STRINGSTRING
AGBL3 AGBL3 CPA1 CPA1 VASH1 VASH1 CPB2 CPB2 FAP FAP CTSZ CTSZ MMP15 MMP15 CTSH CTSH CPQ CPQ CPA2 CPA2 CPA4 CPA4 AEBP1 AEBP1 CPD CPD LAP3 LAP3 CTSC CTSC LTA4H LTA4H PRSS16 PRSS16 MEP1A MEP1A LNPEP LNPEP CPXM2 CPXM2 PEPD PEPD FOLH1 FOLH1 GGH GGH ADAM10 ADAM10 TRHDE TRHDE BLMH BLMH SCPEP1 SCPEP1 HPN HPN DPP9 DPP9 ENPEP ENPEP RNPEPL1 RNPEPL1 SCRN3 SCRN3 CPO CPO PM20D2 PM20D2 MMP16 MMP16 SCRN2 SCRN2 ACE ACE RNPEP RNPEP CPA3 CPA3 METAP1 METAP1 ERAP1 ERAP1 CPA6 CPA6 TPP1 TPP1 ANPEP ANPEP MMP14 MMP14 RCE1 RCE1 METAP1D METAP1D NPEPPS NPEPPS METAP2 METAP2 CNDP2 CNDP2 AGTPBP1 AGTPBP1 CPM CPM DPP8 DPP8 ERMP1 ERMP1 NPEPL1 NPEPL1 XPNPEP3 XPNPEP3 LVRN LVRN NAALADL1 NAALADL1 CNDP1 CNDP1 AGBL5 AGBL5 DPP4 DPP4 MMP17 MMP17 CPZ CPZ MINDY1 MINDY1 CPN1 CPN1 XPNPEP2 XPNPEP2 DPP7 DPP7 AGBL4 AGBL4 CTSA CTSA ZMPSTE24 ZMPSTE24 AOPEP AOPEP TPP2 TPP2 CPXM1 CPXM1 DPEP1 DPEP1 PRCP PRCP JMJD7 JMJD7 F11 F11 CPE CPE CPVL CPVL SCRN1 SCRN1 ACE2 ACE2 KDM8 KDM8 ERAP2 ERAP2 AGBL1 AGBL1 CPB1 CPB1 MME MME CPA5 CPA5 XPNPEP1 XPNPEP1 NUDT16 NUDT16 VASH2 VASH2 DNPEP DNPEP NAALAD2 NAALAD2 AGBL2 AGBL2 DPP3 DPP3 MINDY2 MINDY2 DPEP2 DPEP2 DPEP3 DPEP3
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AGBL3Cytosolic carboxypeptidase 3; Metallocarboxypeptidase that mediates both deglutamylation and deaspartylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene- encoded polyglutamates or polyaspartates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. (920 aa)
CPA1Carboxypeptidase A1; Carboxypeptidase that catalyzes the release of a C-terminal amino acid, but has little or no action with -Asp, -Glu, -Arg, -Lys or -Pro; Belongs to the peptidase M14 family. (419 aa)
VASH1Tubulinyl-Tyr carboxypeptidase 1; Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Acts as an angiogenesis inhibitor: inhibits migration, proliferation and network formation by endothelial cells as well as angiogenesis. This inhibitory effect is selective to endothelial cells as it does not affect the migration of smooth muscle cells [...] (365 aa)
CPB2Carboxypeptidase B2; Cleaves C-terminal arginine or lysine residues from biologically active peptides such as kinins or anaphylatoxins in the circulation thereby regulating their activities. Down-regulates fibrinolysis by removing C-terminal lysine residues from fibrin that has already been partially degraded by plasmin. Belongs to the peptidase M14 family. (423 aa)
FAPAntiplasmin-cleaving enzyme FAP, soluble form; Cell surface glycoprotein serine protease that participates in extracellular matrix degradation and involved in many cellular processes including tissue remodeling, fibrosis, wound healing, inflammation and tumor growth. Both plasma membrane and soluble forms exhibit post-proline cleaving endopeptidase activity, with a marked preference for Ala/Ser-Gly-Pro-Ser/Asn/Ala consensus sequences, on substrate such as alpha-2-antiplasmin SERPINF2 and SPRY2. Degrade also gelatin, heat-denatured type I collagen, but not native collagen type I and IV, [...] (760 aa)
CTSZCathepsin Z; Exhibits carboxy-monopeptidase as well as carboxy-dipeptidase activity. Capable of producing kinin potentiating peptides (By similarity); Belongs to the peptidase C1 family. (303 aa)
MMP15Matrix metalloproteinase-15; Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A. Belongs to the peptidase M10A family. (669 aa)
CTSHCathepsin H heavy chain; Important for the overall degradation of proteins in lysosomes; Belongs to the peptidase C1 family. (335 aa)
CPQCarboxypeptidase Q; Carboxypeptidase that may play an important role in the hydrolysis of circulating peptides. Catalyzes the hydrolysis of dipeptides with unsubstituted terminals into amino acids. May play a role in the liberation of thyroxine hormone from its thyroglobulin (Tg) precursor. (472 aa)
CPA2Carboxypeptidase A2. (419 aa)
