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EGR1 (Early Growth Response 1)

Written2014-01Young Han Lee
Department of Biological Sciences, Konkuk University, 120 Neungdong-ro, Gwangjin-gu, Seoul
This article is an update of :
2010-05Reeti Bandyopadhyay, Véronique Baron
University of California San Diego, BioChemistry & Cell Biology, San Diego, CA 92122, USA (RB); Vaccine Research Institute of San Diego, 10835 road to the cure, Suite 150, San Diego, CA 92121, USA (VB)

(Note : for Links provided by Atlas : click)


Alias (NCBI)AT225
HGNC (Hugo) EGR1
HGNC Alias symbTIS8
HGNC Alias namenerve growth factor-induced protein A
 transcription factor ETR103
 zinc finger protein 225
 early growth response protein 1
LocusID (NCBI) 1958
Atlas_Id 496
Location 5q31.2  [Link to chromosome band 5q31]
Location_base_pair Starts at 138465479 and ends at 138469303 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping EGR1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
EGR1 (5q31.2)::ARL6IP4 (12q24.31)EGR1 (5q31.2)::DAXX (6p21.32)EGR1 (5q31.2)::EGR1 (5q31.2)
FBXL15 (10q24.32)::EGR1 (5q31.2)HSPB1 (7q11.23)::EGR1 (5q31.2)


Note The gene is conserved in chimpanzee, dog, cow, mouse, rat, chicken, and zebrafish.
Description Genomic size 3824 bp; 2 exons; + strand of chromosome 5.
Transcription mRNA size: 3132, ORF 271-1902 (1632 nt coding sequence).
Rare occurrence of splice variants (2 variants have been described in the brain).
The EGR1 promoter contains five SREs (serum response elements). Increased transcription in response to growth factors or stress is most commonly mediated by transcription factors of the Elk-1/SAP-1/SAP-2 family, which are activated by MAP-Kinase family (mitogen activated protein kinase). Elk-1 associates with CBP (CREB binding protein) and SRF (serum response factor) to form the Ternary Complex Factor, which binds to the SREs.
The promoter also contains several SP1 consensus sequences; a putative AP-1 binding site (not conserved); at least one functional CRE (cAMP regulatory element). EGR1 regulates its own transcription by binding to functional EBS (EGR1 binding sites). A functional NFkB (p65/RelA) binding site is contained in the EGR1 promoter that allows NF-kB to increase EGR1 transcription in response to UV (ultra-violet) irradiation. EGR1 is a target of ETS transcription factors that are involved in hematopoiesis, angiogenesis and neoplasia. Finally, EGR1 promoter contains two ATF5 (activating transcription factor 5) consensus sequences at a conserved promoter position and is induced by ATF5 in cancer cell lines.


  Figure 1.
Description The protein contains 543 amino acids. Its predicted molecular weight is 57.5 kDa, however the protein migrates at an apparent molecular weight of 75-85 kDa in SDS-PAGE. It has a very short half-life of ~30 minutes to 1 hour.
EGR1 contains a highly conserved DNA-binding domain composed of three Cys2-His2 type zinc-fingers that bind to the prototype target sequence GCG(G/T)GGGCG; a nuclear localization signal that requires amino acids 361-419 (zinc fingers 2 and 3) and amino acids 315-330; two activator domains; a repressor domain between amino acids 281-314. EGR1 binds to regulatory proteins called NAB-1 (NGFA-I binding protein) and NAB2 through its repressor domain.
Post-translational modifications include phosphorylation, acetylation, ubiquitination and sumoylation (figure 1).
Expression Ubiquitous. Exhibits a distinct expression pattern in the brain. Constitutive protein expression is low in many tissues. EGR1 expression is very rapidly and strongly induced by growth factors and mitogens, cytokines, environmental and mechanical stresses, as well as DNA damage (hpr).
Localisation Nuclear. Occasional cytoplasmic localization observed in cancer cells.
Function EGR1 is an early response transcription factor with DNA binding activity that activates the transcription of several hundred genes. Depending on the cell type and the stimulus, EGR1 induces the expression of growth factors, growth factor receptors, extracellular matrix proteins, proteins involved in the regulation of cell growth or differentiation, and proteins involved in apoptosis, growth arrest, and stress responses.
EGR1 can compete with transcription factor SP1, which is involved in the constitutive expression of housekeeping genes and other regulatory genes. Because the consensus sequence for SP1 and EGR1 binding overlaps, EGR1 often displaces SP1 from gene promoters.
EGR1 transcriptional activity is inhibited by direct interaction with the proteins NAB1 and NAB2. Their expression is also inducible, albeit delayed compared to EGR1 induction. NAB1 and NAB2 impose an early negative feedback and thus ensure that EGR1 activity is transient, before the protein is degraded. It should be noted that deregulated expression of NAB proteins in disease may contribute to alteration of EGR1 function. For example, elevated expression of NAB2 in endothelial cells reduces angiogenesis, whereas loss of NAB2 in prostate cancer contributes to increased EGR1 activity.
EGR1 has various neurocognitive functions. It is involved in the regulation of neuronal activity and may control neuronal plasticity. EGR1 controls tissue repair, wound healing, liver regeneration, atherosclerosis, fibrosis, and other inflammation or stress-related responses. It is considered a key master regulator in cardiovascular pathology by promoting atherosclerosis, intimal thickening following vascular injury, ischemia, allograft rejection and cardiac hypertrophy. Finally, EGR1 regulates cell response to hypoxia, promotes the formation of new blood vessels from the pre-existing vasculature, and triggers tumor angiogenesis.
In cancer, EGR1 is traditionally considered a tumor suppressor. However, accumulating evidence now indicates that it can act both as a tumor suppressor and as a tumor promoter, depending on the context.
EGR1 protects normal cells from transformation by inducing apoptosis or growth arrest upon DNA damage. A strong evidence for EGR1 pro-apoptotic function is that EGR1-/- mouse embryo fibroblasts are resistant to apoptosis induced by ionizing radiation. Although EGR1-deficient mice do not spontaneously develop tumors, they display accelerated tumor growth in a two-step carcinogenesis model of skin cancer. As an example, UV-B radiation of keratinocytes induces EGR1 expression through activation of NFkB (p65/RelA), which mediates apoptosis and acts as a protection mechanism against the tumorigenic effect of UV. These observations support the notion that EGR1 participates in the suppression of DNA damage-induced tumors.
EGR1 is involved in the chemopreventive or antiproliferative effect of natural compounds such as curcumin, genistein, isoflavone, green tea extracts, and others. It also mediates the anti-proliferative effects of NSAIDs (non-steroid anti-inflammatory drug) and of other chemotherapeutic agents such as cisplatin.
In many cancer cells, EGR1 is induced by radiation, chemotherapeutic drugs, steroids and anti-inflammatory drugs, and is required for the growth arrest or apoptotic effect of these treatments. Lack of EGR1 response confers chemoresistance. This may be exploited by restoring EGR1 expression through gene therapy to increase the efficacy of radiotherapy of chemotherapy.
At later stages of cancer EGR1 tumor suppressor function is impaired by the frequent inactivation, in human tumors, of two major tumor suppressor targets of EGR1 (namely PTEN and TP53). In addition, EGR1 induction by growth factors or stress is blocked in some types of cancer cells ("resistance" to induction). This has been described in fibrosarcoma, prostate cancer, colon cancer, and RAS-transformed cells. Several mechanisms are involved. For example, RAS-induced transformation of fibroblasts results in the aberrant constitutive activation of PI3-kinase (phosphatidyl inositol 3-kinase), which causes degradation of SRF and prevents Elk-1-mediated induction of EGR1. In colon cancer cells, it is the mutational activation of Wnt-1 that prevents the SRF-mediated induction of EGR1 and other early genes in response to mitogens. Alternatively, overexpression of phospholipase D in glioma cells attenuates mitogen-induced EGR1 expression through activation of PI3-kinase.
