EC Number |
Recommended Name |
Localization |
GeneOntology No. |
Reference |
---|
3.4.24.11 | neprilysin |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
709805 |
3.4.24.13 | IgA-specific metalloendopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
755335 |
3.4.24.13 | IgA-specific metalloendopeptidase |
cell surface |
associated via an N-terminal membrane anchor, release upon proteolytic cleavage |
GO:0009986 AmiGO QuickGO |
666834 |
3.4.24.13 | IgA-specific metalloendopeptidase |
cell surface |
surface distribution of IgA1 protease on SS2 strain ZYS, overview |
GO:0009986 AmiGO QuickGO |
-, 754643 |
3.4.24.15 | thimet oligopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 752926 |
3.4.24.15 | thimet oligopeptidase |
cell surface |
secretion to the medium |
GO:0009986 AmiGO QuickGO |
683813 |
3.4.24.16 | neurolysin |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
683087 |
3.4.24.18 | meprin A |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
650462, 652104 |
3.4.24.23 | matrilysin |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
755514 |
3.4.24.23 | matrilysin |
cell surface |
extracellular MMP-7 binds to cell-surface cholesterol sulfate (CS) and acts as a membrane-associated protease |
GO:0009986 AmiGO QuickGO |
754150 |
3.4.24.23 | matrilysin |
cell surface |
syndecan-2 functions as a cell surface docking receptor for pro-MMP-7, overview |
GO:0009986 AmiGO QuickGO |
709073 |
3.4.24.23 | matrilysin |
cell surface |
the enzyme is secreted |
GO:0009986 AmiGO QuickGO |
717801 |
3.4.24.23 | matrilysin |
cell surface |
the MMP-7 Asp137 genetic variant is preferentially localized to the cell surface plasma membrane |
GO:0009986 AmiGO QuickGO |
708642 |
3.4.24.24 | gelatinase A |
cell surface |
besides MT-MMPs, which efficiently bind proMMP-2 to induce its activation, a limited number of cell-surface molecules have been shown to contribute to enhance proteolytic activity at the migrating front of invasive cells by clustering active MMP-2 at the cell membrane. Among them the heat shock protein HSP90a expressed at the surface of tumor cells promotes MMP-2 activity and tumor invasion by binding to the Hpx-like domain of MMP-2. The alphanybeta3 integrin is first identified as a binding site for the C-terminal Hpx-like domain of MMP-2 in studies investigating in vivo and in vitro interactions between angiogenic blood vessels and melanoma cells |
GO:0009986 AmiGO QuickGO |
752865 |
3.4.24.24 | gelatinase A |
cell surface |
complex formed by MT1-MMP, TIMP-2 |
GO:0009986 AmiGO QuickGO |
683846 |
3.4.24.34 | neutrophil collagenase |
cell surface |
binding of MMP-8 to the surface of polymorphonuclear cells promotes stability |
GO:0009986 AmiGO QuickGO |
669709 |
3.4.24.35 | gelatinase B |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 708445 |
3.4.24.36 | leishmanolysin |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 683079, 683418, 683897 |
3.4.24.36 | leishmanolysin |
cell surface |
about two-thirds of newly synthesized enzyme becomes surface localized, the rest of enzyme does not reach the cell surface. Surface-localized enzyme is released at different rates from logarithmic and stationary phase virulent promastigotes. Major mechanism regulating enzyme abundance is the rate of loss of surface-localized enzyme from promastigote surface |
GO:0009986 AmiGO QuickGO |
670182 |
3.4.24.36 | leishmanolysin |
cell surface |
GP63 is able to act on its substrate proteins within the nucleus of its host cell |
GO:0009986 AmiGO QuickGO |
718304 |
3.4.24.36 | leishmanolysin |
cell surface |
major surface protein |
GO:0009986 AmiGO QuickGO |
-, 31226 |
3.4.24.36 | leishmanolysin |
cell surface |
surface molecules are glycosylphosphatidylinositol-anchored |
