ZFHX3_HUMAN
ID ZFHX3_HUMAN Reviewed; 3703 AA.
AC Q15911; D3DWS8; O15101; Q13719; Q6ZP98;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 206.
DE RecName: Full=Zinc finger homeobox protein 3;
DE AltName: Full=AT motif-binding factor 1;
DE AltName: Full=AT-binding transcription factor 1;
DE AltName: Full=Alpha-fetoprotein enhancer-binding protein;
DE AltName: Full=Zinc finger homeodomain protein 3;
DE Short=ZFH-3;
GN Name=ZFHX3; Synonyms=ATBF1, C16orf47 {ECO:0000312|HGNC:HGNC:777};
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 A), AND VARIANTS ALA-72 AND ALA-777.
RC TISSUE=Lung;
RX PubMed=7592926; DOI=10.1074/jbc.270.45.26840;
RA Miura Y., Tam T., Ido A., Morinaga T., Miki T., Hashimoto T., Tamaoki T.;
RT "Cloning and characterization of an ATBF1 isoform that expresses in a
RT neuronal differentiation-dependent manner.";
RL J. Biol. Chem. 270:26840-26848(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RC TISSUE=Hepatoma;
RX PubMed=1719379; DOI=10.1128/mcb.11.12.6041-6049.1991;
RA Morinaga T., Yasuda H., Higashio K., Tamaoki T.;
RT "A human alpha-fetoprotein enhancer-binding protein, ATBF1, contains four
RT homeodomains and seventeen zinc fingers.";
RL Mol. Cell. Biol. 11:6041-6049(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-1190 (ISOFORM A), AND
RP VARIANT SER-997.
RX PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA Adams M.D.;
RT "Genome duplications and other features in 12 Mb of DNA sequence from human
RT chromosome 16p and 16q.";
RL Genomics 60:295-308(1999).
RN [7]
RP FUNCTION AS REGULATOR OF MYOBLASTS DIFFERENTIATION.
RX PubMed=11312261; DOI=10.1074/jbc.m010378200;
RA Berry F.B., Miura Y., Mihara K., Kaspar P., Sakata N.,
RA Hashimoto-Tamaoki T., Tamaoki T.;
RT "Positive and negative regulation of myogenic differentiation of C2C12
RT cells by isoforms of the multiple homeodomain zinc finger transcription
RT factor ATBF1.";
RL J. Biol. Chem. 276:25057-25065(2001).
RN [8]
RP INTERACTION WITH PIAS3.
RX PubMed=14715251; DOI=10.1016/j.bbrc.2003.12.054;
RA Nojiri S., Joh T., Miura Y., Sakata N., Nomura T., Nakao H., Sobue S.,
RA Ohara H., Asai K., Ito M.;
RT "ATBF1 enhances the suppression of STAT3 signaling by interaction with
RT PIAS3.";
RL Biochem. Biophys. Res. Commun. 314:97-103(2004).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-571, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [10]
RP FUNCTION IN GASTRIC CANCER, AND TISSUE SPECIFICITY.
RX PubMed=17330845; DOI=10.1002/ijc.22654;
RA Mori Y., Kataoka H., Miura Y., Kawaguchi M., Kubota E., Ogasawara N.,
RA Oshima T., Tanida S., Sasaki M., Ohara H., Mizoshita T., Tatematsu M.,
RA Asai K., Joh T.;
RT "Subcellular localization of ATBF1 regulates MUC5AC transcription in
RT gastric cancer.";
RL Int. J. Cancer 121:241-247(2007).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1197, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP ASSOCIATION WITH ATRIAL FIBRILLATION AND ISCHEMIC STROKE.
RX PubMed=19597491; DOI=10.1038/ng.417;
RA Gudbjartsson D.F., Holm H., Gretarsdottir S., Thorleifsson G.,
RA Walters G.B., Thorgeirsson G., Gulcher J., Mathiesen E.B., Njolstad I.,
RA Nyrnes A., Wilsgaard T., Hald E.M., Hveem K., Stoltenberg C., Kucera G.,
RA Stubblefield T., Carter S., Roden D., Ng M.C.Y., Baum L., So W.Y.,
RA Wong K.S., Chan J.C.N., Gieger C., Wichmann H.-E., Gschwendtner A.,
RA Dichgans M., Kuhlenbaeumer G., Berger K., Ringelstein E.B., Bevan S.,
RA Markus H.S., Kostulas K., Hillert J., Sveinbjoernsdottir S.,
RA Valdimarsson E.M., Lochen M.-L., Ma R.C.W., Darbar D., Kong A., Arnar D.O.,
RA Thorsteinsdottir U., Stefansson K.;
RT "A sequence variant in ZFHX3 on 16q22 associates with atrial fibrillation
RT and ischemic stroke.";
RL Nat. Genet. 41:876-878(2009).