On the other hand, EGR1 overexpression in some cancer types directly promotes cancer progression and tumor growth by increasing the expression and secretion of growth factors and cytokines, extracellular matrix proteins (Barbolina et al., 2007; Shin et al., 2010) and proteases. Egr-1 mediates growth factor-induced downregulation of E-cadherin by inducing an E-cadherin transcription repressor, Snail or Slug, which contributes to tumor invasion (Grotegut et al., 2006; Cheng et al., 2013). Mechanisms that can cause EGR1 overexpression in tumor cells include p53 mutations (observed in gliomas and prostate cancer). Mutant p53 upregulates EGR1 in prostate cancer cells by activating ERK (extracellular regulated kinase) through undefined mechanism. Constitutive activation of the ERK pathway in tumor cells appears to be a consistent cause of EGR1 expression and is often due to genetic defects affecting upstream regulators of the ERK pathway. For example, a mutation of EGFR (epidermal growth factor receptor) commonly found in lung cancer cells causes EGR1 overexpression and activation through activation of the ERK pathway. Similarly, a mutation of B-RAF present in a high percentage of melanoma results in constitutive activation of ERK and up-regulation of EGR1.
Homology Three other family members: EGR2, EGR3 and EGR4 (see figure 2).


Note Mutations in the EGR1 gene have not been found; altered expression level is the most common contributor to tumorigenesis.
Chromosome loss/deletions:
- The long arm of chromosome 5 in which EGR1 is located is consistently deleted in myelodysplastic syndrome (MDS) and acute myeloid leukemia (AML). Loss of chromosome 5 or deletion in 5q is the most common karyotypic abnormality in MDS, occurring in 10% of new MDS/AML patients and in 40% of patients with therapy-related MDS or AML. Mice lacking at least one allele of EGR1 develop symptoms similar to that of MDS after they are exposed to a carcinogen (i.e. mono- or bi-allelic loss of EGR1 accelerates the development of pre-leukemic disorders).
- Loss of 5q is consistently associated with estrogen receptor-negative (ER-) breast carcinoma and is seen in 86% of breast carcinomas carriers of BRCA1 (breast cancer 1) and BRCA2 mutations. Fluorescence in situ hybridization confirmed the association of EGR1 loss with ER- breast carcinoma; loss of EGR1 correlated with high grade.
- In mouse model with a deletion of chromosome 5, loss of Tp53 activity in cooperation with EGR1 and adenomatous polyposis coli (APC) haploinsufficiency, accelerates the development of AML (Stoddart et al., 2013).

Implicated in

Entity Various cancers
Note EGR1 (protein and/or mRNA) is downregulated in colon cancer, lung cancer, esophageal carcinoma, astrocytomas, glioblastomas, breast cancer, compared to non-cancer tissue. EGR1 expression is sharply decreased in leiomyoma compared to normal myometrium (reduction in 100% of tumors). Transfection of EGR1 into myometrial cells decreases cell proliferation.
In some types of cancers EGR1 expression is high in the adjacent tissue of the tumors, but low in the tumor cells. In esophageal carcinoma, EGR1 expression is higher in the dysplastic tissue, whereas no expression is detected in the tumor tissue. This may reflect the existence of a reactive stroma, and possibly inflammation.
Early observations indicated that in v-sis-transformed NIH-3T3 cells, transfection of EGR1 inhibits colony formation and growth in soft agar. It also delays tumorigenicity in nude mice. Conversely, EGR1 antisense accelerates cell growth and colony formation.
EGR1 expression is upregulated in human diffuse large B cell lymphoma because of constitutively active ERK and JNK (Jun N-terminal kinase) pathways and promotes cancer cells survival. Overexpression of EGR1 (both mRNA and protein) is observed in gastric cancer and in prostate cancer. It is also seen in the "normal" tissue adjacent to the tumors, but it is not expressed in the normal tissues from healthy patients. The mRNA expression is higher in metastatic cases of gastric cancer. EGR1 is much higher expressed in cervical cancer tissues than in the normal cervix.
Entity Leukemia
Note In myeloblastic leukemia, upregulation of oncogene E2F-1 blocks the myeloid terminal differentiation program, resulting in proliferation of immature cells in the presence of interleukin-6. EGR1 abrogates the E2F-1-driven block in myeloid terminal differentiation, decreases the tumorigenic potential of leukemia cells in vivo and their aggressiveness. EGR1 also abrogates the block in terminal myeloid differentiation imparted by oncogenic c-myc.
Entity Fibrosarcoma
Note Human fibrosarcoma cells express almost no EGR1 and are "resistant" to EGR1 induction in response to growth factors or stress. Forced expression of EGR1 inhibits cell growth and suppresses xenograft tumor growth in athymic mice. Conversely, silencing EGR1 using antisense increases the transformed character of these cells.
The effect of EGR1 in HT-1080 fibrosarcoma cells is mediated by increased secretion of active TGFbeta-1 (transforming growth factor-beta1), a direct target of EGR1. TGFbeta-1 strongly inhibits cell growth in an autocrine mechanism. Further, EGR1 regulates cell adhesion and migration through increased secretion of fibronectin and plasminogen activator inhibitor-1 (PAI-1). Although fibronectin is a direct target of EGR1, PAI-1 increase is mediated by EGR1-induced TGFbeta-1.
Entity Lung cancer
Note EGR1 (RNA and protein) is expressed at higher levels in human normal lung tissue adjacent to non-small cell lung cancer (NSCLC), and is downregulated in the tumor tissue compared with normal lung. Also downregulated in human lung adenocarcinomas and lung squamous cell carcinomas.
High expression of EGR1 in NSCLC patients correlates with high PTEN expression. Low levels of EGR1 after surgical resection are associated with poor outcome.
Entity Brain cancer (astrocytoma/glioblastoma/neuroblastoma)
Note EGR1 mRNA and protein are strongly suppressed in astrocytomas and glioblastomas compared to normal brain. Downregulation correlates with grade in human tissue, or with the presence of wild-type p53 in cell cultures. Tumors or primary cell lines that exhibit higher EGR1 expression contain p53 mutations. EGR1 induces growth arrest of glioma cells mediated by increased secretion of TGF-beta1, PAI-1 and fibronectin. EGR1 expression is induced by hypoxia in glioblastoma multiforme and up-regulates tissue factor that promotes plasma clotting.
Two EGR1 mRNA variants are detected in astrocytomas, one that contains N-methyl-D-aspartate-receptor (NMDA-R)-responsive element. An increase in the expression of this EGR1 variant is seen in astrocytoma cells following NMDA stimulation. EGR1 expression is restricted to tumor cells expressing NMDA-R, is up-regulated in astrocytomas compared with normal brain, and is associated with enhanced patient survival.
In neuroblastoma cells, re-expression of EGR1 induces apoptosis, whereas EGR1 antisense increases cell viability. The apoptotic activity of the EGR1 is mediated by activation of p73 (a member of the p53 family).
Entity Breast cancer
Note Breast cancer cell lines and clinical cancer tissues exhibit reduced EGR1 expression while normal mammary tissues express high levels. EGR1 is also downregulated in experimentally induced rat mammary tumors. Downregulation of gelsolin, which is an indicator of breast cancer, is correlated with suppression of EGR1.
