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Search results 201 to 268 out of 268 for Erap1

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Type Details Score
Publication      
First Author: Mouse Genome Informatics and the International Mouse Phenotyping Consortium (IMPC)
Year: 2014
Journal: Database Release
Title: Obtaining and Loading Phenotype Annotations from the International Mouse Phenotyping Consortium (IMPC) Database
Publication        
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Rat to Mouse ISO GO annotation transfer
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication        
First Author: MGD Nomenclature Committee
Year: 1995
Title: Nomenclature Committee Use
Publication
First Author: Skarnes WC
Year: 2011
Journal: Nature
Title: A conditional knockout resource for the genome-wide study of mouse gene function.
Volume: 474
Issue: 7351
Pages: 337-42
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2000
Title: Gene Ontology Annotation by electronic association of SwissProt Keywords with GO terms
Publication        
First Author: AgBase, BHF-UCL, Parkinson's UK-UCL, dictyBase, HGNC, Roslin Institute, FlyBase and UniProtKB curators
Year: 2011
Title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity
Publication
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication
First Author: Tsui FW
Year: 2010
Journal: Ann Rheum Dis
Title: Association of an ERAP1 ERAP2 haplotype with familial ankylosing spondylitis.
Volume: 69
Issue: 4
Pages: 733-6
Publication
First Author: Fruci D
Year: 2008
Journal: J Cell Physiol
Title: Altered expression of endoplasmic reticulum aminopeptidases ERAP1 and ERAP2 in transformed non-lymphoid human tissues.
Volume: 216
Issue: 3
Pages: 742-9
Allele
Name: endoplasmic reticulum aminopeptidase 1; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type: Endonuclease-mediated
Attribute String: Null/knockout
Publication
First Author: Tanioka T
Year: 2003
Journal: J Biol Chem
Title: Human leukocyte-derived arginine aminopeptidase. The third member of the oxytocinase subfamily of aminopeptidases.
Volume: 278
Issue: 34
Pages: 32275-83
Publication
First Author: Fruci D
Year: 2006
Journal: J Immunol
Title: Expression of endoplasmic reticulum aminopeptidases in EBV-B cell lines from healthy donors and in leukemia/lymphoma, carcinoma, and melanoma cell lines.
Volume: 176
Issue: 8
Pages: 4869-79
Publication
First Author: van Endert P
Year: 2011
Journal: Cell Mol Life Sci
Title: Post-proteasomal and proteasome-independent generation of MHC class I ligands.
Volume: 68
Issue: 9
Pages: 1553-67
Publication
First Author: Franke A
Year: 2010
Journal: Nat Genet
Title: Genome-wide meta-analysis increases to 71 the number of confirmed Crohn's disease susceptibility loci.
Volume: 42
Issue: 12
Pages: 1118-25
Publication
First Author: Johnson MP
Year: 2009
Journal: Hum Genet
Title: The ERAP2 gene is associated with preeclampsia in Australian and Norwegian populations.
Volume: 126
Issue: 5
Pages: 655-66
Protein Domain
Type: Family
Description: The ERAP2 aminopeptidase (endoplasmic reticulum aminopeptidase 2; MEROPS identifier M01.024) releases an amino acid from the N terminus of a peptide or protein but is unable to cleave Xaa-Pro and Pro-Xaa bonds. Preferentially, arginyl bonds are hydrolysed most efficiantly, followed by lysyl bonds []. ERAP2 is localized to the endoplasmic reticulum of B lymphocytes []and epithelial components of non-lymphoid tissue.Human ERAP1 and 2 co-localize in breast, endometrium, epididymus and ovary, whereas ERAP2 only is found in kidney, gall bladder and urinary bladder []. ERAP2 is important for antigen presentation on the cell surface by the major histocompatabiity complex (MHC). The proteasome degrades cytoplasmic proteins and generates peptides. Some of these peptides are transported to the lumen of the endoplasmic reticulum by a transport associated with antigen presntation (TAP). Trimming at the amino terminus by the aminopeptidases ERAP1 and ERAP2 generates a peptide of the correct length which can then associate with the MHC [, ]. Polymorphisms of ERAP2 have been implicated in ankylosing spondylitis [], Crohn's disease []and pre-eclampsia [].
Publication
First Author: Fujiwara H
Year: 2004
Journal: Biochem Biophys Res Commun
Title: Human extravillous trophoblasts express laeverin, a novel protein that belongs to membrane-bound gluzincin metallopeptidases.
Volume: 313
Issue: 4
Pages: 962-8
Publication
First Author: Maruyama M
Year: 2009
Journal: J Biol Chem
Title: Histidine 379 of human laeverin/aminopeptidase Q, a nonconserved residue within the exopeptidase motif, defines its distinctive enzymatic properties.
Volume: 284
Issue: 50
Pages: 34692-702
Publication
First Author: Haroon N
Year: 2010
Journal: Nat Rev Rheumatol
Title: Endoplasmic reticulum aminopeptidases: Biology and pathogenic potential.
