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P37275

- ZEB1_HUMAN

UniProt

P37275 - ZEB1_HUMAN

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Protein
Zinc finger E-box-binding homeobox 1
Gene
ZEB1, AREB6, TCF8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Acts as a transcriptional repressor. Inhibits interleukin-2 (IL-2) gene expression. Enhances or represses the promoter activity of the ATP1A1 gene depending on the quantity of cDNA and on the cell type. 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. 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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri170 – 19324C2H2-type 1
Add
BLAST
Zinc fingeri200 – 22223C2H2-type 2
Add
BLAST
Zinc fingeri240 – 26223C2H2-type 3
Add
BLAST
Zinc fingeri268 – 29225C2H2-type 4; atypical
Add
BLAST
DNA bindingi581 – 64060Homeobox; atypical
Add
BLAST
Zinc fingeri904 – 92623C2H2-type 5
Add
BLAST
Zinc fingeri932 – 95423C2H2-type 6
Add
BLAST
Zinc fingeri960 – 98122C2H2-type 7; atypical
Add
BLAST

GO - Molecular functioni

  1. E-box binding Source: UniProtKB
  2. chromatin binding Source: Ensembl
  3. double-stranded DNA binding Source: Ensembl
  4. protein binding Source: UniProtKB
  5. sequence-specific DNA binding Source: InterPro
  6. sequence-specific DNA binding transcription factor activity Source: ProtInc
  7. transcription coactivator activity Source: ProtInc
  8. transcription corepressor activity Source: ProtInc
  9. zinc ion binding Source: ProtInc

GO - Biological processi

  1. cartilage development Source: Ensembl
  2. cell proliferation Source: ProtInc
  3. cellular response to amino acid stimulus Source: Ensembl
  4. cellular response to transforming growth factor beta stimulus Source: Ensembl
  5. cochlea morphogenesis Source: Ensembl
  6. embryonic camera-type eye morphogenesis Source: Ensembl
  7. embryonic skeletal system morphogenesis Source: Ensembl
  8. forebrain development Source: Ensembl
  9. immune response Source: ProtInc
  10. negative regulation of cell proliferation Source: Ensembl
  11. negative regulation of epithelial cell differentiation Source: Ensembl
  12. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
  13. negative regulation of transcription, DNA-templated Source: UniProtKB
  14. pattern specification process Source: Ensembl
  15. positive regulation of neuron differentiation Source: UniProtKB
  16. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  17. regulation of T cell differentiation in thymus Source: Ensembl
  18. regulation of mesenchymal cell proliferation Source: Ensembl
  19. regulation of smooth muscle cell differentiation Source: Ensembl
  20. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  21. regulation of transforming growth factor beta receptor signaling pathway Source: Ensembl
  22. response to activity Source: Ensembl
  23. response to nutrient levels Source: Ensembl
  24. semicircular canal morphogenesis Source: Ensembl
  25. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiP37275.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger E-box-binding homeobox 1
Alternative name(s):
NIL-2-A zinc finger protein
Negative regulator of IL2
Transcription factor 8
Short name:
TCF-8
Gene namesi
Name:ZEB1
Synonyms:AREB6, TCF8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:11642. ZEB1.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
  3. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Corneal dystrophy, posterior polymorphous, 3 (PPCD3) [MIM:609141]: A subtype of posterior corneal dystrophy, a disease characterized by alterations of Descemet membrane presenting as vesicles, opacities or band-like lesions on slit-lamp examination and specular microscopy. Affected patient typically are asymptomatic.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Corneal dystrophy, Fuchs endothelial, 6 (FECD6) [MIM:613270]: A corneal disease caused by loss of endothelium of the central cornea. It is characterized by focal wart-like guttata that arise from Descemet membrane and develop in the central cornea, epithelial blisters, reduced vision and pain. Descemet membrane is thickened by abnormal collagenous deposition.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781N → T in FECD6. 1 Publication
Corresponds to variant rs80194531 [ dbSNP | Ensembl ].
VAR_063759
Natural varianti649 – 6491P → A in FECD6. 1 Publication
VAR_063760
Natural varianti810 – 8101Q → P in FECD6. 1 Publication
VAR_063761
Natural varianti840 – 8401Q → P in FECD6. 1 Publication
Corresponds to variant rs118020901 [ dbSNP | Ensembl ].
VAR_063762
Natural varianti905 – 9051A → T in FECD6. 1 Publication
VAR_063763

Keywords - Diseasei

Corneal dystrophy, Disease mutation

Organism-specific databases

MIMi609141. phenotype.
613270. phenotype.
Orphaneti98974. Fuchs endothelial corneal dystrophy.
98973. Posterior polymorphous corneal dystrophy.
PharmGKBiPA162409589.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11241124Zinc finger E-box-binding homeobox 1
PRO_0000047231Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei322 – 3221Phosphoserine1 Publication
Cross-linki347 – 347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
Modified residuei642 – 6421Phosphoserine1 Publication
Modified residuei679 – 6791Phosphoserine2 Publications
Modified residuei702 – 7021Phosphothreonine1 Publication
Cross-linki774 – 774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP37275.
PaxDbiP37275.
PRIDEiP37275.