Some studies have shown that re-expression of EGR1 inhibits human tumor cell growth and suppresses tumorigenicity in mice. However, two other studies found that EGR1 silencing decreases breast cancer cell proliferation, migration, and growth of xenograft tumors in nude mice.
In estrogen receptor-positive breast cancer cell lines, EGR1 expression is induced by estrogen through activation of RAF-1 kinase, the MAP-kinase pathway, and Elk-1/SRF.
Entity Hepatocellular carcinoma (liver cancer)
Note While one study reports EGR1 overexpression, another one describes the downregulation of EGR1 expression in hepatocellular carcinoma. In the latter study, re-expression of EGR1 decreased cell growth and tumorigenicity in nude mice.
There are arguments in favor of a pro-tumorigenic function: HGF (hepatocyte growth factor), a cytokine involved in the progression of hepatocarcinoma, up-regulates EGR1 and increases cell scattering and migration through EGR1-mediated up-regulation of snail. HGF also increases angiogenesis through up-regulation of EGR1-mediated VEGF (vascular endothelial growth factor) and interleukin 8. Of note, EGR1 is crucial for the proliferation of hepatocytes and plays an important role in liver regeneration: liver regeneration following partial hepatectomy is impaired in EGR1-null mice.
Entity Skin cancer/melanoma
Note EGR1 expression is decreased in basal cell carcinoma (BCC) and squamous cell carcinoma (SCC) but is elevated in psoriasis. EGR1 inhibits the growth of benign and malignant epidermal cells in vitro.
A single topical treatment with the tumor promoter TPA in a multistage carcinogenesis model induces EGR1 mRNA expression both epidermis and dermis of the mice. Primary papillomas and carcinomas generated in these animals contain high EGR1 mRNA compared with normal epidermis. EGR1-null mice reveal an accelerated development of skin tumors in the multistage carcinogenesis model compared to EGR1+ mice.
On the other hand, EGR1 may contribute to cancer progression in melanoma. The HGF receptor c-Met induces EGR1 activation via the Ras/ERK1/2 pathway in melanoma cells, which in turn induces fibronectin expression and its extracellular assembly. Fibronectin promotes migration and invasiveness of melanomas and is associated with metastatic potential.
About 60% of melanoma contain an activating mutation in the B-RAF gene. In these cells, constitutive up-regulation of EGR1 caused by activation of RAF/ERK signaling results in high fibronectin levels and increases invasiveness.
Entity Prostate cancer
Note EGR1 mRNA is expressed at higher levels in prostate tumors compared with normal tissues and correlates with Gleason score (a measure of prostate cancer stage). EGR1 expression in the primary tumor correlates with complete control of the local tumor by radiation, whereas in post-irradiated tissue EGR1 expression correlates with treatment failure. NAB2 is down-regulated in clinical primary carcinoma. Thus, upregulation of EGR1 and loss of NAB2 both determine the high level of EGR1 activity in human prostate tumors.
EGR1 knock-out mice crossed with transgenic mouse models of prostate cancer show significantly impaired tumor growth compared to Egr+/+ mice and increased survival. Although it does not prevent tumor initiation, EGR1 deficiency delays the progression of prostate carcinoma. EGR1 is also overexpressed in the tumors of the transgenic mice, whereas NAB2 expression is decreased.
Silencing of EGR1 in prostate cancer cells decreases cell proliferation in vitro, and injection of EGR1 antisense in vivo delays the occurrence of prostate cancer. Alternatively, forced expression of EGR1 in non-cancer cells increases proliferation in vitro.
EGR1 up-regulation in prostate cell lines is due to mutation of the TP53 gene. EGR1 is also up-regulated by SV40-T antigen, a viral oncogene that is used very often to immortalize non-transformed cells. In human prostate cancer cells EGR1 stimulates the production of many growth factors and cytokines that are involved in the progression of prostate cancer and of proteins involved in metastasis.
A crosstalk between EGR1 and the androgen receptor (AR) may explain the particular role of EGR1 in prostate cancer. EGR1 physically interacts with AR in hormone-sensitive prostate cancer cells and the complex binds to the promoter of endogenous targets of AR. Forcing EGR1 activity in hormone-sensitive cancer cells increases proliferation in vitro. It enhances tumor growth in mice upon castration (which mimics hormone therapy in human patients): EGR1 may be involved in the acquisition of resistance to hormone therapy.
Entity Esophageal carcinoma
Note According to some reports, the expression of EGR1 (mRNA and protein) is high in pre-cancerous human lesions of the esophagus and in dysplastic tissue adjacent to esophageal carcinoma, but is very low in cancer tissue. The number of apoptotic cells in EGR1-positive tumors is higher than in EGR1 negative tumors, suggesting that EGR1 promotes apoptosis. In addition, EGR1 is up-regulated in the tumors of patients treated by irradiation compared to the tumor tissue of non-irradiated patients, and EGR1 expression level seems to correlate with better prognosis.
Another study, however, shows overexpression of EGR1 in esophageal tumor tissues and constitutive expression in esophageal cancer cell lines.
EGR1 silencing inhibits cell proliferation through G2/M cell cycle block. On the other hand, forced stable expression of EGR1 into esophageal carcinoma cells also decreases cell proliferation in vitro and tumor growth in vivo.
Entity Cervical cancer
Note The melanoma growth stimulatory activity/Growth-regulated oncogene α (MGSA/GROα), which is designated as a CXC chemokine ligand 1 (CXCL1), plays an important role in the regulation of inflammation and the progression of tumor development through stimulation of angiogenesis and metastasis. EGR1 mediates ERK and JNK MAPKs-dependent GROα transcription in response to TNFα stimulation in HeLa cervix cancer cells (Shin et al., 2013).


Impaired prostate tumorigenesis in Egr1-deficient mice.
Abdulkadir SA, Qu Z, Garabedian E, Song SK, Peters TJ, Svaren J, Carbone JM, Naughton CK, Catalona WJ, Ackerman JJ, Gordon JI, Humphrey PA, Milbrandt J.
Nat Med. 2001b Jan;7(1):101-7.
PMID 11135623
Early growth response-1 gene: potential radiation response gene marker in prostate cancer.
Ahmed MM, Chendil D, Lele S, Venkatasubbarao K, Dey S, Ritter M, Rowland RG, Mohiuddin M.
Am J Clin Oncol. 2001 Oct;24(5):500-5.
PMID 11586104
EGR-1 induction is required for maximal radiosensitivity in A375-C6 melanoma cells.
Ahmed MM, Venkatasubbarao K, Fruitwala SM, Muthukkumar S, Wood DP Jr, Sells SF, Mohiuddin M, Rangnekar VM.
J Biol Chem. 1996 Nov 15;271(46):29231-7.
PMID 8910582
Phorbol myristate acetate-induced Egr-1 expression is suppressed by phospholipase D isozymes in human glioma cells.
Ahn BH, Park MH, Lee YH, Min do S.
FEBS Lett. 2007 Dec 22;581(30):5940-4. Epub 2007 Dec 5.
PMID 18067864
Early growth response-1 mediates downregulation of telomerase in cervical cancer.
Akutagawa O, Nishi H, Kyo S, Terauchi F, Yamazawa K, Higuma C, Inoue M, Isaka K.
Cancer Sci. 2008 Jul;99(7):1401-6. doi: 10.1111/j.1349-7006.2008.00835.x. Epub 2008 May 2.
PMID 18460021
[Alteration of early growth response 1 expression in gastroenterological cancers and its biological significance].
An J, Guo RF, Zhang L, Geng PL, Lu YY.
Zhonghua Yi Xue Za Zhi. 2008 May 27;88(20):1384-9.
