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P37275 (ZEB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ZEB1
Synonyms:AREB6, TCF8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1124 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13 Ref.15 Ref.16

Subunit structure

Interacts (via N-terminus) with SMARCA4/BRG1. Ref.16

Subcellular location

Nucleus Ref.16.

Tissue specificity

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. Ref.16

Involvement in disease

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. Ref.8

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. Ref.20

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.

Sequence caution

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

Ontologies

Keywords
   Biological processDifferentiation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCorneal dystrophy
Disease mutation
   DomainHomeobox
Repeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionActivator
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcartilage development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.7. Source: ProtInc

cellular response to amino acid stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

cochlea morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic camera-type eye morphogenesis

Inferred from electronic annotation. Source: Ensembl

embryonic skeletal system morphogenesis

Inferred from electronic annotation. Source: Ensembl

forebrain development

Inferred from electronic annotation. Source: Ensembl

immune response

Traceable author statement Ref.7. Source: ProtInc

negative regulation of cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of epithelial cell differentiation

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.7. Source: ProtInc

negative regulation of transcription, DNA-templated

Inferred from direct assay Ref.16. Source: UniProtKB

pattern specification process

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

regulation of T cell differentiation in thymus

Inferred from electronic annotation. Source: Ensembl

regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

regulation of smooth muscle cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

regulation of transforming growth factor beta receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

response to activity

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

semicircular canal morphogenesis

Inferred from electronic annotation. Source: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

transcription factor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionE-box binding

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction Ref.16. Source: UniProtKB

sequence-specific DNA binding

Inferred from electronic annotation. Source: InterPro

sequence-specific DNA binding transcription factor activity

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Traceable author statement Ref.1. Source: ProtInc

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

zinc ion binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P37275-1)

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.
Isoform 2 (identifier: P37275-2)

The sequence of this isoform differs from the canonical sequence as follows:
     87-87: R → TG
Note: No experimental confirmation available.
Isoform 3 (identifier: P37275-3)

The sequence of this isoform differs from the canonical sequence as follows:
     20-87: VTNYNTVVETNSDSDDEDKLHIVEEESVTDAADCEGVPEDDLPTDQTVLPGRSSEREGNAKNCWEDDR → G
Isoform 4 (identifier: P37275-4)

The sequence of this isoform differs from the canonical sequence as follows:
     87-107: RKEGQEILGPEAQADEAGCTV → I
Isoform 5 (identifier: P37275-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 11241124Zinc finger E-box-binding homeobox 1
PRO_0000047231

Regions

Zinc finger170 – 19324C2H2-type 1
Zinc finger200 – 22223C2H2-type 2
Zinc finger240 – 26223C2H2-type 3
Zinc finger268 – 29225C2H2-type 4; atypical
DNA binding581 – 64060Homeobox; atypical
Zinc finger904 – 92623C2H2-type 5
Zinc finger932 – 95423C2H2-type 6
Zinc finger960 – 98122C2H2-type 7; atypical
Compositional bias989 – 1124136Glu-rich (acidic)

Amino acid modifications

Modified residue3221Phosphoserine Ref.11
Modified residue6421Phosphoserine Ref.14
Modified residue6791Phosphoserine Ref.14 Ref.17
Modified residue7021Phosphothreonine Ref.14
Cross-link347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9
Cross-link774Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.9

Natural variations

Alternative sequence1 – 1919MADGP…PRRNN → MK in isoform 5.
VSP_047279
Alternative sequence20 – 8768VTNYN…WEDDR → G in isoform 3.
VSP_047280
Alternative sequence87 – 10721RKEGQ…AGCTV → I in isoform 4.
VSP_047281
Alternative sequence871R → TG in isoform 2 and isoform 5.
VSP_045184
Natural variant781N → T in FECD6. Ref.20
Corresponds to variant rs80194531 [ dbSNP | Ensembl ].
VAR_063759
Natural variant901G → R.
Corresponds to variant rs12217419 [ dbSNP | Ensembl ].
VAR_052731
Natural variant5531K → R.
Corresponds to variant rs35753967 [ dbSNP | Ensembl ].
VAR_031824
Natural variant6491P → A in FECD6. Ref.20
VAR_063760
Natural variant8101Q → P in FECD6. Ref.20
VAR_063761
Natural variant8401Q → P in FECD6. Ref.20
Corresponds to variant rs118020901 [ dbSNP | Ensembl ].
VAR_063762
Natural variant9051A → T in FECD6. Ref.20
VAR_063763

Experimental info

Sequence conflict121Q → R in BAC03673. Ref.3
Sequence conflict811N → S in BAC03673. Ref.3
Sequence conflict841E → K in BAC03673. Ref.3
Sequence conflict2201T → A in BAG62481. Ref.3
Sequence conflict3901M → T in BAG62481. Ref.3
Sequence conflict4201V → I in AAA20602. Ref.2
Sequence conflict4721K → R in BAG58962. Ref.3
Sequence conflict6091E → Q in M81699. Ref.7
Sequence conflict6541I → T in AAA20602. Ref.2
Sequence conflict6721D → H in M81699. Ref.7
Sequence conflict6811L → S in M81699. Ref.7
Sequence conflict7751K → T in BAG62481. Ref.3
Sequence conflict793 – 7942IP → KY in BAG58962. Ref.3
Sequence conflict7971A → N in BAG58962. Ref.3
Sequence conflict8181A → V in BAG62481. Ref.3
Sequence conflict8381I → T in BAC03673. Ref.3
Sequence conflict10661E → G in BAC03673. Ref.3

Secondary structure

....... 1124
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 15, 1999. Version 2.
Checksum: 0A2714CC37C848D1

FASTA1,124124,074
        10         20         30         40         50         60 
MADGPRCKRR KQANPRRNNV TNYNTVVETN SDSDDEDKLH IVEEESVTDA ADCEGVPEDD 

        70         80         90        100        110        120 
LPTDQTVLPG RSSEREGNAK NCWEDDRKEG QEILGPEAQA DEAGCTVKDD ECESDAENEQ 

       130        140        150        160        170        180 
NHDPNVEEFL QQQDTAVIFP EAPEEDQRQG TPEASGHDEN GTPDAFSQLL TCPYCDRGYK 

       190        200        210        220        230        240 
RFTSLKEHIK YRHEKNEDNF SCSLCSYTFA YRTQLERHMT SHKSGRDQRH VTQSGCNRKF 

       250        260        270        280        290        300 
KCTECGKAFK YKHHLKEHLR IHSGEKPYEC PNCKKRFSHS GSYSSHISSK KCISLIPVNG 

       310        320        330        340        350        360 
RPRTGLKTSQ CSSPSLSASP GSPTRPQIRQ KIENKPLQEQ LSVNQIKTEP VDYEFKPIVV 

       370        380        390        400        410        420 
ASGINCSTPL QNGVFTGGGP LQATSSPQGM VQAVVLPTVG LVSPISINLS DIQNVLKVAV 

       430        440        450        460        470        480 
DGNVIRQVLE NNQANLASKE QETINASPIQ QGGHSVISAI SLPLVDQDGT TKIIINYSLE 

       490        500        510        520        530        540 
QPSQLQVVPQ NLKKENPVAT NSCKSEKLPE DLTVKSEKDK SFEGGVNDST CLLCDDCPGD 

       550        560        570        580        590        600 
INALPELKHY DLKQPTQPPP LPAAEAEKPE SSVSSATGDG NLSPSQPPLK NLLSLLKAYY 

       610        620        630        640        650        660 
ALNAQPSAEE LSKIADSVNL PLDVVKKWFE KMQAGQISVQ SSEPSSPEPG KVNIPAKNND 

       670        680        690        700        710        720 
QPQSANANEP QDSTVNLQSP LKMTNSPVLP VGSTTNGSRS STPSPSPLNL SSSRNTQGYL 

       730        740        750        760        770        780 
YTAEGAQEEP QVEPLDLSLP KQQGELLERS TITSVYQNSV YSVQEEPLNL SCAKKEPQKD 

       790        800        810        820        830        840 
SCVTDSEPVV NVIPPSANPI NIAIPTVTAQ LPTIVAIADQ NSVPCLRALA ANKQTILIPQ 

       850        860        870        880        890        900 
VAYTYSTTVS PAVQEPPLKV IQPNGNQDER QDTSSEGVSN VEDQNDSDST PPKKKMRKTE 

       910        920        930        940        950        960 
NGMYACDLCD KIFQKSSSLL RHKYEHTGKR PHECGICKKA FKHKHHLIEH MRLHSGEKPY 

       970        980        990       1000       1010       1020 
QCDKCGKRFS HSGSYSQHMN HRYSYCKREA EERDSTEQEE AGPEILSNEH VGARASPSQG 

      1030       1040       1050       1060       1070       1080 
DSDERESLTR EEDEDSEKEE EEEDKEMEEL QEEKECEKPQ GDEEEEEEEE EVEEEEVEEA 

      1090       1100       1110       1120 
ENEGEEAKTE GLMKDDRAES QASSLGQKVG ESSEQVSEEK TNEA 

« Hide

Isoform 2 [UniParc].

Checksum: 3C327EEBBA18D19B
Show »

FASTA1,125124,076
Isoform 3 [UniParc].

