THOP1: Difference between revisions

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{{Underlinked|date=March 2014}}
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{{Infobox_gene}}
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'''Thimet oligopeptidase''' is an [[enzyme]] that in humans is encoded by the ''THOP1'' [[gene]].<ref name="pmid9790774">{{cite journal |vauthors=Torres MP, Prange C, Lennon G | title = Human endopeptidase 24.15 (THOP1) is localized on chromosome 19p13.3 and is excluded from the linkage region for late-onset Alzheimer disease | journal = Genomics | volume = 53 | issue = 2 | pages = 239–40 |date=Dec 1998 | pmid = 9790774 | pmc =  | doi = 10.1006/geno.1998.5487 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: THOP1 thimet oligopeptidase 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7064| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_THOP1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s4b.
| PDB = {{PDB2|1s4b}}, {{PDB2|2o36}}
| Name = Thimet oligopeptidase 1
| HGNCid = 11793
| Symbol = THOP1
| AltSymbols =; EP24.15; MEPD_HUMAN; MP78
| OMIM = 601117
| ECnumber = 
| Homologene = 55726
| MGIid = 1354165
| GeneAtlas_image1 = PBB_GE_THOP1_203235_at_tn.png
| Function = {{GNF_GO|id=GO:0004222 |text = metalloendopeptidase activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component =
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006518 |text = peptide metabolic process}} {{GNF_GO|id=GO:0007243 |text = protein kinase cascade}}
  | Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 7064
    | Hs_Ensembl = ENSG00000172009
    | Hs_RefseqProtein = NP_003240
    | Hs_RefseqmRNA = NM_003249
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 19
    | Hs_GenLoc_start = 2736506
    | Hs_GenLoc_end = 2764588
    | Hs_Uniprot = P52888
    | Mm_EntrezGene = 50492
    | Mm_Ensembl = ENSMUSG00000004929
    | Mm_RefseqmRNA = NM_022653
    | Mm_RefseqProtein = NP_073144
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 10
    | Mm_GenLoc_start = 80473279
    | Mm_GenLoc_end = 80485687
    | Mm_Uniprot = 
  }}
}}
'''Thimet oligopeptidase 1''', also known as '''THOP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: THOP1 thimet oligopeptidase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7064| accessdate = }}</ref>


