ZEB1_HUMAN
ID ZEB1_HUMAN Reviewed; 1124 AA.
AC P37275; B4DJV0; B4DUW9; E9PCM7; F5H4I8; Q12924; Q13800; Q2KJ05; Q5T968;
AC Q5VZ84; Q8NB68;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=Zinc finger E-box-binding homeobox 1;
DE AltName: Full=NIL-2-A zinc finger protein;
DE AltName: Full=Negative regulator of IL2;
DE AltName: Full=Transcription factor 8;
DE Short=TCF-8;
GN Name=ZEB1; Synonyms=AREB6, TCF8;
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).
RX PubMed=8138542; DOI=10.1093/oxfordjournals.jbchem.a124267;
RA Watanabe Y., Kawakami K., Hirayama Y., Nagano K.;
RT "Transcription factors positively and negatively regulating the Na,K-ATPase
RT alpha 1 subunit gene.";
RL J. Biochem. 114:849-855(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Bachman N.J., Scarpulla R.C.;
RT "A human zinc finger homeodomain protein homologous to the chicken delta-
RT crystallin enhancer binding protein, delta EF1.";
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-798 (ISOFORM 5).
RC TISSUE=Brain, and Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 390-1124.
RX PubMed=1840704; DOI=10.1126/science.1840704;
RA Williams T.M., Moolten D., Burlein J., Romano J., Bhaerman R., Godillot A.,
RA Mellon M., Rauscher F.J. III, Kant J.A.;
RT "Identification of a zinc finger protein that inhibits IL-2 gene
RT expression.";
RL Science 254:1791-1794(1991).
RN [8]
RP INVOLVEMENT IN PPCD3.
RX PubMed=16252232; DOI=10.1086/497348;
RA Krafchak C.M., Pawar H., Moroi S.E., Sugar A., Lichter P.R., Mackey D.A.,
RA Mian S., Nairus T., Elner V., Schteingart M.T., Downs C.A., Kijek T.G.,
RA Johnson J.M., Trager E.H., Rozsa F.W., Mandal M.N.A., Epstein M.P.,
RA Vollrath D., Ayyagari R., Boehnke M., Richards J.E.;
RT "Mutations in TCF8 cause posterior polymorphous corneal dystrophy and
RT ectopic expression of COL4A3 by corneal endothelial cells.";
RL Am. J. Hum. Genet. 77:694-708(2005).
RN [9]
RP SUMOYLATION AT LYS-347 AND LYS-774.
RX PubMed=16061479; DOI=10.1074/jbc.m504477200;
RA Long J., Zuo D., Park M.;
RT "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates
RT transcriptional repression of E-cadherin.";
RL J. Biol. Chem. 280:35477-35489(2005).
RN [10]
RP IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, 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 [12]
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 [13]
RP FUNCTION.
RX PubMed=19935649; DOI=10.1038/ncb1998;
RA Wellner U., Schubert J., Burk U.C., Schmalhofer O., Zhu F., Sonntag A.,
RA Waldvogel B., Vannier C., Darling D., zur Hausen A., Brunton V.G.,
RA Morton J., Sansom O., Schuler J., Stemmler M.P., Herzberger C., Hopt U.,
RA Keck T., Brabletz S., Brabletz T.;
RT "The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-
RT inhibiting microRNAs.";
RL Nat. Cell Biol. 11:1487-1495(2009).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-679 AND THR-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP FUNCTION.
RX PubMed=20175752; DOI=10.1042/bj20091578;
RA Papadopoulou V., Postigo A., Sanchez-Tillo E., Porter A.C., Wagner S.D.;
RT "ZEB1 and CtBP form a repressive complex at a distal promoter element of
RT the BCL6 locus.";
RL Biochem. J. 427:541-550(2010).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA4, AND TISSUE
RP SPECIFICITY.
RX PubMed=20418909; DOI=10.1038/onc.2010.102;
RA Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C.,
RA Castells A., Engel P., Postigo A.;
RT "ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF
RT chromatin-remodeling protein BRG1.";
RL Oncogene 29:3490-3500(2010).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, AND IDENTIFICATION BY
RP 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 [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679 AND THR-702, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493; LYS-504 AND LYS-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493; LYS-504 AND LYS-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-493; LYS-504 AND LYS-515, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-186; LYS-195; LYS-307; LYS-331;
RP LYS-335; LYS-347; LYS-439; LYS-493; LYS-504; LYS-515; LYS-548; LYS-553 AND
RP LYS-774, AND IDENTIFICATION BY MASS 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 [25]
RP STRUCTURE BY NMR OF 583-642.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the homeobox domain from human NIL-2-A zinc finger
RT protein, transcription factor 8.";
RL Submitted (APR-2007) to the PDB data bank.