RN [15]
RP ASSOCIATION WITH ATRIAL FIBRILLATION.
RX PubMed=19597492; DOI=10.1038/ng.416;
RA Benjamin E.J., Rice K.M., Arking D.E., Pfeufer A., van Noord C.,
RA Smith A.V., Schnabel R.B., Bis J.C., Boerwinkle E., Sinner M.F.,
RA Dehghan A., Lubitz S.A., D'Agostino R.B. Sr., Lumley T., Ehret G.B.,
RA Heeringa J., Aspelund T., Newton-Cheh C., Larson M.G., Marciante K.D.,
RA Soliman E.Z., Rivadeneira F., Wang T.J., Eiriksdottir G., Levy D.,
RA Psaty B.M., Li M., Chamberlain A.M., Hofman A., Vasan R.S., Harris T.B.,
RA Rotter J.I., Kao W.H., Agarwal S.K., Stricker B.H.C., Wang K., Launer L.J.,
RA Smith N.L., Chakravarti A., Uitterlinden A.G., Wolf P.A., Sotoodehnia N.,
RA Koettgen A., van Duijn C.M., Meitinger T., Mueller M., Perz S.,
RA Steinbeck G., Wichmann H.-E., Lunetta K.L., Heckbert S.R., Gudnason V.,
RA Alonso A., Kaab S., Ellinor P.T., Witteman J.C.M.;
RT "Variants in ZFHX3 are associated with atrial fibrillation in individuals
RT of European ancestry.";
RL Nat. Genet. 41:879-881(2009).
RN [16]
RP FUNCTION, INTERACTION WITH RUNX3, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=20599712; DOI=10.1016/j.bbrc.2010.06.090;
RA Mabuchi M., Kataoka H., Miura Y., Kim T.S., Kawaguchi M., Ebi M.,
RA Tanaka M., Mori Y., Kubota E., Mizushima T., Shimura T., Mizoshita T.,
RA Tanida S., Kamiya T., Asai K., Joh T.;
RT "Tumor suppressor, AT motif binding factor 1 (ATBF1), translocates to the
RT nucleus with runt domain transcription factor 3 (RUNX3) in response to TGF-
RT beta signal transduction.";
RL Biochem. Biophys. Res. Commun. 398:321-325(2010).
RN [17]
RP FUNCTION, INTERACTION WITH ESR1, AND TISSUE SPECIFICITY.
RX PubMed=20720010; DOI=10.1074/jbc.m110.128330;
RA Dong X.Y., Sun X., Guo P., Li Q., Sasahara M., Ishii Y., Dong J.T.;
RT "ATBF1 inhibits estrogen receptor (ER) function by selectively competing
RT with AIB1 for binding to the ER in ER-positive breast cancer cells.";
RL J. Biol. Chem. 285:32801-32809(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533 AND SER-571, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [19]
RP UBIQUITINATION, PROTEASOMAL DEGRADATION, AND INTERACTION WITH TRIM25.
RX PubMed=22452784; DOI=10.1042/bj20111890;
RA Dong X.Y., Fu X., Fan S., Guo P., Su D., Dong J.T.;
RT "Oestrogen causes ATBF1 protein degradation through the oestrogen-
RT responsive E3 ubiquitin ligase EFP.";
RL Biochem. J. 444:581-590(2012).
RN [20]
RP INTERACTION WITH ALKBH4.
RX PubMed=23145062; DOI=10.1371/journal.pone.0049045;
RA Bjornstad L.G., Meza T.J., Otterlei M., Olafsrud S.M., Meza-Zepeda L.A.,
RA Falnes P.O.;
RT "Human ALKBH4 interacts with proteins associated with transcription.";
RL PLoS ONE 7:E49045-E49045(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-426; SER-571; SER-1204;
RP SER-2795; SER-2896 AND SER-3432, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [23]
RP FUNCTION, AND INTERACTION WITH SMAD2 AND SMAD3.
RX PubMed=25105025; DOI=10.1155/2014/970346;
RA Sakata N., Kaneko S., Ikeno S., Miura Y., Nakabayashi H., Dong X.Y.,
RA Dong J.T., Tamaoki T., Nakano N., Itoh S.;
RT "TGF-beta signaling cooperates with AT motif-binding factor-1 for
RT repression of the alpha -fetoprotein promoter.";
RL J. Signal Transduct. 2014:970346-970346(2014).
RN [24]
RP SUMOYLATION AT LYS-2349; LYS-2806 AND LYS-3258, SUBCELLULAR LOCATION,
RP NUCLEAR LOCALIZATION SIGNAL, AND MUTAGENESIS OF 2615-LYS--LYS-2617;
RP LYS-2349; LYS-2806 AND LYS-3258.
