EGR1_MOUSE
ID EGR1_MOUSE Reviewed; 533 AA.
AC P08046; Q61777;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 2.
DT 03-AUG-2022, entry version 205.
DE RecName: Full=Early growth response protein 1;
DE Short=EGR-1;
DE AltName: Full=Nerve growth factor-induced protein A {ECO:0000303|PubMed:1740423};
DE Short=NGFI-A {ECO:0000303|PubMed:1740423};
DE AltName: Full=Transcription factor Zif268 {ECO:0000303|PubMed:2028256};
DE AltName: Full=Zinc finger protein Krox-24 {ECO:0000303|PubMed:2511075};
GN Name=Egr1; Synonyms=Egr-1, Krox-24 {ECO:0000303|PubMed:2511075};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3127059; DOI=10.1016/0092-8674(88)90485-0;
RA Sukhatme V.P., Cao X., Chang L.C., Tsai-Morris C.-H., Stamenkovich D.,
RA Ferreira P.C.P., Cohen D.R., Edwards S.A., Shows T.B., Curran T.,
RA le Beau M.M., Adamson E.D.;
RT "A zinc finger-encoding gene coregulated with c-fos during growth and
RT differentiation, and after cellular depolarization.";
RL Cell 53:37-43(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3141919; DOI=10.1073/pnas.85.21.7857;
RA Christy B.A., Lau L.F., Nathans D.;
RT "A gene activated in mouse 3T3 cells by serum growth factors encodes a
RT protein with 'zinc finger' sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:7857-7861(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2511075; DOI=10.1016/0378-1119(89)90296-5;
RA Janssen-Timmen U., Lemaire P., Mattei M.-G., Revelant O., Charnay P.;
RT "Structure, chromosome mapping and regulation of the mouse zinc-finger gene
RT Krox-24; evidence for a common regulatory pathway for immediate-early
RT serum-response genes.";
RL Gene 80:325-336(1989).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 50-533, AND INDUCTION BY GROWTH FACTORS.
RX PubMed=3133658; DOI=10.1073/pnas.85.13.4691;
RA Lemaire P., Revelant O., Bravo R., Charnay P.;
RT "Two mouse genes encoding potential transcription factors with identical
RT DNA-binding domains are activated by growth factors in cultured cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:4691-4695(1988).
RN [5]
RP MUTAGENESIS OF ZINC-FINGERS, AND DOMAIN.
RX PubMed=1740423; DOI=10.1016/s0021-9258(19)50584-1;
RA Wilson T.E., Day M.L., Pexton T., Padgett K.A., Johnston M., Milbrandt J.;
RT "In vivo mutational analysis of the NGFI-A zinc fingers.";
RL J. Biol. Chem. 267:3718-3724(1992).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8336701; DOI=10.1128/mcb.13.8.4556-4571.1993;
RA Gashler A.L., Swaminathan S., Sukhatme V.P.;
RT "A novel repression module, an extensive activation domain, and a bipartite
RT nuclear localization signal defined in the immediate-early transcription
RT factor Egr-1.";
RL Mol. Cell. Biol. 13:4556-4571(1993).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8703054; DOI=10.1126/science.273.5279.1219;
RA Lee S.L., Sadovsky Y., Swirnoff A.H., Polish J.A., Goda P., Gavrilina G.,
RA Milbrandt J.;
RT "Luteinizing hormone deficiency and female infertility in mice lacking the
RT transcription factor NGFI-A (Egr-1).";
RL Science 273:1219-1221(1996).
RN [8]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP AND INDUCTION BY ISCHEMIA.
RX PubMed=11100120; DOI=10.1038/82168;
RA Yan S.F., Fujita T., Lu J., Okada K., Shan Zou Y., Mackman N., Pinsky D.J.,
RA Stern D.M.;
RT "Egr-1, a master switch coordinating upregulation of divergent gene
RT families underlying ischemic stress.";
RL Nat. Med. 6:1355-1361(2000).
RN [9]
RP DISRUPTION PHENOTYPE, FUNCTION, TISSUE SPECIFICITY, AND INDUCTION BY
RP PARTIAL HEPATECTOMY.
RX PubMed=15265859; DOI=10.1074/jbc.m407969200;
RA Liao Y., Shikapwashya O.N., Shteyer E., Dieckgraefe B.K., Hruz P.W.,
RA Rudnick D.A.;
RT "Delayed hepatocellular mitotic progression and impaired liver regeneration
RT in early growth response-1-deficient mice.";
RL J. Biol. Chem. 279:43107-43116(2004).
