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Zinc finger E-box-binding homeobox 1 (Delta EF1) (Transcription factor 8) (TCF-8) (Zinc finger homeobox protein 1a) (MEB1)

 ZEB1_MOUSE              Reviewed;        1117 AA.
Q64318; A4QPD2; Q62519;
21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
10-OCT-2018, entry version 164.
RecName: Full=Zinc finger E-box-binding homeobox 1;
AltName: Full=Delta EF1;
AltName: Full=Transcription factor 8;
Short=TCF-8;
AltName: Full=Zinc finger homeobox protein 1a;
Short=MEB1;
Name=Zeb1; Synonyms=Tcf8, Zfhx1a, Zfx1a, Zfx1ha;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=8964504; DOI=10.1016/0378-1119(96)00185-0;
Sekido R., Takagi T., Okanami M., Moribe H., Yamamura M., Higashi Y.,
Kondoh H.;
"Organization of the gene encoding transcriptional repressor deltaEF1
and cross-species conservation of its domains.";
Gene 173:227-232(1996).
[2]
NUCLEOTIDE SEQUENCE.
TISSUE=Spleen;
Wu Y., Montoya G.D., Rubin S.E., Brodie S.G., Jenkins N.,
Williams T.M.;
Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Brain;
PubMed=8647466; DOI=10.1016/0378-1119(95)00824-1;
Genetta T., Kadesch T.;
"Cloning of a cDNA encoding a mouse transcriptional repressor
displaying striking sequence conservation across vertebrates.";
Gene 169:289-290(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=19935649; DOI=10.1038/ncb1998;
Wellner U., Schubert J., Burk U.C., Schmalhofer O., Zhu F.,
Sonntag A., Waldvogel B., Vannier C., Darling D., zur Hausen A.,
Brunton V.G., Morton J., Sansom O., Schuler J., Stemmler M.P.,
Herzberger C., Hopt U., Keck T., Brabletz S., Brabletz T.;
"The EMT-activator ZEB1 promotes tumorigenicity by repressing
stemness-inhibiting microRNAs.";
Nat. Cell Biol. 11:1487-1495(2009).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; SER-302; SER-657;
SER-664; SER-671; SER-678 AND SER-682, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[7]
FUNCTION, DNA-BINDING, INDUCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=20346398; DOI=10.1016/j.mcn.2010.03.006;
Ravanpay A.C., Hansen S.J., Olson J.M.;
"Transcriptional inhibition of REST by NeuroD2 during neuronal
differentiation.";
Mol. Cell. Neurosci. 44:178-189(2010).
-!- FUNCTION: Acts as a transcriptional repressor. Binds to E-box
sequences in the immunoglobulin heavy chain enhancer as well as in
the regulatory regions of many other tissue-specific genes.
Represses E-cadherin promoter and induces an epithelial-
mesenchymal transition (EMT) by recruiting SMARCA4/BRG1. Represses
BCL6 transcription in the presence of the corepressor CTBP1 (By
similarity). Positively regulates neuronal differentiation.
Represses RCOR1 transcription activation during neurogenesis.
Represses transcription by binding to the E box (5'-CANNTG-3').
Promotes tumorigenicity by repressing stemness-inhibiting
microRNAs. {ECO:0000250, ECO:0000269|PubMed:19935649,
ECO:0000269|PubMed:20346398}.
-!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1.
{ECO:0000250}.
-!- INTERACTION:
O88712:Ctbp1; NbExp=5; IntAct=EBI-8560245, EBI-604547;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20346398}.
-!- TISSUE SPECIFICITY: Expressed in the external germinal layer (EGL)
and internal granular layer (IGL) of the cerebellum (at protein
level). {ECO:0000269|PubMed:20346398}.
-!- INDUCTION: Up-regulated during NEUROD2-induced neurogenesis.
{ECO:0000269|PubMed:20346398}.
-!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
family. {ECO:0000305}.
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U26259; AAA67564.1; -; mRNA.