RX PubMed=24651376; DOI=10.1371/journal.pone.0092746;
RA Sun X., Li J., Dong F.N., Dong J.T.;
RT "Characterization of nuclear localization and SUMOylation of the ATBF1
RT transcription factor in epithelial cells.";
RL PLoS ONE 9:E92746-E92746(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2806, 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 [26]
RP STRUCTURE BY NMR OF 2241-2305 AND 2629-2698.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the second and third homeobox domain of AT-binding
RT transcription factor 1 (ATBF1).";
RL Submitted (JUN-2006) to the PDB data bank.
CC -!- FUNCTION: Transcriptional regulator which can act as an activator or a
CC repressor. Inhibits the enhancer element of the AFP gene by binding to
CC its AT-rich core sequence. In concert with SMAD-dependent TGF-beta
CC signaling can repress the transcription of AFP via its interaction with
CC SMAD2/3 (PubMed:25105025). Regulates the circadian locomotor rhythms
CC via transcriptional activation of neuropeptidergic genes which are
CC essential for intercellular synchrony and rhythm amplitude in the
CC suprachiasmatic nucleus (SCN) of the brain (By similarity). Regulator
CC of myoblasts differentiation through the binding to the AT-rich
CC sequence of MYF6 promoter and promoter repression (PubMed:11312261).
CC Down-regulates the MUC5AC promoter in gastric cancer (PubMed:17330845).
CC In association with RUNX3, up-regulates CDKN1A promoter activity
CC following TGF-beta stimulation (PubMed:20599712). Inhibits estrogen
CC receptor (ESR1) function by selectively competing with coactivator
CC NCOA3 for binding to ESR1 in ESR1-positive breast cancer cells
CC (PubMed:20720010). {ECO:0000250|UniProtKB:Q61329,
CC ECO:0000269|PubMed:11312261, ECO:0000269|PubMed:17330845,
CC ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:20720010,
CC ECO:0000269|PubMed:25105025}.
CC -!- SUBUNIT: Interacts with FNBP3 (By similarity). Interacts with ALKBH4
CC and PIAS3. Interacts with ESR1. Interacts with RUNX3. Interacts with
CC TRIM25. Interacts with SMAD2 and SMAD3. {ECO:0000250|UniProtKB:Q61329,
CC ECO:0000269|PubMed:14715251, ECO:0000269|PubMed:20599712,
CC ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:22452784,
CC ECO:0000269|PubMed:23145062, ECO:0000269|PubMed:25105025}.
CC -!- INTERACTION:
CC Q15911-2; O14503: BHLHE40; NbExp=3; IntAct=EBI-10237226, EBI-711810;
CC Q15911-2; Q9H6J7-2: C11orf49; NbExp=3; IntAct=EBI-10237226, EBI-13328871;
CC Q15911-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-10237226, EBI-739624;
CC Q15911-2; Q9NZN8: CNOT2; NbExp=3; IntAct=EBI-10237226, EBI-743033;
CC Q15911-2; Q7L5N1: COPS6; NbExp=3; IntAct=EBI-10237226, EBI-486838;
CC Q15911-2; Q05D60: DEUP1; NbExp=3; IntAct=EBI-10237226, EBI-748597;
CC Q15911-2; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-10237226, EBI-2349927;
CC Q15911-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-10237226, EBI-618309;
CC Q15911-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-10237226, EBI-5916454;
CC Q15911-2; Q15323: KRT31; NbExp=3; IntAct=EBI-10237226, EBI-948001;
CC Q15911-2; O76011: KRT34; NbExp=5; IntAct=EBI-10237226, EBI-1047093;
CC Q15911-2; Q6A162: KRT40; NbExp=3; IntAct=EBI-10237226, EBI-10171697;
CC Q15911-2; Q03252: LMNB2; NbExp=3; IntAct=EBI-10237226, EBI-2830427;
CC Q15911-2; P35548: MSX2; NbExp=3; IntAct=EBI-10237226, EBI-6447480;
CC Q15911-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-10237226, EBI-11522433;
CC Q15911-2; Q4G0R1: PIBF1; NbExp=3; IntAct=EBI-10237226, EBI-14066006;
CC Q15911-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-10237226, EBI-79165;
CC Q15911-2; P14859-6: POU2F1; NbExp=3; IntAct=EBI-10237226, EBI-11526590;
CC Q15911-2; P78424: POU6F2; NbExp=3; IntAct=EBI-10237226, EBI-12029004;
CC Q15911-2; P57052: RBM11; NbExp=3; IntAct=EBI-10237226, EBI-741332;
CC Q15911-2; Q69YQ0: SPECC1L; NbExp=3; IntAct=EBI-10237226, EBI-351113;
CC Q15911-2; O75410-7: TACC1; NbExp=3; IntAct=EBI-10237226, EBI-12007872;
CC Q15911-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-10237226, EBI-11741437;
CC Q15911-2; P14373: TRIM27; NbExp=3; IntAct=EBI-10237226, EBI-719493;
CC Q15911-2; Q9BYV2: TRIM54; NbExp=3; IntAct=EBI-10237226, EBI-2130429;
CC Q15911-2; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-10237226, EBI-11059915;
CC Q15911-2; Q5W5X9-3: TTC23; NbExp=3; IntAct=EBI-10237226, EBI-9090990;
CC Q15911-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10237226, EBI-739895;
CC Q15911-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-10237226, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20599712,
CC ECO:0000269|PubMed:24651376}. Cytoplasm {ECO:0000269|PubMed:20599712}.