RN [10]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=15958557; DOI=10.1158/0008-5472.can-04-3742;
RA Krones-Herzig A., Mittal S., Yule K., Liang H., English C., Urcis R.,
RA Soni T., Adamson E.D., Mercola D.;
RT "Early growth response 1 acts as a tumor suppressor in vivo and in vitro
RT via regulation of p53.";
RL Cancer Res. 65:5133-5143(2005).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=26471974; DOI=10.1038/srep15212;
RA Tao W., Wu J., Zhang Q., Lai S.S., Jiang S., Jiang C., Xu Y., Xue B.,
RA Du J., Li C.J.;
RT "EGR1 regulates hepatic clock gene amplitude by activating Per1
RT transcription.";
RL Sci. Rep. 5:15212-15212(2015).
RN [12]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=29138967; DOI=10.1007/s12031-017-0996-8;
RA Riedel C.S., Georg B., Joergensen H.L., Hannibal J., Fahrenkrug J.;
RT "Mice lacking EGR1 have impaired clock gene (BMAL1) oscillation, locomotor
RT activity, and body temperature.";
RL J. Mol. Neurosci. 64:9-19(2018).
RN [13] {ECO:0007744|PDB:1ZAA}
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 332-418 IN COMPLEX WITH ZINC AND
RP TARGET DNA, DOMAIN, AND FUNCTION.
RX PubMed=2028256; DOI=10.1126/science.2028256;
RA Pavletich N.P., Pabo C.O.;
RT "Zinc finger-DNA recognition: crystal structure of a Zif268-DNA complex at
RT 2.1 A.";
RL Science 252:809-817(1991).
RN [14] {ECO:0007744|PDB:1AAY}
RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 333-421 IN COMPLEX WITH ZINC AND
RP TARGET DNA, DOMAIN, AND FUNCTION.
RX PubMed=8939742; DOI=10.1016/s0969-2126(96)00125-6;
RA Elrod-Erickson M., Rould M.A., Nekludova L., Pabo C.O.;
RT "Zif268 protein-DNA complex refined at 1.6 A: a model system for
RT understanding zinc finger-DNA interactions.";
RL Structure 4:1171-1180(1996).
CC -!- FUNCTION: Transcriptional regulator (PubMed:8336701, PubMed:8703054,
CC PubMed:15958557). Recognizes and binds to the DNA sequence 5'-
CC GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes
CC (PubMed:8703054, PubMed:15958557, PubMed:2028256, PubMed:8939742).
CC Binds double-stranded target DNA, irrespective of the cytosine
CC methylation status (By similarity). Regulates the transcription of
CC numerous target genes, and thereby plays an important role in
CC regulating the response to growth factors, DNA damage, and ischemia
CC (PubMed:11100120, PubMed:15958557). Plays a role in the regulation of
CC cell survival, proliferation and cell death (PubMed:15265859,
CC PubMed:15958557). Activates expression of p53/TP53 and TGFB1, and
CC thereby helps prevent tumor formation (PubMed:15958557). Required for
CC normal progress through mitosis and normal proliferation of hepatocytes
CC after partial hepatectomy (PubMed:15265859). Mediates responses to
CC ischemia and hypoxia; regulates the expression of proteins such as IL1B
CC and CXCL2 that are involved in inflammatory processes and development
CC of tissue damage after ischemia (PubMed:11100120). Regulates
CC biosynthesis of luteinizing hormone (LHB) in the pituitary
CC (PubMed:8703054). Regulates the amplitude of the expression rhythms of
CC clock genes: ARNTL/BMAL1, PER2 and NR1D1 in the liver via the
CC activation of PER1 (clock repressor) transcription (PubMed:26471974).
CC Regulates the rhythmic expression of core-clock gene ARNTL/BMAL1 in the
CC suprachiasmatic nucleus (SCN) (PubMed:29138967).
CC {ECO:0000250|UniProtKB:P18146, ECO:0000269|PubMed:11100120,
CC ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:15958557,
CC ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:26471974,
CC ECO:0000269|PubMed:29138967, ECO:0000269|PubMed:8336701,
CC ECO:0000269|PubMed:8703054, ECO:0000269|PubMed:8939742, ECO:0000305}.
CC -!- SUBUNIT: Interacts with SNAI1 and SP1 upon 12-O-tetradecanoylphorbol-
CC 13-acetate (TPA) induction. {ECO:0000250|UniProtKB:P18146}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11100120,
CC ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:8336701}. Cytoplasm
CC {ECO:0000250|UniProtKB:P18146}.