PMID 18953875
Egr1 regulates the coordinated expression of numerous EGF receptor target genes as identified by ChIP-on-chip.
Arora S, Wang Y, Jia Z, Vardar-Sengul S, Munawar A, Doctor KS, Birrer M, McClelland M, Adamson E, Mercola D.
Genome Biol. 2008;9(11):R166. doi: 10.1186/gb-2008-9-11-r166. Epub 2008 Nov 25.
PMID 19032775
Regulation of Egr-1 by association with the proteasome component C8.
Bae MH, Jeong CH, Kim SH, Bae MK, Jeong JW, Ahn MY, Bae SK, Kim ND, Kim CW, Kim KR, Kim KW.
Biochim Biophys Acta. 2002 Oct 21;1592(2):163-7.
PMID 12379479
Microenvironmental regulation of membrane type 1 matrix metalloproteinase activity in ovarian carcinoma cells via collagen-induced EGR1 expression.
Barbolina MV, Adley BP, Ariztia EV, Liu Y, Stack MS.
J Biol Chem. 2007 Feb 16;282(7):4924-31. Epub 2006 Dec 11.
PMID 17158885
The transcription factor Egr1 is a direct regulator of multiple tumor suppressors including TGFbeta1, PTEN, p53, and fibronectin.
Baron V, Adamson ED, Calogero A, Ragona G, Mercola D.
Cancer Gene Ther. 2006 Feb;13(2):115-24. (REVIEW)
PMID 16138117
Inhibition of Egr-1 expression reverses transformation of prostate cancer cells in vitro and in vivo.
Baron V, De Gregorio G, Krones-Herzig A, Virolle T, Calogero A, Urcis R, Mercola D.
Oncogene. 2003a Jul 3;22(27):4194-204.
PMID 12833142
Antisense to the early growth response-1 gene (Egr-1) inhibits prostate tumor development in TRAMP mice.
Baron V, Duss S, Rhim J, Mercola D.
Ann N Y Acad Sci. 2003b Dec;1002:197-216.
PMID 14751836
Inhibition of cell growth by EGR-1 in human primary cultures from malignant glioma.
Calogero A, Lombari V, De Gregorio G, Porcellini A, Ucci S, Arcella A, Caruso R, Gagliardi FM, Gulino A, Lanzetta G, Frati L, Mercola D, Ragona G.
Cancer Cell Int. 2004 Jan 7;4(1):1.
PMID 14711380
Egr-1 is activated by 17beta-estradiol in MCF-7 cells by mitogen-activated protein kinase-dependent phosphorylation of ELK-1.
Chen CC, Lee WR, Safe S.
J Cell Biochem. 2004 Nov 15;93(5):1063-74.
PMID 15449318
Egr-1 mediates epidermal growth factor-induced downregulation of E-cadherin expression via Slug in human ovarian cancer cells.
Cheng JC, Chang HM, Leung PC.
Oncogene. 2013 Feb 21;32(8):1041-9. doi: 10.1038/onc.2012.127. Epub 2012 Apr 16.
PMID 22508482
p21 Waf1/Cip1 expression by curcumin in U-87MG human glioma cells: role of early growth response-1 expression.
Choi BH, Kim CG, Bae YS, Lim Y, Lee YH, Shin SY.
Cancer Res. 2008 Mar 1;68(5):1369-77. doi: 10.1158/0008-5472.CAN-07-5222.
PMID 18316600
A gene activated in mouse 3T3 cells by serum growth factors encodes a protein with "zinc finger" sequences.
Christy BA, Lau LF, Nathans D.
Proc Natl Acad Sci U S A. 1988 Nov;85(21):7857-61.
PMID 3141919
Ionizing radiation down-regulates p53 protein in primary Egr-1-/- mouse embryonic fibroblast cells causing enhanced resistance to apoptosis.
Das A, Chendil D, Dey S, Mohiuddin M, Mohiuddin M, Milbrandt J, Rangnekar VM, Ahmed MM.
J Biol Chem. 2001 Feb 2;276(5):3279-86. Epub 2000 Oct 16.
PMID 11035041
How necessary is the activation of the immediate early gene zif268 in synaptic plasticity and learning?
Davis S, Bozon B, Laroche S.
Behav Brain Res. 2003 Jun 16;142(1-2):17-30. (REVIEW)
PMID 12798262
Expression of early growth response genes in human prostate cancer.
Eid MA, Kumar MV, Iczkowski KA, Bostwick DG, Tindall DJ.
Cancer Res. 1998 Jun 1;58(11):2461-8.
PMID 9622090
5q- myelodysplastic syndromes: chromosome 5q genes direct a tumor-suppression network sensing actin dynamics.
Eisenmann KM, Dykema KJ, Matheson SF, Kent NF, DeWard AD, West RA, Tibes R, Furge KA, Alberts AS.
Oncogene. 2009 Oct 1;28(39):3429-41. doi: 10.1038/onc.2009.207. Epub 2009 Jul 13. (REVIEW)
PMID 19597464
Transcription factor Egr-1 supports FGF-dependent angiogenesis during neovascularization and tumor growth.
Fahmy RG, Dass CR, Sun LQ, Chesterman CN, Khachigian LM.
Nat Med. 2003 Aug;9(8):1026-32. Epub 2003 Jul 20.
PMID 12872165
Evidence of EGR1 as a differentially expressed gene among proliferative skin diseases.
Fang M, Wee SA, Ronski K, Fan H, Tao S, Lin Q.
Genomic Med. 2007;1(1-2):75-85. doi: 10.1007/s11568-007-9010-9. Epub 2007 Jul 25.
PMID 18923931
EGR1 predicts PTEN and survival in patients with non-small-cell lung cancer.
Ferraro B, Bepler G, Sharma S, Cantor A, Haura EB.
J Clin Oncol. 2005 Mar 20;23(9):1921-6.
PMID 15774784
Tumor-derived fibronectin is involved in melanoma cell invasion and regulated by V600E B-Raf signaling pathway.
Gaggioli C, Robert G, Bertolotto C, Bailet O, Abbe P, Spadafora A, Bahadoran P, Ortonne JP, Baron V, Ballotti R, Tartare-Deckert S.
J Invest Dermatol. 2007 Feb;127(2):400-10. Epub 2006 Sep 7.
PMID 16960555
A novel repression module, an extensive activation domain, and a bipartite nuclear localization signal defined in the immediate-early transcription factor Egr-1.
Gashler AL, Swaminathan S, Sukhatme VP.
Mol Cell Biol. 1993 Aug;13(8):4556-71.
PMID 8336701
Egr-1 abrogates the E2F-1 block in terminal myeloid differentiation and suppresses leukemia.
Gibbs JD, Liebermann DA, Hoffman B.
Oncogene. 2008 Jan 3;27(1):98-106. Epub 2007 Jun 25.
PMID 17599039
Is EGR1 a potential target for prostate cancer therapy?
Gitenay D, Baron VT.
Future Oncol. 2009 Sep;5(7):993-1003. doi: 10.2217/fon.09.67. (REVIEW)
PMID 19792968
Hepatocyte growth factor induces cell scattering through MAPK/Egr-1-mediated upregulation of Snail.
Grotegut S, von Schweinitz D, Christofori G, Lehembre F.
EMBO J. 2006 Aug 9;25(15):3534-45. Epub 2006 Jul 13.
PMID 16858414
Transcription factor EGR-1 inhibits growth of hepatocellular carcinoma and esophageal carcinoma cell lines.
Hao MW, Liang YR, Liu YF, Liu L, Wu MY, Yang HX.
World J Gastroenterol. 2002 Apr;8(2):203-7.