CPA4Carboxypeptidase A4; Metalloprotease that could be involved in the histone hyperacetylation pathway. Releases a C-terminal amino acid, with preference for -Phe, -Leu, -Ile, -Met, -Tyr and -Val ; Belongs to the peptidase M14 family. (421 aa)
AEBP1Adipocyte enhancer-binding protein 1; [Isoform 1]: As a positive regulator of collagen fibrillogenesis, it is probably involved in the organization and remodeling of the extracellular matrix; Belongs to the peptidase M14 family. (1158 aa)
CPDCarboxypeptidase D. (1380 aa)
LAP3Cytosol aminopeptidase; Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N- terminal amino acids from various peptides; Belongs to the peptidase M17 family. (519 aa)
CTSCDipeptidyl peptidase 1 exclusion domain chain; Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B. Can also activate neuraminidase and factor XIII; Belongs to the peptidase C1 family. (463 aa)
LTA4HLeukotriene A-4 hydrolase; Epoxide hydrolase that catalyzes the final step in the biosynthesis of the proinflammatory mediator leukotriene B4. Has also aminopeptidase activity. (611 aa)
PRSS16Thymus-specific serine protease; Protease that may play a role in T-cell development; Belongs to the peptidase S28 family. (514 aa)
MEP1AMeprin A subunit alpha. (746 aa)
LNPEPLeucyl-cystinyl aminopeptidase, pregnancy serum form; 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)
CPXM2Inactive carboxypeptidase-like protein X2; May be involved in cell-cell interactions; Belongs to the peptidase M14 family. (756 aa)
PEPDXaa-Pro dipeptidase; Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen; Belongs to the peptidase M24B family. Eukaryotic-type prolidase subfamily. (493 aa)
FOLH1Glutamate carboxypeptidase 2; Has both folate hydrolase and N-acetylated-alpha-linked- acidic dipeptidase (NAALADase) activity. Has a preference for tri- alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Involved in prostate tumor progression. (750 aa)
GGHGamma-glutamyl hydrolase; Hydrolyzes the polyglutamate sidechains of pteroylpolyglutamates. Progressively removes gamma-glutamyl residues from pteroylpoly-gamma-glutamate to yield pteroyl-alpha-glutamate (folic acid) and free glutamate. May play an important role in the bioavailability of dietary pteroylpolyglutamates and in the metabolism of pteroylpolyglutamates and antifolates; Belongs to the peptidase C26 family. (318 aa)
ADAM10Disintegrin and metalloproteinase domain-containing protein 10; Cleaves the membrane-bound precursor of TNF-alpha at '76- Ala-|-Val-77' to its mature soluble form. Responsible for the proteolytical release of soluble JAM3 from endothelial cells surface. Responsible for the proteolytic release of several other cell-surface proteins, including heparin-binding epidermal growth-like factor, ephrin-A2, CD44, CDH2 and for constitutive and regulated alpha-secretase cleavage of amyloid precursor protein (APP). Contributes to the normal cleavage of the cellular prion protein. Involved in the cl [...] (748 aa)
TRHDEThyrotropin-releasing hormone-degrading ectoenzyme; Specific inactivation of TRH after its release; Belongs to the peptidase M1 family. (1024 aa)
BLMHBleomycin hydrolase; The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B- aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity. (455 aa)
SCPEP1Retinoid-inducible serine carboxypeptidase; May be involved in vascular wall and kidney homeostasis. Belongs to the peptidase S10 family. (452 aa)
HPNSerine protease hepsin non-catalytic chain; Serine protease that cleaves extracellular substrates, and contributes to the proteolytic processing of growth factors, such as HGF and MST1/HGFL. Plays a role in cell growth and maintenance of cell morphology. Plays a role in the proteolytic processing of ACE2. Mediates the proteolytic cleavage of urinary UMOD that is required for UMOD polymerization. Belongs to the peptidase S1 family. (417 aa)
