P37275 (ZEB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	ZEB1
Synonyms:	AREB6, TCF8

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1124 AA.
Sequence status	Complete.
Protein existence	Evidence 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.11 Ref.13 Ref.14
Subunit structure	Interacts (via N-terminus) with SMARCA4/BRG1. Ref.14
Subcellular location	Nucleus Ref.14.
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.14
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.7 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.18
Sequence similarities	Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger family. Contains 7 C2H2-type zinc fingers. Contains 1 homeobox DNA-binding domain.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Corneal dystrophy Disease mutation
Domain	Homeobox Repeat Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
Molecular function	Activator Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Traceable author statement Ref.6. Source: ProtInc immune response Traceable author statement Ref.6. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.6. Source: ProtInc positive regulation of neuron differentiation Inferred from sequence or structural similarity. Source: UniProtKB transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.14. Source: UniProtKB
Molecular_function	E-box binding Inferred from sequence or structural similarity. 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 2 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1124

1124

Zinc finger E-box-binding homeobox 1

PRO_0000047231

Regions

Zinc finger

170 – 193

24

C2H2-type 1

Zinc finger

200 – 222

23

C2H2-type 2

Zinc finger

240 – 262

23

C2H2-type 3

Zinc finger

268 – 292

25

C2H2-type 4; atypical

DNA binding

581 – 640

60

Homeobox; atypical

Zinc finger

904 – 926

23

C2H2-type 5

Zinc finger

932 – 954

23

C2H2-type 6

Zinc finger

960 – 981

22

C2H2-type 7; atypical

Compositional bias

989 – 1124

136

Glu-rich (acidic)

Amino acid modifications

Modified residue

322

1

Phosphoserine Ref.10

Modified residue

642

1

Phosphoserine Ref.12

Modified residue

679

1

Phosphoserine Ref.12 Ref.15

Modified residue

702

1

Phosphothreonine Ref.12

Cross-link

347

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Cross-link

774

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.8

Natural variations

Alternative sequence

87

1

R → TG in isoform 2.

VSP_045184

Natural variant

78

1

N → T in FECD6. Ref.18

VAR_063759

Natural variant

90

1

G → R.
Corresponds to variant rs12217419 [ dbSNP | Ensembl ].

VAR_052731

Natural variant

553

1

K → R.
Corresponds to variant rs35753967 [ dbSNP | Ensembl ].

VAR_031824

Natural variant

649

1

P → A in FECD6. Ref.18

VAR_063760

Natural variant

810

1

Q → P in FECD6. Ref.18

VAR_063761

Natural variant

840

1

Q → P in FECD6. Ref.18

VAR_063762

Natural variant

905

1

A → T in FECD6. Ref.18

VAR_063763

Experimental info

Sequence conflict

420

1

V → I in AAA20602. Ref.2

Sequence conflict

609

1

E → Q in M81699. Ref.6

Sequence conflict

654

1

I → T in AAA20602. Ref.2

Sequence conflict

672

1

D → H in M81699. Ref.6

Sequence conflict

681

1

L → S in M81699. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

1124

Helix Strand Turn

Details...

Helix

590 – 600

11

Helix

608 – 618

11

Helix

622 – 634

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 15, 1999. Version 2. Checksum: 0A2714CC37C848D1	FASTA	1,124	124,074
	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
	Isoform 2 [UniParc]. Checksum: 3C327EEBBA18D19B	FASTA	1,125	124,076
	10 20 30 40 50 60 MADGPRCKRR KQANPRRNNV TNYNTVVETN SDSDDEDKLH IVEEESVTDA ADCEGVPEDD 70 80 90 100 110 120 LPTDQTVLPG RSSEREGNAK NCWEDDTGKE GQEILGPEAQ ADEAGCTVKD DECESDAENE 130 140 150 160 170 180 QNHDPNVEEF LQQQDTAVIF PEAPEEDQRQ GTPEASGHDE NGTPDAFSQL LTCPYCDRGY 190 200 210 220 230 240 KRFTSLKEHI KYRHEKNEDN FSCSLCSYTF AYRTQLERHM TSHKSGRDQR HVTQSGCNRK 250 260 270 280 290 300 FKCTECGKAF KYKHHLKEHL RIHSGEKPYE CPNCKKRFSH SGSYSSHISS KKCISLIPVN 310 320 330 340 350 360 GRPRTGLKTS QCSSPSLSAS PGSPTRPQIR QKIENKPLQE QLSVNQIKTE PVDYEFKPIV 370 380 390 400 410 420 VASGINCSTP LQNGVFTGGG PLQATSSPQG MVQAVVLPTV GLVSPISINL SDIQNVLKVA 430 440 450 460 470 480 VDGNVIRQVL ENNQANLASK EQETINASPI QQGGHSVISA ISLPLVDQDG TTKIIINYSL 490 500 510 520 530 540 EQPSQLQVVP QNLKKENPVA TNSCKSEKLP EDLTVKSEKD KSFEGGVNDS TCLLCDDCPG 550 560 570 580 590 600 DINALPELKH YDLKQPTQPP PLPAAEAEKP ESSVSSATGD GNLSPSQPPL KNLLSLLKAY 610 620 630 640 650 660 YALNAQPSAE ELSKIADSVN LPLDVVKKWF EKMQAGQISV QSSEPSSPEP GKVNIPAKNN 670 680 690 700 710 720 DQPQSANANE PQDSTVNLQS PLKMTNSPVL PVGSTTNGSR SSTPSPSPLN LSSSRNTQGY 730 740 750 760 770 780 LYTAEGAQEE PQVEPLDLSL PKQQGELLER STITSVYQNS VYSVQEEPLN LSCAKKEPQK 790 800 810 820 830 840 DSCVTDSEPV VNVIPPSANP INIAIPTVTA QLPTIVAIAD QNSVPCLRAL AANKQTILIP 850 860 870 880 890 900 QVAYTYSTTV SPAVQEPPLK VIQPNGNQDE RQDTSSEGVS NVEDQNDSDS TPPKKKMRKT 910 920 930 940 950 960 ENGMYACDLC DKIFQKSSSL LRHKYEHTGK RPHECGICKK AFKHKHHLIE HMRLHSGEKP 970 980 990 1000 1010 1020 YQCDKCGKRF SHSGSYSQHM NHRYSYCKRE AEERDSTEQE EAGPEILSNE HVGARASPSQ 1030 1040 1050 1060 1070 1080 GDSDERESLT REEDEDSEKE EEEEDKEMEE LQEEKECEKP QGDEEEEEEE EEVEEEEVEE 1090 1100 1110 1120 AENEGEEAKT EGLMKDDRAE SQASSLGQKV GESSEQVSEE KTNEA