CC -!- TISSUE SPECIFICITY: Detected in lung vasculature and in mononuclear
CC phagocytes (PubMed:11100120). Detected in liver (at protein level)
CC (PubMed:15265859). Detected in lung vasculature and in mononuclear
CC phagocytes (PubMed:11100120). Expressed in the liver in a circadian
CC manner (PubMed:26471974). {ECO:0000269|PubMed:11100120,
CC ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:26471974}.
CC -!- INDUCTION: By growth factors (PubMed:3133658). Up-regulated in lung
CC vasculature in response to reperfusion after ischemia
CC (PubMed:11100120). Up-regulated in liver in response to partial
CC hepatectomy (PubMed:15265859). {ECO:0000269|PubMed:11100120,
CC ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:3133658}.
CC -!- DOMAIN: Binds to DNA motifs with the sequence 5'-GCG(T/G)GGGCG-3' via
CC its C2H2-type zinc fingers (PubMed:1740423, PubMed:8336701,
CC PubMed:2028256, PubMed:8939742). The first, most N-terminal zinc finger
CC binds to the 3'-GCG motif, the middle zinc finger interacts with the
CC central TGG motif, and the C-terminal zinc finger binds to the 5'-GCG
CC motif (PubMed:2028256, PubMed:8939742). Binds double-stranded target
CC DNA, irrespective of the cytosine methylation status. Has reduced
CC affinity for target DNA where the cytosines have been oxidized to 5-
CC hydroxymethylcytosine. Does not bind target DNA where the cytosines
CC have been oxidized to 5-formylcytosine or 5-carboxylcytosine (By
CC similarity). {ECO:0000250|UniProtKB:P18146, ECO:0000269|PubMed:1740423,
CC ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742}.
CC -!- DISRUPTION PHENOTYPE: Mice appear grossly normal, but females are
CC anestrous and infertile with an uterus weight that is roughly 30% of
CC that of wild-type. Ovaries contain normal numbers of follicles, but
CC lack corpora lutea. Serum progesterone levels are strongly reduced;
CC estradiol levels are normal. The level of luteinizing hormone (LHB) in
CC the pituitary is strongly reduced in males and not detectable in
CC females (PubMed:8703054). Responses to ischemia and hypoxia are
CC blunted, leading to reduced tissue damage in response to ischemia and
CC increased survival (PubMed:11100120). Liver regeneration is impaired
CC after partial hepatectomy, due to impaired mitotic progress and reduced
CC proliferation of hepatocytes (PubMed:15265859). Untreated mutant mice
CC do not display an increased tendency to develop tumors, but develop
CC tumors earlier than wild-type when treated first with a tumor
CC initiator, and then with a tumor promoter (PubMed:15958557). Mice lack
CC daily rhythmicity in the expression of the core-clock gene ARNTL/BMAL1
CC and display a reduced and altered locomotor activity and altered
CC temperature regulation (PubMed:29138967). {ECO:0000269|PubMed:11100120,
CC ECO:0000269|PubMed:15265859, ECO:0000269|PubMed:15958557,
CC ECO:0000269|PubMed:29138967, ECO:0000269|PubMed:8703054}.
CC -!- SIMILARITY: Belongs to the EGR C2H2-type zinc-finger protein family.
CC {ECO:0000305}.
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DR EMBL; M20157; AAA37544.1; -; mRNA.
DR EMBL; M22326; AAA40416.1; -; mRNA.
DR EMBL; M28845; AAB00468.1; -; Genomic_DNA.
DR EMBL; M28844; AAB00468.1; JOINED; Genomic_DNA.
DR EMBL; M19643; AAA39382.1; -; mRNA.
DR CCDS; CCDS29136.1; -.
DR PIR; JS0304; JS0304.
DR RefSeq; NP_031939.1; NM_007913.5.
DR PDB; 1A1F; X-ray; 2.10 A; A=333-421.
DR PDB; 1A1G; X-ray; 1.90 A; A=333-421.
DR PDB; 1A1H; X-ray; 1.60 A; A=333-421.
DR PDB; 1A1I; X-ray; 1.60 A; A=333-421.
DR PDB; 1A1J; X-ray; 2.00 A; A=333-421.
DR PDB; 1A1K; X-ray; 1.90 A; A=333-421.