PTM databases

PhosphoSiteiP37275.

Expressioni

Tissue specificityi

Colocalizes with SMARCA4/BRG1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level). Expressed in heart and skeletal muscle, but not in liver, spleen, or pancreas.1 Publication

Gene expression databases

ArrayExpressiP37275.
BgeeiP37275.
CleanExiHS_ZEB1.
GenevestigatoriP37275.

Organism-specific databases

HPAiCAB058686.
HPA027524.

Interactioni

Subunit structurei

Interacts (via N-terminus) with SMARCA4/BRG1.1 Publication

Protein-protein interaction databases

BioGridi112796. 18 interactions.
IntActiP37275. 2 interactions.
MINTiMINT-94525.
STRINGi9606.ENSP00000319248.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi590 – 60011
Helixi608 – 61811
Helixi622 – 63413

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E19NMR-A586-642[»]
ProteinModelPortaliP37275.
SMRiP37275. Positions 172-336, 583-642, 903-1003.

Miscellaneous databases

EvolutionaryTraceiP37275.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi989 – 1124136Glu-rich (acidic)
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Homeobox, Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
HOGENOMiHOG000264256.
HOVERGENiHBG004697.
KOiK09299.
OMAiCPGDINA.
OrthoDBiEOG790G0D.
PhylomeDBiP37275.
TreeFamiTF331759.

Family and domain databases

Gene3Di1.10.10.60. 1 hit.
3.30.160.60. 5 hits.
InterProiIPR008598. Di19_Zn_binding.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00046. Homeobox. 1 hit.
PF05605. zf-Di19. 1 hit.
[Graphical view]
SMARTiSM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMiSSF46689. SSF46689. 1 hit.
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P37275-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MADGPRCKRR KQANPRRNNV TNYNTVVETN SDSDDEDKLH IVEEESVTDA     50
ADCEGVPEDD LPTDQTVLPG RSSEREGNAK NCWEDDRKEG QEILGPEAQA 100
DEAGCTVKDD ECESDAENEQ NHDPNVEEFL QQQDTAVIFP EAPEEDQRQG 150
TPEASGHDEN GTPDAFSQLL TCPYCDRGYK RFTSLKEHIK YRHEKNEDNF 200
SCSLCSYTFA YRTQLERHMT SHKSGRDQRH VTQSGCNRKF KCTECGKAFK 250
YKHHLKEHLR IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLIPVNG 300
RPRTGLKTSQ CSSPSLSASP GSPTRPQIRQ KIENKPLQEQ LSVNQIKTEP 350
VDYEFKPIVV ASGINCSTPL QNGVFTGGGP LQATSSPQGM VQAVVLPTVG 400
LVSPISINLS DIQNVLKVAV DGNVIRQVLE NNQANLASKE QETINASPIQ 450
QGGHSVISAI SLPLVDQDGT TKIIINYSLE QPSQLQVVPQ NLKKENPVAT 500
NSCKSEKLPE DLTVKSEKDK SFEGGVNDST CLLCDDCPGD INALPELKHY 550
DLKQPTQPPP LPAAEAEKPE SSVSSATGDG NLSPSQPPLK NLLSLLKAYY 600
ALNAQPSAEE LSKIADSVNL PLDVVKKWFE KMQAGQISVQ SSEPSSPEPG 650
KVNIPAKNND QPQSANANEP QDSTVNLQSP LKMTNSPVLP VGSTTNGSRS 700
STPSPSPLNL SSSRNTQGYL YTAEGAQEEP QVEPLDLSLP KQQGELLERS 750
TITSVYQNSV YSVQEEPLNL SCAKKEPQKD SCVTDSEPVV NVIPPSANPI 800
NIAIPTVTAQ LPTIVAIADQ NSVPCLRALA ANKQTILIPQ VAYTYSTTVS 850
PAVQEPPLKV IQPNGNQDER QDTSSEGVSN VEDQNDSDST PPKKKMRKTE 900
NGMYACDLCD KIFQKSSSLL RHKYEHTGKR PHECGICKKA FKHKHHLIEH 950
MRLHSGEKPY QCDKCGKRFS HSGSYSQHMN HRYSYCKREA EERDSTEQEE 1000
AGPEILSNEH VGARASPSQG DSDERESLTR EEDEDSEKEE EEEDKEMEEL 1050
QEEKECEKPQ GDEEEEEEEE EVEEEEVEEA ENEGEEAKTE GLMKDDRAES 1100
QASSLGQKVG ESSEQVSEEK TNEA 1124
Length:1,124
Mass (Da):124,074
Last modified:July 15, 1999 - v2
Checksum:i0A2714CC37C848D1
GO
Isoform 2 (identifier: P37275-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-87: R → TG

