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EREG
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1K36, 1K37, 5E8D
Identifiers
Aliases	EREG, EPR, ER, Ep, epiregulin
External IDs	OMIM: 602061; MGI: 107508; HomoloGene: 1097; GeneCards: EREG; OMA:EREG - orthologs
Gene location (Human) Chr. Chromosome 4 (human) Band 4q13.3 Start 74,365,145 bp End 74,388,749 bp
Gene location (Mouse) Chr. Chromosome 5 (mouse) Band 5|5 E1 Start 91,222,481 bp End 91,241,505 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in buccal mucosa cell amniotic fluid skin of thigh skin of arm human penis cervix epithelium oral cavity bone marrow cells skin of abdomen gums Top expressed in skin of external ear conjunctival fornix esophagus umbilical cord endothelial cell of lymphatic vessel tunica media of zone of aorta skin of back ileum cornea epidermis More reference expression data BioGPS n/a
Gene ontology Molecular function epidermal growth factor receptor binding protein binding growth factor activity protein tyrosine kinase activity phosphatidylinositol-4,5-bisphosphate 3-kinase activity Cellular component integral component of membrane membrane plasma membrane integral component of plasma membrane extracellular region intracellular anatomical structure extracellular space clathrin-coated vesicle membrane Biological process luteinizing hormone signaling pathway positive regulation of epidermal growth factor-activated receptor activity cell differentiation ovarian cumulus expansion negative regulation of smooth muscle cell differentiation positive regulation of cytokine production cytokine-mediated signaling pathway positive regulation of fibroblast proliferation cell-cell signaling anatomical structure morphogenesis response to peptide hormone wound healing mRNA transcription female meiotic nuclear division primary follicle stage keratinocyte differentiation MAPK cascade multicellular organism development positive regulation of DNA replication keratinocyte proliferation oocyte maturation angiogenesis positive regulation of cell population proliferation positive regulation of innate immune response negative regulation of epithelial cell proliferation animal organ morphogenesis positive regulation of phosphorylation negative regulation of transcription, DNA-templated positive regulation of mitotic nuclear division ovulation positive regulation of cell division negative regulation of cell population proliferation positive regulation of smooth muscle cell proliferation positive regulation of protein kinase activity ERBB2 signaling pathway regulation of cell motility epidermal growth factor receptor signaling pathway peptidyl-tyrosine phosphorylation phosphatidylinositol phosphate biosynthetic process positive regulation of protein kinase B signaling signal transduction negative regulation of epidermal growth factor receptor signaling pathway membrane organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2069 13874 Ensembl ENSG00000124882 ENSMUSG00000029377 UniProt O14944 Q61521 RefSeq (mRNA) NM_001432 NM_007950 RefSeq (protein) NP_001423 NP_031976 Location (UCSC) Chr 4: 74.37 – 74.39 Mb Chr 5: 91.22 – 91.24 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Epiregulin (EPR) is a protein that in humans is encoded by the EREG gene.

Structure

Epiregulin consists of 46 amino acid residues. Its secondary structure contains approximately 30 percent of β-sheet in the strand. Some of the residues form loops and turns due to the hydrogen bonding. The percentage of β-sheet in epiregulin depends on the domain and the secondary structures that they occupy. The polymeric molecules of epiregulin has the formula weight of 5280.1 g/mol with a polypeptide(L), a polymer type.

Structural motifs in most proteins have typical connections in an all β motif. Meaning that the polypeptide chains do not make a crossover connection or in so far as this type of connection has not been observed. Epiregulin is one of the proteins that occupies a typical connection in all β motif. Furthermore, as the structure of epiregulin forms a chain in an all β motif, it also forms β hairpin structural motif. A β hairpin is when the two adjacent anti-parallel β strands connected by a β-turn.

Function

Epiregulin is a member of the epidermal growth factor family. Epiregulin can function as a ligand of epidermal growth factor receptor (EGFR), as well as a ligand of most members of the ERBB (v-erb-b2 oncogene homolog) family of tyrosine-kinase receptors. The secondary structure at the C-terminus epiregulin is different from other epidermal growth factor family ligands because of the lack of hydrogen bonds. The structural difference at the C-terminus may provide an explanation for the reduced binding affinity of epiregulin to the ERBB receptors.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000124882 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029377 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Toyoda H, Komurasaki T, Uchida D, Morimoto S (August 1997). "Distribution of mRNA for human epiregulin, a differentially expressed member of the epidermal growth factor family". Biochem. J. 326 (1): 69–75. doi:10.1042/bj3260069. PMC 1218638. PMID 9337852.
6. ^ "Entrez Gene: epiregulin".
7. ^ Sato K, Nakamura T, Mizuguchi M, Miura K, Tada M, Aizawa T, Gomi T, Miyamoto K, Kawano K (October 2003). "Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity". FEBS Lett. 553 (3): 232–8. doi:10.1016/s0014-5793(03)01005-6. PMID 14572630. S2CID 24761378.