RN [26]
RP VARIANTS FECD6 THR-78; ALA-649; PRO-810; PRO-840 AND THR-905.
RX PubMed=20036349; DOI=10.1016/j.ajhg.2009.12.001;
RA Riazuddin S.A., Zaghloul N.A., Al-Saif A., Davey L., Diplas B.H.,
RA Meadows D.N., Eghrari A.O., Minear M.A., Li Y.J., Klintworth G.K.,
RA Afshari N., Gregory S.G., Gottsch J.D., Katsanis N.;
RT "Missense mutations in TCF8 cause late-onset Fuchs corneal dystrophy and
RT interact with FCD4 on chromosome 9p.";
RL Am. J. Hum. Genet. 86:45-53(2010).
RN [27]
RP INVOLVEMENT IN FECD6 AND PPCD3, VARIANT FECD6 HIS-640, CHARACTERIZATION OF
RP VARIANTS FECD6 THR-78 AND HIS-640, AND VARIANT GLU-525.
RX PubMed=23599324; DOI=10.1167/iovs.13-11781;
RA Lechner J., Dash D.P., Muszynska D., Hosseini M., Segev F., George S.,
RA Frazer D.G., Moore J.E., Kaye S.B., Young T., Simpson D.A., Churchill A.J.,
RA Heon E., Willoughby C.E.;
RT "Mutational spectrum of the ZEB1 gene in corneal dystrophies supports a
RT genotype-phenotype correlation.";
RL Invest. Ophthalmol. Vis. Sci. 54:3215-3223(2013).
RN [28]
RP VARIANTS FECD6 THR-78; ALA-649; SER-696; PRO-810; PRO-840 AND GLY-905,
RP CHARACTERIZATION OF VARIANTS FECD6 THR-78; ALA-649; SER-696; PRO-810;
RP PRO-840 AND GLY-905, AND SUBCELLULAR LOCATION.
RX PubMed=25190660; DOI=10.1167/iovs.14-15247;
RA Chung D.W., Frausto R.F., Ann L.B., Jang M.S., Aldave A.J.;
RT "Functional impact of ZEB1 mutations associated with posterior polymorphous
RT and Fuchs' endothelial corneal dystrophies.";
RL Invest. Ophthalmol. Vis. Sci. 55:6159-6166(2014).
CC -!- FUNCTION: Acts as a transcriptional repressor. Inhibits interleukin-2
CC (IL-2) gene expression. Enhances or represses the promoter activity of
CC the ATP1A1 gene depending on the quantity of cDNA and on the cell type.
CC Represses E-cadherin promoter and induces an epithelial-mesenchymal
CC transition (EMT) by recruiting SMARCA4/BRG1. Represses BCL6
CC transcription in the presence of the corepressor CTBP1. Positively
CC regulates neuronal differentiation. Represses RCOR1 transcription
CC activation during neurogenesis. Represses transcription by binding to
CC the E box (5'-CANNTG-3'). Promotes tumorigenicity by repressing
CC stemness-inhibiting microRNAs. {ECO:0000269|PubMed:19935649,
CC ECO:0000269|PubMed:20175752, ECO:0000269|PubMed:20418909}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1.
CC {ECO:0000269|PubMed:20418909}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20418909,
CC ECO:0000269|PubMed:25190660}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P37275-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P37275-2; Sequence=VSP_045184;
CC Name=3;
CC IsoId=P37275-3; Sequence=VSP_047280;
CC Name=4;
CC IsoId=P37275-4; Sequence=VSP_047281;
CC Name=5;
CC IsoId=P37275-5; Sequence=VSP_047279, VSP_045184;
CC -!- TISSUE SPECIFICITY: Colocalizes with SMARCA4/BRG1 in E-cadherin-
CC negative cells from established lines, and stroma of normal colon as
CC well as in de-differentiated epithelial cells at the invasion front of
CC colorectal carcinomas (at protein level). Expressed in heart and
CC skeletal muscle, but not in liver, spleen, or pancreas.
CC {ECO:0000269|PubMed:20418909}.
CC -!- DISEASE: Corneal dystrophy, posterior polymorphous, 3 (PPCD3)
CC [MIM:609141]: A subtype of posterior corneal dystrophy, a disease
CC characterized by alterations of Descemet membrane presenting as
CC vesicles, opacities or band-like lesions on slit-lamp examination and
CC specular microscopy. Affected patient typically are asymptomatic.
