBL; AC139618; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC144521; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471055; EAW64291.1; -; Genomic_DNA. DR EMBL; BC001744; AAH01744.1; -; mRNA. DR CCDS; CCDS2631.1; -. [Q01826-1] DR CCDS; CCDS56242.1; -. [Q01826-2] DR PIR; A43314; A43314. DR RefSeq; NP_001124482.1; NM_001131010.3. [Q01826-1] DR RefSeq; NP_001182399.1; NM_001195470.2. [Q01826-2] DR RefSeq; NP_001309800.1; NM_001322871.1. [Q01826-2] DR RefSeq; NP_001309801.1; NM_001322872.1. [Q01826-1] DR RefSeq; NP_001309802.1; NM_001322873.1. [Q01826-1] DR RefSeq; NP_001309803.1; NM_001322874.1. [Q01826-1] DR RefSeq; NP_001309804.1; NM_001322875.1. [Q01826-1] DR RefSeq; NP_002962.1; NM_002971.5. [Q01826-1] DR RefSeq; XP_011532290.1; XM_011533988.2. [Q01826-2] DR RefSeq; XP_011532291.1; XM_011533989.2. [Q01826-2] DR PDB; 1YSE; NMR; -; A=353-490. DR PDB; 2L1P; NMR; -; A=179-250. DR PDB; 2MW8; NMR; -; A=641-707. DR PDB; 2O49; X-ray; 2.00 A; A=368-452. DR PDB; 2O4A; X-ray; 1.75 A; A=368-452. DR PDB; 3NZL; X-ray; 1.20 A; A=179-250. DR PDB; 3TUO; X-ray; 1.70 A; A/B/C/D=71-171. DR PDB; 6LFF; X-ray; 1.79 A; A/B=368-452. DR PDBsum; 1YSE; -. DR PDBsum; 2L1P; -. DR PDBsum; 2MW8; -. DR PDBsum; 2O49; -. DR PDBsum; 2O4A; -. DR PDBsum; 3NZL; -. DR PDBsum; 3TUO; -. DR PDBsum; 6LFF; -. DR AlphaFoldDB; Q01826; -. DR BMRB; Q01826; -. DR SMR; Q01826; -. DR BioGRID; 112211; 107. DR DIP; DIP-48757N; -. DR IntAct; Q01826; 68. DR MINT; Q01826; -. DR STRING; 9606.ENSP00000399518; -. DR GlyCosmos; Q01826; 2 sites, 2 glycans. DR GlyGen; Q01826; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q01826; -. DR MetOSite; Q01826; -. DR PhosphoSitePlus; Q01826; -. DR BioMuta; SATB1; -. DR DMDM; 417747; -. DR EPD; Q01826; -. DR jPOST; Q01826; -. DR MassIVE; Q01826; -. DR MaxQB; Q01826; -. DR PaxDb; 9606-ENSP00000399518; -. DR PeptideAtlas; Q01826; -. DR ProteomicsDB; 58001; -. [Q01826-1] DR ProteomicsDB; 58002; -. [Q01826-2] DR Pumba; Q01826; -. DR Antibodypedia; 11251; 656 antibodies from 44 providers. DR DNASU; 6304; -. DR Ensembl; ENST00000338745.11; ENSP00000341024.5; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000415069.6; ENSP00000390529.2; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000417717.6; ENSP00000399518.1; ENSG00000182568.18. [Q01826-2] DR Ensembl; ENST00000454909.6; ENSP00000399708.2; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000457005.6; ENSP00000398072.2; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000700177.1; ENSP00000514845.1; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000700178.1; ENSP00000514846.1; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000700179.1; ENSP00000514847.1; ENSG00000182568.18. [Q01826-1] DR Ensembl; ENST00000700180.1; ENSP00000514848.1; ENSG00000182568.18. [Q01826-1] DR GeneID; 6304; -. DR KEGG; hsa:6304; -. DR MANE-Select; ENST00000338745.11; ENSP00000341024.5; NM_002971.6; NP_002962.1. DR UCSC; uc003cbh.4; human. [Q01826-1] DR AGR; HGNC:10541; -. DR CTD; 6304; -. DR DisGeNET; 6304; -. DR GeneCards; SATB1; -. DR HGNC; HGNC:10541; SATB1. DR HPA; ENSG00000182568; Group enriched (lymphoid tissue, skeletal muscle). DR MalaCards; SATB1; -. DR MIM; 602075; gene. DR MIM; 619228; phenotype. DR MIM; 619229; phenotype. DR neXtProt; NX_Q01826; -. DR OpenTargets; ENSG00000182568; -. DR Orphanet; 528084; Non-specific syndromic intellectual disability. DR PharmGKB; PA34951; -. DR VEuPathDB; HostDB:ENSG00000182568; -. DR eggNOG; KOG3755; Eukaryota. DR GeneTree; ENSGT00390000008096; -. DR HOGENOM; CLU_012559_1_0_1; -. DR