GO:0009986 AmiGO QuickGO |
710519 |
3.4.24.36 | leishmanolysin |
cell surface |
two-third of MSPs in promastigotes is orientated along the cell surface, whereas most MSPs in amastigotes are localized in the flagellar pocket |
GO:0009986 AmiGO QuickGO |
-, 683857 |
3.4.24.56 | insulysin |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
683342, 710682 |
3.4.24.63 | meprin B |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 650462, 652104, 752709, 753172, 753218, 753321, 753536, 753697, 754028, 754236, 754779, 755294, 755466 |
3.4.24.71 | endothelin-converting enzyme 1 |
cell surface |
ECE-1 shedding from the surface of endothelial cells |
GO:0009986 AmiGO QuickGO |
683474 |
3.4.24.71 | endothelin-converting enzyme 1 |
cell surface |
isozyme ECE-1c |
GO:0009986 AmiGO QuickGO |
683435 |
3.4.24.79 | pappalysin-1 |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
735323 |
3.4.24.79 | pappalysin-1 |
cell surface |
detachment of pregnancy-associated plasma protein-A requires the formation of intermolecular proteinase-inhibitor disulfide bonds and glycosaminoglycan covalently bound to the inhibitor, mechanism, overview, the PAPP-A-proMBP complex is unable to bind to the cell surface |
GO:0009986 AmiGO QuickGO |
683645 |
3.4.24.79 | pappalysin-1 |
cell surface |
surface association of PAPP-A accounts for its colocalization with activated macrophages in human atherosclerotic plaque, immunohistochemic analysis, overview |
GO:0009986 AmiGO QuickGO |
683050 |
3.4.24.80 | membrane-type matrix metalloproteinase-1 |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
638809, 638810, 678111, 679042, 680921, 683787, 709058, 709415, 734409, 753242, 753773, 754158, 754175, 755435 |
3.4.24.80 | membrane-type matrix metalloproteinase-1 |
cell surface |
MT1-MMP forms a homophilic complex required for activity |
GO:0009986 AmiGO QuickGO |
717536 |
3.4.24.80 | membrane-type matrix metalloproteinase-1 |
cell surface |
MT1-MMP on cell surface rapidly turns over by auto-degradation or clathrin-dependent internalization. MT1-MMP inactivated by TIMP-2 avoids auto-degradation, and accumulates on the cell surface, overview |
GO:0009986 AmiGO QuickGO |
707998 |
3.4.24.81 | ADAM10 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
667528, 668181, 668305, 668372, 668407 |
3.4.24.82 | ADAMTS-4 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
669205, 697804 |
3.4.24.86 | ADAM 17 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
638989, 638994, 638995, 639003, 639006 |
3.4.24.86 | ADAM 17 endopeptidase |
cell surface |
most mature ADAM17 is localised intracellularly, with only a small amount at the cell surface |
GO:0009986 AmiGO QuickGO |
755446 |
3.4.24.87 | ADAMTS13 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
713561 |
3.4.24.87 | ADAMTS13 endopeptidase |
cell surface |
ADAMTS13 binds to endothelial cells in a specific, reversible, and time-dependent manner with a Kd of 58 nM. Binding requires the COOH-terminal thrombospondin type 1 repeats of the protease. Binding is inhibited in the presence of heparin and by trypsin treatment of the cells |
GO:0009986 AmiGO QuickGO |
712393 |
3.4.24.89 | Pro-Pro endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 754764 |
3.4.24.B10 | ADAM12 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
668997, 755025 |
3.4.24.B11 | ADAMTS1 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
697804 |
3.4.24.B12 | ADAMTS5 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
679600, 697804 |
3.4.24.B14 | neprilysin-2 |
cell surface |
human neprilysin-2-beta is either localized to the extracellular surface or secreted |
GO:0009986 AmiGO QuickGO |
733906 |
3.4.24.B28 | ADAM15 |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