Further reading

• Yamamoto T, Akisue T, Marui T, et al. (2004). "Expression of betacellulin, heparin-binding epidermal growth factor and epiregulin in human malignant fibrous histiocytoma". Anticancer Res. 24 (3b): 2007–10. PMID 15274392.
• Li S, Takeuchi F, Wang JA, et al. (2008). "Mesenchymal-epithelial interactions involving epiregulin in tuberous sclerosis complex hamartomas". Proc. Natl. Acad. Sci. U.S.A. 105 (9): 3539–44. Bibcode:2008PNAS..105.3539L. doi:10.1073/pnas.0712397105. PMC 2265180. PMID 18292222.
• Cho MC, Choi HS, Lee S, et al. (2008). "Epiregulin expression by Ets-1 and ERK signaling pathway in Ki-ras-transformed cells". Biochem. Biophys. Res. Commun. 377 (3): 832–7. doi:10.1016/j.bbrc.2008.10.053. PMID 18948081.
• Lindvall C, Hou M, Komurasaki T, et al. (2003). "Molecular characterization of human telomerase reverse transcriptase-immortalized human fibroblasts by gene expression profiling: activation of the epiregulin gene". Cancer Res. 63 (8): 1743–7. PMID 12702554.
• Morita S, Shirakata Y, Shiraishi A, et al. (2007). "Human corneal epithelial cell proliferation by epiregulin and its cross-induction by other EGF family members". Mol. Vis. 13: 2119–28. PMID 18079685.
• Freimann S, Ben-Ami I, Dantes A, et al. (2004). "EGF-like factor epiregulin and amphiregulin expression is regulated by gonadotropins/cAMP in human ovarian follicular cells". Biochem. Biophys. Res. Commun. 324 (2): 829–34. doi:10.1016/j.bbrc.2004.09.129. PMID 15474502.
• Ben-Ami I, Armon L, Freimann S, et al. (2009). "EGF-like growth factors as LH mediators in the human corpus luteum". Hum. Reprod. 24 (1): 176–84. doi:10.1093/humrep/den359. PMID 18835871.
• Shigeishi H, Higashikawa K, Hiraoka M, et al. (2008). "Expression of epiregulin, a novel epidermal growth factor ligand associated with prognosis in human oral squamous cell carcinomas". Oncol. Rep. 19 (6): 1557–64. doi:10.3892/or.19.6.1557. PMID 18497965.
• Taylor DS, Cheng X, Pawlowski JE, et al. (1999). "Epiregulin is a potent vascular smooth muscle cell-derived mitogen induced by angiotensin II, endothelin-1, and thrombin". Proc. Natl. Acad. Sci. U.S.A. 96 (4): 1633–8. Bibcode:1999PNAS...96.1633T. doi:10.1073/pnas.96.4.1633. PMC 15542. PMID 9990076.
• Zhang J, Iwanaga K, Choi KC, et al. (2008). "Intratumoral epiregulin is a marker of advanced disease in non-small cell lung cancer patients and confers invasive properties on EGFR-mutant cells". Cancer Prev Res (Phila). 1 (3): 201–7. doi:10.1158/1940-6207.CAPR-08-0014. PMC 3375599. PMID 19138957.
• Draper BK, Komurasaki T, Davidson MK, Nanney LB (2003). "Epiregulin is more potent than EGF or TGFalpha in promoting in vitro wound closure due to enhanced ERK/MAPK activation". J. Cell. Biochem. 89 (6): 1126–37. doi:10.1002/jcb.10584. PMID 12898511. S2CID 24643892.
• Révillion F, Lhotellier V, Hornez L, Bonneterre J, Peyrat JP (January 2008). "ErbB/HER ligands in human breast cancer, and relationships with their receptors, the bio-pathological features and prognosis". Ann. Oncol. 19 (1): 73–80. doi:10.1093/annonc/mdm431. PMID 17962208.
• Ben-Ami I, Freimann S, Armon L, et al. (2006). "PGE2 up-regulates EGF-like growth factor biosynthesis in human granulosa cells: new insights into the coordination between PGE2 and LH in ovulation". Mol. Hum. Reprod. 12 (10): 593–9. doi:10.1093/molehr/gal068. PMID 16888076.
• Takahashi M, Hayashi K, Yoshida K, et al. (2003). "Epiregulin as a major autocrine/paracrine factor released from ERK- and p38MAPK-activated vascular smooth muscle cells". Circulation. 108 (20): 2524–9. doi:10.1161/01.CIR.0000096482.02567.8C. PMID 14581411. S2CID 8012969.
• Lasky-Su J, Neale BM, Franke B, et al. (2008). "Genome-wide association scan of quantitative traits for attention deficit hyperactivity disorder identifies novel associations and confirms candidate gene associations". Am. J. Med. Genet. B Neuropsychiatr. Genet. 147B (8): 1345–54. doi:10.1002/ajmg.b.30867. PMID 18821565. S2CID 9493672.
• Gupta GP, Nguyen DX, Chiang AC, et al. (2007). "Mediators of vascular remodelling co-opted for sequential steps in lung metastasis". Nature. 446 (7137): 765–70. Bibcode:2007Natur.446..765G. doi:10.1038/nature05760. PMID 17429393. S2CID 4420038.
• Shirakata Y, Komurasaki T, Toyoda H, et al. (2000). "Epiregulin, a novel member of the epidermal growth factor family, is an autocrine growth factor in normal human keratinocytes". J. Biol. Chem. 275 (8): 5748–53. doi:10.1074/jbc.275.8.5748. PMID 10681561.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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