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==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Thompson A, Huber G, Malherbe P |title=Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide. |journal=Biochem. Biophys. Res. Commun. |volume=213 |issue= 1 |pages= 66-73 |year= 1995 |pmid= 7639763 |doi= 10.1006/bbrc.1995.2099 }}
*{{cite journal  |vauthors=Thompson A, Huber G, Malherbe P |title=Cloning and functional expression of a metalloendopeptidase from human brain with the ability to cleave a beta-APP substrate peptide. |journal=Biochem. Biophys. Res. Commun. |volume=213 |issue= 1 |pages= 66–73 |year= 1995 |pmid= 7639763 |doi= 10.1006/bbrc.1995.2099 }}
*{{cite journal  | author=Papastoitsis G, Siman R, Scott R, Abraham CR |title=Identification of a metalloprotease from Alzheimer's disease brain able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments. |journal=Biochemistry |volume=33 |issue= 1 |pages= 192-9 |year= 1994 |pmid= 8286339 |doi=  }}
*{{cite journal  |vauthors=Papastoitsis G, Siman R, Scott R, Abraham CR |title=Identification of a metalloprotease from Alzheimer's disease brain able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments. |journal=Biochemistry |volume=33 |issue= 1 |pages= 192–9 |year= 1994 |pmid= 8286339 |doi=10.1021/bi00167a025 }}
*{{cite journal  | author=Dando PM, Brown MA, Barrett AJ |title=Human thimet oligopeptidase. |journal=Biochem. J. |volume=294 ( Pt 2) |issue=  |pages= 451-7 |year= 1993 |pmid= 8373360 |doi=  }}
*{{cite journal  |vauthors=Dando PM, Brown MA, Barrett AJ |title=Human thimet oligopeptidase |journal=Biochem. J. |volume=294 |issue=  Pt 2|pages= 451–7 |year= 1993 |pmid= 8373360 |doi= | pmc=1134475 }}
*{{cite journal  | author=Meckelein B, de Silva HA, Roses AD, ''et al.'' |title=Human endopeptidase (THOP1) is localized on chromosome 19 within the linkage region for the late-onset alzheimer disease AD2 locus. |journal=Genomics |volume=31 |issue= 2 |pages= 246-9 |year= 1997 |pmid= 8824811 |doi= 10.1006/geno.1996.0041 }}
*{{cite journal  | author=Meckelein B |title=Human endopeptidase (THOP1) is localized on chromosome 19 within the linkage region for the late-onset alzheimer disease AD2 locus |journal=Genomics |volume=31 |issue= 2 |pages= 246–9 |year= 1997 |pmid= 8824811 |doi= 10.1006/geno.1996.0041  |name-list-format=vanc| author2=de Silva HA  | author3=Roses AD  | display-authors=3  | last4=Rao  | first4=P.Nagesh  | last5=Pettenati  | first5=Mark J.  | last6=Xu  | first6=Pu-Ting  | last7=Hodge  | first7=Rosa  | last8=Glucksman  | first8=Marc J. | last9=Abraham  | first9=Carmela R. }}
*{{cite journal | author=Torres MP, Prange C, Lennon G |title=Human endopeptidase 24.15 (THOP1) is localized on chromosome 19p13.3 and is excluded from the linkage region for late-onset Alzheimer disease. |journal=Genomics |volume=53 |issue= 2 |pages= 239-40 |year= 1998 |pmid= 9790774 |doi= 10.1006/geno.1998.5487 }}
*{{cite journal  | author=Crack PJ |title=The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane |journal=Brain Res. |volume=835 |issue= 2 |pages= 113–24 |year= 1999 |pmid= 10415366 |doi=10.1016/S0006-8993(99)01494-8 |name-list-format=vanc| author2=Wu TJ  | author3=Cummins PM | display-authors=3  | last4=Ferro  | first4=Emer S  | last5=Tullai  | first5=John W  | last6=Glucksman  | first6=Marc J | last7=Roberts  | first7=James L }}
*{{cite journal  | author=Crack PJ, Wu TJ, Cummins PM, ''et al.'' |title=The association of metalloendopeptidase EC 3.4.24.15 at the extracellular surface of the AtT-20 cell plasma membrane. |journal=Brain Res. |volume=835 |issue= 2 |pages= 113-24 |year= 1999 |pmid= 10415366 |doi=  }}
*{{cite journal  | author=Pineau C |title=Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testes |journal=J. Cell Sci. |volume=112 |issue= 20|pages= 3455–62 |year= 2000 |pmid= 10504294 |doi= |name-list-format=vanc| author2=McCool S  | author3=Glucksman MJ  | display-authors=3  | last4=Jégou  | first4=B  | last5=Pierotti  | first5=AR  }}
*{{cite journal | author=Pineau C, McCool S, Glucksman MJ, ''et al.'' |title=Distribution of thimet oligopeptidase (E.C. 3.4.24.15) in human and rat testes. |journal=J. Cell. Sci. |volume=112 ( Pt 20) |issue=  |pages= 3455-62 |year= 2000 |pmid= 10504294 |doi=  }}
*{{cite journal  |vauthors=Ferro ES, Tullai JW, Glucksman MJ, Roberts JL |title=Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15) |journal=DNA Cell Biol. |volume=18 |issue= 10 |pages= 781–9 |year= 1999 |pmid= 10541437 |doi= 10.1089/104454999314926 }}
*{{cite journal  | author=Ferro ES, Tullai JW, Glucksman MJ, Roberts JL |title=Secretion of metalloendopeptidase 24.15 (EC 3.4.24.15). |journal=DNA Cell Biol. |volume=18 |issue= 10 |pages= 781-9 |year= 1999 |pmid= 10541437 |doi= 10.1089/104454999314926 }}
*{{cite journal  | author=Tullai JW |title=The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36514–22 |year= 2001 |pmid= 10969067 |doi= 10.1074/jbc.M001843200 |name-list-format=vanc| author2=Cummins PM  | author3=Pabon A  | display-authors=3  | last4=Roberts  | first4=JL  | last5=Lopingco  | first5=MC  | last6=Shrimpton  | first6=CN  | last7=Smith  | first7=AI | last8=Martignetti  | first8=JA  | last9=Ferro  | first9=ES }}
*{{cite journal  | author=Tullai JW, Cummins PM, Pabon A, ''et al.'' |title=The neuropeptide processing enzyme EC 3.4.24.15 is modulated by protein kinase A phosphorylation. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36514-22 |year= 2001 |pmid= 10969067 |doi= 10.1074/jbc.M001843200 }}