735237 |
3.4.24.B9 | ADAM9 endopeptidase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
754597 |
3.5.1.19 | nicotinamidase |
cell surface |
surface location |
GO:0009986 AmiGO QuickGO |
246587 |
3.5.1.2 | glutaminase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 656204, 719119 |
3.5.1.2 | glutaminase |
cell surface |
of neutrophils, isozyme LGA |
GO:0009986 AmiGO QuickGO |
670391 |
3.5.1.24 | choloylglycine hydrolase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 752522 |
3.5.1.28 | N-acetylmuramoyl-L-alanine amidase |
cell surface |
LytA is a surface-exposed enzyme |
GO:0009986 AmiGO QuickGO |
656504 |
3.5.1.28 | N-acetylmuramoyl-L-alanine amidase |
cell surface |
recombinant PGRP-L shows primarily intracellular and cell surface location |
GO:0009986 AmiGO QuickGO |
656179 |
3.5.1.41 | chitin deacetylase |
cell surface |
at early parasite life cycle |
GO:0009986 AmiGO QuickGO |
668662 |
3.5.1.92 | pantetheine hydrolase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 734537 |
3.5.1.92 | pantetheine hydrolase |
cell surface |
a glycosylphosphatidylinositol (GPI)-anchored ectoenzyme |
GO:0009986 AmiGO QuickGO |
733009 |
3.5.1.92 | pantetheine hydrolase |
cell surface |
pantetheinase is an ectoenzyme that is attached to the outer plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. GPI anchors consist of three domains: a phosphoethanolamine linker that attaches to the C terminal end of the target protein, a conserved glycan core and a phospholipid tail for anchoring to the lipid membrane |
GO:0009986 AmiGO QuickGO |
-, 756537 |
3.5.2.6 | beta-lactamase |
cell surface |
the class A beta-lactamase BlaC is a cell surface expressed serine hydrolase |
GO:0009986 AmiGO QuickGO |
-, 756194 |
3.5.3.15 | protein-arginine deiminase |
cell surface |
90% of enzyme activity is cell surface associated |
GO:0009986 AmiGO QuickGO |
-, 733075 |
3.6.1.15 | nucleoside-triphosphate phosphatase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 756676, 758530 |
3.6.1.22 | NAD+ diphosphatase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
656433 |
3.6.1.5 | apyrase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 699181, 719597, 758530 |
3.6.1.5 | apyrase |
cell surface |
NTPDase8 is a cell surface ectonucleotidase with a large extracellular domain containing the active site and is anchored to the membrane by two transmembrane domains at the N- and C-termini |
GO:0009986 AmiGO QuickGO |
718863 |
3.6.1.5 | apyrase |
cell surface |
the enzyme contains two transmembrane domains and five apyrase conserved regions, ACRs. ACR1 is located near the N-terminal transmembrane domain, whereas ACR5 is located near the C-terminal transmembrane domain |
GO:0009986 AmiGO QuickGO |
695854 |
3.6.1.9 | nucleotide diphosphatase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
711034, 720186 |
3.6.5.2 | small monomeric GTPase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
756101 |
3.6.5.5 | dynamin GTPase |
cell surface |
dynamin-1 |
GO:0009986 AmiGO QuickGO |
669580 |
3.6.5.5 | dynamin GTPase |
cell surface |
dynamin-2 |
GO:0009986 AmiGO QuickGO |
669580 |
4.1.2.13 | fructose-bisphosphate aldolase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 727893, 747043, 747971, 748619 |
4.1.2.13 | fructose-bisphosphate aldolase |
cell surface |
surface-exposed enzyme |
GO:0009986 AmiGO QuickGO |
748619 |
4.2.1.1 | carbonic anhydrase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
666801 |
4.2.1.1 | carbonic anhydrase |
cell surface |
murine sperm possesses extracellular isozyme CA IV that is transferred to the sperm surface as the sperm pass through the epididymis, the transfer takes place in the corpus epididymidis |
GO:0009986 AmiGO QuickGO |
