3.4.21.79: granzyme B
This is an abbreviated version!
For detailed information about granzyme B, go to the full flat file.
Word Map on EC 3.4.21.79
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3.4.21.79
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perforin
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t-cells
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cd8
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cytolytic
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immunotherapy
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vaccine
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lymphoma
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rejection
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tnf
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dendritic
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cell-mediated
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ifn-gamma
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allograft
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tregs
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tia-1
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fasl
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foxp3
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autologous
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interferon-gamma
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caspases
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degranulation
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allogeneic
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epstein-barr
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antigen-specific
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virus-specific
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immunophenotype
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ctla-4
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anti-cd3
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tumor-infiltrating
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nk-cell
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extranodal
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elispot
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synthesis
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eomes
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graft-versus-leukemia
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cd45ro
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alcls
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biotechnology
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death-1
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analysis
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intragraft
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lag-3
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hiv-specific
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medicine
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diagnostics
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degradation
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alloreactive
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lymphocyte-mediated
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lymphokine-activated
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crma
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b-mediated
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pharmacology
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ag-specific
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banff
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hepatosplenic
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anti-pd-1
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interleukin-15
- 3.4.21.79
- perforin
- t-cells
- cd8
-
cytolytic
-
immunotherapy
- vaccine
- lymphoma
-
rejection
- tnf
- dendritic
-
cell-mediated
- ifn-gamma
-
allograft
-
tregs
- tia-1
- fasl
- foxp3
-
autologous
- interferon-gamma
-
caspases
-
degranulation
-
allogeneic
-
epstein-barr
-
antigen-specific
-
virus-specific
-
immunophenotype
-
ctla-4
-
anti-cd3
-
tumor-infiltrating
-
nk-cell
-
extranodal
-
elispot
- synthesis
-
eomes
-
graft-versus-leukemia
-
cd45ro
-
alcls
- biotechnology
-
death-1
- analysis
-
intragraft
- lag-3
-
hiv-specific
- medicine
- diagnostics
- degradation
-
alloreactive
-
lymphocyte-mediated
-
lymphokine-activated
- crma
-
b-mediated
- pharmacology
-
ag-specific
-
banff
-
hepatosplenic
-
anti-pd-1
- interleukin-15
Reaction
preferential cleavage: -Asp-/- >> -Asn-/- > -Met-/-, -Ser-/- =
Synonyms
Asp-ase, C11, CCP1, CCPII, CTLA1, CTSGL1, Cytotoxic cell proteinase-1, cytotoxic lymphocyte-associated protease, cytotoxic lymphocyte-specific protein, cytotoxic serine protease granzyme B, cytotoxic T-lymphocyte-associated gene transcript-1, gB, Gra-b, granzyme B, Granzyme G, Granzyme H, GrB, GrzmB, GzB, Gzm, Gzm B, GzmB, GzmB-like enzyme, GzmH, HLp, Human lymphocyte protein, Lymphocyte protease, natural killer cell protease 1, pro-apoptotic serine protease, proGrB, Proteinase, CCP1, rat grB[N66Q], SECT, T-cell serine protease 1-3E
ECTree
3.4.21.79 granzyme BAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 3.4.21.79 - granzyme B
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminobenzoyl-IEPDSSMESK-dinitrophenyl + H2O
?
-
susbtrate is specific for human GrB
-
-
?
Ace-Ile-Glu-Pro-Asp-p-nitroanilide + H2O
Ace-Ile-Glu-Pro-Asp + p-nitroaniline
-
-
-
-
?
acetyl-DEVD-7-amido-4-methylcoumarin + H2O
?
-
efficient cleavage by GzmB after K562 cells are exposed to sublytic perforin or streptolysin O. GzmH shows only baseline readings
-
-
?
acetyl-IAPD-7-amido-4-methylcoumarin + H2O
acetyl-IAPD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-IEFD-7-amido-4-methylcoumarin + H2O
acetyl-IEFD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-IEPD-7-amido-4-methylcoumarin + H2O
acetyl-IEPD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-IKPD-7-amido-4-methylcoumarin + H2O
acetyl-IKPD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-LEFD-7-amido-4-methylcoumarin + H2O
acetyl-LEFD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-LEPD-7-amido-4-methylcoumarin + H2O
acetyl-LEPD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-YVAD-4-nitroanilide + H2O
acetyl-YVAD + 4-nitroaniline
-
an asp-ase substrate
-
-
?
acetylcholine receptor
?