CC Note=Translocates from the cytoplasm to the nucleus following TGF-beta
CC stimulation. Expressed in nuclear body (NB)-like dots in the nucleus
CC some of which overlap or closely associate with PML body.
CC {ECO:0000269|PubMed:20599712, ECO:0000269|PubMed:24651376}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A;
CC IsoId=Q15911-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q15911-2; Sequence=VSP_006825;
CC -!- TISSUE SPECIFICITY: Not found in normal gastric mucosa but found in
CC gastric carcinoma cells (at protein level). Expression is higher in ER-
CC positive breast tumors than ER-negative breast tumors (at protein
CC level). {ECO:0000269|PubMed:17330845, ECO:0000269|PubMed:20599712,
CC ECO:0000269|PubMed:20720010, ECO:0000269|PubMed:22452784}.
CC -!- PTM: Phosphorylation decreases its sensitivity to calpain-mediated
CC proteolysis. {ECO:0000250|UniProtKB:Q61329}.
CC -!- PTM: Adult brain-derived ZFHX3 is sensitive, but embryonic brain-
CC derived ZFHX3 is resistant to calpain 1-mediated proteolysis.
CC {ECO:0000250|UniProtKB:Q61329}.
CC -!- PTM: Ubiquitinated, leading to its proteasomal degradation.
CC {ECO:0000269|PubMed:22452784}.
CC -!- PTM: Nuclear localization is essential for its sumoylation.
CC {ECO:0000269|PubMed:24651376}.
CC -!- POLYMORPHISM: Genetic variations in ZFHX3 are associated with atrial
CC fibrillation and ischemic stroke in individuals of European ancestry.
CC {ECO:0000269|PubMed:19597491, ECO:0000269|PubMed:19597492}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC85221.1; Type=Miscellaneous discrepancy; Note=The sequence differs from that shown due translation of the 5'-UTR region.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/ATBF1ID357.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; L32832; AAC14462.1; -; mRNA.
DR EMBL; D10250; BAA01095.1; -; mRNA.
DR EMBL; AK129695; BAC85221.1; ALT_SEQ; mRNA.
DR EMBL; AC004943; AAC79153.1; -; Genomic_DNA.
DR EMBL; AC132068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471166; EAW59168.1; -; Genomic_DNA.
DR EMBL; CH471166; EAW59170.1; -; Genomic_DNA.
DR EMBL; AC002044; AAC31674.1; -; Genomic_DNA.
DR CCDS; CCDS10908.1; -. [Q15911-1]
DR CCDS; CCDS54035.1; -. [Q15911-2]
DR PIR; A41948; A41948.
DR RefSeq; NP_001158238.1; NM_001164766.1. [Q15911-2]
DR RefSeq; NP_008816.3; NM_006885.3. [Q15911-1]
DR RefSeq; NP_997268.1; NM_207385.1.
DR RefSeq; XP_016878717.1; XM_017023228.1.
DR RefSeq; XP_016878718.1; XM_017023229.1.
DR PDB; 2DA1; NMR; -; A=2146-2202.
DR PDB; 2DA2; NMR; -; A=2243-2299.
DR PDB; 2DA3; NMR; -; A=2632-2698.
DR PDBsum; 2DA1; -.
DR PDBsum; 2DA2; -.
DR PDBsum; 2DA3; -.
DR SMR; Q15911; -.
DR BioGRID; 106954; 81.
DR BioGRID; 132632; 1.
DR IntAct; Q15911; 53.
DR STRING; 9606.ENSP00000268489; -.
DR GlyGen; Q15911; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q15911; -.
DR PhosphoSitePlus; Q15911; -.
DR BioMuta; HGNC:28329; -.
DR BioMuta; ZFHX3; -.
DR DMDM; 108935822; -.
DR EPD; Q15911; -.
DR jPOST; Q15911; -.
DR MassIVE; Q15911; -.
DR MaxQB; Q15911; -.
DR PaxDb; Q15911; -.
DR PeptideAtlas; Q15911; -.