-, 716685 |
4.2.1.11 | phosphopyruvate hydratase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 651496, 666252, 696424, 698247, 704073, 704963, 705569, 706933, 715161, 730857 |
4.2.1.11 | phosphopyruvate hydratase |
cell surface |
associated to the external surface of the parasite |
GO:0009986 AmiGO QuickGO |
714875 |
4.2.1.11 | phosphopyruvate hydratase |
cell surface |
putative ENOA translocation mechanism, overview |
GO:0009986 AmiGO QuickGO |
714970 |
4.2.1.11 | phosphopyruvate hydratase |
cell surface |
secreted enzyme associated to the external surface of the parasite |
GO:0009986 AmiGO QuickGO |
714875 |
4.2.2.1 | hyaluronate lyase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
664708, 666077, 680874 |
4.4.1.3 | dimethylpropiothetin dethiomethylase |
cell surface |
extracellular |
GO:0009986 AmiGO QuickGO |
-, 34604 |
5.2.1.8 | peptidylprolyl isomerase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
680130 |
5.2.1.8 | peptidylprolyl isomerase |
cell surface |
enzymes EF0685 and EF1534 |
GO:0009986 AmiGO QuickGO |
727618 |
5.3.1.1 | triose-phosphate isomerase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
-, 705563, 747934 |
5.3.4.1 | protein disulfide-isomerase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
679122, 679424, 679678, 706459, 727573, 728220, 747835, 747836 |
5.6.1.6 | channel-conductance-controlling ATPase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
734398 |
6.1.1.17 | glutamate-tRNA ligase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
675229 |
6.1.1.2 | tryptophan-tRNA ligase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
745941 |
6.1.1.6 | lysine-tRNA ligase |
cell surface |
the enzyme is exposed on the surface of stressed cells, on which it co-localized with calreticulin in lipid rafts |
GO:0009986 AmiGO QuickGO |
714671 |
7.1.2.2 | H+-transporting two-sector ATPase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
686272, 695945, 711983 |
7.1.2.2 | H+-transporting two-sector ATPase |
cell surface |
the ectopic expression of ATP synthase is a consequence of translocation from the mitochondria |
GO:0009986 AmiGO QuickGO |
718469 |
7.2.2.12 | P-type Zn2+ transporter |
cell surface |
lipoprotein, detected by antibodies |
GO:0009986 AmiGO QuickGO |
210345 |
7.2.2.19 | H+/K+-exchanging ATPase |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
687724 |
7.4.2.1 | ABC-type polar-amino-acid transporter |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
718559 |
7.4.2.14 | ABC-type antigen peptide transporter |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
761023 |
7.4.2.6 | ABC-type oligopeptide transporter |
cell surface |
- |
GO:0009986 AmiGO QuickGO |
734416 |
7.4.2.6 | ABC-type oligopeptide transporter |
cell surface |
more than 80% of the surface-localised ATPase activity of Mycoplasma hominis is derived from OppA, implicating that OppA is the main ATPase on the surface of mycoplasma cells |
GO:0009986 AmiGO QuickGO |
685829 |
7.4.2.6 | ABC-type oligopeptide transporter |
cell surface |
substrate binding protein OppA of the permease complex |
GO:0009986 AmiGO QuickGO |
655869 |
7.4.2.7 | ABC-type alpha-factor-pheromone transporter |
cell surface |
enzyme variant with a deletion in the linker region |
GO:0009986 AmiGO QuickGO |
670202 |
7.6.2.1 | P-type phospholipid transporter |
cell surface |
AP-1 is required, and GGA proteins, Golgi localized, gamma-ear containing, Arf-binding proteins acting as chlatrin adaptos, are dispensable, for efficient exclusion of Drs2p from exocytic vesicles targeted to the plasma membrane |
GO:0009986 AmiGO QuickGO |
688911 |
7.6.2.2 | ABC-type xenobiotic transporter |
cell surface |
of tumor cells |
GO:0009986 AmiGO QuickGO |
696241 |