InParanoid; Q01826; -. DR OMA; SGHLMKS; -. DR OrthoDB; 2969903at2759; -. DR PhylomeDB; Q01826; -. DR TreeFam; TF332714; -. DR PathwayCommons; Q01826; -. DR Reactome; R-HSA-111465; Apoptotic cleavage of cellular proteins. DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins. DR SignaLink; Q01826; -. DR SIGNOR; Q01826; -. DR BioGRID-ORCS; 6304; 18 hits in 1170 CRISPR screens. DR ChiTaRS; SATB1; human. DR EvolutionaryTrace; Q01826; -. DR GeneWiki; SATB1; -. DR GenomeRNAi; 6304; -. DR Pharos; Q01826; Tbio. DR PRO; PR:Q01826; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q01826; Protein. DR Bgee; ENSG00000182568; Expressed in orbitofrontal cortex and 220 other cell types or tissues. DR ExpressionAtlas; Q01826; baseline and differential. DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0016605; C:PML body; IDA:UniProtKB. DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB. DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IDA:NTNU_SB. DR GO; GO:0003690; F:double-stranded DNA binding; TAS:ProtInc. 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:0043565; F:sequence-specific DNA binding; IDA:NTNU_SB. DR GO; GO:0006325; P:chromatin organization; TAS:ProtInc. DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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; Q01826; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Alternative splicing; Chromatin regulator; KW Chromosomal rearrangement; Disease variant; DNA-binding; Homeobox; KW Host-virus interaction; Intellectual disability; Isopeptide bond; Nucleus; KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; KW Transcription regulation; Ubl conjugation. FT CHAIN 1..763 FT /note="DNA-binding protein SATB1" FT /id="PRO_0000202398" 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 645..704 FT /note="Homeobox" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108" FT REGION 1..54 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 224..278 FT /note="Nuclear matrix targeting sequence (NMTS)" FT REGION 266..307 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 591..649 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 20..40 FT /note="Nuclear localization signal" FT /evidence="ECO:0000269|PubMed:15970696" FT MOTIF 139..143 FT /note="Protein interaction" FT COMPBIAS 266..299 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 591..606 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 607..629 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 BINDING 400..410 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_part="matrix attachment region (MAR) of DNA" FT BINDING 425 FT /ligand="DNA" FT /ligand_id="ChEBI:CHEBI:16991" FT /ligand_part="matrix attachment region (MAR) of DNA" FT SITE 254..255 FT /note="Cleavage; by caspases" FT MOD_RES 136 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:16630892" FT MOD_RES 185 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:16630892" FT MOD_RES 637 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q60611" FT CROSSLNK 51 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 744 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000269|PubMed:18408014" FT VAR_SEQ 592 FT /note="I -> IQSPSPTTLGKGESRGVFLPGLPTPAPWLGAAP (in isoform FT 2)" FT /evidence="ECO:0000303|Ref.3" FT /id="VSP_038296" FT VARIANT 181 FT /note="P -> L (in DHDBV; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085437" FT VARIANT 323 FT /note="M -> V (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085438" FT VARIANT 366 FT /note="S -> L (no effect on DNA-binding or transcriptional FT repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085439" FT VARIANT 402 FT /note="Q -> R (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085440" FT VARIANT 407 FT /note="E -> G (in DHDBV; stabilized DNA-binding and FT increased transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085441" FT VARIANT 407 FT /note="E -> Q (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085442" FT VARIANT 410..763 FT /note="Missing (in DEFDA; reduced transcriptional FT repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085443" FT VARIANT 413 FT /note="E -> K (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085444" FT VARIANT 420 FT /note="Q -> R (in DHDBV; stabilized DNA-binding and FT increased transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085445" FT VARIANT 519 FT /note="V -> L (no effect on DNA-binding or transcriptional FT repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085446" FT VARIANT 525 FT /note="Q -> R (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085447" FT VARIANT 530 FT /note="E -> G (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085448" FT VARIANT 530 FT /note="E -> K (in DHDBV; stabilized DNA-binding and FT increased transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085449" FT VARIANT 530 FT /note="E -> Q (in DHDBV; stabilized DNA-binding and FT increased transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085450" FT VARIANT 547 FT /note="E -> K (in DHDBV; stabilized DNA-binding and FT increased transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085451" FT VARIANT 573 FT /note="A -> T (no effect on DNA-binding or transcriptional FT repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085452" FT VARIANT 577 FT /note="H -> R (in DHDBV)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085453" FT VARIANT 619 FT /note="Q -> R (in DHDBV; uncertain significance)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085454" FT VARIANT 682 FT /note="L -> V (in DHDBV; uncertain significance; no effect FT on DNA-binding or transcriptional repression)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085455" FT VARIANT 694..763 FT /note="Missing (in DEFDA; altered subcellular localization FT forming nuclear puncta; reduced transcriptional repression FT of some target genes)" FT /evidence="ECO:0000269|PubMed:33513338" FT /id="VAR_085456" FT MUTAGEN 29 FT /note="K->A: Loss of nuclear localization, cytoplasmic." FT /evidence="ECO:0000269|PubMed:15970696" FT MUTAGEN 32 FT /note="R->A: Loss of nuclear localization, cytoplasmic." FT /evidence="ECO:0000269|PubMed:15970696" FT MUTAGEN 34 FT /note="E->A: Normal nuclear localization." FT /evidence="ECO:0000269|PubMed:15970696" FT MUTAGEN 36 FT /note="N->A: Normal nuclear localization." FT /evidence="ECO:0000269|PubMed:15970696" FT MUTAGEN 136 FT /note="K->A,Q,R: No acetylation." FT /evidence="ECO:0000269|PubMed:16630892, FT ECO:0000269|PubMed:19103759" FT MUTAGEN 185 FT /note="S->A: No phosphorylation." FT /evidence="ECO:0000269|PubMed:16630892" FT MUTAGEN 254 FT /note="D->A: CASP6-resistant." FT /evidence="ECO:0000269|PubMed:11463840" FT MUTAGEN 373 FT /note="S->A: Slightly reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 380 FT /note="R->N: Reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 384 FT /note="K->N: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 395 FT /note="R->N: Reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 402 FT /note="Q->A: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:17652321" FT MUTAGEN 403 FT /note="G->A: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:17652321" FT MUTAGEN 406 FT /note="S->A: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 410 FT /note="R->N: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 411 FT /note="K->R: Normal sumoylation." FT /evidence="ECO:0000269|PubMed:18408014" FT MUTAGEN 416 FT /note="K->N: Impaired MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 427 FT /note="R->N: Reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 442 FT /note="R->N: Reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 451 FT /note="S->A: Slightly reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 475 FT /note="K->N: Reduced MAR-DNA-binding." FT /evidence="ECO:0000269|PubMed:16371359" FT MUTAGEN 486 FT /note="K->R: Normal sumoylation." FT /evidence="ECO:0000269|PubMed:18408014" FT MUTAGEN 646 FT /note="R->A: Reduced interaction with matrix attachment FT region (MAR) DNA; when associated with A-648." FT /evidence="ECO:0000269|PubMed:9111059" FT MUTAGEN 648 FT /note="R->A: Reduced interaction with matrix attachment FT region (MAR) DNA; when associated with A-646." FT /evidence="ECO:0000269|PubMed:9111059" FT MUTAGEN 693..695 FT /note="FQN->AAA: Reduced interaction with matrix attachment FT region (MAR) DNA." FT /evidence="ECO:0000269|PubMed:9111059" FT MUTAGEN 720 FT /note="K->R: Normal sumoylation." FT /evidence="ECO:0000269|PubMed:18408014" FT MUTAGEN 744 FT /note="K->R: Loss of sumoylation." FT /evidence="ECO:0000269|PubMed:18408014" FT STRAND 72..83 FT /evidence="ECO:0007829|PDB:3TUO" FT STRAND 92..102 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 107..109 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 110..117 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 122..127 FT /evidence="ECO:0007829|PDB:3TUO" FT STRAND 129..134 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 142..144 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 153..157 FT /evidence="ECO:0007829|PDB:3TUO" FT TURN 158..163 FT /evidence="ECO:0007829|PDB:3TUO" FT STRAND 164..169 FT /evidence="ECO:0007829|PDB:3TUO" FT HELIX 181..183 FT /evidence="ECO:0007829|PDB:3NZL" FT HELIX 186..196 FT /evidence="ECO:0007829|PDB:3NZL" FT TURN 197..199 FT /evidence="ECO:0007829|PDB:3NZL" FT HELIX 202..208 FT /evidence="ECO:0007829|PDB:3NZL" FT STRAND 209..211 FT /evidence="ECO:0007829|PDB:3NZL" FT HELIX 213..221 FT /evidence="ECO:0007829|PDB:3NZL" FT HELIX 230..245 FT /evidence="ECO:0007829|PDB:3NZL" FT HELIX 375..386 FT /evidence="ECO:0007829|PDB:2O4A" FT HELIX 390..398 FT /evidence="ECO:0007829|PDB:2O4A" FT HELIX 402..411 FT /evidence="ECO:0007829|PDB:2O4A" FT HELIX 415..417 FT /evidence="ECO:0007829|PDB:2O49" FT HELIX 420..433 FT /evidence="ECO:0007829|PDB:2O4A" FT HELIX 437..452 FT /evidence="ECO:0007829|PDB:2O4A" FT HELIX 653..665 FT /evidence="ECO:0007829|PDB:2MW8" FT HELIX 672..681 FT /evidence="ECO:0007829|PDB:2MW8" FT HELIX 687..702 FT /evidence="ECO:0007829|PDB:2MW8" SQ SEQUENCE 763 AA; 85957 MW; D4FE09B09FB7683B CRC64; MDHLNEATQG KEHSEMSNNV SDPKGPPAKI ARLEQNGSPL GRGRLGSTGA 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 APLISTPPSR PPQVKTATIA TERNGKPENN TMNINASIYD EIQQEMKRAK VSQALFAKVA ATKSQGWLCE LLRWKEDPSP ENRTLWENLS MIRRFLSLPQ PERDAIYEQE SNAVHHHGDR PPHIIHVPAE QIQQQQQQQQ QQQQQQQAPP PPQPQQQPQT GPRLPPRQPT VASPAESDEE NRQKTRPRTK ISVEALGILQ SFIQDVGLYP DEEAIQTLSA QLDLPKYTII KFFQNQRYYL KHHGKLKDNS GLEVDVAEYK EEELLKDLEE SVQDKNTNTL FSVKLEEELS VEGNTDINTD LKD //