DR PRIDE; Q15911; -.
DR ProteomicsDB; 60814; -. [Q15911-1]
DR ProteomicsDB; 60815; -. [Q15911-2]
DR ProteomicsDB; 68069; -.
DR Antibodypedia; 16704; 98 antibodies from 26 providers.
DR DNASU; 463; -.
DR Ensembl; ENST00000268489.10; ENSP00000268489.5; ENSG00000140836.17. [Q15911-1]
DR Ensembl; ENST00000397992.5; ENSP00000438926.3; ENSG00000140836.17. [Q15911-2]
DR Ensembl; ENST00000641206.2; ENSP00000493252.1; ENSG00000140836.17. [Q15911-1]
DR GeneID; 463; -.
DR KEGG; hsa:463; -.
DR MANE-Select; ENST00000268489.10; ENSP00000268489.5; NM_006885.4; NP_008816.3.
DR UCSC; uc002fck.4; human. [Q15911-1]
DR CTD; 463; -.
DR DisGeNET; 463; -.
DR GeneCards; ZFHX3; -.
DR HGNC; HGNC:777; ZFHX3.
DR HPA; ENSG00000140836; Tissue enriched (brain).
DR MalaCards; ZFHX3; -.
DR MIM; 104155; gene.
DR neXtProt; NX_Q15911; -.
DR OpenTargets; ENSG00000140836; -.
DR PharmGKB; PA162409676; -.
DR VEuPathDB; HostDB:ENSG00000140836; -.
DR eggNOG; KOG1146; Eukaryota.
DR GeneTree; ENSGT00940000156149; -.
DR HOGENOM; CLU_000245_0_0_1; -.
DR InParanoid; Q15911; -.
DR OMA; PEQKTNA; -.
DR OrthoDB; 1502452at2759; -.
DR PhylomeDB; Q15911; -.
DR TreeFam; TF323288; -.
DR TreeFam; TF353775; -.
DR PathwayCommons; Q15911; -.
DR Reactome; R-HSA-8941855; RUNX3 regulates CDKN1A transcription.
DR SignaLink; Q15911; -.
DR SIGNOR; Q15911; -.
DR BioGRID-ORCS; 388289; 3 hits in 220 CRISPR screens.
DR BioGRID-ORCS; 463; 15 hits in 1097 CRISPR screens.
DR ChiTaRS; C16orf47; human.
DR ChiTaRS; ZFHX3; human.
DR EvolutionaryTrace; Q15911; -.
DR GeneWiki; ATBF1; -.
DR GenomeRNAi; 463; -.
DR Pharos; Q15911; Tbio.
DR PRO; PR:Q15911; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q15911; protein.
DR Bgee; ENSG00000140836; Expressed in saphenous vein and 191 other tissues.
DR Genevisible; Q15911; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0016604; C:nuclear body; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; NAS: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:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007420; P:brain development; IBA:GO_Central.
DR GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
DR GO; GO:0007517; P:muscle organ development; IEA:UniProtKB-KW.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; ISS:ARUK-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0051726; P:regulation of cell cycle; IEA:Ensembl.
DR GO; GO:1904059; P:regulation of locomotor rhythm; ISS:UniProtKB.
DR GO; GO:0045664; P:regulation of neuron differentiation; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; TAS:UniProtKB.
DR GO; GO:0071559; P:response to transforming growth factor beta; IDA:UniProtKB.
DR CDD; cd00086; homeodomain; 4.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR017970; Homeobox_CS.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00046; Homeodomain; 4.
DR Pfam; PF00096; zf-C2H2; 2.
DR SMART; SM00389; HOX; 4.
DR SMART; SM00355; ZnF_C2H2; 23.
DR SMART; SM00451; ZnF_U1; 7.
DR SUPFAM; SSF46689; SSF46689; 4.
DR SUPFAM; SSF57667; SSF57667; 6.
DR PROSITE; PS00027; HOMEOBOX_1; 2.