-
granzyme B efficiently and specifically cleaves alpha and epsilon subunits of acetylcholine receptor, especially the epsilon subunit
-
-
?
acetylcholine receptor + H2O
?
-
extracellular GrB substrate. Implication: cleavage results in a reduction of the receptor in neuromuscular junctions and yields an autoantigenic fragment
-
-
?
adenovirus DNA-binding protein + H2O
?
-
gzmB and gzmH. Direct cleavage of DNA-binding protein by gzmH is a critical component of the cytotoxic antiviral response against adenovirus, which slows down DNA viral replication. Cleaved by gzmH at multiple sites, most efficient cleavage at Met118, when this site is mutated, gzmH instead cleaves at Phe121
-
-
?
aggrecan + H2O
?
-
extracellular GrB substrate. Implication: Disruption of structural integrity in cartilage
-
-
?
AHNAK + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: calcium signalling, associated disease: systemic lupus erythematosus
-
-
?
alanyl tRNA synthetase + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: translation, associated disease: myositis
-
-
?
alpha-fodrin + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: cytoskeletal protein, associated disease: Sjörgen's syndrome
-
-
?
alpha-tubulin + H2O
truncated alpha-tubulin
-
alpha-tubulin derived from HeLa S100 extracts or Jurkat S100 extracts is cleaved by grB in a caspase-independent manner. Cleavage occurs at D438. Polymerized and soluble alpha-tubulin can be cleaved
-
-
?
ATSY-7-amido-4-methylcoumarin + H2O
ATSY + 7-amino-4-methylcoumarin
-
GzmH
-
-
?
Bcl-2-associated athano gene-1 + H2O
?
-
GrB proteolysis is independent of caspase activity
-
-
?
BCL2/adenovirus E1B 19 kDa protein-interacting protein 2 + H2O
?
-
generated with similar efficiency by mouse and human recombinant granzyme B
-
-
?
BCL2/adenovirus E1B 19-kDa protein-interacting protein 2 + H2O
?
-
generated with similar efficiency by mouse and human recombinant granzyme B
-
-
?
beta-actin + H2O
?
-
GrB cleavage fragments of beta-actin are detected in medullary carcinoma of the breast tumor lysates, suggesting that CTL-mediated death of medullary carcinoma of the breast tumor cells and actin redistribution may have a function in the generation of autoimmunity to beta-actin
-
-
?
cartilage proteoglycans + H2O
?
-
extracellular GrB substrate. Implication: Disruption of structural integrity in cartilage
-
-
?
caspase-8 + H2O
?
-
cleaves human caspase-8 but fails to cleave the mouse counterpart of caspase-8. Mouse caspase-8 is processed only upon addition of cytochrome c and dATP to J774 extracts to activate the apoptosome pathway to caspase activation
-
-
?
centromere protein B + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: mitosis, associated disease: Scleroderma
-
-
?
centromere protein C + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: mitosis, associated disease: Scleroderma
-
-
?
chromodomain helicase DNA binding 4 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: gene expression, associated disease: myositis
-
-
?
DNA binding protein + H2O
?
-
granzyme B and granzyme H (cleavage at Met118 and Phe121)
-
-
?
DNA-PK catalytic subunit + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: DNA repair, associated disease: myositis
-
-
?
FGFR1 + H2O
?
-
extracellular GrB substrate. Implication: cleavage activates pro-cell death functions as well as inactivates pro-growth signals
-
-
?
glutamate receptor subunit 3 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: Glutamate receptor, associated disease: Rasmussen's encephalitis
-
-
?
hepatitis antigen lamin B + H2O
?
