SATB1_HUMAN
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 03-AUG-2022, entry version 207.
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 KTZSL 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 KTZSL 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: Kohlschutter-Tonz syndrome-like (KTZSL) [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. KTZSL 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="http://atlasgeneticsoncology.org/Genes/SATB1ID44225ch3p24.html";
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; 99.
DR DIP; DIP-48757N; -.
DR IntAct; Q01826; 67.
DR MINT; Q01826; -.
DR STRING; 9606.ENSP00000399518; -.
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 PeptideAtlas; Q01826; -.
DR PRIDE; Q01826; -.
DR ProteomicsDB; 58001; -. [Q01826-1]
DR ProteomicsDB; 58002; -. [Q01826-2]
DR Antibodypedia; 11251; 520 antibodies from 44 providers.
DR DNASU; 6304; -.
DR Ensembl; ENST00000338745.11; ENSP00000341024.5; ENSG00000182568.17. [Q01826-1]
DR Ensembl; ENST00000417717.6; ENSP00000399518.1; ENSG00000182568.17. [Q01826-2]
DR Ensembl; ENST00000454909.6; ENSP00000399708.2; ENSG00000182568.17. [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 CTD; 6304; -.
DR DisGeNET; 6304; -.
DR GeneCards; SATB1; -.
DR HGNC; HGNC:10541; SATB1.
DR HPA; ENSG00000182568; Tissue enriched (lymphoid).
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; DVADYKD; -.
DR OrthoDB; 204499at2759; -.
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; 17 hits in 1091 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 218 other tissues.
DR ExpressionAtlas; Q01826; baseline and differential.
DR Genevisible; Q01826; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
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; 1.10.260.40; -; 2.
DR Gene3D; 1.10.260.70; -; 1.
DR Gene3D; 3.10.20.710; -; 1.
DR InterPro; IPR003350; CUT_dom.
DR InterPro; IPR032355; CUTL.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR010982; Lambda_DNA-bd_dom_sf.
DR InterPro; IPR039673; SATB1/SATB2.
DR InterPro; IPR038216; SATB_CUTL_sf.
DR InterPro; IPR038224; SATB_ULD_sf.
DR InterPro; IPR032392; ULD.
DR PANTHER; PTHR15116; PTHR15116; 1.
DR Pfam; PF02376; CUT; 2.
DR Pfam; PF16557; CUTL; 1.
DR Pfam; PF00046; Homeodomain; 1.
DR Pfam; PF16534; ULD; 1.
DR SMART; SM01109; CUT; 2.
DR SMART; SM00389; HOX; 1.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF47413; SSF47413; 2.
DR PROSITE; PS51042; CUT; 2.
DR PROSITE; PS51983; CUTL; 1.
DR PROSITE; PS50071; HOMEOBOX_2; 1.
DR PROSITE; PS51982; ULD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; 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 KTZSL; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085437"
FT VARIANT 323
FT /note="M -> V (in KTZSL)"
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 KTZSL)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085440"
FT VARIANT 407
FT /note="E -> G (in KTZSL; 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 KTZSL)"
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 KTZSL)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085444"
FT VARIANT 420
FT /note="Q -> R (in KTZSL; 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 KTZSL)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085447"
FT VARIANT 530
FT /note="E -> G (in KTZSL)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085448"
FT VARIANT 530
FT /note="E -> K (in KTZSL; 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 KTZSL; 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 KTZSL; 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 KTZSL)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085453"
FT VARIANT 619
FT /note="Q -> R (in KTZSL; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:33513338"
FT /id="VAR_085454"
FT VARIANT 682
FT /note="L -> V (in KTZSL; unknown pathological significance;
FT no effect 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