EMBL; D76432; BAA11177.1; -; mRNA.
EMBL; L48363; AAB08442.1; -; Genomic_DNA.
EMBL; BC139769; AAI39770.1; -; mRNA.
CCDS; CCDS29039.1; -.
PIR; JC4934; JC4934.
RefSeq; NP_035676.1; NM_011546.3.
UniGene; Mm.3929; -.
UniGene; Mm.487317; -.
ProteinModelPortal; Q64318; -.
SMR; Q64318; -.
BioGrid; 204010; 3.
DIP; DIP-60280N; -.
IntAct; Q64318; 3.
MINT; Q64318; -.
STRING; 10090.ENSMUSP00000025081; -.
iPTMnet; Q64318; -.
PhosphoSitePlus; Q64318; -.
EPD; Q64318; -.
MaxQB; Q64318; -.
PaxDb; Q64318; -.
PRIDE; Q64318; -.
Ensembl; ENSMUST00000025081; ENSMUSP00000025081; ENSMUSG00000024238.
GeneID; 21417; -.
KEGG; mmu:21417; -.
UCSC; uc008dyy.2; mouse.
CTD; 6935; -.
MGI; MGI:1344313; Zeb1.
eggNOG; ENOG410IMF6; Eukaryota.
eggNOG; ENOG41105SH; LUCA.
GeneTree; ENSGT00630000089829; -.
HOGENOM; HOG000264256; -.
HOVERGEN; HBG004697; -.
InParanoid; Q64318; -.
KO; K09299; -.
OMA; ECEKPQG; -.
OrthoDB; EOG091G0F7Y; -.
PhylomeDB; Q64318; -.
TreeFam; TF331759; -.
ChiTaRS; Zeb1; mouse.
PRO; PR:Q64318; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024238; Expressed in 300 organ(s), highest expression level in cardiac ventricle.
CleanEx; MM_ZEB1; -.
ExpressionAtlas; Q64318; baseline and differential.
Genevisible; Q64318; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:MGI.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:MGI.
GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
GO; GO:0070888; F:E-box binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0043565; F:sequence-specific DNA binding; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0048513; P:animal organ development; IMP:MGI.
GO; GO:0051216; P:cartilage development; IMP:MGI.
GO; GO:0071230; P:cellular response to amino acid stimulus; IDA:MGI.
GO; GO:0007417; P:central nervous system development; IGI:MGI.
GO; GO:0090103; P:cochlea morphogenesis; IMP:MGI.
GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IMP:MGI.
GO; GO:0048598; P:embryonic morphogenesis; IGI:MGI.
GO; GO:0048704; P:embryonic skeletal system morphogenesis; IMP:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:MGI.
GO; GO:0045602; P:negative regulation of endothelial cell differentiation; ISO:MGI.
GO; GO:0030857; P:negative regulation of epithelial cell differentiation; IMP:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0007389; P:pattern specification process; IMP:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IMP:MGI.
GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IMP:MGI.
GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:MGI.
GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IGI:MGI.
GO; GO:0048752; P:semicircular canal morphogenesis; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00086; homeodomain; 1.
InterPro; IPR008598; Di19_Zn_binding_dom.
InterPro; IPR009057; Homeobox-like_sf.
InterPro; IPR001356; Homeobox_dom.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00096; zf-C2H2; 4.
Pfam; PF05605; zf-Di19; 1.
SMART; SM00355; ZnF_C2H2; 7.
SUPFAM; SSF46689; SSF46689; 1.
SUPFAM; SSF57667; SSF57667; 4.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
1: Evidence at protein level;
Activator; Complete proteome; Differentiation; DNA-binding; Homeobox;
Isopeptide bond; Metal-binding; Neurogenesis; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 1117 Zinc finger E-box-binding homeobox 1.
/FTId=PRO_0000047233.
ZN_FING 150 173 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 180 202 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 220 242 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 248 272 C2H2-type 4; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
DNA_BIND 559 618 Homeobox; atypical.
ZN_FING 882 904 C2H2-type 5. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 910 932 C2H2-type 6. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 938 959 C2H2-type 7; atypical.
{ECO:0000255|PROSITE-ProRule:PRU00042}.
COMPBIAS 969 1117 Glu-rich (acidic).
MOD_RES 31 31 Phosphoserine.
{ECO:0000250|UniProtKB:Q62947}.
MOD_RES 33 33 Phosphoserine.
{ECO:0000250|UniProtKB:Q62947}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 657 657 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 664 664 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 671 671 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 678 678 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 680 680 Phosphothreonine.
{ECO:0000250|UniProtKB:P37275}.
MOD_RES 682 682 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 175 175 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 287 287 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 311 311 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 315 315 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 327 327 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 327 327 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 419 419 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 473 473 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 484 484 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 495 495 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 528 528 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P37275}.
CROSSLNK 752 752 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 752 752 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate.
{ECO:0000250|UniProtKB:P37275}.
CONFLICT 33 33 S -> A (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 57 57 M -> K (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 125 125 Missing (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 146 146 F -> L (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 313 313 E -> EV (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 353 353 G -> A (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 400 400 V -> L (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 461 461 Q -> E (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 528 528 K -> KK (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 664 664 S -> T (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 744 744 E -> L (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 822 822 T -> A (in Ref. 3; AAB08442).
{ECO:0000305}.
CONFLICT 1062 1062 Missing (in Ref. 3; AAB08442).
{ECO:0000305}.
SEQUENCE 1117 AA; 122465 MW; D1FAC2D048D34237 CRC64;
MADGPRCKRR KQANPRRNNV TNYNTVVEAN SDSDDEDKLH IVEEESITDA ADCEGGMPDD
ELPADQTVLP GGSDRGGGAK NCWQDNVKDN ECDSDAENEQ NHDPNVEEFL QQQDTAVIYP
EAPEEDQRQG TPEASSHDEN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF
SCSLCSYTFA YRTQLERHMT SHKSGREQRH VTQSGGNRKF KCTECGKAFK YKHHLKEHLR
IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLMPVNG RPRSGLKTSQ CSSPSLSTSP
GSPTRPQIRQ KIENKPLQEP LSVNQIKTEP VDYEFKPIVV ASGINCSTPL QNGVFSSGGQ
LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV DGNVIRQVLE TNQASLASKE
QEAVSASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPSQLQVVPQ NLKKEIPAPT
NSCKSEKLPE DLTVKSETDK SFEGARDDST CLLCEDCPGD LNALPELKHY DPECPAQPPP
PAPATEKPES SASSAGNGDL SPSQPPLKNL LSLLKAYYAL NAQPSTEELS KIADSVNLPL
DGVKKWFEKM QAGQIPGQSP DPPSPGTGSV NIPTKTDEQP QPADGNEPQE DSTRGQSPVK
IRSSPVLPVG SAMNGSRSCT SSPSPLNLCS ARNPQGYSCV AEGAQEEPQV EPLDLSLPKQ
QGELLERSTV SSVYQNSVYS VQEEPLNLSC AKKEPQKDSC VTDSEPVVNV VPPSANPINI
AIPTVTAQLP TIVAIADQNS VPCLRALAAN KQTILIPQVA YTYSATVSPA VQEPPVKVIQ
PNGNQDERQD TSSEGVSTVE DQNDSDSTPP KKKTRKTENG MYACDLCDKI FQKSSSLLRH
KYEHTGKRPH ECGICRKAFK HKHHLIEHMR LHSGEKPYQC DKCGKRFSHS GSYSQHMNHR
YSYCKRGAED RDAMEQEDAG PEVLPEVLAT EHVGARASPS QADSDERESL TREEDEDSEK
EEEEEDKEME ELQEGKECEN PQGEEEEEEE EEEEEEEEEE EEVEADEAEH EAAAKTDGTV
EVGAAQQAGS LEQKASESEM ESESESEQLS EEKTNEA


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