DR PROSITE; PS50071; HOMEOBOX_2; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 14.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cytoplasm; DNA-binding;
KW Homeobox; Isopeptide bond; Metal-binding; Myogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..3703
FT /note="Zinc finger homeobox protein 3"
FT /id="PRO_0000046930"
FT ZN_FING 79..101
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 282..305
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 640..663
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 671..694
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 726..750
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 804..828
FT /note="C2H2-type 6; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 945..968
FT /note="C2H2-type 7; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 984..1008
FT /note="C2H2-type 8; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1040..1064
FT /note="C2H2-type 9; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1088..1112
FT /note="C2H2-type 10; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1223..1246
FT /note="C2H2-type 11; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1252..1275
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1360..1385
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1401..1423
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1429..1452
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1545..1569
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1596..1620
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1983..2006
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2145..2204
FT /note="Homeobox 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT DNA_BIND 2242..2301
FT /note="Homeobox 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2328..2351
FT /note="C2H2-type 19; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 2530..2552
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2641..2700
FT /note="Homeobox 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 2711..2734
FT /note="C2H2-type 21"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 2944..3003
FT /note="Homeobox 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00108"
FT ZN_FING 3024..3048
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 3529..3553
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 588..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1148..1214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1303..1354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1490..1529
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1629..1727
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1865..1938
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2030..2082
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2204..2244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2376..2400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2422..2520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2619..2647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2771..2796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2841..2871
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2912..2947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3137..3267
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3386..3449
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3565..3703
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 2615..2617
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000269|PubMed:24651376"
FT COMPBIAS 16..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..456
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 457..491
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..511
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 520..536
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1174..1208
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1328..1344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1632..1685
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1876..1900
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2033..2077
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2436..2476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2477..2497
