Zinc finger E-box-binding homeobox 1

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Q64318 (ZEB1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Zinc finger E-box-binding homeobox 1

Alternative name(s):
Delta EF1
Transcription factor 8
Short name=TCF-8
Zinc finger homeobox protein 1a
Short name=MEB1

Gene names

Name:	Zeb1
Synonyms:	Tcf8, Zfhx1a, Zfx1a, Zfx1ha

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1117 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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. Ref.5 Ref.6
Subunit structure	Interacts (via N-terminus) with SMARCA4/BRG1 By similarity.
Subcellular location	Nucleus Ref.6.
Tissue specificity	Expressed in the external germinal layer (EGL) and internal granular layer (IGL) of the cerebellum (at protein level). Ref.6
Induction	Up-regulated during NEUROD2-induced neurogenesis. Ref.6
Sequence similarities	Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger family. Contains 7 C2H2-type zinc fingers. Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Domain	Homeobox Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cartilage development Inferred from mutant phenotype PubMed 9389660. Source: MGI cellular response to amino acid stimulus Inferred from direct assay PubMed 20548288. Source: MGI cellular response to transforming growth factor beta stimulus Inferred from electronic annotation. Source: Compara central nervous system development Inferred from genetic interaction PubMed 16598713. Source: MGI cochlea morphogenesis Inferred from mutant phenotype PubMed 21980308. Source: MGI embryonic camera-type eye morphogenesis Inferred from mutant phenotype PubMed 18436818. Source: MGI embryonic skeletal system morphogenesis Inferred from mutant phenotype PubMed 9389660. Source: MGI forebrain development Inferred from electronic annotation. Source: Compara negative regulation of cell proliferation Inferred from mutant phenotype PubMed 18436818. Source: MGI negative regulation of epithelial cell differentiation Inferred from mutant phenotype PubMed 18192284. Source: MGI negative regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype PubMed 17392792. Source: MGI pattern specification process Inferred from mutant phenotype PubMed 9389660. Source: MGI positive regulation of neuron differentiation Inferred from direct assay Ref.6. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 16824956. Source: MGI regulation of T cell differentiation in thymus Inferred from mutant phenotype PubMed 9126927 PubMed 9389660. Source: MGI regulation of mesenchymal cell proliferation Inferred from mutant phenotype PubMed 18192284. Source: MGI regulation of smooth muscle cell differentiation Inferred from mutant phenotype PubMed 16824956. Source: MGI regulation of transforming growth factor beta receptor signaling pathway Inferred from genetic interaction PubMed 16824956. Source: MGI response to activity Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara semicircular canal morphogenesis Inferred from mutant phenotype PubMed 21980308. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: Compara transcription factor complex Inferred from direct assay PubMed 17392792. Source: MGI
Molecular_function	E-box binding Inferred from direct assay Ref.6. Source: UniProtKB chromatin binding Inferred from direct assay PubMed 16824956. Source: MGI double-stranded DNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding transcription factor activity Inferred from direct assay PubMed 17392792. Source: MGI zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1117

1117

Zinc finger E-box-binding homeobox 1

PRO_0000047233

Regions

Zinc finger

150 – 173

C2H2-type 1

Zinc finger

180 – 202

C2H2-type 2

Zinc finger

220 – 242

C2H2-type 3

Zinc finger

248 – 272

C2H2-type 4; atypical

DNA binding

559 – 618

Homeobox; atypical Ref.6

Zinc finger

882 – 904

C2H2-type 5

Zinc finger

910 – 932

C2H2-type 6

Zinc finger

938 – 959

C2H2-type 7; atypical

Compositional bias

969 – 1117

149

Glu-rich (acidic)

Amino acid modifications

Modified residue

302

Phosphoserine By similarity

Modified residue

657

Phosphoserine By similarity

Modified residue

680

Phosphothreonine By similarity

Cross-link

327

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

752

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Experimental info

Sequence conflict

S → A in AAB08442. Ref.3

Sequence conflict

M → K in AAB08442. Ref.3

Sequence conflict

125

Missing in AAB08442. Ref.3

Sequence conflict

146

F → L in AAB08442. Ref.3

Sequence conflict

313

E → EV in AAB08442. Ref.3

Sequence conflict

353

G → A in AAB08442. Ref.3

Sequence conflict

400

V → L in AAB08442. Ref.3

Sequence conflict

461

Q → E in AAB08442. Ref.3

Sequence conflict

528

K → KK in AAB08442. Ref.3

Sequence conflict

664

S → T in AAB08442. Ref.3

Sequence conflict

744

E → L in AAB08442. Ref.3

Sequence conflict

822

T → A in AAB08442. Ref.3

Sequence conflict

1062

Missing in AAB08442. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

Q64318 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: D1FAC2D048D34237
Show »

FASTA

1,117

122,465

        10         20         30         40         50         60 
MADGPRCKRR KQANPRRNNV TNYNTVVEAN SDSDDEDKLH IVEEESITDA ADCEGGMPDD 

        70         80         90        100        110        120 
ELPADQTVLP GGSDRGGGAK NCWQDNVKDN ECDSDAENEQ NHDPNVEEFL QQQDTAVIYP 

       130        140        150        160        170        180 
EAPEEDQRQG TPEASSHDEN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF 

       190        200        210        220        230        240 
SCSLCSYTFA YRTQLERHMT SHKSGREQRH VTQSGGNRKF KCTECGKAFK YKHHLKEHLR 

       250        260        270        280        290        300 
IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLMPVNG RPRSGLKTSQ CSSPSLSTSP 

       310        320        330        340        350        360 
GSPTRPQIRQ KIENKPLQEP LSVNQIKTEP VDYEFKPIVV ASGINCSTPL QNGVFSSGGQ 