-
cleavage of autoimmune hepatitis antigen lamin B by GrA and B causes disruption of the nuclear lamina, by uncoupling lamin B from its nuclear localisation signal
-
-
?
histidyl tRNA synthetase + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: translation, associated disease: myositis
-
-
?
Hsc70/Hsp70-interacting protein + H2O
?
-
Hsc70/Hsp70-interacting protein is cleaved at both GrB cleavage sites (at sequences IEPD92-TD and INPD180-SA) during NK-mediated cell death in a caspase-independent manner. Hsc70/Hsp70-interacting protein is a substrate unique to GrB
-
-
?
Hsp90 + H2O
?
-
is proteolyzed at multiple sites by GrB. Cleavage at sequences IDED693-EV and INPD631-PI in Hsp90beta. Cleavage at sequences IDED701-DP, INPD639-HS and VRTD175-TG in Hsp90alpha
-
-
?
human endogenous retrovirus K-10 gag + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: endogenous retrovirus, associated disease: systemic lupus erythematosus
-
-
?
ICAD + H2O
?
-
cleaves human ICAD but fails to cleave the mouse counterpart
-
-
?
inhibitor of caspase-activated DNase + H2O
caspase-activated DNase
-
cleaved in a dose-dependent fashion
-
-
?
interleukin IL-1alpha + H2O
?
-
cleavage after the motif IAND103, no substrate for caspases -1, -3, -4, -5, and -7
granzyme B-mediated processing of IL-1alpha potently enhances the biological activity
-
?
interleukin proIL-18 + H2O
interleukin IL-18 + ?
-
-
cleavage at residues D35-Y36 of proIL-18, identical to cleavage site of caspase-1
-
?
Ki-67 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: proliferation, associated disease: myositis
-
-
?
Ku-70 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: DNA repair, associated disease: myositis
-
-
?
La protein + H2O
?
-
La is cleaved by gzmB and gzmH. La is a direct target of gzmH during cytotoxic-mediated cell death. Cleavage of La by gzmH occurs at Phe-364 (P(1) site) and generates a COOH-terminal truncated form of La that loses nuclear localization and decreases hepatitis C virus-internal ribosome entry site-mediated translational activity
-
-
?
Laminin + H2O
?
-
extracellular GrB substrate. Implication: cell adhesion, anoikis
-
-
?
neuronal glutamate receptor + H2O
?
-
extracellular GrB substrate. Implication: GrB cleaves the non-glycosylated form of the receptor into an autoantigenic fragment
-
-
?
nuclear mitotic apparatus protein 1 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: mitosis, associated disease: Sjörgen's syndrome
-
-
?
nucleolus organizing region 90 kDa (NOR-90/UBF) + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: transcription factor, associated disease: Scleroderma
-
-
?
nucleophosmin (B23) + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: rRNA processing, associated disease: Scleroderma
-
-
?
nucleophosmin + H2O
?
-
efficiently cleaves nucleophosmin of human origin, does not cleave nucleophosmin within J774 cell free extracts
-
-
?
PEG-P + H2O
?
-
virtually all soluble PEG-P is cleaved in 3 min, suggesting PEG-P is a sensitive indicator of granzyme B activity. The granzyme can not access PEG-P when encapsulated in 1,2-dioleoyl-sn-glycero-3-phosphocholine large unilamellar vesicles
-
-
?
plasmin + H2O
?
-
extracellular GrB substrate. Implication: as plasmin is pro-angiogenic, cleavage results in the reduction of angiogenesis
-
-
?
plasminogen + H2O
?
-
extracellular GrB substrate. Implication: cleavage yields angiostatin, which is anti-angiogenic. Implications in angiogenesis
-
-
?
PMScl/EXOSC10 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: mRNA degradation, associated disease: myositis/Scleroderma
-
-
?
poly(ADP)ribose polymerase 1 (PARP1) + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: ribosylation, associated disease: systemic lupus erythematosus
-
-
?
postmeiotic segregation 1 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: DNA mismatch repair, associated disease: myositis
-
-
?
postmeiotic segregation 2 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: DNA mismatch repair, associated disease: myositis
-
-
?
pro-CPP32 + H2O
?