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2498..2520
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2771..2785
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2912..2934
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3137..3205
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3206..3225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3231..3259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3386..3400
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3413..3427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3579..3596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3606..3620
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3631..3659
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 426
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 428
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 571
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1197
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1204
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 2625
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 2786
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 2795
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 2896
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 3418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 3432
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT MOD_RES 3677
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q61329"
FT CROSSLNK 2349
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:24651376"
FT CROSSLNK 2806
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000269|PubMed:24651376"
FT CROSSLNK 2806
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 3258
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000269|PubMed:24651376"
FT VAR_SEQ 1..914
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:1719379"
FT /id="VSP_006825"
FT VARIANT 72
FT /note="S -> A (in dbSNP:rs7193297)"
FT /evidence="ECO:0000269|PubMed:7592926"
FT /id="VAR_026663"
FT VARIANT 146
FT /note="S -> G (in dbSNP:rs58480263)"
FT /id="VAR_061927"
FT VARIANT 428
FT /note="T -> P (in dbSNP:rs16971436)"
FT /id="VAR_026664"
FT VARIANT 460
FT /note="E -> Q (in dbSNP:rs2073852)"
FT /id="VAR_019968"
FT VARIANT 777
FT /note="V -> A (in dbSNP:rs4788682)"
FT /evidence="ECO:0000269|PubMed:7592926"
FT /id="VAR_026665"
FT VARIANT 997
FT /note="A -> S (in dbSNP:rs2213978)"
FT /evidence="ECO:0000269|PubMed:10493829"
FT /id="VAR_052733"
FT VARIANT 3374
FT /note="A -> V"
FT /id="VAR_011694"
FT VARIANT 3377..3384
FT /note="Missing"
FT /id="VAR_011695"
FT VARIANT 3421
FT /note="P -> A (in dbSNP:rs8044440)"
FT /id="VAR_026666"
FT VARIANT 3527
FT /note="G -> GGG"
FT /id="VAR_011696"
FT MUTAGEN 2349
FT /note="K->A: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:24651376"
FT MUTAGEN 2615..2617
FT /note="KRK->AAA: Loss of nuclear localization."
FT /evidence="ECO:0000269|PubMed:24651376"
FT MUTAGEN 2806
FT /note="K->A: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:24651376"
FT MUTAGEN 3258
FT /note="K->A: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:24651376"
FT CONFLICT 422
FT /note="P -> A (in Ref. 1; AAC14462)"
FT /evidence="ECO:0000305"
FT CONFLICT 579
FT /note="A -> T (in Ref. 1; AAC14462)"
FT /evidence="ECO:0000305"
FT CONFLICT 767
FT /note="S -> I (in Ref. 1; AAC14462)"
FT /evidence="ECO:0000305"
FT CONFLICT 846..849
FT /note="RHLG -> HHRV (in Ref. 1; AAC14462)"
FT /evidence="ECO:0000305"
FT CONFLICT 1150..1190
FT /note="EEAIEDVEGPSETAADPEELAKDQEGGASSSQAEKELTDSP -> GEWSHRH
FT GRPRLGLGVHLLETSRGLLFEGDVTDPAGPHVPY (in Ref. 6; AAC31674)"
FT /evidence="ECO:0000305"
FT HELIX 2154..2166
FT /evidence="ECO:0007829|PDB:2DA1"
FT HELIX 2174..2182
FT /evidence="ECO:0007829|PDB:2DA1"
FT HELIX 2186..2201
FT /evidence="ECO:0007829|PDB:2DA1"
FT HELIX 2251..2263
FT /evidence="ECO:0007829|PDB:2DA2"
FT HELIX 2269..2278
FT /evidence="ECO:0007829|PDB:2DA2"
FT HELIX 2283..2297
FT /evidence="ECO:0007829|PDB:2DA2"
FT TURN 2650..2652
FT /evidence="ECO:0007829|PDB:2DA3"
FT HELIX 2653..2662
FT /evidence="ECO:0007829|PDB:2DA3"
FT HELIX 2668..2678
FT /evidence="ECO:0007829|PDB:2DA3"