CC {ECO:0000269|PubMed:16252232, ECO:0000269|PubMed:23599324}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 6 (FECD6) [MIM:613270]:
CC A corneal disease caused by loss of endothelium of the central cornea.
CC It is characterized by focal wart-like guttata that arise from Descemet
CC membrane and develop in the central cornea, epithelial blisters,
CC reduced vision and pain. Descemet membrane is thickened by abnormal
CC collagenous deposition. {ECO:0000269|PubMed:20036349,
CC ECO:0000269|PubMed:23599324, ECO:0000269|PubMed:25190660}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAG62481.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D15050; BAA03646.1; -; mRNA.
DR EMBL; U12170; AAA20602.1; -; mRNA.
DR EMBL; AK091478; BAC03673.1; -; mRNA.
DR EMBL; AK296244; BAG58962.1; -; mRNA.
DR EMBL; AK300830; BAG62481.1; ALT_FRAME; mRNA.
DR EMBL; AL158080; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355148; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471072; EAW85989.1; -; Genomic_DNA.
DR EMBL; BC112392; AAI12393.1; -; mRNA.
DR EMBL; M81699; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS44370.1; -. [P37275-5]
DR CCDS; CCDS53505.1; -. [P37275-2]
DR CCDS; CCDS53506.1; -. [P37275-4]
DR CCDS; CCDS53507.1; -. [P37275-3]
DR CCDS; CCDS7169.1; -. [P37275-1]
DR PIR; JX0293; JX0293.
DR RefSeq; NP_001121600.1; NM_001128128.2. [P37275-5]
DR RefSeq; NP_001167564.1; NM_001174093.1. [P37275-4]
DR RefSeq; NP_001167565.1; NM_001174094.1.
DR RefSeq; NP_001167566.1; NM_001174095.1. [P37275-3]
DR RefSeq; NP_001167567.1; NM_001174096.1. [P37275-2]
DR RefSeq; NP_110378.3; NM_030751.5. [P37275-1]
DR PDB; 2E19; NMR; -; A=586-642.
DR PDBsum; 2E19; -.
DR AlphaFoldDB; P37275; -.
DR SMR; P37275; -.
DR BioGRID; 112796; 161.
DR CORUM; P37275; -.
DR ELM; P37275; -.
DR IntAct; P37275; 26.
DR MINT; P37275; -.
DR STRING; 9606.ENSP00000354487; -.
DR GlyGen; P37275; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P37275; -.
DR PhosphoSitePlus; P37275; -.
DR BioMuta; ZEB1; -.
DR DMDM; 6166575; -.
DR EPD; P37275; -.
DR jPOST; P37275; -.
DR MassIVE; P37275; -.
DR MaxQB; P37275; -.
DR PaxDb; P37275; -.
DR PeptideAtlas; P37275; -.
DR PRIDE; P37275; -.
DR ProteomicsDB; 19473; -.
DR ProteomicsDB; 26586; -.
DR ProteomicsDB; 55272; -. [P37275-1]
DR ProteomicsDB; 61322; -.
DR ProteomicsDB; 65678; -.
DR Antibodypedia; 12930; 754 antibodies from 45 providers.
DR CPTC; P37275; 3 antibodies.
DR DNASU; 6935; -.
DR Ensembl; ENST00000320985.14; ENSP00000319248.9; ENSG00000148516.23. [P37275-1]
DR Ensembl; ENST00000424869.6; ENSP00000415961.2; ENSG00000148516.23. [P37275-2]
DR Ensembl; ENST00000446923.7; ENSP00000391612.2; ENSG00000148516.23. [P37275-5]
DR Ensembl; ENST00000542815.7; ENSP00000444891.2; ENSG00000148516.23. [P37275-3]
DR Ensembl; ENST00000560721.6; ENSP00000452787.1; ENSG00000148516.23. [P37275-4]
DR GeneID; 6935; -.
DR KEGG; hsa:6935; -.
DR MANE-Select; ENST00000424869.6; ENSP00000415961.2; NM_001174096.2; NP_001167567.1. [P37275-2]
DR UCSC; uc001ivs.5; human. [P37275-1]
DR CTD; 6935; -.
DR DisGeNET; 6935; -.
DR GeneCards; ZEB1; -.
DR HGNC; HGNC:11642; ZEB1.
DR HPA; ENSG00000148516; Low tissue specificity.
DR MalaCards; ZEB1; -.
DR MIM; 189909; gene.
DR MIM; 609141; phenotype.
DR MIM; 613270; phenotype.
DR neXtProt; NX_P37275; -.
DR OpenTargets; ENSG00000148516; -.
DR Orphanet; 98974; Fuchs endothelial corneal dystrophy.
