Search results for O89023
Showing 16 results out of 108 in All results
Protein sequences (6 results found)
Tripeptidyl-peptidase 1 TPP-1
Mus musculus (Reviewed)
Secondary accession number(s): Q543Q8, Q9QUS7
Genomes (1 results found)
tripeptidyl peptidase I [Source:MGI Symbol;Acc:MGI:1336194]
Species: Mus musculus
Nucleotide sequences (74 results found)
Mus musculus adult male kidney cDNA, RIKEN full-length enriched library, clone:0610009K21 product:ceroid-lipofuscinosis, neuronal 2, full insert sequence.
Mus musculus NOD-derived CD11c +ve dendritic cells cDNA, RIKEN full-length enriched library, clone:F630119J11 product:ceroid-lipofuscinosis, neuronal 2, full insert sequence.
Mus musculus 16 days embryo head cDNA, RIKEN full-length enriched library, clone:C130046C03 product:ceroid-lipofuscinosis, neuronal 2, full insert sequence.
Small molecules (18 results found)
Gene expression (2 results found)
Mus musculus Tpp1, tripeptidyl peptidase I [Source:MGI Symbol;Acc:MGI:1336194], is expressed in 4 baseline experiment(s); developmental stage: DN3, DN2b, DP, DN1, DN2a; organism part: skeletal muscle, cerebellum, heart, brain, lung, kidney, testis, liver, thymus, hippocampus, spleen; organism: Mus musculus
Mus musculus Tpp1, tripeptidyl peptidase I [Source:MGI Symbol;Acc:MGI:1336194], is differentially expressed in 9 experiment(s); time: 336 hours, 21 hours, 216 hours, 24 hours, 30 hours; diet: calorie restricted diet; growth condition: chemical hypoxia, hypobaric hypoxia; compound: dibenzazepine 10 micromoles per kilogram, cAMP, estradiol; genotype: ...
Protein families (4 results found)
Proteinase propeptide inhibitors (sometimes refered to as activation peptides) are responsible for the modulation of folding and activity of the pro-enzyme or zymogen. The pro-segment docks into the enzyme moiety shielding the substrate binding site, thereby promoting inhibition of the enzyme. Several such propeptides share a similar topology, despi...
This entry represents a domain found in serine peptidases belonging to the MEROPS peptidase families S8 (subfamilies S8A (subtilisin) and S8B (kexin)) and S53 (sedolisin), both of which are members of clan SB. The subtilisin family is the second largest serine protease family characterised to date. Over 200 subtilises are presently known, more than ...
Proteolytic enzymes that exploit serine in their catalytic activity are ubiquitous, being found in viruses, bacteria and eukaryotes. They include a wide range of peptidase activity, including exopeptidase, endopeptidase, oligopeptidase and omega-peptidase activity. Many families of serine protease have been identified, these being grouped into clans...