(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 192.
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;
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;
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:0000244|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:0000244|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}.
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   SMR; P08046; -.
DR   BioGrid; 199404; 8.
DR   STRING; 10090.ENSMUSP00000069616; -.
DR   iPTMnet; P08046; -.
DR   PhosphoSitePlus; P08046; -.
DR   PaxDb; P08046; -.
DR   PRIDE; P08046; -.
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   eggNOG; KOG1721; Eukaryota.
DR   eggNOG; COG5048; LUCA.
DR   GeneTree; ENSGT00940000160184; -.
DR   HOGENOM; HOG000036856; -.
DR   InParanoid; P08046; -.
DR   KO; K09203; -.
DR   OMA; CSNSLWA; -.
DR   OrthoDB; 1318335at2759; -.
DR   PhylomeDB; P08046; -.
DR   TreeFam; TF318980; -.
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 340 organ(s), highest expression level in cumulus cell.
DR   ExpressionAtlas; P08046; baseline and differential.
DR   Genevisible; P08046; MM.
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:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR   GO; GO:0043565; F:sequence-specific DNA binding; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; ISO:MGI.
DR   GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:BHF-UCL.
DR   GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISO:MGI.
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:0045080; P:positive regulation of chemokine biosynthetic process; 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:0050725; P:positive regulation of interleukin-1 beta biosynthetic process; IMP:UniProtKB.
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   GO; GO:0006366; P:transcription by RNA polymerase II; ISO: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;
DR   PRODOM; P08046.
DR   SWISS-2DPAGE; P08046.
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   COMPBIAS        57..81
FT                   /note="Gly/Ser-rich"
FT   SITE            334
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            345
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            349
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            355
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            373
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            377
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            401
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            405
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
FT   SITE            411
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000244|PDB:1AAY, ECO:0000244|PDB:1ZAA,
FT                   ECO:0000269|PubMed:2028256, ECO:0000269|PubMed:8939742"
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:0000244|PDB:1P47"
FT   STRAND          340..342
FT                   /evidence="ECO:0000244|PDB:1A1H"
FT   STRAND          346..349
FT                   /evidence="ECO:0000244|PDB:1A1H"
FT   HELIX           350..361
FT                   /evidence="ECO:0000244|PDB:1A1H"
FT   TURN            369..371
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   STRAND          374..376
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   HELIX           378..389
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   TURN            397..399
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   STRAND          402..405
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   HELIX           406..412
FT                   /evidence="ECO:0000244|PDB:1LLM"
FT   HELIX           414..417
FT                   /evidence="ECO:0000244|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
//

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