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 27-MAR-2024, entry version 214. 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: BMAL1, PER2 and NR1D1 in the liver via the activation of CC PER1 (clock repressor) transcription (PubMed:26471974). Regulates the CC rhythmic expression of core-clock gene BMAL1 in the suprachiasmatic CC nucleus (SCN) (PubMed:29138967). {ECO:0000250|UniProtKB:P18146, CC ECO:0000269|PubMed:11100120, ECO:0000269|PubMed:15265859, CC ECO:0000269|PubMed:15958557, ECO:0000269|PubMed:2028256, CC ECO:0000269|PubMed:26471974, ECO:0000269|PubMed:29138967, CC ECO:0000269|PubMed:8336701, ECO:0000269|PubMed:8703054, CC 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). Expressed in the liver in a circadian manner CC (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 BMAL1 and CC 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}. 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; 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 GlyGen; P08046; 2 sites, 1 O-linked glycan (2 sites). DR iPTMnet; P08046; -. DR PhosphoSitePlus; P08046; -. DR PaxDb; 10090-ENSMUSP00000069616; -. DR ProteomicsDB; 275907; -. DR Pumba; P08046; -. DR Antibodypedia; 14988; 616 antibodies from 42 providers. DR DNASU; 13653; -. DR Ensembl; ENSMUST00000064795.6; ENSMUSP00000069616.6; ENSMUSG00000038418.8. DR Ensembl; ENSMUST00000165033.2; ENSMUSP00000126931.2; ENSMUSG00000038418.8. DR GeneID; 13653; -. DR KEGG; mmu:13653; -. DR UCSC; uc008elt.1; mouse. DR AGR; MGI:95295; -. 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; 2912670at2759; -. DR PhylomeDB; P08046; -. DR TreeFam; TF318980; -. DR BioGRID-ORCS; 13653; 4 hits in 83 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 293 other cell types or tissues. DR ExpressionAtlas; P08046; baseline and differential. 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; IDA:BHF-UCL. 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; IBA:GO_Central. 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; IDA:BHF-UCL. 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:0032722; P:positive regulation of chemokine production; IMP:UniProtKB. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA: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:1901875; P:positive regulation of post-translational protein modification; 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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IMP:MGI. DR GO; GO:0048169; P:regulation of long-term neuronal synaptic plasticity; ISO:MGI. DR GO; GO:0043523; P:regulation of neuron apoptotic process; 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; IDA: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 Gene3D; 3.30.160.60; Classic Zinc Finger; 3. DR InterPro; IPR021839; EGR1_C. DR InterPro; IPR021849; EGR_N. DR InterPro; IPR036236; Znf_C2H2_sf. DR InterPro; IPR013087; Znf_C2H2_type. DR PANTHER; PTHR23235:SF42; EARLY GROWTH RESPONSE PROTEIN 1; 1. DR PANTHER; PTHR23235; KRUEPPEL-LIKE TRANSCRIPTION FACTOR; 1. 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; beta-beta-alpha zinc fingers; 2. DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3. DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3. DR Genevisible; P08046; MM. 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 //