Checksum: 7C683713C6562DC8
Show »

FASTA1,057116,593
Isoform 4 [UniParc].

Checksum: 3F8DAA9A05DFA6E4
Show »

FASTA1,104122,003
Isoform 5 [UniParc].

Checksum: 33855F3B478635C8
Show »

FASTA1,108122,084

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Mutations in TCF8 cause posterior polymorphous corneal dystrophy and ectopic expression of COL4A3 by corneal endothelial cells."
Krafchak C.M., Pawar H., Moroi S.E., Sugar A., Lichter P.R., Mackey D.A., Mian S., Nairus T., Elner V., Schteingart M.T., Downs C.A., Kijek T.G., Johnson J.M., Trager E.H., Rozsa F.W., Mandal M.N.A., Epstein M.P., Vollrath D. expand/collapse author list , Ayyagari R., Boehnke M., Richards J.E.
Am. J. Hum. Genet. 77:694-708(2005) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"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.
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AL117340, AL161935, AL355148 Genomic DNA. Translation: CAI17320.1.
AL161935 expand/collapse EMBL AC list , AL117340, AL158080, AL355148 Genomic DNA. Translation: CAH74132.1.
AL117340 expand/collapse EMBL AC list , AL158080, AL161935, AL355148 Genomic DNA. Translation: CAI12550.1.
AL355148 expand/collapse EMBL AC list , AL117340, AL158080, AL161935 Genomic DNA. Translation: CAI15108.1.
CH471072 Genomic DNA. Translation: EAW85989.1.
BC112392 mRNA. Translation: AAI12393.1.
M81699 mRNA. No translation available.
CCDSCCDS44370.1. [P37275-5]
CCDS53505.1. [P37275-2]
CCDS53506.1. [P37275-4]
CCDS53507.1. [P37275-3]
CCDS7169.1. [P37275-1]
PIRJX0293.
RefSeqNP_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]
UniGeneHs.124503.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E19NMR-A586-642[»]
ProteinModelPortalP37275.
SMRP37275. Positions 172-336, 583-642, 903-1003.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112796. 17 interactions.
IntActP37275. 2 interactions.
MINTMINT-94525.
STRING9606.ENSP00000319248.

PTM databases

PhosphoSiteP37275.

Polymorphism databases

DMDM6166575.

Proteomic databases

MaxQBP37275.
PaxDbP37275.
PRIDEP37275.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320985; ENSP00000319248; ENSG00000148516. [P37275-1]
ENST00000361642; ENSP00000354487; ENSG00000148516. [P37275-2]
ENST00000446923; ENSP00000391612; ENSG00000148516. [P37275-5]
ENST00000542815; ENSP00000444891; ENSG00000148516. [P37275-3]
ENST00000560721; ENSP00000452787; ENSG00000148516. [P37275-4]
GeneID6935.
KEGGhsa:6935.
UCSCuc001ivr.4. human. [P37275-1]
uc001ivu.4. human.

Organism-specific databases

CTD6935.
GeneCardsGC10P031648.
HGNCHGNC:11642. ZEB1.
HPACAB058686.
HPA027524.
MIM189909. gene.
609141. phenotype.
613270. phenotype.
neXtProtNX_P37275.
Orphanet98974. Fuchs endothelial corneal dystrophy.
98973. Posterior polymorphous corneal dystrophy.
PharmGKBPA162409589.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5048.
HOGENOMHOG000264256.
HOVERGENHBG004697.
KOK09299.
OMACPGDINA.
OrthoDBEOG790G0D.
PhylomeDBP37275.
TreeFamTF331759.

Enzyme and pathway databases

SignaLinkP37275.

Gene expression databases

ArrayExpressP37275.
BgeeP37275.
CleanExHS_ZEB1.
GenevestigatorP37275.

Family and domain databases

Gene3D1.10.10.60. 1 hit.
3.30.160.60. 5 hits.
InterProIPR008598. Di19_Zn_binding.
IPR001356. Homeobox_dom.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamPF00046. Homeobox. 1 hit.
PF05605. zf-Di19. 1 hit.
[Graphical view]
SMARTSM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]
SUPFAMSSF46689. SSF46689. 1 hit.
PROSITEPS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZEB1. human.
EvolutionaryTraceP37275.
GeneWikiZEB1.
GenomeRNAi6935.
NextBio27137.
PROP37275.
SOURCESearch...

Entry information

Entry nameZEB1_HUMAN
AccessionPrimary (citable) accession number: P37275
Secondary accession number(s): B4DJV0 expand/collapse secondary AC list , B4DUW9, E9PCM7, F5H4I8, Q12924, Q13800, Q2KJ05, Q5T968, Q5VZ84, Q8NB68
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: July 15, 1999
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM