THOP1

THOP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1S4B, 2O36
Identifiers
Aliases	THOP1, EP24.15, MEPD_HUMAN, MP78, TOP, thimet oligopeptidase 1
External IDs	OMIM: 601117; MGI: 1354165; HomoloGene: 55726; GeneCards: THOP1; OMA:THOP1 - orthologs
Gene location (Human) Chr. Chromosome 19 (human) Band 19p13.3 Start 2,785,503 bp End 2,815,807 bp
Gene location (Mouse) Chr. Chromosome 10 (mouse) Band 10 C1|10 39.72 cM Start 80,905,869 bp End 80,918,393 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in left testis right testis right hemisphere of cerebellum right frontal lobe ventricular zone right lobe of liver apex of heart anterior pituitary muscle of thigh mucosa of transverse colon Top expressed in spermatid spermatocyte esophagus seminiferous tubule lip epiblast tail of embryo internal carotid artery embryo genital tubercle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function peptide binding peptidase activity hydrolase activity metallopeptidase activity metal ion binding metalloendopeptidase activity Cellular component cytoplasm mitochondrial intermembrane space cytosol Biological process proteolysis peptide metabolic process protein polyubiquitination Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 7064 50492 Ensembl ENSG00000172009 ENSMUSG00000004929 UniProt P52888 Q8C1A5 RefSeq (mRNA) NM_003249 NM_022653 RefSeq (protein) NP_003240 NP_073144 Location (UCSC) Chr 19: 2.79 – 2.82 Mb Chr 10: 80.91 – 80.92 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Thimet oligopeptidase is an enzyme that in humans is encoded by the THOP1 gene.

Further reading

• Thompson A, Huber G, Malherbe P (1995). "Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide". Biochem. Biophys. Res. Commun. 213 (1): 66–73. doi:10.1006/bbrc.1995.2099. PMID 7639763.
• Papastoitsis G, Siman R, Scott R, Abraham CR (1994). "Identification of a metalloprotease from Alzheimer's disease brain able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments". Biochemistry. 33 (1): 192–9. doi:10.1021/bi00167a025. PMID 8286339.
• Dando PM, Brown MA, Barrett AJ (1993). "Human thimet oligopeptidase". Biochem. J. 294 (Pt 2): 451–7. doi:10.1042/bj2940451. PMC 1134475. PMID 8373360.
• Meckelein B, de Silva HA, Roses AD, et al. (1997). "Human endopeptidase (THOP1) is localized on chromosome 19 within the linkage region for the late-onset alzheimer disease AD2 locus". Genomics. 31 (2): 246–9. doi:10.1006/geno.1996.0041. PMID 8824811.
• Crack PJ, Wu TJ, Cummins PM, et al. (1999). "The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane". Brain Res. 835 (2): 113–24. doi:10.1016/S0006-8993(99)01494-8. PMID 10415366. S2CID 23769423.
• Pineau C, McCool S, Glucksman MJ, et al. (2000). "Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testes". J. Cell Sci. 112 (20): 3455–62. doi:10.1242/jcs.112.20.3455. PMID 10504294.
• Ferro ES, Tullai JW, Glucksman MJ, Roberts JL (1999). "Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15)". DNA Cell Biol. 18 (10): 781–9. doi:10.1089/104454999314926. hdl:11449/37910. PMID 10541437.
• Tullai JW, Cummins PM, Pabon A, et al. (2001). "The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation". J. Biol. Chem. 275 (47): 36514–22. doi:10.1074/jbc.M001843200. PMID 10969067.
• Molina HM, Carmona AK, Kouyoumdjian M, Borges DR (2000). "Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase". Life Sci. 67 (5): 509–20. doi:10.1016/S0024-3205(00)00650-0. PMID 10993116.
• Saric T, Beninga J, Graef CI, et al. (2001). "Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase". J. Biol. Chem. 276 (39): 36474–81. doi:10.1074/jbc.M105517200. PMID 11479311.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Gioli-Pereira L, Fontenele-Neto JD, Borges DR, Kouyoumdjian M (2003). "Localization of EP24.15, a major liver kininase". J. Histochem. Cytochem. 51 (1): 125–7. doi:10.1177/002215540305100115. PMID 12502762.
• York IA, Mo AX, Lemerise K, et al. (2003). "The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation". Immunity. 18 (3): 429–40. doi:10.1016/S1074-7613(03)00058-X. PMID 12648459.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW (2004). "Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization". J. Biol. Chem. 279 (19): 20480–9. doi:10.1074/jbc.M400795200. PMID 14998993.
• Grimwood J, Gordon LA, Olsen A, et al. (2004). "The DNA sequence and biology of human chromosome 19". Nature. 428 (6982): 529–35. Bibcode:2004Natur.428..529G. doi:10.1038/nature02399. PMID 15057824.
• Lehner B, Sanderson CM (2004). "A Protein Interaction Framework for Human mRNA Degradation". Genome Res. 14 (7): 1315–23. doi:10.1101/gr.2122004. PMC 442147. PMID 15231747.
• Saric T, Graef CI, Goldberg AL (2004). "Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases". J. Biol. Chem. 279 (45): 46723–32. doi:10.1074/jbc.M406537200. PMID 15328361.
• Shivakumar BR, Wang Z, Hammond TG, Harris RC (2005). "EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor". Cell Biochem. Funct. 23 (3): 195–204. doi:10.1002/cbf.1176. PMID 15376229. S2CID 5695331.