-
processes the caspase into its enzymatically active form
-
?
Protease CMH-1 + H2O
?
-
a close homologue of CPP32, granzyme B specifically cleaves at Asp198-Ser199 between the p20 and p12 and activates the cysteine protease
-
-
?
PTSY-7-amido-4-methylcoumarin + H2O
PTSY + 7-amino-4-methylcoumarin
-
GzmH
-
-
?
pyruvate dehydrogenase complex E2 (PDC-E2) + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: acetyl CoA synthesis, associated disease: primary biliary cirrhosis
-
-
?
RNA polymerase I + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: transcription, associated disease: Scleroderma
-
-
?
RNA polymerase II + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: transcription, associated disease: Scleroderma
-
-
?
signal recognition particle 72 kDa + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: translation, associated disease: myositis, systemic lupus erythematosus
-
-
?
smooth muscle cell matrix + H2O
?
-
extracellular GrB substrate. Implication: cell adhesion, anoikis
-
-
?
topoisomerase 1 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: transcription, associated disease: Scleroderma
-
-
?
transaldolase + H2O
?
-
specifically cleaved by human GrB. The recognition site is a VVAD motif at aa residue 27
the major C-terminal GrB cleavage product of transaldolase, residues 28-337, has no enzymatic activity but retains the antigenicity of full-length transaldolase, effectively stimulating the proliferation and cytotoxic lymphocyte activity of peripheral blood mononuclear cells and of CD8+ T cell lines from patients with multiple sclerosis. Sera of multiple sclerosis patients exhibit similar binding affinity to wild-type and GrB-cleaved transaldolase
-
?
U1 small nuclear ribonucleoprotein 70 kDa + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: RNA processing, associated disease: systemic lupus erythematosus, Scleroderma, myositis
-
-
?
ubiquitin fusion degradation 2 + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: ubiquitination, associated disease: Scleroderma
-
-
?
acetyl-IEPD-4-nitroanilide + H2O
acetyl-IEPD + 4-nitroaniline
an asp-ase substrate, high activity
-
-
?
acetyl-IEPD-4-nitroanilide + H2O
acetyl-IEPD + 4-nitroaniline
-
an asp-ase substrate
-
-
?
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
-
-
-
?
acetyl-IETD-7-amido-4-methylcoumarin + H2O
acetyl-IETD + 7-amino-4-methylcoumarin
-
-
-
?
acetyl-Ile-Glu-Pro-Asp-4-nitroanilide + H2O
acetyl-Ile-Glu-Pro-Asp + 4-nitroaniline
-
-
-
?
acetyl-Ile-Glu-Pro-Asp-4-nitroanilide + H2O
acetyl-Ile-Glu-Pro-Asp + 4-nitroaniline
-
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
an asp-ase substrate, low activity
-
-
?
acetyl-VEID-4-nitroanilide + H2O
acetyl-VEID + 4-nitroaniline
-
an asp-ase substrate
-
-
?
beta-glycan + H2O
?
100 kDa protein, cleavage by the enzyme into fragments of about 60 kDa and 40 kDa
-
-
?
BID + H2O
truncated BID + ?
-
both human and mouse BID are cleaved efficiently
-
-
?
BID + H2O
truncated BID + ?
-
efficient cleavage of mouse and human Bid by human granzyme B
-
-
?
biglycan + H2O
?
40 kDa protein, cleavage by the enzyme into fragments of about 30 kDa and 20 kDa
-
-
?
ClpX unfoldase + H2O
?
Escherichia coli N-terminal GST-tagged 37kDa ClpX. Human GzmB is predicted to cut ClpX after Asp144, in the AAA domain and interfere with its unfolding activity
-
-
?
decorin + H2O
?
65 kDa protein, cleavage by the enzyme into fragments of about 50 kDa and 30 kDa
-
-
?
DNA-PKcs + H2O
?