PMID 11925592
Cryptic deletion of EGR1 in association with a novel balanced t(5;22)(q31;q11.2) in a patient with myelodysplastic syndrome.
Hoffman MW, Janney S, Batanian JR.
Cancer Genet Cytogenet. 2009 Jun;191(2):106-8. doi: 10.1016/j.cancergencyto.2009.02.008.
PMID 19446747
Delineation of a minimal interval and identification of 9 candidates for a tumor suppressor gene in malignant myeloid disorders on 5q31.
Horrigan SK, Arbieva ZH, Xie HY, Kravarusic J, Fulton NC, Naik H, Le TT, Westbrook CA.
Blood. 2000 Apr 1;95(7):2372-7.
PMID 10733509
Suppression of v-sis-dependent transformation by the transcription factor, Egr-1.
Huang RP, Darland T, Okamura D, Mercola D, Adamson ED.
Oncogene. 1994 May;9(5):1367-77.
PMID 8152797
Reciprocal modulation between Sp1 and Egr-1.
Huang RP, Fan Y, Ni Z, Mercola D, Adamson ED.
J Cell Biochem. 1997b Sep 15;66(4):489-99.
PMID 9282327
Egr-1 negatively regulates human tumor cell growth via the DNA-binding domain.
Huang RP, Liu C, Fan Y, Mercola D, Adamson ED.
Cancer Res. 1995 Nov 1;55(21):5054-62.
PMID 7585551
Haploinsufficiency of EGR1, a candidate gene in the del(5q), leads to the development of myeloid disorders.
Joslin JM, Fernald AA, Tennant TR, Davis EM, Kogan SC, Anastasi J, Crispino JD, Le Beau MM.
Blood. 2007 Jul 15;110(2):719-26. Epub 2007 Apr 9.
PMID 17420284
The role of MAPKs in B cell receptor-induced down-regulation of Egr-1 in immature B lymphoma cells.
Ke J, Gururajan M, Kumar A, Simmons A, Turcios L, Chelvarajan RL, Cohen DM, Wiest DL, Monroe JG, Bondada S.
J Biol Chem. 2006 Dec 29;281(52):39806-18. Epub 2006 Oct 24.
PMID 17065146
Early growth response-1 in cardiovascular pathobiology.
Khachigian LM.
Circ Res. 2006 Feb 3;98(2):186-91. (REVIEW)
PMID 16456111
A gene for neuronal plasticity in the mammalian brain: Zif268/Egr-1/NGFI-A/Krox-24/TIS8/ZENK?
Knapska E, Kaczmarek L.
Prog Neurobiol. 2004 Nov;74(4):183-211. (REVIEW)
PMID 15556287
Overexpression of early growth response-1 as a metastasis-regulatory factor in gastric cancer.
Kobayashi D, Yamada M, Kamagata C, Kaneko R, Tsuji N, Nakamura M, Yagihashi A, Watanabe N.
Anticancer Res. 2002 Nov-Dec;22(6C):3963-70.
PMID 12553019
Early growth response 1 acts as a tumor suppressor in vivo and in vitro via regulation of p53.
Krones-Herzig A, Mittal S, Yule K, Liang H, English C, Urcis R, Soni T, Adamson ED, Mercola D.
Cancer Res. 2005 Jun 15;65(12):5133-43.
PMID 15958557
Cytogenetic and molecular delineation of the smallest commonly deleted region of chromosome 5 in malignant myeloid diseases.
Le Beau MM, Espinosa R 3rd, Neuman WL, Stock W, Roulston D, Larson RA, Keinanen M, Westbrook CA.
Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5484-8.
PMID 8516290
Hepatocyte growth factor induced up-regulations of VEGF through Egr-1 in hepatocellular carcinoma cells.
Lee KH, Kim JR.
Clin Exp Metastasis. 2009;26(7):685-92. doi: 10.1007/s10585-009-9266-7. Epub 2009 Jun 13.
PMID 19526316
Two mouse genes encoding potential transcription factors with identical DNA-binding domains are activated by growth factors in cultured cells.
Lemaire P, Revelant O, Bravo R, Charnay P.
Proc Natl Acad Sci U S A. 1988 Jul;85(13):4691-5.
PMID 3133658
Expression patterns of immediate early transcription factors in human non-small cell lung cancer. The Lung Cancer Study Group.
Levin WJ, Press MF, Gaynor RB, Sukhatme VP, Boone TC, Reissmann PT, Figlin RA, Holmes EC, Souza LM, Slamon DJ.
Oncogene. 1995 Oct 5;11(7):1261-9.
PMID 7478546
Identification of a novel DNA binding site and a transcriptional target for activating transcription factor 5 in c6 glioma and mcf-7 breast cancer cells.
Li G, Li W, Angelastro JM, Greene LA, Liu DX.
Mol Cancer Res. 2009 Jun;7(6):933-43. doi: 10.1158/1541-7786.MCR-08-0365. Epub 2009 Jun 16.
PMID 19531563
Delayed hepatocellular mitotic progression and impaired liver regeneration in early growth response-1-deficient mice.
Liao Y, Shikapwashya ON, Shteyer E, Dieckgraefe BK, Hruz PW, Rudnick DA.
J Biol Chem. 2004 Oct 8;279(41):43107-16. Epub 2004 Jul 20.
PMID 15265859
Cloning of tetradecanoyl phorbol ester-induced 'primary response' sequences and their expression in density-arrested Swiss 3T3 cells and a TPA non-proliferative variant.
Lim RW, Varnum BC, Herschman HR.
Oncogene. 1987;1(3):263-70.
PMID 3330774
Transcription factor EGR-1 suppresses the growth and transformation of human HT-1080 fibrosarcoma cells by induction of transforming growth factor beta 1.
Liu C, Adamson E, Mercola D.
Proc Natl Acad Sci U S A. 1996 Oct 15;93(21):11831-6.
PMID 8876223
The transcription factor EGR-1 directly transactivates the fibronectin gene and enhances attachment of human glioblastoma cell line U251.
Liu C, Yao J, Mercola D, Adamson E.
J Biol Chem. 2000 Jul 7;275(27):20315-23.
PMID 10783396
Concurrent down-regulation of Egr-1 and gelsolin in the majority of human breast cancer cells.
Liu J, Liu YG, Huang R, Yao C, Li S, Yang W, Yang D, Huang RP.
Cancer Genomics Proteomics. 2007 Nov-Dec;4(6):377-85.
PMID 18204200
Transcriptional responses to estrogen and progesterone in mammary gland identify networks regulating p53 activity.
Lu S, Becker KA, Hagen MJ, Yan H, Roberts AL, Mathews LA, Schneider SS, Siegelmann HT, MacBeth KJ, Tirrell SM, Blanchard JL, Jerry DJ.
Endocrinology. 2008 Oct;149(10):4809-20. doi: 10.1210/en.2008-0035. Epub 2008 Jun 12.
PMID 18556351
NAB2, a corepressor of EGR-1, inhibits vascular endothelial growth factor-mediated gene induction and angiogenic responses of endothelial cells.
Lucerna M, Mechtcheriakova D, Kadl A, Schabbauer G, Schafer R, Gruber F, Koshelnick Y, Muller HD, Issbrucker K, Clauss M, Binder BR, Hofer E.
J Biol Chem. 2003 Mar 28;278(13):11433-40. Epub 2002 Nov 8.
PMID 12427750
EGFR mutation up-regulates EGR1 expression through the ERK pathway.
Maegawa M, Arao T, Yokote H, Matsumoto K, Kudo K, Tanaka K, Kaneda H, Fujita Y, Ito F, Nishio K.
