Epiregulin

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Protein found in humans
EREG
Available structures
PDBOrtholog search:PDBeRCSB
List of PDB id codes

1K36,1K37,5E8D

Identifiers
AliasesEREG, EPR, ER, Ep, epiregulin
External IDsOMIM:602061;MGI:107508;HomoloGene:1097;GeneCards:EREG;OMA:EREG - orthologs
Gene location (Human)
Chromosome 4 (human)
Chr.Chromosome 4 (human)[1]
Chromosome 4 (human)
Genomic location for EREG
Genomic location for EREG
Band4q13.3Start74,365,145bp[1]
End74,388,749bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for EREG
Genomic location for EREG
Band5|5 E1Start91,222,481bp[2]
End91,241,505bp[2]
RNA expression pattern
Bgee
HumanMouse (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
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
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 MbChr 5: 91.22 – 91.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Epiregulin (EPR) is aprotein that in humans is encoded by theEREGgene.[5][6]

Structure

Epiregulin consists of 46 amino acid residues. Itssecondary structure contains approximately 30 percent ofβ-sheet in the strand.[7] Some of the residues form loops and turns due to thehydrogen bonding.[7] The percentage of β-sheet in epiregulin depends on thedomain 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.[7]

Structural motifs in most proteins have typical connections in anall 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 formsβ hairpinstructural motif. A β hairpin is when the two adjacent anti-parallel β strands connected by a β-turn.

Function

Epiregulin is a member of theepidermal growth factor family. Epiregulin can function as a ligand ofepidermal growth factor receptor (EGFR), as well as a ligand of most members of theERBB (v-erb-b2 oncogene homolog) family oftyrosine-kinase receptors.[6] 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.[7]

References

  1. ^abcGRCh38: Ensembl release 89: ENSG00000124882Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000029377Ensembl, 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. ^ab"Entrez Gene: epiregulin".
  7. ^abcdSato 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

PDB gallery
  • 1k36: NMR Structure of human Epiregulin
    1k36: NMR Structure of human Epiregulin
  • 1k37: NMR Structure of human Epiregulin
    1k37: NMR Structure of human Epiregulin

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

Angiopoietin
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