       370        380        390        400        410        420 
LQATSSPQGV VQAVVLPTVG LVSPISINLS DIQNVLKVAV DGNVIRQVLE TNQASLASKE 

       430        440        450        460        470        480 
QEAVSASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPSQLQVVPQ NLKKEIPAPT 

       490        500        510        520        530        540 
NSCKSEKLPE DLTVKSETDK SFEGARDDST CLLCEDCPGD LNALPELKHY DPECPAQPPP 

       550        560        570        580        590        600 
PAPATEKPES SASSAGNGDL SPSQPPLKNL LSLLKAYYAL NAQPSTEELS KIADSVNLPL 

       610        620        630        640        650        660 
DGVKKWFEKM QAGQIPGQSP DPPSPGTGSV NIPTKTDEQP QPADGNEPQE DSTRGQSPVK 

       670        680        690        700        710        720 
IRSSPVLPVG SAMNGSRSCT SSPSPLNLCS ARNPQGYSCV AEGAQEEPQV EPLDLSLPKQ 

       730        740        750        760        770        780 
QGELLERSTV SSVYQNSVYS VQEEPLNLSC AKKEPQKDSC VTDSEPVVNV VPPSANPINI 

       790        800        810        820        830        840 
AIPTVTAQLP TIVAIADQNS VPCLRALAAN KQTILIPQVA YTYSATVSPA VQEPPVKVIQ 

       850        860        870        880        890        900 
PNGNQDERQD TSSEGVSTVE DQNDSDSTPP KKKTRKTENG MYACDLCDKI FQKSSSLLRH 

       910        920        930        940        950        960 
KYEHTGKRPH ECGICRKAFK HKHHLIEHMR LHSGEKPYQC DKCGKRFSHS GSYSQHMNHR 

       970        980        990       1000       1010       1020 
YSYCKRGAED RDAMEQEDAG PEVLPEVLAT EHVGARASPS QADSDERESL TREEDEDSEK 

      1030       1040       1050       1060       1070       1080 
EEEEEDKEME ELQEGKECEN PQGEEEEEEE EEEEEEEEEE EEVEADEAEH EAAAKTDGTV 

      1090       1100       1110 
EVGAAQQAGS LEQKASESEM ESESESEQLS EEKTNEA

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Organization of the gene encoding transcriptional repressor deltaEF1 and cross-species conservation of its domains." Sekido R., Takagi T., Okanami M., Moribe H., Yamamura M., Higashi Y., Kondoh H. Gene 173:227-232(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Strain: C57BL/6. Tissue: Embryo.
[2]	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 Cited for: NUCLEOTIDE SEQUENCE. Tissue: Spleen.
[3]	"Cloning of a cDNA encoding a mouse transcriptional repressor displaying striking sequence conservation across vertebrates." Genetta T., Kadesch T. Gene 169:289-290(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Brain.
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]	"The EMT-activator ZEB1 promotes tumorigenicity by repressing stemness-inhibiting microRNAs." 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. Nat. Cell Biol. 11:1487-1495(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[6]	"Transcriptional inhibition of REST by NeuroD2 during neuronal differentiation." Ravanpay A.C., Hansen S.J., Olson J.M. Mol. Cell. Neurosci. 44:178-189(2010) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DNA-BINDING, INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U26259 mRNA. Translation: AAA67564.1. D76432 mRNA. Translation: BAA11177.1. L48363 Genomic DNA. Translation: AAB08442.1. BC139769 mRNA. Translation: AAI39770.1.
IPI	IPI00133262.
PIR	JC4934.
RefSeq	NP_035676.1. NM_011546.3.
UniGene	Mm.3929.
3D structure databases
ProteinModelPortal	Q64318.
SMR	Q64318. Positions 152-320, 561-619, 882-962.
ModBase	Search...
PTM databases
PhosphoSite	Q64318.
Proteomic databases
PRIDE	Q64318.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000025081; ENSMUSP00000025081; ENSMUSG00000024238.
GeneID	21417.
KEGG	mmu:21417.
UCSC	uc008dyy.1. mouse.
Organism-specific databases
CTD	6935.
MGI	MGI:1344313. Zeb1.
Phylogenomic databases
eggNOG	COG5048.
GeneTree	ENSGT00630000089829.
HOGENOM	HOG000264256.
HOVERGEN	HBG004697.
InParanoid	A4QPD2.
KO	K09299.
OMA	TQGYLYT.
OrthoDB	EOG49CQ6Z.
Gene expression databases
ArrayExpress	Q64318.
Bgee	Q64318.
CleanEx	MM_ZEB1.
Genevestigator	Q64318.
GermOnline	ENSMUSG00000024238. Mus musculus.
Family and domain databases
Gene3D	1.10.10.60. 1 hit. 3.30.160.60. 5 hits.
InterPro	IPR001356. Homeodomain. IPR009057. Homeodomain-like. IPR007087. Znf_C2H2. IPR015880. Znf_C2H2-like. IPR013087. Znf_C2H2/integrase_DNA-bd. [Graphical view]
SMART	SM00389. HOX. 1 hit. SM00355. ZnF_C2H2. 7 hits. [Graphical view]
PROSITE	PS00027. HOMEOBOX_1. False negative. PS50071. HOMEOBOX_2. False negative. PS00028. ZINC_FINGER_C2H2_1. 5 hits. PS50157. ZINC_FINGER_C2H2_2. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ZEB1. mouse.
NextBio	300720.
SOURCE	Search...

Entry information

Entry name

ZEB1_MOUSE

Accession

Primary (citable) accession number: Q64318
Secondary accession number(s): A4QPD2, Q62519

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 119 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents