THOP1

File:Ambox wikify.svg

This article needs more links to other articles to help integrate it into the encyclopedia. Please help improve this article by adding links that are relevant to the context within the existing text. (March 2014) (Learn how and when to remove this template message)

|

VALUE_ERROR (nil)

Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
Entrez| |

n/a

n/a

Ensembl| |

n/a

n/a

UniProt| |

n/a

n/a

RefSeq (mRNA)| |

n/a

n/a

RefSeq (protein)| |

n/a

n/a

Location (UCSC)| n/a| n/a
PubMed search| n/a| n/a
Wikidata
| View/Edit Human|

|

Thimet oligopeptidase is an enzyme that in humans is encoded by the THOP1 gene.[1][2]

## References

[edit | edit source]

1. ↑ Torres MP, Prange C, Lennon G (Dec 1998). "Human endopeptidase 24.15 (THOP1) is localized on chromosome 19p13.3 and is excluded from the linkage region for late-onset Alzheimer disease". Genomics. 53 (2): 239–40. doi:10.1006/geno.1998.5487. PMID 9790774.
2. ↑ "Entrez Gene: THOP1 thimet oligopeptidase 1".

## Further reading

[edit | edit source]

* 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. 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.
* 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. 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. 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. 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. 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.

* v
* t
* e

PDB gallery

* 1s4b: Crystal structure of human thimet oligopeptidase.

1s4b: Crystal structure of human thimet oligopeptidase.

* 2o36: Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in neurotensin cleavage site

2o36: Crystal structure of engineered thimet oligopeptidase with neurolysin specificity in neurotensin cleavage site

| This article on a gene on human chromosome 19 is a stub. You can help Wikipedia by expanding it.

* v
* t
* e

|

*[v]: View this template
*[t]: Discuss this template
*[e]: Edit this template