ERAP2

Endoplasmic reticulum aminopeptidase 2 is a protein that in humans is encoded by the ERAP2 gene.[3]

ERAP2
Available structures PDB Human UniProt search: PDBe RCSB List of PDB id codes 3SE6, 4E36, 4JBS, 5CU5, 5AB2, 5AB0
Identifiers
Aliases	ERAP2, L-RAP, LRAP, endoplasmic reticulum aminopeptidase 2
External IDs	OMIM: 609497 HomoloGene: 75183 GeneCards: ERAP2
Gene location (Human) Chr. Chromosome 5 (human)[1] Band 5q15 Start 96,875,986 bp[1] End 96,919,703 bp[1]
Gene ontology Molecular function • aminopeptidase activity • metallopeptidase activity • peptidase activity • hydrolase activity • zinc ion binding • metal ion binding • peptide binding • metalloaminopeptidase activity • endopeptidase activity Cellular component • integral component of membrane • endoplasmic reticulum lumen • endoplasmic reticulum membrane • membrane • endoplasmic reticulum • cell membrane • cytoplasm Biological process • immune system process • adaptive immune response • proteolysis • regulation of blood pressure • antigen processing and presentation of peptide antigen via MHC class I • peptide catabolic process • antigen processing and presentation of endogenous peptide antigen via MHC class I • signal transduction • cell-cell signaling Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	64167	n/a
Ensembl	ENSG00000164308	n/a
UniProt	Q6P179	n/a
RefSeq (mRNA)	NM_001130140 NM_022350 NM_001329229 NM_001329233	n/a
RefSeq (protein)	NP_001123612 NP_001316158 NP_001316162 NP_071745	n/a
Location (UCSC)	Chr 5: 96.88 – 96.92 Mb	n/a
PubMed search	[2]	n/a
Wikidata
View/Edit Human

Function

Aminopeptidases hydrolyze N-terminal amino acids of proteins or peptide substrates. Major histocompatibility complex (MHC) class I molecules rely on aminopeptidases such as ERAP1 and LRAP to trim precursors to antigenic peptides in the endoplasmic reticulum (ER) following cleavage in the cytoplasm by tripeptidyl peptidase II (TPP2).[4]

References

1. GRCh38: Ensembl release 89: ENSG00000164308 - Ensembl, May 2017
2. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
3. "Entrez Gene: Endoplasmic reticulum amino peptidase 2".
4. Tanioka T, Hattori A, Masuda S, Nomura Y, Nakayama H, Mizutani S, Tsujimoto M (Aug 2003). "Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases". The Journal of Biological Chemistry. 278 (34): 32275–83. doi:10.1074/jbc.M305076200. PMID 12799365.

Further reading

• Xu XR, Huang J, Xu ZG, Qian BZ, Zhu ZD, Yan Q, Cai T, Zhang X, Xiao HS, Qu J, Liu F, Huang QH, Cheng ZH, Li NG, Du JJ, Hu W, Shen KT, Lu G, Fu G, Zhong M, Xu SH, Gu WY, Huang W, Zhao XT, Hu GX, Gu JR, Chen Z, Han ZG (Dec 2001). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 15089–15094. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
• Hill LD, Hilliard DD, York TP, Srinivas S, Kusanovic JP, Gomez R, Elovitz MA, Romero R, Strauss JF. "Fetal ERAP2 variation is associated with preeclampsia in African Americans in a case-control study". BMC Medical Genetics. 12: 64. doi:10.1186/1471-2350-12-64. PMC 3103419. PMID 21569342.
• Ascher DB, Polekhina G, Parker MW (Apr 2012). "Crystallization and preliminary X-ray diffraction analysis of human endoplasmic reticulum aminopeptidase 2". Acta Crystallographica Section F. 68 (Pt 4): 468–471. doi:10.1107/S1744309112006963. PMC 3325822. PMID 22505422.
• Kamphausen E, Kellert C, Abbas T, Akkad N, Tenzer S, Pawelec G, Schild H, van Endert P, Seliger B (Aug 2010). "Distinct molecular mechanisms leading to deficient expression of ER-resident aminopeptidases in melanoma". Cancer Immunology, Immunotherapy. 59 (8): 1273–84. doi:10.1007/s00262-010-0856-7. PMID 20419298.
• Stratikos E, Stern LJ (Oct 2013). "Antigenic peptide trimming by ER aminopeptidases--insights from structural studies". Molecular Immunology. 55 (3–4): 212–219. doi:10.1016/j.molimm.2013.03.002. PMC 3657621. PMID 23545452.
• Bjornsson HT, Albert TJ, Ladd-Acosta CM, Green RD, Rongione MA, Middle CM, Irizarry RA, Broman KW, Feinberg AP (May 2008). "SNP-specific array-based allele-specific expression analysis". Genome Research. 18 (5): 771–779. doi:10.1101/gr.073254.107. PMC 2336807. PMID 18369178.
• Mason CC, Hanson RL, Ossowski V, Bian L, Baier LJ, Krakoff J, Bogardus C. "Bimodal distribution of RNA expression levels in human skeletal muscle tissue". BMC Genomics. 12: 98. doi:10.1186/1471-2164-12-98. PMC 3044673. PMID 21299892.
• Haroon N, Tsui FW, Chiu B, Tsui HW, Inman RD (Sep 2010). "Serum cytokine receptors in ankylosing spondylitis: relationship to inflammatory markers and endoplasmic reticulum aminopeptidase polymorphisms". The Journal of Rheumatology. 37 (9): 1907–10. doi:10.3899/jrheum.100019. PMID 20595269.
• Qu HQ, Marchand L, Fréchette R, Bacot F, Lu Y, Polychronakos C (Mar 2007). "No association of type 1 diabetes with a functional polymorphism of the LRAP gene". Molecular Immunology. 44 (8): 2135–8. doi:10.1016/j.molimm.2006.10.015. PMID 17129607.

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