-
directly and efficiently cleaved in vitro and in vivo, abolishes kinase activity
-
?
DNA-PKcs + H2O
?
-
directly and efficiently cleaved in vitro and in vivo, abolishes kinase activity
-
?
fibrillarin + H2O
?
-
autoantigen cleaved by granzyme B, function of substrate: rRNA processing, associated disease: Scleroderma
-
-
?
Fibrinogen + H2O
?
-
granzyme B is unable to cleave soluble fibrinogen, granzyme B cleaves the matrix form at several sites
-
-
?
Fibrinogen + H2O
?
-
extracellular GrB substrate. Implication: matrix form of fibrinogen is cleaved. The uncleaved protein is responsible for platelet adhesion and thrombus growth. Cleavage results in anti-thrombosis implications
-
-
?
Fibronectin + H2O
?
-
extracellular GrB substrate. Implication: cell adhesion, migration, and anoikis
-
-
?
Hsp70/Hsp90-organizing protein + H2O
?
-
directly cleaved at Asp186 in vitro and in cells undergoing GzmB-induced death. Processing by GzmB is caspase-independent. Cleavage by GzmB destroys known functions of Hsp70/Hsp90-organizing protein in Hsp binding and hormone receptor assembly
-
-
?
LEADKGKLEYD + H2O
LEAD + KGKLEYD
-
is a far better substrate for mouse granzyme B as compared with human granzyme B
-
-
?
LEADKGKLEYD + H2O
LEAD + KGKLEYD
-
is a far better substrate for mouse granzyme B as compared with human granzyme B
-
-
?
Nalpha-tert-Butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester + H2O
?
-
-
-
-
?
Nalpha-tert-Butyloxycarbonyl-Ala-Ala-Met thiobenzyl ester + H2O
?
-
-
-
-
?
Nalpha-tert-Butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl ester + H2O
?
-
-
-
-
?
Nalpha-tert-Butyloxycarbonyl-L-Ala-L-Ala-L-Asp thiobenzyl ester + H2O
?
-
-
-
-
?
Notch1 + H2O
?
-
extracellular GrB substrate. Implication: cleavage results in cell signaling affecting tumor survival and antiviral activities
-
-
?
Notch1 + H2O
?
-
transmembrane receptor, Notch1 is a direct and caspase-independent substrate. GrB cleaves the intracellular Notch1 domain at least twice, at residues D1860 and D1961. GrB cleavage of Notch1 can occur in all subcellular compartments, during maturation of the receptor, at the membrane, and in the nucleus. GrB also displays perforin-independent functions by cleaving the extracellular domain of Notch1
cleavage of Notch1 by GrB results in a loss of transcriptional activity, independent of Notch1 activation. GrB disables Notch1 function, probably resulting in anti-cellular proliferation and cell death signals
-
?
peptidylarginine deiminase 4 + H2O
PAD4 peptides
-
GrB cleaves PAD4 exclusively at D388
-
-
?
peptidylarginine deiminase 4 + H2O
PAD4 peptides
-
PAD4, is cleaved by GrB at a single site, aspartic acid 388 (D388). Dynamic changes occur in the PAD4 structure induced by GrB cleavage. Recombinant N-terminal 6xHis tagged PAD4 (NP_036519) is expressed and purified from Escherichia coli BL21(DE3)pLysS competent cells
-
-
?
polypyrimidine tract-binding protein + H2O
?
-
2times more efficiently cleaved by mouse versus human recombinant granzyme B
-
-
?
polypyrimidine tract-binding protein + H2O
?
-
2times more efficiently cleaved by mouse versus human recombinant granzyme B
-
-
?
pro-caspase-3 + H2O
?
-
activates caspase-3, whether of human or murine origin, with a similar efficiency
-
-
?
pro-caspase-3 + H2O
?
-
activates caspase-3, whether of human or murine origin, with a similar efficiency
-
-
?
pro-caspase-3 + H2O
caspase-3 + ?
-
cleaves human pro-caspase-3 generating a 21-kDa and a 17-kDa fragment (autocatalytic removal of the caspase-3 prodomain)
-
-
?
pro-caspase-3 + H2O
caspase-3 + ?