Note: No experimental confirmation available.

Show »
Length:1,125
Mass (Da):124,076
Checksum:i3C327EEBBA18D19B
GO
Isoform 3 (identifier: P37275-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     20-87: VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDR → G

Show »
Length:1,057
Mass (Da):116,593
Checksum:i7C683713C6562DC8
GO
Isoform 4 (identifier: P37275-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     87-107: RKEGQEILGPEAQADEAGCTV → I

Show »
Length:1,104
Mass (Da):122,003
Checksum:i3F8DAA9A05DFA6E4
GO
Isoform 5 (identifier: P37275-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-19: MADGPRCKRRKQANPRRNN → MK
     87-87: R → TG

Show »
Length:1,108
Mass (Da):122,084
Checksum:i33855F3B478635C8
GO

Sequence cautioni

The sequence BAG62481.1 differs from that shown. Reason: Frameshift at position 177.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti78 – 781N → T in FECD6. 1 Publication
Corresponds to variant rs80194531 [ dbSNP | Ensembl ].
VAR_063759
Natural varianti90 – 901G → R.
Corresponds to variant rs12217419 [ dbSNP | Ensembl ].
VAR_052731
Natural varianti553 – 5531K → R.
Corresponds to variant rs35753967 [ dbSNP | Ensembl ].
VAR_031824
Natural varianti649 – 6491P → A in FECD6. 1 Publication
VAR_063760
Natural varianti810 – 8101Q → P in FECD6. 1 Publication
VAR_063761
Natural varianti840 – 8401Q → P in FECD6. 1 Publication
Corresponds to variant rs118020901 [ dbSNP | Ensembl ].
VAR_063762
Natural varianti905 – 9051A → T in FECD6. 1 Publication
VAR_063763

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 1919MADGP…PRRNN → MK in isoform 5.
VSP_047279Add
BLAST
Alternative sequencei20 – 8768VTNYN…WEDDR → G in isoform 3.
VSP_047280Add
BLAST
Alternative sequencei87 – 10721RKEGQ…AGCTV → I in isoform 4.
VSP_047281Add
BLAST
Alternative sequencei87 – 871R → TG in isoform 2 and isoform 5.
VSP_045184

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121Q → R in BAC03673. 1 Publication
Sequence conflicti81 – 811N → S in BAC03673. 1 Publication
Sequence conflicti84 – 841E → K in BAC03673. 1 Publication
Sequence conflicti220 – 2201T → A in BAG62481. 1 Publication
Sequence conflicti390 – 3901M → T in BAG62481. 1 Publication
Sequence conflicti420 – 4201V → I in AAA20602. 1 Publication
Sequence conflicti472 – 4721K → R in BAG58962. 1 Publication
Sequence conflicti609 – 6091E → Q in M81699. 1 Publication
Sequence conflicti654 – 6541I → T in AAA20602. 1 Publication
Sequence conflicti672 – 6721D → H in M81699. 1 Publication
Sequence conflicti681 – 6811L → S in M81699. 1 Publication
Sequence conflicti775 – 7751K → T in BAG62481. 1 Publication
Sequence conflicti793 – 7942IP → KY in BAG58962. 1 Publication
Sequence conflicti797 – 7971A → N in BAG58962. 1 Publication
Sequence conflicti818 – 8181A → V in BAG62481. 1 Publication
Sequence conflicti838 – 8381I → T in BAC03673. 1 Publication
Sequence conflicti1066 – 10661E → G in BAC03673. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D15050 mRNA. Translation: BAA03646.1.
U12170 mRNA. Translation: AAA20602.1.
AK091478 mRNA. Translation: BAC03673.1.
AK296244 mRNA. Translation: BAG58962.1.
AK300830 mRNA. Translation: BAG62481.1. Frameshift.
AL158080
, AL117340, AL161935, AL355148 Genomic DNA. Translation: CAI17320.1.
AL161935
, AL117340, AL158080, AL355148 Genomic DNA. Translation: CAH74132.1.
AL117340
, AL158080, AL161935, AL355148 Genomic DNA. Translation: CAI12550.1.
AL355148
, AL117340, AL158080, AL161935 Genomic DNA. Translation: CAI15108.1.
CH471072 Genomic DNA. Translation: EAW85989.1.
BC112392 mRNA. Translation: AAI12393.1.
M81699 mRNA. No translation available.
CCDSiCCDS44370.1. [P37275-5]
CCDS53505.1. [P37275-2]
CCDS53506.1. [P37275-4]
CCDS53507.1. [P37275-3]
CCDS7169.1. [P37275-1]
PIRiJX0293.
RefSeqiNP_001121600.1. NM_001128128.2. [P37275-5]
NP_001167564.1. NM_001174093.1. [P37275-4]
NP_001167565.1. NM_001174094.1.
NP_001167566.1. NM_001174095.1. [P37275-3]
NP_001167567.1. NM_001174096.1. [P37275-2]
NP_110378.3. NM_030751.5. [P37275-1]
UniGeneiHs.124503.