DPP9Dipeptidyl peptidase 9; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. (892 aa)
ENPEPGlutamyl aminopeptidase; Regulates central hypertension through its calcium-modulated preference to cleave N-terminal acidic residues from peptides such as angiotensin II. (957 aa)
RNPEPL1Aminopeptidase RNPEPL1; Broad specificity aminopeptidase which preferentially hydrolyzes an N-terminal methionine, citrulline or glutamine. Belongs to the peptidase M1 family. (725 aa)
SCRN3Secernin-3; Secernin 3. (424 aa)
CPOCarboxypeptidase O; Carboxypeptidase which preferentially cleaves C-terminal acidic residues from peptides and proteins. Can also cleave C-terminal hydrophobic amino acids, with a preference for small residues over large residues. (374 aa)
PM20D2Peptidase M20 domain containing 2. (436 aa)
MMP16Matrix metalloproteinase-16; Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. Isoform short cleaves fibronectin and also collagen type III, but at lower rate. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells. Belongs to the peptidase M10A family. (607 aa)
SCRN2Secernin-2; Secernin 2; Belongs to the peptidase C69 family. Secernin subfamily. (425 aa)
ACEAngiotensin-converting enzyme, soluble form; Converts angiotensin I to angiotensin II by release of the terminal His-Leu, this results in an increase of the vasoconstrictor activity of angiotensin. Also able to inactivate bradykinin, a potent vasodilator. Has also a glycosidase activity which releases GPI- anchored proteins from the membrane by cleaving the mannose linkage in the GPI moiety; Belongs to the peptidase M2 family. (1306 aa)
RNPEPAminopeptidase 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)
CPA3Carboxypeptidase A3. (417 aa)
METAP1Methionine aminopeptidase 1; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Required for normal progression through the cell cycle. (386 aa)
ERAP1Endoplasmic 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)
CPA6Carboxypeptidase A6; May be involved in the proteolytic inactivation of enkephalins and neurotensin in some brain areas. May convert inactive angiotensin I into the biologically active angiotensin II. Releases a C-terminal amino acid, with preference for large hydrophobic C-terminal amino acids and shows only very weak activity toward small amino acids and histidine. (437 aa)
TPP1Tripeptidyl-peptidase 1; Lysosomal serine protease with tripeptidyl-peptidase I activity. May act as a non-specific lysosomal peptidase which generates tripeptides from the breakdown products produced by lysosomal proteinases. Requires substrates with an unsubstituted N-terminus. (563 aa)
ANPEPAminopeptidase N; Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding [...] (967 aa)
MMP14Matrix metalloproteinase-14; Endopeptidase that degrades various components of the extracellular matrix such as collagen. Activates progelatinase A. Essential for pericellular collagenolysis and modeling of skeletal and extraskeletal connective tissues during development (By similarity). May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro-MMP2. Cleaves ADGRB1 to release vasculostatin-40 which inhibits angiog [...] (582 aa)
RCE1CAAX prenyl protease 2; Proteolytically removes the C-terminal three residues of farnesylated and geranylated proteins. Seems to be able to process K- Ras, N-Ras, H-Ras, RAP1B and G-gamma-1. (329 aa)
METAP1DMethionine aminopeptidase 1D, mitochondrial; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed (By similarity). May play a role in colon tumorigenesis; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily. (335 aa)
NPEPPSPuromycin-sensitive aminopeptidase; 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)