References

	« Hide 'large scale' referencesShow '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]	"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].
[4]	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. , 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].
[5]	"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).
[6]	"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.
[7]	"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. , Ayyagari R., Boehnke M., Richards J.E. Am. J. Hum. Genet. 77:694-708(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN PPCD3.
[8]	"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.
[9]	"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.
[10]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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.
[14]	"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.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"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].
[17]	"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.
[18]	"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.
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.

IPI

IPI00375505.
IPI00514481.

PIR

JX0293.

RefSeq

NP_001121600.1. NM_001128128.2.
NP_001167564.1. NM_001174093.1.
NP_001167565.1. NM_001174094.1.
NP_001167566.1. NM_001174095.1.
NP_001167567.1. NM_001174096.1.
NP_110378.3. NM_030751.5.

UniGene

Hs.124503.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E19	NMR	-	A	586-642	[»]

ProteinModelPortal

P37275.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37275. 2 interactions.

MINT

MINT-94525.

STRING

9606.ENSP00000319248.

PTM databases

PhosphoSite

P37275.

Polymorphism databases

DMDM

6166575.

Proteomic databases

PaxDb

P37275.

PRIDE

P37275.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000320985; ENSP00000319248; ENSG00000148516.
ENST00000361642; ENSP00000354487; ENSG00000148516.

GeneID

6935.

KEGG

hsa:6935.

UCSC

uc001ivr.4. human.

Organism-specific databases

CTD

6935.

GeneCards

GC10P031648.

HGNC

HGNC:11642. ZEB1.

HPA

CAB058686.
HPA027524.

MIM

189909. gene.
609141. phenotype.
613270. phenotype.

neXtProt

NX_P37275.

Orphanet

98974. Fuchs endothelial corneal dystrophy.
98973. Posterior polymorphous corneal dystrophy.

PharmGKB

PA162409589.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5048.

HOVERGEN

HBG004697.

KO

K09299.

OMA

TQGYLYT.

OrthoDB

EOG49CQ6Z.

PhylomeDB

P37275.

Gene expression databases

ArrayExpress

P37275.

Bgee

P37275.

CleanEx

HS_ZEB1.

Genevestigator

P37275.

GermOnline

ENSG00000148516. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.60. 1 hit.
3.30.160.60. 5 hits.

InterPro

IPR001356. Homeodomain.
IPR009057. Homeodomain-like.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]

Pfam

PF00046. Homeobox. 1 hit.
PF00096. zf-C2H2. 1 hit.
[Graphical view]

SMART

SM00389. HOX. 1 hit.
SM00355. ZnF_C2H2. 7 hits.
[Graphical view]

PROSITE

PS00027. HOMEOBOX_1. False negative.
PS50071. HOMEOBOX_2. False negative.
PS00028. ZINC_FINGER_C2H2_1. 5 hits.
PS50157. ZINC_FINGER_C2H2_2. 6 hits.
[Graphical view]

ProtoNet

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Other

ChiTaRS

ZEB1. human.

EvolutionaryTrace

P37275.

GenomeRNAi

6935.

NextBio

27137.

SOURCE

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Entry information

Entry name

ZEB1_HUMAN

Accession

Primary (citable) accession number: P37275
Secondary accession number(s): Q12924 , Q13800, Q2KJ05, Q5T968

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	July 15, 1999
Last modified:	May 1, 2013
This is version 137 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.