Your Input:
|
||||
GSS | glutathione synthetase (474 aa) | |||
LTA4H | leukotriene A4 hydrolase; Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity (611 aa) | |||
LNPEP | leucyl/cystinyl aminopeptidase; Release of an N-terminal amino acid, cleaves before cysteine, leucine as well as other amino acids. Degrades peptide hormones such as oxytocin, vasopressin and angiotensin III, and plays a role in maintaining homeostasis during pregnancy. May be involved in the inactivation of neuronal peptides in the brain. Cleaves Met-enkephalin and dynorphin. Binds angiotensin IV and may be the angiotensin IV receptor in the brain (1025 aa) | |||
NAA50 | N(alpha)-acetyltransferase 50, NatE catalytic subunit; Probable catalytic component of the NAA11-NAA15 complex which displays alpha (N-terminal) acetyltransferase activity (169 aa) | |||
ACLY | ATP citrate lyase; ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA in many tissues. Has a central role in de novo lipid synthesis. In nervous tissue it may be involved in the biosynthesis of acetylcholine (1101 aa) | |||
TRHDE | thyrotropin-releasing hormone degrading enzyme; Specific inactivation of TRH after its release (1024 aa) | |||
ENPEP | glutamyl aminopeptidase (aminopeptidase A); Appears to have a role in the catabolic pathway of the renin-angiotensin system. Probably plays a role in regulating growth and differentiation of early B-lineage cells (957 aa) | |||
RNPEPL1 | arginyl aminopeptidase (aminopeptidase B)-like 1 (494 aa) | |||
NAT8 | N-acetyltransferase 8 (GCN5-related, putative); Plays a role in regulation of gastrulation (227 aa) | |||
NUBPL | nucleotide binding protein-like; Required for the assembly of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). May deliver of one or more Fe-S clusters to complex I subunits (319 aa) | |||
NAA11 | N(alpha)-acetyltransferase 11, NatA catalytic subunit; In complex with NAA15, displays alpha (N-terminal) acetyltransferase activity (229 aa) | |||
RNPEP | arginyl aminopeptidase (aminopeptidase B); Exopeptidase which selectively removes arginine and/or lysine residues from the N-terminus of several peptide substrates including Arg(0)-Leu-enkephalin, Arg(0)-Met-enkephalin and Arg(- 1)-Lys(0)-somatostatin-14. Can hydrolyze leukotriene A4 (LTA-4) into leukotriene B4 (LTB-4) (By similarity) (650 aa) | |||
ERAP1 | endoplasmic reticulum aminopeptidase 1; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Strongly prefers substrates 9-16 residues long. Rapidly degrades 13-mer to a 9-mer and then stops. Preferentially hydrolyzes the residue Leu and peptides with a hydrophobic C-terminus, while it has weak activity toward peptides with charged C-terminus. May play [...] (948 aa) | |||
ANPEP | alanyl (membrane) aminopeptidase; Broad specificity aminopeptidase. Plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. May play a critical role in the pathogenesis of cholesterol gallstone disease. May be involved in the metabolism of regulatory peptides of diverse cell types, responsible for the processing of peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. Found to cleave antigen peptides bound to major histocompatibility complex class II molecules of presenting cells and to degrad [...] (967 aa) | |||
ENSG00000174093 | Uncharacterized protein (478 aa) | |||
NPEPPS | aminopeptidase puromycin sensitive; Aminopeptidase with broad substrate specificity for several peptides. Involved in proteolytic events essential for cell growth and viability. May act as regulator of neuropeptide activity. Plays a role in the antigen-processing pathway for MHC class I molecules. Involved in the N-terminal trimming of cytotoxic T-cell epitope precursors. Digests the poly-Q peptides found in many cellular proteins. Digests tau from normal brain more efficiently than tau from Alzheimer disease brain (919 aa) | |||
NAA20 | N(alpha)-acetyltransferase 20, NatB catalytic subunit; Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration (178 aa) | |||
CS | citrate synthase (466 aa) | |||
RIMKLB | ribosomal modification protein rimK-like family member B; Catalyzes the synthesis of beta-citryl-glutamate and N- acetyl-aspartyl-glutamate. Beta-citryl-glutamate is synthesized more efficiently than N-acetyl-aspartyl-glutamate (By similarity) (386 aa) | |||
AQPEP | Aminopeptidase Q ; Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo- maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met- MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C (990 aa) | |||
C9orf3 | chromosome 9 open reading frame 3; Aminopeptidases catalyze the hydrolysis of amino acid residues from the N-terminus of peptide or protein substrates. Able to cleave angiotensin III to generate angiotensin IV, a bioactive peptide of the renin-angiotensin pathway. Not able to cleave angiotensin I and angiotensin II. May play a role in the proteolytic processing of bioactive peptides in tissues such as testis and heart (819 aa) | |||
ERAP2 | endoplasmic reticulum aminopeptidase 2; Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I- binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC class I molecules. Preferentially hydrolyzes the basic residues Arg and Lys (960 aa) | |||
RIMKLA | ribosomal modification protein rimK-like family member A; Catalyzes the synthesis of N-acetylaspartyl-glutamate (NAAG) (391 aa) | |||
NAA10 | N(alpha)-acetyltransferase 10, NatA catalytic subunit; In complex with NAA15, displays alpha (N-terminal) acetyltransferase activity. Without NAA15, displays epsilon (internal) acetyltransferase activity towards HIF1A, thereby promoting its degradation. Represses MYLK kinase activity by acetylation, and thus represses tumor cell migration (235 aa) | |||
GGTLC2 | gamma-glutamyltransferase light chain 2 (218 aa) | |||
NAA30 | N(alpha)-acetyltransferase 30, NatC catalytic subunit; Catalytic subunit of the N-terminal acetyltransferase C (NatC) complex. Catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Leu-Ala and Met-Leu-Gly. Necessary for the lysosomal localization and function of ARL8B (362 aa) |