METAP2Methionine aminopeptidase 2; Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met- Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo; Belongs to the peptidase M24A family. Methionine aminopeptidase eukaryotic typ [...] (478 aa)
CNDP2Cytosolic non-specific dipeptidase; Hydrolyzes a variety of dipeptides including L-carnosine but has a strong preference for Cys-Gly. Acts as a functional tumor suppressor in gastric cancer via activation of the mitogen-activated protein kinase (MAPK) pathway. An elevated level of CNDP2 activates the p38 and JNK MAPK pathways to induce cell apoptosis, and a lower level of CNDP2 activates the ERK MAPK pathway to promote cell proliferation. Isoform 2 may play a role as tumor suppressor in hepatocellular carcinoma (HCC) cells. Catalyzes the production of N-lactoyl-amino acids from lactate [...] (475 aa)
AGTPBP1Cytosolic carboxypeptidase 1; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. (1278 aa)
CPMCarboxypeptidase M; Specifically removes C-terminal basic residues (Arg or Lys) from peptides and proteins. It is believed to play important roles in the control of peptide hormone and growth factor activity at the cell surface, and in the membrane-localized degradation of extracellular proteins; Belongs to the peptidase M14 family. (443 aa)
DPP8Dipeptidyl peptidase 8; Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. (898 aa)
ERMP1Endoplasmic reticulum metallopeptidase 1; Within the ovary, required for the organization of somatic cells and oocytes into discrete follicular structures. Belongs to the peptidase M28 family. (904 aa)
NPEPL1Probable aminopeptidase NPEPL1; Probably catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. (523 aa)
XPNPEP3Xaa-Pro aminopeptidase 3; Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position. (507 aa)
LVRNAminopeptidase 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)
NAALADL1Aminopeptidase NAALADL1; Aminopeptidase with broad substrate specificity. Has lower activity with substrates that have Asp or Glu in the P2' position, or Pro in the P3' position. Lacks activity with substrates that have both Pro in the P3' position and Asp or Glu in the P2' position. Lacks carboxypeptidase activity. Lacks dipeptidyl- peptidase IV type activity. Belongs to the peptidase M28 family. M28B subfamily. (740 aa)
CNDP1Carnosine dipeptidase 1; Belongs to the peptidase M20A family. (507 aa)
AGBL5Cytosolic carboxypeptidase-like protein 5; Metallocarboxypeptidase that mediates protein deglutamylation. Specifically catalyzes the deglutamylation of the branching point glutamate side chains generated by post-translational glutamylation in proteins such as tubulins. In contrast, it is not able to act as a long-chain deglutamylase that shortens long polyglutamate chains, a process catalyzed by AGTPBP1/CCP1, AGBL2/CCP2, AGBL3/CCP3, AGBL1/CCP4 and AGBL4/CCP6. Mediates deglutamylation of CGAS, regulating the antiviral activity of CGAS. (886 aa)
DPP4Dipeptidyl peptidase 4 membrane form; Cell surface glycoprotein receptor involved in the costimulatory signal essential for T-cell receptor (TCR)-mediated T- cell activation. Acts as a positive regulator of T-cell coactivation, by binding at least ADA, CAV1, IGF2R, and PTPRC. Its binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM), the mi [...] (766 aa)
MMP17Matrix metalloproteinase-17; Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin. (603 aa)
CPZCarboxypeptidase Z; Cleaves substrates with C-terminal arginine residues. Probably modulates the Wnt signaling pathway, by cleaving some undefined protein. May play a role in cleavage during prohormone processing. (652 aa)
MINDY1Ubiquitin carboxyl-terminal hydrolase MINDY-1; Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins. Has exodeubiquitinase activity and has a preference for long polyubiquitin chains. May play a regulatory role at the level of protein turnover; Belongs to the MINDY deubiquitinase family. FAM63 subfamily. (517 aa)