-
cleaves human pro-caspase-3 but only generates a 21-kDa fragment, no autocatalytic removal of the caspase-3 prodomain. Efficiently cleaves and activates mouse procaspase-3, producing predominantly the 17-kDa fragment
-
-
?
pro-caspase-7 + H2O
?
-
activates caspase-7, whether of human or murine origin, with a similar efficiency
-
-
?
pro-caspase-7 + H2O
?
-
activates caspase-7, whether of human or murine origin, with a similar efficiency
-
-
?
pro-mCASP-3 + H2O
caspase-3 + ?
-
activational cleavage of the caspase proform
-
?
pro-mCASP-7 + H2O
caspase-7 + ?
-
activational cleavage of the caspase proform
-
?
Protease CPP32 + H2O
?
-
CPP32 is the precursor of the protease responsible for cleavage of poly(ADPribose)polymerase
-
-
?
Protease CPP32 + H2O
?
-
granzyme B activates CPP32, which is now able to bind inhibitors and cleave the substrate poly(ADPribose)polymerase whose proteolysis is a marker of apoptosis initiated by several other stimuli
-
-
?
Vitronectin + H2O
?
-
Grb expressed in human bladder cancer cell lines 1512 and RT112 cleave vitronectin
-
-
?
Vitronectin + H2O
?
-
extracellular GrB substrate. Implication: GrB cleavage site in integrin-binding domain, implications in cell adhesion, migration, and anoikis
-
-
?
von Willebrand factor + H2O
?
-
granzyme B delays ristocetin-induced platelet aggregation and inhibits platelet adhesion and spreading on immobilized von Willebrand factor under static conditions. In vitro, granzyme B cannot cleave the von Willebrand factor conformer in solution, but cleavage is induced when von Willebrand factor is artificially unfolded or presented as a matrix. Granzyme B cleaves von Willebrand factor with comparable efficiency to proteinase ADAMTS-13 and rapidly processes ultra-large von Willebrand factor multimers released from activated endothelial cells under physiological shear. Granzyme B cleaves the A1 and A3 domains of von Willebrand factor
-
-
?
von Willebrand factor + H2O
?
-
extracellular GrB substrate. Implication: GrB cleavage site in the domain of platelet interaction, prevention/delay of thrombosis
-
-
?
additional information
?
-
no activity with succinyl-Gly-Gly-Phe-4-nitroanilide
-
-
?
additional information
?
-
-
no activity with succinyl-Gly-Gly-Phe-4-nitroanilide
-
-
?
additional information
?
-
no activity with succinyl-Gly-Gly-Phe-4-nitroanilide
-
-
?
additional information
?
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preference for substrates with Glu or Asp as the residue amino-terminal to the scissile bond, little or no activity with oligopeptide substrates for trypsin-like, chymotrypsin-like, and elastase-like proteases
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additional information
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preference for substrates with Glu or Asp as the residue amino-terminal to the scissile bond, little or no activity with oligopeptide substrates for trypsin-like, chymotrypsin-like, and elastase-like proteases
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induces DNA degradation and apoptosis of cells
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requirement for aspartic acid in the substrate P1 position
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requirement for aspartic acid in the substrate P1 position
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additional information
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plays an essential role in cytotoxic T-lymphocyte-mediated cell killing
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additional information
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the enzyme cleaves and activates CPP32, the precursor of the protease responsible for cleavage of poly(ADPribose)polymerase
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additional information
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participates in target cell death inflicted by cytotoxic lymphocytes
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induces apoptosis of abnormal cells by cleaving intracellular proteins
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protects the organism against intracellular infections and cellular transformation, implicated in the generation of tissue damage in a variety of chronic conditions, including autoimmunity and transplant rejection
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triggers apoptosis in target cells by activating the caspase pathway, implicated in the etiology of rheumatoid arthritis
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triggers apoptosis in target cells by activating the caspase pathway, implicated in the etiology of rheumatoid arthritis <6>