Anticancer Res. 2009 Apr;29(4):1111-7.
PMID 19414352
Differential gene expression in human lung adenocarcinomas and squamous cell carcinomas.
McDoniels-Silvers AL, Nimri CF, Stoner GD, Lubet RA, You M.
Clin Cancer Res. 2002 Apr;8(4):1127-38.
PMID 11948124
A nerve growth factor-induced gene encodes a possible transcriptional regulatory factor.
Milbrandt J.
Science. 1987 Nov 6;238(4828):797-9.
PMID 3672127
Inhibition of human breast carcinoma proliferation, migration, chemoinvasion and solid tumour growth by DNAzymes targeting the zinc finger transcription factor EGR-1.
Mitchell A, Dass CR, Sun LQ, Khachigian LM.
Nucleic Acids Res. 2004 Jun 4;32(10):3065-9. Print 2004.
PMID 15181171
EGR-1 is regulated by N-methyl-D-aspartate-receptor stimulation and associated with patient survival in human high grade astrocytomas.
Mittelbronn M, Harter P, Warth A, Lupescu A, Schilbach K, Vollmann H, Capper D, Goeppert B, Frei K, Bertalanffy H, Weller M, Meyermann R, Lang F, Simon P.
Brain Pathol. 2009 Apr;19(2):195-204. doi: 10.1111/j.1750-3639.2008.00175.x. Epub 2008 May 16.
PMID 18489490
Role of EGR-1 in thapsigargin-inducible apoptosis in the melanoma cell line A375-C6.
Muthukkumar S, Nair P, Sells SF, Maddiwar NG, Jacob RJ, Rangnekar VM.
Mol Cell Biol. 1995 Nov;15(11):6262-72.
PMID 7565779
Early growth response-1-dependent apoptosis is mediated by p53.
Nair P, Muthukkumar S, Sells SF, Han SS, Sukhatme VP, Rangnekar VM.
J Biol Chem. 1997 Aug 8;272(32):20131-8.
PMID 9242687
Activated Ki-Ras suppresses 12-O-tetradecanoylphorbol-13-acetate-induced activation of the c-Jun NH2-terminal kinase pathway in human colon cancer cells.
Okumura K, Shirasawa S, Nishioka M, Sasazuki T.
Cancer Res. 1999 May 15;59(10):2445-50.
PMID 10344756
Reduced expression of early growth response-1 gene in leiomyoma as identified by mRNA differential display.
Pambuccian CA, Oprea GM, Lakatua DJ.
Gynecol Oncol. 2002 Mar;84(3):431-6.
PMID 11855883
The effect of siRNA-Egr-1 and camptothecin on growth and chemosensitivity of breast cancer cell lines.
Parra E, Ferreira J.
Oncol Rep. 2010 Apr;23(4):1159-65.
PMID 20204305
The transcription factor early growth response factor-1 (EGR-1) promotes apoptosis of neuroblastoma cells.
Pignatelli M, Luna-Medina R, Perez-Rendon A, Santos A, Perez-Castillo A.
Biochem J. 2003 Aug 1;373(Pt 3):739-46.
PMID 12755686
Estrogen activates raf-1 kinase and induces expression of Egr-1 in MCF-7 breast cancer cells.
Pratt MA, Satkunaratnam A, Novosad DM.
Mol Cell Biochem. 1998 Dec;189(1-2):119-25.
PMID 9879662
Hepatocyte growth factor/scatter factor induces feedback up-regulation of CD44v6 in melanoma cells through Egr-1.
Recio JA, Merlino G.
Cancer Res. 2003 Apr 1;63(7):1576-82.
PMID 12670907
Alteration of Egr-1 mRNA during multistage carcinogenesis in mouse skin.
Riggs PK, Rho O, DiGiovanni J.
Mol Carcinog. 2000 Apr;27(4):247-51.
PMID 10747287
ETS target genes: identification of egr1 as a target by RNA differential display and whole genome PCR techniques.
Robinson L, Panayiotakis A, Papas TS, Kola I, Seth A.
Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7170-5.
PMID 9207063
Early growth response gene-1 regulates hypoxia-induced expression of tissue factor in glioblastoma multiforme through hypoxia-inducible factor-1-independent mechanisms.
Rong Y1, Hu F, Huang R, Mackman N, Horowitz JM, Jensen RL, Durden DL, Van Meir EG, Brat DJ.
Cancer Res. 2006 Jul 15;66(14):7067-74.
PMID 16849552
Early growth response gene 1 (EGR1) is deleted in estrogen receptor-negative human breast carcinoma.
Ronski K, Sanders M, Burleson JA, Moyo V, Benn P, Fang M.
Cancer. 2005 Sep 1;104(5):925-30.
PMID 15999367
Identification of NAB1, a repressor of NGFI-A- and Krox20-mediated transcription.
Russo MW, Sevetson BR, Milbrandt J.
Proc Natl Acad Sci U S A. 1995 Jul 18;92(15):6873-7.
PMID 7624335
Growth regulation via insulin-like growth factor binding protein-4 and -2 in association with mutant K-ras in lung epithelia.
Sato H, Yazawa T, Suzuki T, Shimoyamada H, Okudela K, Ikeda M, Hamada K, Yamada-Okabe H, Yao M, Kubota Y, Takahashi T, Kamma H, Kitamura H.
Am J Pathol. 2006 Nov;169(5):1550-66.
PMID 17071580
Mutant p53 initiates a feedback loop that involves Egr-1/EGF receptor/ERK in prostate cancer cells.
Sauer L, Gitenay D, Vo C, Baron VT.
Oncogene. 2010 May 6;29(18):2628-37. doi: 10.1038/onc.2010.24. Epub 2010 Mar 1.
PMID 20190820
The zinc finger transcription factor EGR-1 impedes interleukin-1-inducible tumor growth arrest.
Sells SF, Muthukumar S, Sukhatme VP, Crist SA, Rangnekar VM.
Mol Cell Biol. 1995 Feb;15(2):682-92.
PMID 7823937
Suppression of Egr-1 transcription through targeting of the serum response factor by oncogenic H-Ras.
Shin SY, Bahk YY, Ko J, Chung IY, Lee YS, Downward J, Eibel H, Sharma PM, Olefsky JM, Kim YH, Lee B, Lee YH.
EMBO J. 2006 Mar 8;25(5):1093-103. Epub 2006 Feb 2.
PMID 16456537
Transcription factor Egr-1 is essential for maximal matrix metalloproteinase-9 transcription by tumor necrosis factor alpha.
Shin SY, Kim JH, Baker A, Lim Y, Lee YH.
Mol Cancer Res. 2010 Apr;8(4):507-19. doi: 10.1158/1541-7786.MCR-09-0454. Epub 2010 Mar 23.
PMID 20332214
Transcriptional regulation of the growth-regulated oncogene α gene by early growth response protein-1 in response to tumor necrosis factor α stimulation.
Shin SY, Lee JM, Lim Y, Lee YH.
Biochim Biophys Acta. 2013 Oct;1829(10):1066-74. doi: 10.1016/j.bbagrm.2013.07.005. Epub 2013 Jul 18.
PMID 23872552
Decreased expression of early growth response-1 and its role in uterine leiomyoma growth.
Shozu M, Murakami K, Segawa T, Kasai T, Ishikawa H, Shinohara K, Okada M, Inoue M.
Cancer Res. 2004 Jul 1;64(13):4677-84.
PMID 15231681
Haploinsufficiency of del(5q) genes, Egr1 and Apc, cooperate with Tp53 loss to induce acute myeloid leukemia in mice.