*{{cite journal  |vauthors=Molina HM, Carmona AK, Kouyoumdjian M, Borges DR |title=Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase |journal=Life Sci. |volume=67 |issue= 5 |pages= 509–20 |year= 2000 |pmid= 10993116 |doi=10.1016/S0024-3205(00)00650-0  }}
*{{cite journal  | author=Molina HM, Carmona AK, Kouyoumdjian M, Borges DR |title=Thimet oligopeptidase EC 3.4.24.15 is a major liver kininase. |journal=Life Sci. |volume=67 |issue= 5 |pages= 509-20 |year= 2000 |pmid= 10993116 |doi=  }}
*{{cite journal  | author=Saric T |title=Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36474–81 |year= 2001 |pmid= 11479311 |doi= 10.1074/jbc.M105517200 |name-list-format=vanc| author2=Beninga J | author3=Graef CI  | display-authors=3  | last4=Akopian  | first4=TN  | last5=Rock  | first5=KL  | last6=Goldberg  | first6=AL }}
*{{cite journal  | author=Saric T, Beninga J, Graef CI, ''et al.'' |title=Major histocompatibility complex class I-presented antigenic peptides are degraded in cytosolic extracts primarily by thimet oligopeptidase. |journal=J. Biol. Chem. |volume=276 |issue= 39 |pages= 36474-81 |year= 2001 |pmid= 11479311 |doi= 10.1074/jbc.M105517200 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Gioli-Pereira L, Fontenele-Neto JD, Borges DR, Kouyoumdjian M |title=Localization of EP24.15, a major liver kininase |journal=J. Histochem. Cytochem. |volume=51 |issue= 1 |pages= 125–7 |year= 2003 |pmid= 12502762 |doi=10.1177/002215540305100115  }}
*{{cite journal  | author=Gioli-Pereira L, Fontenele-Neto JD, Borges DR, Kouyoumdjian M |title=Localization of EP24.15, a major liver kininase. |journal=J. Histochem. Cytochem. |volume=51 |issue= 1 |pages= 125-7 |year= 2003 |pmid= 12502762 |doi=  }}
*{{cite journal  | author=York IA |title=The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation |journal=Immunity |volume=18 |issue= 3 |pages= 429–40 |year= 2003 |pmid= 12648459 |doi=10.1016/S1074-7613(03)00058-X  |name-list-format=vanc| author2=Mo AX  | author3=Lemerise K  | display-authors=3  | last4=Zeng  | first4=Wanyong  | last5=Shen  | first5=Yuelei  | last6=Abraham  | first6=Carmela R.  | last7=Saric  | first7=Tomo  | last8=Goldberg  | first8=Alfred L.  | last9=Rock  | first9=Kenneth L.  }}
*{{cite journal | author=York IA, Mo AX, Lemerise K, ''et al.'' |title=The cytosolic endopeptidase, thimet oligopeptidase, destroys antigenic peptides and limits the extent of MHC class I antigen presentation. |journal=Immunity |volume=18 |issue= 3 |pages= 429-40 |year= 2003 |pmid= 12648459 |doi=  }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW |title=Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20480–9 |year= 2004 |pmid= 14998993 |doi= 10.1074/jbc.M400795200 }}
*{{cite journal | author=Ray K, Hines CS, Coll-Rodriguez J, Rodgers DW |title=Crystal structure of human thimet oligopeptidase provides insight into substrate recognition, regulation, and localization. |journal=J. Biol. Chem. |volume=279 |issue= 19 |pages= 20480-9 |year= 2004 |pmid= 14998993 |doi= 10.1074/jbc.M400795200 }}
*{{cite journal  | author=Grimwood J |title=The DNA sequence and biology of human chromosome 19 |journal=Nature |volume=428 |issue= 6982 |pages= 529–35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399  |name-list-format=vanc| author2=Gordon LA  | author3=Olsen A  | display-authors=3  | last4=Terry  | first4=Astrid  | last5=Schmutz  | first5=Jeremy  | last6=Lamerdin  | first6=Jane  | last7=Hellsten  | first7=Uffe  | last8=Goodstein  | first8=David  | last9=Couronne  | first9=Olivier }}
*{{cite journal  | author=Grimwood J, Gordon LA, Olsen A, ''et al.'' |title=The DNA sequence and biology of human chromosome 19. |journal=Nature |volume=428 |issue= 6982 |pages= 529-35 |year= 2004 |pmid= 15057824 |doi= 10.1038/nature02399 }}
*{{cite journal  |vauthors=Lehner B, Sanderson CM |title=A Protein Interaction Framework for Human mRNA Degradation |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315–23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004  | pmc=442147 }}
*{{cite journal  | author=Lehner B, Sanderson CM |title=A protein interaction framework for human mRNA degradation. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1315-23 |year= 2004 |pmid= 15231747 |doi= 10.1101/gr.2122004 }}
*{{cite journal  |vauthors=Saric T, Graef CI, Goldberg AL |title=Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46723–32 |year= 2004 |pmid= 15328361 |doi= 10.1074/jbc.M406537200 }}
*{{cite journal  | author=Saric T, Graef CI, Goldberg AL |title=Pathway for degradation of peptides generated by proteasomes: a key role for thimet oligopeptidase and other metallopeptidases. |journal=J. Biol. Chem. |volume=279 |issue= 45 |pages= 46723-32 |year= 2004 |pmid= 15328361 |doi= 10.1074/jbc.M406537200 }}
*{{cite journal  |vauthors=Shivakumar BR, Wang Z, Hammond TG, Harris RC |title=EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor |journal=Cell Biochem. Funct. |volume=23 |issue= 3 |pages= 195–204 |year= 2005 |pmid= 15376229 |doi= 10.1002/cbf.1176 }}
*{{cite journal  | author=Shivakumar BR, Wang Z, Hammond TG, Harris RC |title=EP24.15 interacts with the angiotensin II type I receptor and bradykinin B2 receptor. |journal=Cell Biochem. Funct. |volume=23 |issue= 3 |pages= 195-204 |year= 2005 |pmid= 15376229 |doi= 10.1002/cbf.1176 }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=7064}}
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Revision as of 21:00, 8 November 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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


References

  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



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