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additional information
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after prolonged incubation, enzyme causes pronounced morphological changes in human tumor cells, leading to partial loss of contact to the culture support
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compared with granzyme B, granzyme A is minor effector of target cell lysis by natural killer cells
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caspases 2, 3 and 7 (C285A mutants) and purified BID are not directly cleaved by GzmH. No activity of GzmH toward Ac-LEHD-7-amino-4-methylcouramin
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granzyme H does not cleave BID or inhibitor of caspase-activated death, does not activate caspases
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granzyme B does not bind membrane phospholipids nor has intrinsic membranolytic properties
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granzyme B has no effect on platelet adhesion and spreading on immobilized collagen. Granzyme B does not cleave glycocalicin (extracellular domain of GPIbalpha)
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mediates cleavage at Asn36 (neo-N terminus: LALLEEIEAENR) in the mouse and at Asp37 (neo-N terminus: LALMEEMEAEHR) in the human DNA polymerase delta catalytic subunit
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tetrapeptide substrate specificity of human GrB: In addition to the requirement for aspartic acid in the P1 position, P4 is specific for Ile, Val, and Leu, whereas P3 and P2 are able to accommodate a wider range of amino acids
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the GrB cleavage sites defined within autoantigens reveal several features: first, all have Ile, Leu, or Val in P4 and are cleaved after the P1 aspartic acid. Second, amino acids in the P2 and P3 positions in autoantigens are almost universally favored by human GrB, but not tolerated by caspases (e.g. proline in P2)
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the enzyme cleaves exracellular matrix proteins, release of active TGF-beta1
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granzyme B cleaves a highly conserved set of proteins in all three bacteria, i.e. Escherichia coli, Listeria monocytogenes, and Mycobacteria tuberculosis, which function in vital biosynthetic and metabolic pathways that are critical for bacterial survival under diverse environmental conditions. Key proteins required for protein synthesis, folding and degradation are also substrates, including multiple aminoacyl-tRNA synthetases, ribosomal proteins, protein chaperones and the Clp system. GzmB cleaves core metabolic enzymes and disrupts protein synthesis globally. GzmB disrupts Escherichia coli ribosomes (crude ribosomal fraction or purified 70S, 50S and 30S subunits) by cleaving ribosome proteins. GzmB cleaves and inactivates aminoacyl tRNA synthetases. And GzmB disrupts bacterial protein folding and removal of misfolded proteins. Substrate specificity and metabolic effect of granzyme B, overview
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additional information
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granzyme B cleaves a highly conserved set of proteins in all three bacteria, i.e. Escherichia coli, Listeria monocytogenes, and Mycobacteria tuberculosis, which function in vital biosynthetic and metabolic pathways that are critical for bacterial survival under diverse environmental conditions. Key proteins required for protein synthesis, folding and degradation are also substrates, including multiple aminoacyl-tRNA synthetases, ribosomal proteins, protein chaperones and the Clp system. GzmB cleaves core metabolic enzymes and disrupts protein synthesis globally. GzmB disrupts Escherichia coli ribosomes (crude ribosomal fraction or purified 70S, 50S and 30S subunits) by cleaving ribosome proteins. GzmB cleaves and inactivates aminoacyl tRNA synthetases. And GzmB disrupts bacterial protein folding and removal of misfolded proteins. Substrate specificity and metabolic effect of granzyme B, overview
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many autoantigens are substrates for the protease granzyme B
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granzyme B (GzmB) is an asp-ase. Granzyme B is a hematopoietic serine protease, which cleaves after negatively charged amino acids. Cleavage specificity analysis using chromogenic and recombinant substrates. Comparisons of GzmB consensus sequences, overview
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additional information