Genome annotation databases

EnsembliENST00000320985; ENSP00000319248; ENSG00000148516. [P37275-1]
ENST00000361642; ENSP00000354487; ENSG00000148516. [P37275-2]
ENST00000446923; ENSP00000391612; ENSG00000148516. [P37275-5]
ENST00000542815; ENSP00000444891; ENSG00000148516. [P37275-3]
ENST00000560721; ENSP00000452787; ENSG00000148516. [P37275-4]
GeneIDi6935.
KEGGihsa:6935.
UCSCiuc001ivr.4. human. [P37275-1]
uc001ivu.4. human.

Polymorphism databases

DMDMi6166575.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D15050 mRNA. Translation: BAA03646.1 .
U12170 mRNA. Translation: AAA20602.1 .
AK091478 mRNA. Translation: BAC03673.1 .
AK296244 mRNA. Translation: BAG58962.1 .
AK300830 mRNA. Translation: BAG62481.1 . Frameshift.
AL158080
, AL117340 , AL161935 , AL355148 Genomic DNA. Translation: CAI17320.1 .
AL161935
, AL117340 , AL158080 , AL355148 Genomic DNA. Translation: CAH74132.1 .
AL117340
, AL158080 , AL161935 , AL355148 Genomic DNA. Translation: CAI12550.1 .
AL355148
, AL117340 , AL158080 , AL161935 Genomic DNA. Translation: CAI15108.1 .
CH471072 Genomic DNA. Translation: EAW85989.1 .
BC112392 mRNA. Translation: AAI12393.1 .
M81699 mRNA. No translation available.
CCDSi CCDS44370.1. [P37275-5 ]
CCDS53505.1. [P37275-2 ]
CCDS53506.1. [P37275-4 ]
CCDS53507.1. [P37275-3 ]
CCDS7169.1. [P37275-1 ]
PIRi JX0293.
RefSeqi NP_001121600.1. NM_001128128.2. [P37275-5 ]
NP_001167564.1. NM_001174093.1. [P37275-4 ]
NP_001167565.1. NM_001174094.1.
NP_001167566.1. NM_001174095.1. [P37275-3 ]
NP_001167567.1. NM_001174096.1. [P37275-2 ]
NP_110378.3. NM_030751.5. [P37275-1 ]
UniGenei Hs.124503.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E19 NMR - A 586-642 [» ]
ProteinModelPortali P37275.
SMRi P37275. Positions 172-336, 583-642, 903-1003.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112796. 18 interactions.
IntActi P37275. 2 interactions.
MINTi MINT-94525.
STRINGi 9606.ENSP00000319248.

PTM databases

PhosphoSitei P37275.

Polymorphism databases

DMDMi 6166575.

Proteomic databases

MaxQBi P37275.
PaxDbi P37275.
PRIDEi P37275.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000320985 ; ENSP00000319248 ; ENSG00000148516 . [P37275-1 ]
ENST00000361642 ; ENSP00000354487 ; ENSG00000148516 . [P37275-2 ]
ENST00000446923 ; ENSP00000391612 ; ENSG00000148516 . [P37275-5 ]
ENST00000542815 ; ENSP00000444891 ; ENSG00000148516 . [P37275-3 ]
ENST00000560721 ; ENSP00000452787 ; ENSG00000148516 . [P37275-4 ]
GeneIDi 6935.
KEGGi hsa:6935.
UCSCi uc001ivr.4. human. [P37275-1 ]
uc001ivu.4. human.

