ZEB1_MESAU
ID ZEB1_MESAU Reviewed; 1043 AA.
AC Q60542;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Zinc finger E-box-binding homeobox 1;
DE AltName: Full=Transcription factor 8;
DE Short=TCF-8;
DE AltName: Full=Zinc finger protein BZP;
GN Name=ZEB1; Synonyms=BZP, TCF8;
OS Mesocricetus auratus (Golden hamster).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Mesocricetus.
OX NCBI_TaxID=10036;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Insulinoma;
RX PubMed=7935395; DOI=10.1128/mcb.14.10.6773-6788.1994;
RA Franklin A.J., Jetton T.L., Shelton K.D., Magnuson M.A.;
RT "BZP, a novel serum-responsive zinc finger protein that inhibits gene
RT transcription.";
RL Mol. Cell. Biol. 14:6773-6788(1994).
CC -!- FUNCTION: Acts as a transcriptional repressor. Binds to E-box sequences
CC in the immunoglobulin heavy chain enhancer as well as in the regulatory
CC regions of many other tissue-specific genes. Represses E-cadherin
CC promoter and induces an epithelial-mesenchymal transition (EMT) by
CC recruiting SMARCA4/BRG1. Represses BCL6 transcription in the presence
CC of the corepressor CTBP1. Positively regulates neuronal
CC differentiation. Represses RCOR1 transcription activation during
CC neurogenesis. Represses transcription by binding to the E box (5'-
CC CANNTG-3'). Promotes tumorigenicity by repressing stemness-inhibiting
CC microRNAs (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via N-terminus) with SMARCA4/BRG1. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- SIMILARITY: Belongs to the delta-EF1/ZFH-1 C2H2-type zinc-finger
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L13856; AAC37667.1; -; mRNA.
DR PIR; A56037; A56037.
DR RefSeq; NP_001268549.1; NM_001281620.1.
DR AlphaFoldDB; Q60542; -.
DR STRING; 10036.XP_005085224.1; -.
DR GeneID; 101832581; -.
DR CTD; 6935; -.
DR eggNOG; KOG3623; Eukaryota.
DR OrthoDB; 890458at2759; -.
DR Proteomes; UP000189706; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; IEA:Ensembl.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051216; P:cartilage development; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0071230; P:cellular response to amino acid stimulus; IEA:Ensembl.
DR GO; GO:0007417; P:central nervous system development; IEA:Ensembl.
DR GO; GO:0090103; P:cochlea morphogenesis; IEA:Ensembl.
DR GO; GO:0048596; P:embryonic camera-type eye morphogenesis; IEA:Ensembl.
DR GO; GO:0048704; P:embryonic skeletal system morphogenesis; IEA:Ensembl.
DR GO; GO:0043616; P:keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0045602; P:negative regulation of endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0010839; P:negative regulation of keratinocyte proliferation; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:0007389; P:pattern specification process; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010464; P:regulation of mesenchymal cell proliferation; IEA:Ensembl.
DR GO; GO:0051150; P:regulation of smooth muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
DR GO; GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:0048752; P:semicircular canal morphogenesis; IEA:Ensembl.
DR CDD; cd00086; homeodomain; 1.
DR InterPro; IPR008598; Di19_Zn-bd.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001356; Homeobox_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 4.
DR Pfam; PF05605; zf-Di19; 1.
DR SMART; SM00389; HOX; 1.
DR SMART; SM00355; ZnF_C2H2; 7.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 4.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 5.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 6.
PE 2: Evidence at transcript level;
KW Activator; Differentiation; DNA-binding; Homeobox; Isopeptide bond;
KW Metal-binding; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Repeat; Repressor; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1043
FT /note="Zinc finger E-box-binding homeobox 1"
FT /id="PRO_0000047232"
FT ZN_FING 94..117
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 124..146
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 164..186
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 192..216
FT /note="C2H2-type 4; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT DNA_BIND 504..563
FT /note="Homeobox; atypical"
FT ZN_FING 827..849
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 855..877
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 883..904
FT /note="C2H2-type 7; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 222..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..444
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..821
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 937..1043
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 574..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 783..809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 952..976
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 984..1000
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1022..1043
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 237
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 246
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 616
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q64318"
FT MOD_RES 625
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 119
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 231
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 255
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 259
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 271
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 363
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 417
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 428
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 439
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 472
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P37275"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT /evidence="ECO:0000250"
FT CROSSLNK 697
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P37275"
SQ SEQUENCE 1043 AA; 114203 MW; 5F8BE23DD1BCC667 CRC64;
MPEDELPADQ TVLPGGSDRE GGAKNCWQDD VKDDECDSDA ENEQNHDPNV EEFLQQQDTA
IIYPEAPEED QRQGTPEASG QDENGAADAF SQLLTCPYCD RGYKRFTSLK EHIKYRHEKN
EDNFSCSLCS YTFAYRTQLE RHMTSHKSGR EQRHVTQSGG NRKFKCTECG KAFKYKHHLK
EHLRIHSGEK PYECPNCKKR FSHSGSYSSH ISSKKCISLM PVNGRPRSGL KTSQCPSPSL
SASPGSPTRP QIRQKIENKP LQEPLSVNQI KTEPVDYEFK PIVVASGINC STPLQNGVFS
GGGQLQATSS PQGVVQAVVL PTVGLVSPIS INLSDIQNVL KVALDGNVIR QVLENNQASL
ASKEQEAVNA SSIQQGGHSV ISAISLPLVD QDGTTKIIIN YSLEQPSQLQ VVPQNLKIEN
PAPTNSCKSE KLPEDLTVKS EKDKGFDGAV DGSTCLLYDD CPGDLNALPE LKKHYDPEHP
AQPPPPAPEA EKPEASASSA RDGDLSPSQP PLKNLLSLLK AYYALNAQPN SEELSKIADS
VNLPLDVVKK WFEKMQAGQI PGQSPEPPSP ETGTVNIPAK SDEQPQPADG SEPQEDSASG
QSPLKMTSSP VLPVGSAING SRSCTSPPSP LNLSSARSLQ GYFCVADGAQ EEPQVEPLDL
SLPKQQGELL ERSTISSVYQ NSVYSVQEEP LNLSCVKKEP QEDSCVTDSE PVVNVIPPSA
NPINIAIPTV TAQLPTIVAI ADQNSVPCLR ALAANKQTIL IPQVAYTYAT TVSPAMQEPP
VKVIQPNGNQ DERQDTSSEG VSTVEDQNDS DSTPPKKKTR KTENGMYACD LCDKIFQKSS
SLLRHKYEHT GKRPHECGIC KKAFKHKHHL IEHMRLHSGE KPYQCDKCGK RFSHSGSYSQ
HMNHRYSYCK REAEERDGTE QEQEEAGLEA LMNEHVGARA SPSQADSDER ESLTREEDED
SEKEEEEEED KEMEELQEEK ECGNAQAEEE EEEEEEEMDG AKDEAAAKTD GAVENGAAPQ
AGSLEQKASE SSEQLSEETT NEA
