node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
AMELX | ERAP2 | ENSP00000370088 | ENSP00000400376 | Amelogenin, X isoform; Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family | 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; Aminopeptidases | 0.590 |
CAST | ERAP2 | ENSP00000379157 | ENSP00000400376 | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 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; Aminopeptidases | 0.577 |
ERAP2 | AMELX | ENSP00000400376 | ENSP00000370088 | 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; Aminopeptidases | Amelogenin, X isoform; Plays a role in biomineralization. Seems to regulate the formation of crystallites during the secretory stage of tooth enamel development. Thought to play a major role in the structural organization and mineralization of developing enamel; Belongs to the amelogenin family | 0.590 |
ERAP2 | CAST | ENSP00000400376 | ENSP00000379157 | 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; Aminopeptidases | Calpastatin; Specific inhibition of calpain (calcium-dependent cysteine protease). Plays a key role in postmortem tenderization of meat and have been proposed to be involved in muscle protein degradation in living tissue; Belongs to the protease inhibitor I27 (calpastatin) family | 0.577 |
ERAP2 | TAPBP | ENSP00000400376 | ENSP00000404833 | 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; Aminopeptidases | Tapasin; Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading); C1-set domain containing | 0.569 |
ERAP2 | TAPBPL | ENSP00000400376 | ENSP00000266556 | 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; Aminopeptidases | Tapasin-related protein; Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2- microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression; C1-set domain containing | 0.554 |
ERAP2 | TPP2 | ENSP00000400376 | ENSP00000365233 | 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; Aminopeptidases | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity) | 0.769 |
ERAP2 | TREH | ENSP00000400376 | ENSP00000264029 | 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; Aminopeptidases | Trehalase; Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose; Belongs to the glycosyl hydrolase 37 family | 0.554 |
ERAP2 | XPNPEP1 | ENSP00000400376 | ENSP00000421566 | 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; Aminopeptidases | Xaa-Pro aminopeptidase 1; Contributes to the degradation of bradykinin. Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro; Aminopeptidases | 0.650 |
ERAP2 | XPNPEP2 | ENSP00000400376 | ENSP00000360147 | 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; Aminopeptidases | Xaa-Pro aminopeptidase 2; Membrane-bound metalloprotease which catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Arg-Pro-Pro. May play a role in the metabolism of the vasodilator bradykinin; Belongs to the peptidase M24B family | 0.647 |
ERAP2 | XPNPEP3 | ENSP00000400376 | ENSP00000349658 | 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; Aminopeptidases | X-prolyl aminopeptidase 3; Belongs to the peptidase M24B family | 0.647 |
ERAP2 | ZMPSTE24 | ENSP00000400376 | ENSP00000361845 | 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; Aminopeptidases | CAAX prenyl protease 1 homolog; Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C | 0.627 |
TAPBP | ERAP2 | ENSP00000404833 | ENSP00000400376 | Tapasin; Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading); C1-set domain containing | 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; Aminopeptidases | 0.569 |
TAPBP | TAPBPL | ENSP00000404833 | ENSP00000266556 | Tapasin; Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading); C1-set domain containing | Tapasin-related protein; Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2- microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression; C1-set domain containing | 0.443 |
TAPBPL | ERAP2 | ENSP00000266556 | ENSP00000400376 | Tapasin-related protein; Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2- microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression; C1-set domain containing | 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; Aminopeptidases | 0.554 |
TAPBPL | TAPBP | ENSP00000266556 | ENSP00000404833 | Tapasin-related protein; Component of the antigen processing and presentation pathway, which binds to MHC class I coupled with beta2- microglobulin/B2M. Association between TAPBPR and MHC class I occurs in the absence of a functional peptide-loading complex (PLC). Expression seems to slow down and down-regulate MHC class I surface expression; C1-set domain containing | Tapasin; Involved in the association of MHC class I with transporter associated with antigen processing (TAP) and in the assembly of MHC class I with peptide (peptide loading); C1-set domain containing | 0.443 |
TPP2 | ERAP2 | ENSP00000365233 | ENSP00000400376 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity) | 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; Aminopeptidases | 0.769 |
TPP2 | TREH | ENSP00000365233 | ENSP00000264029 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity) | Trehalase; Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose; Belongs to the glycosyl hydrolase 37 family | 0.409 |
TPP2 | ZMPSTE24 | ENSP00000365233 | ENSP00000361845 | Tripeptidyl-peptidase 2; Component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. May be able to complement the 26S proteasome function to some extent under conditions in which the latter is inhibited. Stimulates adipogenesis (By similarity) | CAAX prenyl protease 1 homolog; Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C | 0.420 |
TREH | ERAP2 | ENSP00000264029 | ENSP00000400376 | Trehalase; Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose; Belongs to the glycosyl hydrolase 37 family | 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; Aminopeptidases | 0.554 |