Volume: 6
Issue: 8
Pages: 461-7
Publication
First Author: Maruyama M
Year: 2007
Journal: J Biol Chem
Title: Laeverin/aminopeptidase Q, a novel bestatin-sensitive leucine aminopeptidase belonging to the M1 family of aminopeptidases.
Volume: 282
Issue: 28
Pages: 20088-96
Publication
First Author: Luan Y
Year: 2007
Journal: Curr Med Chem
Title: The structure and main functions of aminopeptidase N.
Volume: 14
Issue: 6
Pages: 639-47
Publication
First Author: Wickström M
Year: 2011
Journal: Cancer Sci
Title: Aminopeptidase N (CD13) as a target for cancer chemotherapy.
Volume: 102
Issue: 3
Pages: 501-8
Publication
First Author: Likitvivatanavong S
Year: 2011
Journal: J Agric Food Chem
Title: Multiple receptors as targets of Cry toxins in mosquitoes.
Volume: 59
Issue: 7
Pages: 2829-38
Protein Domain
Type: Family
Description: This M1 peptidase family includes eukaryotic and bacterial members: aminopeptidase N (APN; MEROPS identifier M01.001), aminopeptidase Q (APQ, laeverin; MEROPS identifier M01.026) [, ], endoplasmic reticulum aminopeptidase 1 (ERAP1; MEROPS identifier M01.018) []as well as tricorn interacting factor F3 (MEROPS identifier M01.021).Aminopeptidase N (APN; CD13; Alanyl aminopeptidase; ), a type II integral membrane protease, consists of a small N-terminal cytoplasmic domain, a single transmembrane domain, and a large extracellular ectodomain that contains the active site. It preferentially cleaves neutral amino acids from the N terminus of oligopeptides and is present in a variety of human tissues and cell types (leukocyte, fibroblast, endothelial and epithelial cells). APN expression is dysregulated in inflammatory diseases such as chronic pain, rheumatoid arthritis, multiple sclerosis, systemic sclerosis, systemic lupus erythematosus, polymyositis/dermatomyosytis and pulmonary sarcoidosis, and is enhanced in tumor cells such as melanoma, renal, prostate, pancreas, colon, gastric and thyroid cancers. It is considered a marker of differentiation since it is predominantly expressed on stem cells and on cells of the granulocytic and monocytic lineages at distinct stages of differentiation. Thus, APN inhibition may lead to the development of anti-cancer and anti-inflammatory drugs [, ].ERAP1 also known as endoplasmic reticulum aminopeptidase associated with antigen processing (ERAAP), adipocyte derived leucine aminopeptidase (A-LAP) or aminopeptidase regulating tumor necrosis factor receptor I (THFRI) shedding (ARTS-1), associates with the closely related ER aminopeptidase ERAP2 (MEROPS identifier M01.024), for the final trimming of peptides within the ER for presentation by MHC class I molecules. ERAP1 is associated with ankylosing spondylitis (AS), an inflammatory arthritis that predominantly affects the spine. ERAP1 also aids in the shedding of membrane-bound cytokine receptors [].The tricorn interacting factor F3, together with factors F1 and F2, degrades the tricorn protease products, producing free amino acids, thus completing the proteasomal degradation pathway. F3 is homologous to F2, but not F1, and shows a strong preference for glutamate in the P1' position [].APQ, also known as laeverin, is specifically expressed in human embryo-derived extravillous trophoblasts (EVTs) that invade the uterus during early placentation []. It cleaves the N-terminal amino acid of various peptides such as angiotensin III, endokinin C, and kisspeptin-10, all expressed in the placenta in large quantities.APN is a receptor for coronaviruses, although the virus receptor interaction site seems to be distinct from the enzymatic site and aminopeptidase activity is not necessary for viral infection []. Insect APNs (MEROPS identifiers M01.013 and M01.030) are also putative Cry toxin receptors. Cry1 proteins are pore-forming toxins that bind to the midgut epithelial cell membrane of susceptible insect larvae, causing extensive damage. Several different toxins, including Cry1Aa, Cry1Ab, Cry1Ac, Cry1Ba, Cry1Ca and Cry1Fa, have been shown to bind to APNs; however, a direct role of APN in cytotoxicity has been yet to be firmly established [].
Publication
First Author: Kyrieleis OJ
Year: 2005
Journal: J Mol Biol
Title: Crystal structures of the tricorn interacting factor F3 from Thermoplasma acidophilum, a zinc aminopeptidase in three different conformations.
Volume: 349
Issue: 4
Pages: 787-800
Protein
Organism: Mus musculus/domesticus
Length: 966  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 945  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1025  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 920  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1025  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 559  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 702  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 841  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 691  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1066  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 674  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 595  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 991  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 711  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 889  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 501  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 792  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 876  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 966  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 945  
Fragment?: false