DR PDB; 1A1L; X-ray; 2.30 A; A=333-421.
DR PDB; 1AAY; X-ray; 1.60 A; A=333-421.
DR PDB; 1F2I; X-ray; 2.35 A; G/H/I/J/K/L=334-389.
DR PDB; 1G2D; X-ray; 2.20 A; C/F=333-421.
DR PDB; 1G2F; X-ray; 2.00 A; C/F=333-421.
DR PDB; 1JK1; X-ray; 1.90 A; A=333-421.
DR PDB; 1JK2; X-ray; 1.65 A; A=333-421.
DR PDB; 1LLM; X-ray; 1.50 A; C/D=364-412.
DR PDB; 1P47; X-ray; 2.20 A; A/B=333-419.
DR PDB; 1ZAA; X-ray; 2.10 A; C=332-418.
DR PDBsum; 1A1F; -.
DR PDBsum; 1A1G; -.
DR PDBsum; 1A1H; -.
DR PDBsum; 1A1I; -.
DR PDBsum; 1A1J; -.
DR PDBsum; 1A1K; -.
DR PDBsum; 1A1L; -.
DR PDBsum; 1AAY; -.
DR PDBsum; 1F2I; -.
DR PDBsum; 1G2D; -.
DR PDBsum; 1G2F; -.
DR PDBsum; 1JK1; -.
DR PDBsum; 1JK2; -.
DR PDBsum; 1LLM; -.
DR PDBsum; 1P47; -.
DR PDBsum; 1ZAA; -.
DR AlphaFoldDB; P08046; -.
DR BMRB; P08046; -.
DR SMR; P08046; -.
DR BioGRID; 199404; 9.
DR IntAct; P08046; 1.
DR STRING; 10090.ENSMUSP00000069616; -.
DR iPTMnet; P08046; -.
DR PhosphoSitePlus; P08046; -.
DR PaxDb; P08046; -.
DR PRIDE; P08046; -.
DR ProteomicsDB; 275907; -.
DR Antibodypedia; 14988; 561 antibodies from 42 providers.
DR DNASU; 13653; -.
DR Ensembl; ENSMUST00000064795; ENSMUSP00000069616; ENSMUSG00000038418.
DR Ensembl; ENSMUST00000165033; ENSMUSP00000126931; ENSMUSG00000038418.
DR GeneID; 13653; -.
DR KEGG; mmu:13653; -.
DR UCSC; uc008elt.1; mouse.
DR CTD; 1958; -.
DR MGI; MGI:95295; Egr1.
DR VEuPathDB; HostDB:ENSMUSG00000038418; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000160184; -.
DR HOGENOM; CLU_043235_2_0_1; -.
DR InParanoid; P08046; -.
DR OMA; NFQVPMI; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; P08046; -.
DR TreeFam; TF318980; -.
DR BioGRID-ORCS; 13653; 4 hits in 78 CRISPR screens.
DR ChiTaRS; Egr1; mouse.
DR EvolutionaryTrace; P08046; -.
DR PRO; PR:P08046; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; P08046; protein.
DR Bgee; ENSMUSG00000038418; Expressed in associated mesenchyme of midgut and 290 other tissues.
DR ExpressionAtlas; P08046; baseline and differential.
DR Genevisible; P08046; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:MGI.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IMP:UniProtKB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:BHF-UCL.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0010385; F:double-stranded methylated DNA binding; ISS:UniProtKB.
DR GO; GO:0044729; F:hemi-methylated DNA-binding; ISS:UniProtKB.
DR GO; GO:0035035; F:histone acetyltransferase binding; ISO:MGI.
DR GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0000976; F:transcription cis-regulatory region binding; IDA:BHF-UCL.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:BHF-UCL.
DR GO; GO:0071504; P:cellular response to heparin; ISS:UniProtKB.
DR GO; GO:0098759; P:cellular response to interleukin-8; ISS:UniProtKB.
DR GO; GO:0071506; P:cellular response to mycophenolic acid; ISS:UniProtKB.
DR GO; GO:0071310; P:cellular response to organic substance; IDA:MGI.
DR GO; GO:0032922; P:circadian regulation of gene expression; IMP:UniProtKB.
DR GO; GO:0060086; P:circadian temperature homeostasis; IMP:UniProtKB.
DR GO; GO:0044849; P:estrous cycle; IMP:UniProtKB.
DR GO; GO:0072110; P:glomerular mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; ISO:MGI.
DR GO; GO:0007611; P:learning or memory; ISO:MGI.