Stoddart A, Fernald AA, Wang J, Davis EM, Karrison T, Anastasi J, Le Beau MM.
Blood. 2014 Feb 13;123(7):1069-78. doi: 10.1182/blood-2013-07-517953. Epub 2013 Dec 31.
PMID 24381225
A zinc finger-encoding gene coregulated with c-fos during growth and differentiation, and after cellular depolarization.
Sukhatme VP, Cao XM, Chang LC, Tsai-Morris CH, Stamenkovich D, Ferreira PC, Cohen DR, Edwards SA, Shows TB, Curran T, et al.
Cell. 1988 Apr 8;53(1):37-43.
PMID 3127059
EGR1 target genes in prostate carcinoma cells identified by microarray analysis.
Svaren J, Ehrig T, Abdulkadir SA, Ehrengruber MU, Watson MA, Milbrandt J.
J Biol Chem. 2000 Dec 8;275(49):38524-31.
PMID 10984481
NAB2, a corepressor of NGFI-A (Egr-1) and Krox20, is induced by proliferative and differentiative stimuli.
Svaren J, Sevetson BR, Apel ED, Zimonjic DB, Popescu NC, Milbrandt J.
Mol Cell Biol. 1996 Jul;16(7):3545-53.
PMID 8668170
Increased expression of early growth response-1 messenger ribonucleic acid in prostatic adenocarcinoma.
Thigpen AE, Cala KM, Guileyardo JM, Molberg KH, McConnell JD, Russell DW.
J Urol. 1996 Mar;155(3):975-81.
PMID 8583621
NF-kappaB/Egr-1/Gadd45 are sequentially activated upon UVB irradiation to mediate epidermal cell death.
Thyss R, Virolle V, Imbert V, Peyron JF, Aberdam D, Virolle T.
EMBO J. 2005 Jan 12;24(1):128-37. Epub 2004 Dec 16.
PMID 15616591
Activation of the Wnt pathway interferes with serum response element-driven transcription of immediate early genes.
Tice DA, Soloviev I, Polakis P.
J Biol Chem. 2002 Feb 22;277(8):6118-23. Epub 2001 Dec 18.
PMID 11751871
The Egr-1 transcription factor directly activates PTEN during irradiation-induced signalling.
Virolle T, Adamson ED, Baron V, Birle D, Mercola D, Mustelin T, de Belle I.
Nat Cell Biol. 2001 Dec;3(12):1124-8.
PMID 11781575
Egr1 promotes growth and survival of prostate cancer cells. Identification of novel Egr1 target genes.
Virolle T, Krones-Herzig A, Baron V, De Gregorio G, Adamson ED, Mercola D.
J Biol Chem. 2003 Apr 4;278(14):11802-10. Epub 2003 Jan 29.
PMID 12556466
A key role for early growth response-1 and nuclear factor-kappaB in mediating and maintaining GRO/CXCR2 proliferative signaling in esophageal cancer.
Wang B, Khachigian LM, Esau L, Birrer MJ, Zhao X, Parker MI, Hendricks DT.
Mol Cancer Res. 2009 May;7(5):755-64. doi: 10.1158/1541-7786.MCR-08-0472. Epub 2009 May 12.
PMID 19435811
Experimental and clinicopathologic study on the relationship between transcription factor Egr-1 and esophageal carcinoma.
Wu MY, Chen MH, Liang YR, Meng GZ, Yang HX, Zhuang CX.
World J Gastroenterol. 2001 Aug;7(4):490-5.
PMID 11819815
Relationship between Egr-1 gene expression and apoptosis in esophageal carcinoma and precancerous lesions.
Wu MY, Liang YR, Wu XY, Zhuang CX.
World J Gastroenterol. 2002 Dec;8(6):971-5.
PMID 12439908
Expression of Egr-1 gene and its correlation with the oncogene proteins in non-irradiated and irradiated esophageal squamous cell carcinoma.
Wu MY, Wu XY, Li QS, Zheng RM.
Dis Esophagus. 2006;19(4):267-72.
PMID 16866858
Expression of Egr-1, c-fos and cyclin D1 in esophageal cancer and its precursors: An immunohistochemical and in situ hybridization study.
Wu MY, Zhuang CX, Yang HX, Liang YR.
World J Gastroenterol. 2004 Feb 15;10(4):476-80.
PMID 14966901
Early growth response gene 1 modulates androgen receptor signaling in prostate carcinoma cells.
Yang SZ, Abdulkadir SA.
J Biol Chem. 2003 Oct 10;278(41):39906-11. Epub 2003 Jul 30.
PMID 12890669
Enhanced EGR1 activity promotes the growth of prostate cancer cells in an androgen-depleted environment.
Yang SZ, Eltoum IA, Abdulkadir SA.
J Cell Biochem. 2006 Apr 15;97(6):1292-9.
PMID 16552752
A network of p73, p53 and Egr1 is required for efficient apoptosis in tumor cells.
Yu J, Baron V, Mercola D, Mustelin T, Adamson ED.
Cell Death Differ. 2007 Mar;14(3):436-46. Epub 2006 Sep 22.
PMID 16990849
PTEN regulation by Akt-EGR1-ARF-PTEN axis.
Yu J, Zhang SS, Saito K, Williams S, Arimura Y, Ma Y, Ke Y, Baron V, Mercola D, Feng GS, Adamson E, Mustelin T.
EMBO J. 2009 Jan 7;28(1):21-33. doi: 10.1038/emboj.2008.238. Epub 2008 Dec 4.
PMID 19057511
Coactivating factors p300 and CBP are transcriptionally crossregulated by Egr1 in prostate cells, leading to divergent responses.
Yu J, de Belle I, Liang H, Adamson ED.
Mol Cell. 2004 Jul 2;15(1):83-94.
PMID 15225550
EGR-1 forms a complex with YAP-1 and upregulates Bax expression in irradiated prostate carcinoma cells.
Zagurovskaya M, Shareef MM, Das A, Reeves A, Gupta S, Sudol M, Bedford MT, Prichard J, Mohiuddin M, Ahmed MM.
Oncogene. 2009 Feb 26;28(8):1121-31. doi: 10.1038/onc.2008.461. Epub 2009 Jan 12.
PMID 19137013


This paper should be referenced as such :
Lee, YH
EGR1 (Early Growth Response 1)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(8):584-593.
Free journal version : [ pdf ]   [ DOI ]
History of this paper:
Bandyopadhyay, R ; Baron, V. EGR1 (early growth response 1). Atlas Genet Cytogenet Oncol Haematol. 2011;15(2):150-158.

