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Early growth response protein 1-B (EGR-1-B)

 EGR1B_XENLA             Reviewed;         475 AA.
Q6NTY6;
13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
25-OCT-2017, entry version 65.
RecName: Full=Early growth response protein 1-B;
Short=EGR-1-B;
Name=egr1-b;
Xenopus laevis (African clawed frog).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Amphibia; Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus;
Xenopus.
NCBI_TaxID=8355;
[1] {ECO:0000312|EMBL:AAH68816.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Gastrula {ECO:0000312|EMBL:AAH68816.1};
NIH - Xenopus Gene Collection (XGC) project;
Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Transcriptional regulator. Recognizes and binds to the
DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region
of target genes (By similarity). Binds double-stranded target DNA,
irrespective of the cytosine methylation status (By similarity).
Regulates the transcription of numerous target genes, and thereby
plays an important role in regulating the response to growth
factors, DNA damage, and ischemia. Plays a role in the regulation
of cell survival, proliferation and cell death. Mediates responses
to ischemia and hypoxia; regulates the expression of proteins that
are involved in inflammatory processes (By similarity).
{ECO:0000250|UniProtKB:P08046, ECO:0000250|UniProtKB:P18146}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P18146}.
Cytoplasm {ECO:0000250|UniProtKB:P18146}.
-!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3'
via its C2H2-type zinc fingers. The first, most N-terminal zinc
finger binds to the 3'-GCG motif, the middle zinc finger interacts
with the central TGG motif, and the C-terminal zinc finger binds
to the 5'-GCG motif. Binds double-stranded target DNA,
irrespective of the cytosine methylation status. Has reduced
affinity for target DNA where the cytosines have been oxidized to
5-hydroxymethylcytosine. Does not bind target DNA where the
cytosines have been oxidized to 5-formylcytosine or 5-
carboxylcytosine. {ECO:0000250|UniProtKB:P18146}.
-!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein
family. {ECO:0000255}.
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EMBL; BC068816; AAH68816.1; -; mRNA.
RefSeq; NP_001084566.1; NM_001091097.1.
UniGene; Xl.46707; -.
ProteinModelPortal; Q6NTY6; -.
SMR; Q6NTY6; -.
GeneID; 414518; -.
KEGG; xla:414518; -.
CTD; 414518; -.
Xenbase; XB-GENE-6252570; egr1.
KO; K09203; -.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
InterPro; IPR021849; EGR.
InterPro; IPR021839; EGR1_C.
InterPro; IPR036236; Znf_C2H2_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF11914; DUF3432; 1.
Pfam; PF11928; DUF3446; 1.
SMART; SM00355; ZnF_C2H2; 3.
SUPFAM; SSF57667; SSF57667; 2.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
2: Evidence at transcript level;
Activator; Cytoplasm; DNA-binding; Metal-binding; Nucleus; Repeat;
Transcription; Transcription regulation; Zinc; Zinc-finger.
CHAIN 1 475 Early growth response protein 1-B.
/FTId=PRO_0000386428.
ZN_FING 284 308 C2H2-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 314 336 C2H2-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
ZN_FING 342 364 C2H2-type 3. {ECO:0000255|PROSITE-
ProRule:PRU00042}.
COMPBIAS 111 160 Ser-rich. {ECO:0000255}.
COMPBIAS 379 468 Ser-rich. {ECO:0000255}.
SITE 282 282 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 293 293 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 297 297 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 303 303 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 321 321 Interaction with DNA.
{ECO:0000250|UniProtKB:P08046}.
SITE 325 325 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 349 349 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 353 353 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SITE 359 359 Interaction with DNA.
{ECO:0000250|UniProtKB:P18146}.
SEQUENCE 475 AA; 51906 MW; 324B69090A9F9C7F CRC64;
MALAKTDMLV SPLQISDPFS SFPHSPTMDN YPKLDGAEQF DHHAADAFSE MSLSNEKAVL
ESSYANHTTR LPSLTYTGRF SLEPAPNSSN TLWPEPLFSL VSGLVGMANV SSSSAPSSSP
SSSSSSSSSS SSQSPPLSCS VQSNESSPIY SAAPTFPNSS PEMFPDHSPQ PFQNASTASI
PYPPPAYPVS KTTFQVPMIP DYLFPQQQGD VSLVSADQKP FQAMENRTQQ PSLTPLSTIK
AFATQTSQDL KTINSTYQSQ IIKPSRMRKY PNRPSKTPPH ERPYACPVES CDRRFSRSDE
LTRHIRIHTG QKPFQCRICM RNFSRSDHLT THIRTHTGEK PFACDICGRK FARSDERKRH
TKIHLRQKDK KADKATPVSI ASPVSAYSPS ASTSYPSPVP TSYSSPVSSC YPSPVHSSFP
SPTTAVTYPS VTSTFQTQCI TSFPSSIVTN SYSSPVSSAL SDMSVTYSPR TIEIC


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