Organism-specific databases

CTDi 6935.
GeneCardsi GC10P031648.
HGNCi HGNC:11642. ZEB1.
HPAi CAB058686.
HPA027524.
MIMi 189909. gene.
609141. phenotype.
613270. phenotype.
neXtProti NX_P37275.
Orphaneti 98974. Fuchs endothelial corneal dystrophy.
98973. Posterior polymorphous corneal dystrophy.
PharmGKBi PA162409589.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
HOGENOMi HOG000264256.
HOVERGENi HBG004697.
KOi K09299.
OMAi CPGDINA.
OrthoDBi EOG790G0D.
PhylomeDBi P37275.
TreeFami TF331759.

Enzyme and pathway databases

SignaLinki P37275.

Miscellaneous databases

ChiTaRSi ZEB1. human.
EvolutionaryTracei P37275.
GeneWikii ZEB1.
GenomeRNAii 6935.
NextBioi 27137.
PROi P37275.
SOURCEi Search...

Gene expression databases

ArrayExpressi P37275.
Bgeei P37275.
CleanExi HS_ZEB1.
Genevestigatori P37275.

Family and domain databases

Gene3Di 1.10.10.60. 1 hit.
3.30.160.60. 5 hits.
InterProi IPR008598. Di19_Zn_binding.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00046. Homeobox. 1 hit.
PF05605. zf-Di19. 1 hit.
[Graphical view ]
SMARTi SM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view ]
SUPFAMi SSF46689. SSF46689. 1 hit.
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Transcription factors positively and negatively regulating the Na,K-ATPase alpha 1 subunit gene."
    Watanabe Y., Kawakami K., Hirayama Y., Nagano K.
    J. Biochem. 114:849-855(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "A human zinc finger homeodomain protein homologous to the chicken delta-crystallin enhancer binding protein, delta EF1."
    Bachman N.J., Scarpulla R.C.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-798 (ISOFORM 5).
    Tissue: Brain and Thalamus.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORM 2).
  7. "Identification of a zinc finger protein that inhibits IL-2 gene expression."
    Williams T.M., Moolten D., Burlein J., Romano J., Bhaerman R., Godillot A., Mellon M., Rauscher F.J. III, Kant J.A.
    Science 254:1791-1794(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 390-1124.
  8. Cited for: INVOLVEMENT IN PPCD3.
  9. "Pc2-mediated sumoylation of Smad-interacting protein 1 attenuates transcriptional repression of E-cadherin."
    Long J., Zuo D., Park M.
    J. Biol. Chem. 280:35477-35489(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-347 AND LYS-774.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: FUNCTION.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; SER-679 AND THR-702, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "ZEB1 and CtBP form a repressive complex at a distal promoter element of the BCL6 locus."
    Papadopoulou V., Postigo A., Sanchez-Tillo E., Porter A.C., Wagner S.D.
    Biochem. J. 427:541-550(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF chromatin-remodeling protein BRG1."
    Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C., Castells A., Engel P., Postigo A.
    Oncogene 29:3490-3500(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SMARCA4, TISSUE SPECIFICITY.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-679, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Solution structure of the homeobox domain from human NIL-2-A zinc finger protein, transcription factor 8."
    RIKEN structural genomics initiative (RSGI)
    Submitted (APR-2007) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 583-642.
  20. "Missense mutations in TCF8 cause late-onset Fuchs corneal dystrophy and interact with FCD4 on chromosome 9p."
    Riazuddin S.A., Zaghloul N.A., Al-Saif A., Davey L., Diplas B.H., Meadows D.N., Eghrari A.O., Minear M.A., Li Y.J., Klintworth G.K., Afshari N., Gregory S.G., Gottsch J.D., Katsanis N.
    Am. J. Hum. Genet. 86:45-53(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS FECD6 THR-78; ALA-649; PRO-810; PRO-840 AND THR-905.

Entry informationi

Entry nameiZEB1_HUMAN
AccessioniPrimary (citable) accession number: P37275
Secondary accession number(s): B4DJV0
, B4DUW9, E9PCM7, F5H4I8, Q12924, Q13800, Q2KJ05, Q5T968, Q5VZ84, Q8NB68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1999
Last modified: September 3, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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