ERp27

ERP27
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2L4C, 4F9Z
Identifiers
Aliases	ERP27, C12orf46, PDIA8, endoplasmic reticulum protein 27
External IDs	OMIM: 610642; MGI: 1916437; HomoloGene: 12303; GeneCards: ERP27; OMA:ERP27 - orthologs
Gene location (Human)
Chr.	Chromosome 12 (human)
End	14,938,537 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	136,899,178 bp
RNA expression pattern
	Top expressed in
	body of pancreas; ; pancreatic epithelial cell; ; right uterine tube; ; tibialis anterior muscle; ; islet of Langerhans; ; human kidney; ; gonad; ; mucosa of ileum; ; urinary bladder; ; granulocyte;
	Top expressed in
	pancreas; ; granulocyte; ; islet of Langerhans; ; embryo; ; stomach; ; duodenum; ; thymus; ; mesenteric lymph nodes; ; migratory enteric neural crest cell; ; gastrula;
	More reference expression data
	n/a
Gene ontology
Molecular function	protein binding; protein disulfide isomerase activity; peptidyl-proline 4-dioxygenase activity;
Cellular component	endoplasmic reticulum lumen; endoplasmic reticulum;
Biological process	protein folding; response to endoplasmic reticulum stress; peptidyl-proline hydroxylation; regulation of oxidative stress-induced intrinsic apoptotic signaling pathway;
	Sources:Amigo / QuickGO
Orthologs
	121506
	69187
	ENSG00000139055
	ENSMUSG00000030219
	Q96DN0
	Q9D8U3
	NM_152321; NM_001300784
	NM_026983
	NP_001287713; NP_689534
	NP_081259
	Wikidata
View/Edit Human	View/Edit Mouse

Endoplasmic reticulum resident protein 27 is a protein that in humans is encoded by the ERP27 gene. It is a homologue of PDI (protein disulfide-isomerase), localised to the Endoplasmic Reticulum. The structure of ERp27 has been solved by both X-ray crystallography and NMR spectroscopy,⁵ showing it to be composed of two thioredoxin-like domains with homology to the non-catalytic b and b' domains of PDI. The function of ERp27 is unknown, but on the basis of its homology with PDI it is thought to possess chaperone activity.⁶

References

GRCh38: Ensembl release 89: ENSG00000139055 – Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000030219 – Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
Amin NT, Wallis AK, Wells SA, Rowe ML, Williamson RA, Howard MJ, et al. (March 2013). "High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility". The Biochemical Journal. 450 (2): 321–332. doi:10.1042/BJ20121635. PMC 4203274. PMID 23234573.
Galligan JJ, Petersen DR (July 2012). "The human protein disulfide isomerase gene family". Human Genomics. 6 (1) 6. doi:10.1186/1479-7364-6-6. PMC 3500226. PMID 23245351.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000139055 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000030219 – 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.

[Amin_2013-5] Amin NT, Wallis AK, Wells SA, Rowe ML, Williamson RA, Howard MJ, et al. (March 2013). "High-resolution NMR studies of structure and dynamics of human ERp27 indicate extensive interdomain flexibility". The Biochemical Journal. 450 (2): 321–332. doi:10.1042/BJ20121635. PMC 4203274. PMID 23234573.

[Galligan_2012-6] Galligan JJ, Petersen DR (July 2012). "The human protein disulfide isomerase gene family". Human Genomics. 6 (1) 6. doi:10.1186/1479-7364-6-6. PMC 3500226. PMID 23245351.

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