CPN1Carboxypeptidase N catalytic chain; Protects the body from potent vasoactive and inflammatory peptides containing C-terminal Arg or Lys (such as kinins or anaphylatoxins) which are released into the circulation. (458 aa)
XPNPEP2Xaa-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. (674 aa)
DPP7Dipeptidyl peptidase 2; Plays an important role in the degradation of some oligopeptides. (492 aa)
AGBL4Cytosolic carboxypeptidase 6; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes polyglutamates from the carboxy-terminus of target proteins such as MYLK. Mediates deglutamylation of CGAS, regulating the antiviral activity of CGAS. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. (503 aa)
CTSALysosomal protective protein 20 kDa chain; Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins. (498 aa)
ZMPSTE24CAAX prenyl protease 1 homolog; Proteolytically removes the C-terminal three residues of farnesylated proteins. Acts on lamin A/C. (475 aa)
AOPEPAminopeptidase O; 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)
TPP2Tripeptidyl-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). (1262 aa)
CPXM1Probable carboxypeptidase X1; May be involved in cell-cell interactions. No carboxypeptidase activity was found yet (By similarity). (734 aa)
DPEP1Dipeptidase 1; Hydrolyzes a wide range of dipeptides. Implicated in the renal metabolism of glutathione and its conjugates. Converts leukotriene D4 to leukotriene E4; it may play an important role in the regulation of leukotriene activity. (411 aa)
PRCPLysosomal Pro-X carboxypeptidase; Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH. (517 aa)
JMJD7Bifunctional peptidase and (3S)-lysyl hydroxylase JMJD7; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Additionally, may play a role in [...] (316 aa)
F11Coagulation factor XIa heavy chain; Factor XI triggers the middle phase of the intrinsic pathway of blood coagulation by activating factor IX. (625 aa)
CPECarboxypeptidase E; Sorting receptor that directs prohormones to the regulated secretory pathway. Acts also as a prohormone processing enzyme in neuro/endocrine cells, removing dibasic residues from the C-terminal end of peptide hormone precursors after initial endoprotease cleavage. Belongs to the peptidase M14 family. (476 aa)
CPVLProbable serine carboxypeptidase CPVL; May be involved in the digestion of phagocytosed particles in the lysosome, participation in an inflammatory protease cascade, and trimming of peptides for antigen presentation; Belongs to the peptidase S10 family. (476 aa)
SCRN1Secernin-1; Regulates exocytosis in mast cells. Increases both the extent of secretion and the sensitivity of mast cells to stimulation with calcium (By similarity). (434 aa)
ACE2Processed angiotensin-converting enzyme 2; Carboxypeptidase which converts angiotensin I to angiotensin 1-9, a peptide of unknown function, and angiotensin II to angiotensin 1-7, a vasodilator. Also able to hydrolyze apelin-13 and dynorphin-13 with high efficiency. By cleavage of angiotensin II, may be an important regulator of heart function. By cleavage of angiotensin II, may also have a protective role in acute lung injury (By similarity). Plays an important role in amino acid transport by acting as binding partner of amino acid transporter SL6A19 in intestine, regulating traffickin [...] (805 aa)
KDM8Bifunctional peptidase and arginyl-hydroxylase JMJD5; Bifunctional enzyme that acts both as an endopeptidase and 2- oxoglutarate-dependent monoxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-term [...] (454 aa)
ERAP2Endoplasmic 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)