DR Orphanet; 98973; Posterior polymorphous corneal dystrophy.
DR PharmGKB; PA162409589; -.
DR VEuPathDB; HostDB:ENSG00000148516; -.
DR eggNOG; KOG3623; Eukaryota.
DR GeneTree; ENSGT00950000183208; -.
DR HOGENOM; CLU_005890_0_1_1; -.
DR InParanoid; P37275; -.
DR OMA; IKTSQCS; -.
DR OrthoDB; 890458at2759; -.
DR PhylomeDB; P37275; -.
DR TreeFam; TF331759; -.
DR PathwayCommons; P37275; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P37275; -.
DR SIGNOR; P37275; -.
DR BioGRID-ORCS; 6935; 34 hits in 1103 CRISPR screens.
DR ChiTaRS; ZEB1; human.
DR EvolutionaryTrace; P37275; -.
DR GeneWiki; ZEB1; -.
DR GenomeRNAi; 6935; -.
DR Pharos; P37275; Tbio.
DR PRO; PR:P37275; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P37275; protein.
DR Bgee; ENSG00000148516; Expressed in calcaneal tendon and 209 other tissues.
DR ExpressionAtlas; P37275; baseline and differential.
DR Genevisible; P37275; HS.
DR GO; GO:0000785; C:chromatin; ISA:NTNU_SB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; TAS:ProtInc.
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:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
DR GO; GO:0048856; P:anatomical structure development; IBA:GO_Central.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0030900; P:forebrain development; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IMP:BHF-UCL.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Corneal dystrophy;
KW Differentiation; Disease variant; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1124
FT /note="Zinc finger E-box-binding homeobox 1"
FT /id="PRO_0000047231"
FT ZN_FING 170..193
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 200..222
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 240..262
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 268..292
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 581..640
FT /note="Homeobox; atypical"
FT ZN_FING 904..926
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 932..954
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 960..981
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 551..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 636..714
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 856..898
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..47
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..95
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..586
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 860..886
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 989..1004
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1027..1050
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1058..1085
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62947"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62947"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 642
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 679
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 686
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 693
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 702
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 704
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT CROSSLNK 186
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 195
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 335
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 347
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 493
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 504
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 515
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 548
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 774
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..19
FT /note="MADGPRCKRRKQANPRRNN -> MK (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047279"
FT VAR_SEQ 20..87
FT /note="VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGR
FT SSEREGNAKNCWEDDR -> G (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047280"
FT VAR_SEQ 87..107
FT /note="RKEGQEILGPEAQADEAGCTV -> I (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_047281"
FT VAR_SEQ 87
FT /note="R -> TG (in isoform 2 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_045184"
FT VARIANT 78
FT /note="N -> T (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs80194531)"
FT /evidence="ECO:0000269|PubMed:20036349,
FT ECO:0000269|PubMed:23599324, ECO:0000269|PubMed:25190660"
FT /id="VAR_063759"