DR GO; GO:0045475; P:locomotor rhythm; IMP:UniProtKB.
DR GO; GO:0007616; P:long-term memory; ISO:MGI.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0010942; P:positive regulation of cell death; ISO:MGI.
DR GO; GO:0032722; P:positive regulation of chemokine production; IMP:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0072303; P:positive regulation of glomerular metanephric mesangial cell proliferation; ISS:UniProtKB.
DR GO; GO:0046886; P:positive regulation of hormone biosynthetic process; IMP:UniProtKB.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; ISO:MGI.
DR GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
DR GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
DR GO; GO:0014911; P:positive regulation of smooth muscle cell migration; ISO:MGI.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
DR GO; GO:1902949; P:positive regulation of tau-protein kinase activity; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI.
DR GO; GO:2000182; P:regulation of progesterone biosynthetic process; IMP:UniProtKB.
DR GO; GO:0033233; P:regulation of protein sumoylation; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; IDA:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:MGI.
DR GO; GO:0009749; P:response to glucose; IDA:UniProtKB.
DR GO; GO:0001666; P:response to hypoxia; IMP:UniProtKB.
DR GO; GO:0032868; P:response to insulin; IDA:UniProtKB.
DR GO; GO:0002931; P:response to ischemia; IMP:UniProtKB.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
DR GO; GO:0030217; P:T cell differentiation; IMP:MGI.
DR InterPro; IPR021839; EGR1_C.
DR InterPro; IPR021849; EGR_N.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF11914; DUF3432; 1.
DR Pfam; PF11928; DUF3446; 1.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF57667; SSF57667; 2.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Biological rhythms; Cytoplasm; DNA-binding;
KW Isopeptide bond; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..533
FT /note="Early growth response protein 1"
FT /id="PRO_0000047110"
FT ZN_FING 336..360
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 366..388
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 394..416
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..94
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 334
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 345
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 349
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 355
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 373
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 377
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 401
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 405
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT SITE 411
FT /note="Interaction with DNA"
FT /evidence="ECO:0000269|PubMed:2028256,
FT ECO:0000269|PubMed:8939742, ECO:0007744|PDB:1AAY,
FT ECO:0007744|PDB:1ZAA"
FT CROSSLNK 303
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P18146"
FT CONFLICT 76
FT /note="S -> T (in Ref. 3; AAB00468 and 4; AAA39382)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="S -> T (in Ref. 3; AAB00468 and 4; AAA39382)"
FT /evidence="ECO:0000305"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1P47"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1A1H"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1A1H"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:1A1H"
FT TURN 369..371
FT /evidence="ECO:0007829|PDB:1LLM"
FT STRAND 374..376
FT /evidence="ECO:0007829|PDB:1LLM"
FT HELIX 378..389
FT /evidence="ECO:0007829|PDB:1LLM"
FT TURN 397..399
FT /evidence="ECO:0007829|PDB:1LLM"
FT STRAND 402..405
FT /evidence="ECO:0007829|PDB:1LLM"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:1LLM"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:1A1H"
SQ SEQUENCE 533 AA; 56590 MW; 36E3935767CEAA0F CRC64;
MAAAKAEMQL MSPLQISDPF GSFPHSPTMD NYPKLEEMML LSNGAPQFLG AAGTPEGSGG
NSSSSTSSGG GGGGGSNSGS SAFNPQGEPS EQPYEHLTTE SFSDIALNNE KAMVETSYPS
QTTRLPPITY TGRFSLEPAP NSGNTLWPEP LFSLVSGLVS MTNPPTSSSS APSPAASSSS
SASQSPPLSC AVPSNDSSPI YSAAPTFPTP NTDIFPEPQS QAFPGSAGTA LQYPPPAYPA
TKGGFQVPMI PDYLFPQQQG DLSLGTPDQK PFQGLENRTQ QPSLTPLSTI KAFATQSGSQ
DLKALNTTYQ SQLIKPSRMR KYPNRPSKTP PHERPYACPV ESCDRRFSRS DELTRHIRIH
TGQKPFQCRI CMRNFSRSDH LTTHIRTHTG EKPFACDICG RKFARSDERK RHTKIHLRQK
DKKADKSVVA SPAASSLSSY PSPVATSYPS PATTSFPSPV PTSYSSPGSS TYPSPAHSGF
PSPSVATTFA SVPPAFPTQV SSFPSAGVSS SFSTSTGLSD MTATFSPRTI EIC