FT HELIX 2682..2697
FT /evidence="ECO:0007829|PDB:2DA3"
SQ SEQUENCE 3703 AA; 404419 MW; 395F5D14A08112CB CRC64;
MEGCDSPVVS GKDNGCGIPQ HQQWTELNST HLPDKPSSME QSTGESHGPL DSLRAPFNER
LAESTASAGP PSEPASKEVT CNECSASFAS LQTYMEHHCP SARPPPPLRE ESASDTGEEG
DEESDVENLA GEIVYQPDGS AYIVESLSQL TQGGGACGSG SGSGPLPSLF LNSLPGAGGK
QGDPSCAAPV YPQIINTFHI ASSFGKWFEG PDQAFPNTSA LAGLSPVLHS FRVFDVRHKS
NKDYLNSDGS AKSSCVSKDV PNNVDLSKFD GFVLYGKRKP ILMCFLCKLS FGYVRSFVTH
AVHDHRMTLS EDERKILSNK NISAIIQGIG KDKEPLVSFL EPKNKNFQHP LVSTANLIGP
GHSFYGKFSG IRMEGEEALP AGSAAGPEQP QAGLLTPSTL LNLGGLTSSV LKTPITSVPL
GPLASSPTKS SEGKDSGAAE GEKQEVGDGD CFSEKVEPAE EEAEEEEEEE EAEEEEEEEE
EEEEEEEDEG CKGLFPSELD EELEDRPHEE PGAAAGSSSK KDLALSNQSI SNSPLMPNVL
QTLSRGTAST SSNSASSFVV FDGANRRNRL SFNSEGVRAN VAEGGRRLDF ADESANKDNA
TAPEPNESTE GDDGGFVPHH QHAGSLCELG VGECPSGSGV ECPKCDTVLG SSRSLGGHMT
MMHSRNSCKT LKCPKCNWHY KYQQTLEAHM KEKHPEPGGS CVYCKSGQPH PRLARGESYT
CGYKPFRCEV CNYSTTTKGN LSIHMQSDKH LNNMQNLQNG GGEQVFSHTA GAAAAAVAAA
AAAANISSSC GAPSPTKPKT KPTWRCEVCD YETNVARNLR IHMTSEKHMH NMMLLQQNMT
QIQHNRHLGL GSLPSPAEAE LYQYYLAQNM NLPNLKMDSA ASDAQFMMSG FQLDPAGPMA
AMTPALVGGE IPLDMRLGGG QLVSEELMNL GESFIQTNDP SLKLFQCAVC NKFTTDNLDM
LGLHMNVERS LSEDEWKAVM GDSYQCKLCR YNTQLKANFQ LHCKTDKHVQ KYQLVAHIKE
GGKANEWRLK CVAIGNPVHL KCNACDYYTN SLEKLRLHTV NSRHEASLKL YKHLQQHESG
VEGESCYYHC VLCNYSTKAK LNLIQHVRSM KHQRSESLRK LQRLQKGLPE EDEDLGQIFT
IRRCPSTDPE EAIEDVEGPS ETAADPEELA KDQEGGASSS QAEKELTDSP ATSKRISFPG
SSESPLSSKR PKTAEEIKPE QMYQCPYCKY SNADVNRLRV HAMTQHSVQP MLRCPLCQDM
LNNKIHLQLH LTHLHSVAPD CVEKLIMTVT TPEMVMPSSM FLPAAVPDRD GNSNLEEAGK
QPETSEDLGK NILPSASTEQ SGDLKPSPAD PGSVREDSGF ICWKKGCNQV FKTSAALQTH
FNEVHAKRPQ LPVSDRHVYK YRCNQCSLAF KTIEKLQLHS QYHVIRAATM CCLCQRSFRT
FQALKKHLET SHLELSEADI QQLYGGLLAN GDLLAMGDPT LAEDHTIIVE EDKEEESDLE
DKQSPTGSDS GSVQEDSGSE PKRALPFRKG PNFTMEKFLD PSRPYKCTVC KESFTQKNIL
LVHYNSVSHL HKLKRALQES ATGQPEPTSS PDNKPFKCNT CNVAYSQSST LEIHMRSVLH
QTKARAAKLE AASGSSNGTG NSSSISLSSS TPSPVSTSGS NTFTTSNPSS AGIAPSSNLL
SQVPTESVGM PPLGNPIGAN IASPSEPKEA NRKKLADMIA SRQQQQQQQQ QQQQQQQQQQ
QAQTLAQAQA QVQAHLQQEL QQQAALIQSQ LFNPTLLPHF PMTTETLLQL QQQQHLLFPF
YIPSAEFQLN PEVSLPVTSG ALTLTGTGPG LLEDLKAQVQ VPQQSHQQIL PQQQQNQLSI
AQSHSALLQP SQHPEKKNKL VIKEKEKESQ RERDSAEGGE GNTGPKETLP DALKAKEKKE
LAPGGGSEPS MLPPRIASDA RGNATKALLE NFGFELVIQY NENKQKVQKK NGKTDQGENL
EKLECDSCGK LFSNILILKS HQEHVHQNYF PFKQLERFAK QYRDHYDKLY PLRPQTPEPP
PPPPPPPPPP LPAAPPQPAS TPAIPASAPP ITSPTIAPAQ PSVPLTQLSM PMELPIFSPL
MMQTMPLQTL PAQLPPQLGP VEPLPADLAQ LYQHQLNPTL LQQQNKRPRT RITDDQLRVL
RQYFDINNSP SEEQIKEMAD KSGLPQKVIK HWFRNTLFKE RQRNKDSPYN FSNPPITSLE
ELKIDSRPPS PEPPKQEYWG SKRSSRTRFT DYQLRVLQDF FDANAYPKDD EFEQLSNLLN
LPTRVIVVWF QNARQKARKN YENQGEGKDG ERRELTNDRY IRTSNLNYQC KKCSLVFQRI
FDLIKHQKKL CYKDEDEEGQ DDSQNEDSMD AMEILTPTSS SCSTPMPSQA YSAPAPSANN
TASSAFLQLT AEAEELATFN SKTEAGDEKP KLAEAPSAQP NQTQEKQGQP KPELQQQEQP
EQKTNTPQQK LPQLVSLPSL PQPPPQAPPP QCPLPQSSPS PSQLSHLPLK PLHTSTPQQL
ANLPPQLIPY QCDQCKLAFP SFEHWQEHQQ LHFLSAQNQF IHPQFLDRSL DMPFMLFDPS
NPLLASQLLS GAIPQIPASS ATSPSTPTST MNTLKRKLEE KASASPGEND SGTGGEEPQR
DKRLRTTITP EQLEILYQKY LLDSNPTRKM LDHIAHEVGL KKRVVQVWFQ NTRARERKGQ
FRAVGPAQAH RRCPFCRALF KAKTALEAHI RSRHWHEAKR AGYNLTLSAM LLDCDGGLQM
KGDIFDGTSF SHLPPSSSDG QGVPLSPVSK TMELSPRTLL SPSSIKVEGI EDFESPSMSS
VNLNFDQTKL DNDDCSSVNT AITDTTTGDE GNADNDSATG IATETKSSSA PNEGLTKAAM
MAMSEYEDRL SSGLVSPAPS FYSKEYDNEG TVDYSETSSL ADPCSPSPGA SGSAGKSGDS
GDRPGQKRFR TQMTNLQLKV LKSCFNDYRT PTMLECEVLG NDIGLPKRVV QVWFQNARAK
EKKSKLSMAK HFGINQTSYE GPKTECTLCG IKYSARLSVR DHIFSQQHIS KVKDTIGSQL
DKEKEYFDPA TVRQLMAQQE LDRIKKANEV LGLAAQQQGM FDNTPLQALN LPTAYPALQG
IPPVLLPGLN SPSLPGFTPS NTALTSPKPN LMGLPSTTVP SPGLPTSGLP NKPSSASLSS
PTPAQATMAM GPQQPPQQQQ QQQQPQVQQP PPPPAAQPPP TPQLPLQQQQ QRKDKDSEKV
KEKEKAHKGK GEPLPVPKKE KGEAPTATAA TISAPLPTME YAVDPAQLQA LQAALTSDPT
ALLTSQFLPY FVPGFSPYYA PQIPGALQSG YLQPMYGMEG LFPYSPALSQ ALMGLSPGSL
LQQYQQYQQS LQEAIQQQQQ RQLQQQQQQK VQQQQPKASQ TPVPPGAPSP DKDPAKESPK
PEEQKNTPRE VSPLLPKLPE EPEAESKSAD SLYDPFIVPK VQYKLVCRKC QAGFSDEEAA
RSHLKSLCFF GQSVVNLQEM VLHVPTGGGG GGSGGGGGGG GGGGGGGSYH CLACESALCG
EEALSQHLES ALHKHRTITR AARNAKEHPS LLPHSACFPD PSTASTSQSA AHSNDSPPPP
SAAAPSSASP HASRKSWPQV VSRASAAKPP SFPPLSSSST VTSSSCSTSG VQPSMPTDDY
SEESDTDLSQ KSDGPASPVE GPKDPSCPKD SGLTSVGTDT FRL