FT VARIANT 90
FT /note="G -> R (in dbSNP:rs12217419)"
FT /id="VAR_052731"
FT VARIANT 525
FT /note="G -> E (found in a patient with FECD6)"
FT /evidence="ECO:0000269|PubMed:23599324"
FT /id="VAR_072897"
FT VARIANT 553
FT /note="K -> R (in dbSNP:rs35753967)"
FT /id="VAR_031824"
FT VARIANT 640
FT /note="Q -> H (in FECD6; down-regulation of several
FT collagen genes expression; dbSNP:rs779148597)"
FT /evidence="ECO:0000269|PubMed:23599324"
FT /id="VAR_072898"
FT VARIANT 649
FT /note="P -> A (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs781750314)"
FT /evidence="ECO:0000269|PubMed:20036349,
FT ECO:0000269|PubMed:25190660"
FT /id="VAR_063760"
FT VARIANT 696
FT /note="N -> S (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs567252241)"
FT /evidence="ECO:0000269|PubMed:25190660"
FT /id="VAR_072899"
FT VARIANT 810
FT /note="Q -> P (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs199944415)"
FT /evidence="ECO:0000269|PubMed:20036349,
FT ECO:0000269|PubMed:25190660"
FT /id="VAR_063761"
FT VARIANT 840
FT /note="Q -> P (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs118020901)"
FT /evidence="ECO:0000269|PubMed:20036349,
FT ECO:0000269|PubMed:25190660"
FT /id="VAR_063762"
FT VARIANT 905
FT /note="A -> G (in FECD6; no effect on protein expression;
FT no effect on nuclear localization; dbSNP:rs78449005)"
FT /evidence="ECO:0000269|PubMed:25190660"
FT /id="VAR_072900"
FT VARIANT 905
FT /note="A -> T (in FECD6)"
FT /evidence="ECO:0000269|PubMed:20036349"
FT /id="VAR_063763"
FT CONFLICT 12
FT /note="Q -> R (in Ref. 3; BAC03673)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="N -> S (in Ref. 3; BAC03673)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="E -> K (in Ref. 3; BAC03673)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="T -> A (in Ref. 3; BAG62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="M -> T (in Ref. 3; BAG62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="V -> I (in Ref. 2; AAA20602)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="K -> R (in Ref. 3; BAG58962)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="E -> Q (in Ref. 7; M81699)"
FT /evidence="ECO:0000305"
FT CONFLICT 654
FT /note="I -> T (in Ref. 2; AAA20602)"
FT /evidence="ECO:0000305"
FT CONFLICT 672
FT /note="D -> H (in Ref. 7; M81699)"
FT /evidence="ECO:0000305"
FT CONFLICT 681
FT /note="L -> S (in Ref. 7; M81699)"
FT /evidence="ECO:0000305"
FT CONFLICT 775
FT /note="K -> T (in Ref. 3; BAG62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 793..794
FT /note="IP -> KY (in Ref. 3; BAG58962)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="A -> N (in Ref. 3; BAG58962)"
FT /evidence="ECO:0000305"
FT CONFLICT 818
FT /note="A -> V (in Ref. 3; BAG62481)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="I -> T (in Ref. 3; BAC03673)"
FT /evidence="ECO:0000305"
FT CONFLICT 1066
FT /note="E -> G (in Ref. 3; BAC03673)"
FT /evidence="ECO:0000305"
FT HELIX 590..600
FT /evidence="ECO:0007829|PDB:2E19"
FT HELIX 608..618
FT /evidence="ECO:0007829|PDB:2E19"
FT HELIX 622..634
FT /evidence="ECO:0007829|PDB:2E19"
SQ SEQUENCE 1124 AA; 124074 MW; 0A2714CC37C848D1 CRC64;
MADGPRCKRR KQANPRRNNV TNYNTVVETN SDSDDEDKLH IVEEESVTDA ADCEGVPEDD
LPTDQTVLPG RSSEREGNAK NCWEDDRKEG QEILGPEAQA DEAGCTVKDD ECESDAENEQ
NHDPNVEEFL QQQDTAVIFP EAPEEDQRQG TPEASGHDEN GTPDAFSQLL TCPYCDRGYK
RFTSLKEHIK YRHEKNEDNF SCSLCSYTFA YRTQLERHMT SHKSGRDQRH VTQSGCNRKF
KCTECGKAFK YKHHLKEHLR IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLIPVNG
RPRTGLKTSQ CSSPSLSASP GSPTRPQIRQ KIENKPLQEQ LSVNQIKTEP VDYEFKPIVV
ASGINCSTPL QNGVFTGGGP LQATSSPQGM VQAVVLPTVG LVSPISINLS DIQNVLKVAV
DGNVIRQVLE NNQANLASKE QETINASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE
QPSQLQVVPQ NLKKENPVAT NSCKSEKLPE DLTVKSEKDK SFEGGVNDST CLLCDDCPGD
INALPELKHY DLKQPTQPPP LPAAEAEKPE SSVSSATGDG NLSPSQPPLK NLLSLLKAYY
ALNAQPSAEE LSKIADSVNL PLDVVKKWFE KMQAGQISVQ SSEPSSPEPG KVNIPAKNND
QPQSANANEP QDSTVNLQSP LKMTNSPVLP VGSTTNGSRS STPSPSPLNL SSSRNTQGYL
YTAEGAQEEP QVEPLDLSLP KQQGELLERS TITSVYQNSV YSVQEEPLNL SCAKKEPQKD
SCVTDSEPVV NVIPPSANPI NIAIPTVTAQ LPTIVAIADQ NSVPCLRALA ANKQTILIPQ
VAYTYSTTVS PAVQEPPLKV IQPNGNQDER QDTSSEGVSN VEDQNDSDST PPKKKMRKTE
NGMYACDLCD KIFQKSSSLL RHKYEHTGKR PHECGICKKA FKHKHHLIEH MRLHSGEKPY
QCDKCGKRFS HSGSYSQHMN HRYSYCKREA EERDSTEQEE AGPEILSNEH VGARASPSQG
DSDERESLTR EEDEDSEKEE EEEDKEMEEL QEEKECEKPQ GDEEEEEEEE EVEEEEVEEA
ENEGEEAKTE GLMKDDRAES QASSLGQKVG ESSEQVSEEK TNEA