AGBL1Cytosolic carboxypeptidase 4; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Acts as a long-chain deglutamylase and specifically shortens long polyglutamate chains, while it is not able to remove the branching point glutamate, a process catalyzed by AGBL5/CCP5. (1112 aa)
CPB1Carboxypeptidase B1; Belongs to the peptidase M14 family. (417 aa)
MMENeprilysin; Thermolysin-like specificity, but is almost confined on acting on polypeptides of up to 30 amino acids. Biologically important in the destruction of opioid peptides such as Met- and Leu-enkephalins by cleavage of a Gly-Phe bond. Able to cleave angiotensin-1, angiotensin-2 and angiotensin 1-9. Involved in the degradation of atrial natriuretic factor (ANF). Displays UV-inducible elastase activity toward skin preelastic and elastic fibers. Belongs to the peptidase M13 family. (750 aa)
CPA5Carboxypeptidase A5; Belongs to the peptidase M14 family. (436 aa)
XPNPEP1Xaa-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. (666 aa)
NUDT16U8 snoRNA-decapping enzyme; RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. Part of the U8 snoRNP complex that is required for the accumulation of mature 5.8S and 28S rRNA. Has diphosphatase activity and removes m7G and/or m227G caps from U8 snoRNA and leaves a 5'monophosphate on the RNA. Catalyzes also the cleavage of the cap structure on mRNAs. Does not hydrolyze cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG). Also hydrolysis m7G- and m227G U3-capped RNAs but with less [...] (227 aa)
VASH2Tubulinyl-Tyr carboxypeptidase 2; Tyrosine carboxypeptidase that removes the C-terminal tyrosine residue of alpha-tubulin, thereby regulating microtubule dynamics and function. Critical for spindle function and accurate chromosome segregation during mitosis since microtuble detyronisation regulates mitotic spindle length and postioning. Acts as an activator of angiogenesis: expressed in infiltrating mononuclear cells in the sprouting front to promote angiogenesis. Plays a role in axon formation. (355 aa)
DNPEPAspartyl aminopeptidase; Aminopeptidase with specificity towards an acidic amino acid at the N-terminus. Likely to play an important role in intracellular protein and peptide metabolism. (493 aa)
NAALAD2N-acetylated-alpha-linked acidic dipeptidase 2; Has N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Also exhibits a dipeptidyl-peptidase IV type activity. Inactivates the peptide neurotransmitter N-acetylaspartylglutamate. (740 aa)
AGBL2Cytosolic carboxypeptidase 2; Metallocarboxypeptidase that mediates deglutamylation of target proteins. Catalyzes the deglutamylation of polyglutamate side chains generated by post-translational polyglutamylation in proteins such as tubulins. Also removes gene-encoded polyglutamates from the carboxy-terminus of target proteins such as MYLK. Does not show detyrosinase or deglycylase activities from the carboxy-terminus of tubulin. (902 aa)
DPP3Dipeptidyl peptidase 3; Cleaves and degrades bioactive peptides, including angiotensin, Leu-enkephalin and Met-enkephalin. Also cleaves Arg-Arg-beta-naphthylamide (in vitro). (737 aa)
MINDY2Ubiquitin carboxyl-terminal hydrolase MINDY-2; Hydrolase that can remove 'Lys-48'-linked conjugated ubiquitin from proteins. Binds to polyubiquitin chains of different linkage types, including 'Lys-6', 'Lys-11', 'Lys- 29', 'Lys-33', 'Lys-48' and 'Lys-63'. May play a regulatory role at the level of protein turnover. (621 aa)
DPEP2Dipeptidase 2; Probable metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4). (486 aa)
DPEP3Dipeptidase 3; Probable metalloprotease which hydrolyzes cystinyl-bis- glycine. May be involved in meiosis (By similarity); Belongs to the metallo-dependent hydrolases superfamily. Peptidase M19 family. (513 aa)
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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