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  Classification of myelodysplastic syndromes 2015

External links


HGNC (Hugo)EGR1   3238
Entrez_Gene (NCBI)EGR1    early growth response 1
AliasesAT225; G0S30; KROX-24; NGFI-A; 
TIS8; ZIF-268; ZNF225
GeneCards (Weizmann)EGR1
Ensembl hg19 (Hinxton)ENSG00000120738 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000120738 [Gene_View]  ENSG00000120738 [Sequence]  chr5:138465479-138469303 [Contig_View]  EGR1 [Vega]
ICGC DataPortalENSG00000120738
TCGA cBioPortalEGR1
AceView (NCBI)EGR1
Genatlas (Paris)EGR1
SOURCE (Princeton)EGR1
Genetics Home Reference (NIH)EGR1
Genomic and cartography
GoldenPath hg38 (UCSC)EGR1  -     chr5:138465479-138469303 +  5q31.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)EGR1  -     5q31.2   [Description]    (hg19-Feb_2009)
GoldenPathEGR1 - 5q31.2 [CytoView hg19]  EGR1 - 5q31.2 [CytoView hg38]
Genome Data Viewer NCBIEGR1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AK298101 AK301065 BC041701 BC073983 KM114058
RefSeq transcript (Entrez)NM_001964
Consensus coding sequences : CCDS (NCBI)EGR1
Gene ExpressionEGR1 [ NCBI-GEO ]   EGR1 [ EBI - ARRAY_EXPRESS ]   EGR1 [ SEEK ]   EGR1 [ MEM ]
Gene Expression Viewer (FireBrowse)EGR1 [ Firebrowse - Broad ]
GenevisibleExpression of EGR1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)1958
GTEX Portal (Tissue expression)EGR1
Human Protein AtlasENSG00000120738-EGR1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP18146   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP18146  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP18146
Domaine pattern : Prosite (Expaxy)ZINC_FINGER_C2H2_1 (PS00028)    ZINC_FINGER_C2H2_2 (PS50157)   
Domains : Interpro (EBI)EGR1_C    EGR_N    Znf_C2H2_sf    Znf_C2H2_type   
Domain families : Pfam (Sanger)DUF3432 (PF11914)    DUF3446 (PF11928)    zf-C2H2 (PF00096)   
Domain families : Pfam (NCBI)pfam11914    pfam11928    pfam00096   
Domain families : Smart (EMBL)ZnF_C2H2 (SM00355)  
Conserved Domain (NCBI)EGR1
PDB (RSDB)4R2A    4R2C    4R2D    4X9J    5N14   
PDB Europe4R2A    4R2C    4R2D    4X9J    5N14   
PDB (PDBSum)4R2A    4R2C    4R2D    4X9J    5N14   
PDB (IMB)4R2A    4R2C    4R2D    4X9J    5N14   
Structural Biology KnowledgeBase4R2A    4R2C    4R2D    4X9J    5N14   
SCOP (Structural Classification of Proteins)4R2A    4R2C    4R2D    4X9J    5N14   
CATH (Classification of proteins structures)4R2A    4R2C    4R2D    4X9J    5N14   
AlphaFold pdb e-kbP18146   
Human Protein Atlas [tissue]ENSG00000120738-EGR1 [tissue]
Protein Interaction databases
IntAct (EBI)P18146
Ontologies - Pathways
Ontology : AmiGOnegative regulation of transcription by RNA polymerase II  chromatin  chromatin  transcription cis-regulatory region binding  RNA polymerase II transcription regulatory region sequence-specific DNA binding  RNA polymerase II cis-regulatory region sequence-specific DNA binding  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription activator activity, RNA polymerase II-specific  response to hypoxia  response to ischemia  DNA binding  DNA-binding transcription factor activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytoplasm  regulation of transcription by RNA polymerase II  zinc ion binding  response to glucose  double-stranded methylated DNA binding  positive regulation of gene expression  T cell differentiation  BMP signaling pathway  positive regulation of chemokine production  positive regulation of interleukin-1 beta production  response to insulin  circadian regulation of gene expression  regulation of protein sumoylation  histone acetyltransferase binding  skeletal muscle cell differentiation  regulation of apoptotic process  sequence-specific DNA binding  hemi-methylated DNA-binding  estrous cycle  locomotor rhythm  positive regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase II  positive regulation of transcription by RNA polymerase II  positive regulation of transcription by RNA polymerase II  positive regulation of hormone biosynthetic process  circadian temperature homeostasis  type I interferon signaling pathway  regulation of transcription from RNA polymerase II promoter in response to hypoxia  interleukin-1-mediated signaling pathway  cellular response to gamma radiation  cellular response to heparin  cellular response to mycophenolic acid  glomerular mesangial cell proliferation  positive regulation of glomerular metanephric mesangial cell proliferation  negative regulation of canonical Wnt signaling pathway  cellular response to interleukin-8  positive regulation of neuron death  positive regulation of pri-miRNA transcription by RNA polymerase II  positive regulation of tau-protein kinase activity  sequence-specific double-stranded DNA binding  promoter-specific chromatin binding  regulation of progesterone biosynthetic process  
Ontology : EGO-EBInegative regulation of transcription by RNA polymerase II  chromatin  chromatin  transcription cis-regulatory region binding  RNA polymerase II transcription regulatory region sequence-specific DNA binding  RNA polymerase II cis-regulatory region sequence-specific DNA binding  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription factor activity, RNA polymerase II-specific  DNA-binding transcription activator activity, RNA polymerase II-specific  response to hypoxia  response to ischemia  DNA binding  DNA-binding transcription factor activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytoplasm  regulation of transcription by RNA polymerase II  zinc ion binding  response to glucose  double-stranded methylated DNA binding  positive regulation of gene expression  T cell differentiation  BMP signaling pathway  positive regulation of chemokine production  positive regulation of interleukin-1 beta production  response to insulin  circadian regulation of gene expression  regulation of protein sumoylation  histone acetyltransferase binding  skeletal muscle cell differentiation  regulation of apoptotic process  sequence-specific DNA binding  hemi-methylated DNA-binding  estrous cycle  locomotor rhythm  positive regulation of transcription, DNA-templated  positive regulation of transcription by RNA polymerase II  positive regulation of transcription by RNA polymerase II  positive regulation of transcription by RNA polymerase II  positive regulation of hormone biosynthetic process  circadian temperature homeostasis  type I interferon signaling pathway  regulation of transcription from RNA polymerase II promoter in response to hypoxia  interleukin-1-mediated signaling pathway  cellular response to gamma radiation  cellular response to heparin  cellular response to mycophenolic acid  glomerular mesangial cell proliferation  positive regulation of glomerular metanephric mesangial cell proliferation  negative regulation of canonical Wnt signaling pathway  cellular response to interleukin-8  positive regulation of neuron death  positive regulation of pri-miRNA transcription by RNA polymerase II  positive regulation of tau-protein kinase activity  sequence-specific double-stranded DNA binding  promoter-specific chromatin binding  regulation of progesterone biosynthetic process  
Pathways : BIOCARTAPhosphorylation of MEK1 by cdk5/p35 down regulates the MAP kinase pathway [Genes]   
Pathways : KEGGPrion diseases    HTLV-I infection   
REACTOMEP18146 [protein]
REACTOME PathwaysR-HSA-909733 [pathway]   
NDEx NetworkEGR1
Atlas of Cancer Signalling NetworkEGR1
Wikipedia pathwaysEGR1
Orthology - Evolution
GeneTree (enSembl)ENSG00000120738
Phylogenetic Trees/Animal Genes : TreeFamEGR1
Homologs : HomoloGeneEGR1
Homology/Alignments : Family Browser (UCSC)EGR1
Gene fusions - Rearrangements
Fusion : QuiverEGR1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerEGR1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)EGR1
Exome Variant ServerEGR1
GNOMAD BrowserENSG00000120738
Varsome BrowserEGR1
ACMGEGR1 variants
Genomic Variants (DGV)EGR1 [DGVbeta]
DECIPHEREGR1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisEGR1 
ICGC Data PortalEGR1 
TCGA Data PortalEGR1 
Broad Tumor PortalEGR1
OASIS PortalEGR1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICEGR1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DEGR1
Mutations and Diseases : HGMDEGR1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)EGR1
DoCM (Curated mutations)EGR1
CIViC (Clinical Interpretations of Variants in Cancer)EGR1
NCG (London)EGR1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry EGR1
NextProtP18146 [Medical]
Target ValidationEGR1
Huge Navigator EGR1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDEGR1
Pharm GKB GenePA27673
Clinical trialEGR1
DataMed IndexEGR1
PubMed476 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:16:51 CEST 2021

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