Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P37275

- ZEB1_HUMAN

UniProt

P37275 - ZEB1_HUMAN

Protein

Zinc finger E-box-binding homeobox 1

Gene

ZEB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (15 Jul 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri200 – 22223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri240 – 26223C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri268 – 29225C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
    BLAST
    DNA bindingi581 – 64060Homeobox; atypicalAdd
    BLAST
    Zinc fingeri904 – 92623C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri932 – 95423C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri960 – 98122C2H2-type 7; atypicalPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. double-stranded DNA binding Source: Ensembl
    3. E-box binding Source: UniProtKB
    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, DNA-templated Source: UniProtKB
    13. negative regulation of transcription from RNA polymerase II promoter Source: ProtInc
    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 mesenchymal cell proliferation Source: Ensembl
    18. regulation of smooth muscle cell differentiation Source: Ensembl
    19. regulation of T cell differentiation in thymus 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

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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 1PRO_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)
    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)

    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

    1
    1124
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP37275.

    Family & Domainsi

    Compositional bias

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

    Sequence similaritiesi

    Contains 7 C2H2-type zinc fingers.PROSITE-ProRule annotation
    Contains 1 homeobox DNA-binding domain.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri170 – 19324C2H2-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri200 – 22223C2H2-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri240 – 26223C2H2-type 3PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri268 – 29225C2H2-type 4; atypicalPROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri904 – 92623C2H2-type 5PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri932 – 95423C2H2-type 6PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri960 – 98122C2H2-type 7; atypicalPROSITE-ProRule annotationAdd
    BLAST

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121Q → R in BAC03673. (PubMed:14702039)Curated
    Sequence conflicti81 – 811N → S in BAC03673. (PubMed:14702039)Curated
    Sequence conflicti84 – 841E → K in BAC03673. (PubMed:14702039)Curated
    Sequence conflicti220 – 2201T → A in BAG62481. (PubMed:14702039)Curated
    Sequence conflicti390 – 3901M → T in BAG62481. (PubMed:14702039)Curated
    Sequence conflicti420 – 4201V → I in AAA20602. 1 PublicationCurated
    Sequence conflicti472 – 4721K → R in BAG58962. (PubMed:14702039)Curated
    Sequence conflicti609 – 6091E → Q in M81699. (PubMed:1840704)Curated
    Sequence conflicti654 – 6541I → T in AAA20602. 1 PublicationCurated
    Sequence conflicti672 – 6721D → H in M81699. (PubMed:1840704)Curated
    Sequence conflicti681 – 6811L → S in M81699. (PubMed:1840704)Curated
    Sequence conflicti775 – 7751K → T in BAG62481. (PubMed:14702039)Curated
    Sequence conflicti793 – 7942IP → KY in BAG58962. (PubMed:14702039)Curated
    Sequence conflicti797 – 7971A → N in BAG58962. (PubMed:14702039)Curated
    Sequence conflicti818 – 8181A → V in BAG62481. (PubMed:14702039)Curated
    Sequence conflicti838 – 8381I → T in BAC03673. (PubMed:14702039)Curated
    Sequence conflicti1066 – 10661E → G in BAC03673. (PubMed:14702039)Curated

    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. 1 PublicationVSP_047279Add
    BLAST
    Alternative sequencei20 – 8768VTNYN…WEDDR → G in isoform 3. 1 PublicationVSP_047280Add
    BLAST
    Alternative sequencei87 – 10721RKEGQ…AGCTV → I in isoform 4. 1 PublicationVSP_047281Add
    BLAST
    Alternative sequencei87 – 871R → TG in isoform 2 and isoform 5. 2 PublicationsVSP_045184

    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

    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: October 1, 2014
    This is version 152 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