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granzyme B (GzmB) is an asp-ase. Granzyme B is a hematopoietic serine protease, which cleaves after negatively charged amino acids. Cleavage specificity analysis using chromogenic and recombinant substrates. Comparisons of GzmB consensus sequences, overview
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additional information
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human GzmB cleaves only two of the three asp-ase substrates (no activity with acetyl-YVAD-4-nitroanilide) and not the chymase substrate succinyl-AAPF-4-nitroanilide or the two elastase substrates, succinyl-AAPV-4-nitroanilide and succinyl-AAPA-4-nitroanilide. This indicates a broader specificity against different asp-ase substrates for the opossum GzmB compared to human GzmB. Also no activity of the oppossum GznB with N-(tert-butoxycarbonyl)-VLGR-4-nitroanilide (a tryptase substrate), N-benzyloxycarbonyl-GPR-4-nitroanilide (a tryptase substrate), succinyl-AAPI-4-nitroanilide (an elastase substrate), succinyl-AAPL-4-nitroanilide, and succinyl-LLVY-4-nitroanilide (a chymase substrate). Both opossum and human GzmB prefer the rat GzmB consensus sequence. The rat GzmB consensus sequence contains two negatively charged amino acids in the P1 and P3 positions of the substrate. The cleavage of these substrates results in two clearly separated smaller bands, indicating cleavage only at one site in the middle of the linker sequence. Human GzmB cleaves the human substrate sequence (LIGAD-VLVQ) almost as efficiently as the rat GzmB consensus (LIETD-SGL)
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additional information
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human GzmB cleaves only two of the three asp-ase substrates (no activity with acetyl-YVAD-4-nitroanilide) and not the chymase substrate succinyl-AAPF-4-nitroanilide or the two elastase substrates, succinyl-AAPV-4-nitroanilide and succinyl-AAPA-4-nitroanilide. This indicates a broader specificity against different asp-ase substrates for the opossum GzmB compared to human GzmB. Also no activity of the oppossum GznB with N-(tert-butoxycarbonyl)-VLGR-4-nitroanilide (a tryptase substrate), N-benzyloxycarbonyl-GPR-4-nitroanilide (a tryptase substrate), succinyl-AAPI-4-nitroanilide (an elastase substrate), succinyl-AAPL-4-nitroanilide, and succinyl-LLVY-4-nitroanilide (a chymase substrate). Both opossum and human GzmB prefer the rat GzmB consensus sequence. The rat GzmB consensus sequence contains two negatively charged amino acids in the P1 and P3 positions of the substrate. The cleavage of these substrates results in two clearly separated smaller bands, indicating cleavage only at one site in the middle of the linker sequence. Human GzmB cleaves the human substrate sequence (LIGAD-VLVQ) almost as efficiently as the rat GzmB consensus (LIETD-SGL)
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no activity with Escherichia coli ClpB protein
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additional information
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no activity with Escherichia coli ClpB protein
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additional information
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granzyme B (GzmB) is an asp-ase. Granzyme B is a hematopoietic serine protease, which cleaves after negatively charged amino acids. Cleavage specificity analysis using chromogenic and recombinant substrates. Comparisons of GzmB consensus sequences, overview
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additional information
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opossum GzmB cleaves all three asp-ase substrates but not the chymase substrate succinyl-AAPF-4-nitroanilide or the two elastase substrates, succinyl-AAPV-4-nitroanilide and succinyl-AAPA-4-nitroanilide. This indicates a broader specificity against different asp-ase substrates for the opossum GzmB compared to human GzmB. Also no activity of the oppossum GznB with N-(tert-butoxycarbonyl)-VLGR-4-nitroanilide (a tryptase substrate), N-benzyloxycarbonyl-GPR-4-nitroanilide (a tryptase substrate), succinyl-AAPI-4-nitroanilide (an elastase substrate), succinyl-AAPL-4-nitroanilide, and succinyl-LLVY-4-nitroanilide (a chymase substrate). The opossum GzmB shows the relatively strict specificity for negatively charged amino acids in the P1 position. Both opossum and human GzmB prefer the rat GzmB consensus sequence. The rat GzmB consensus sequence contains two negatively charged amino acids in the P1 and P3 positions of the substrate. The cleavage of these substrates results in two clearly separated smaller bands, indicating cleavage only at one site in the middle of the linker sequence. The opossum enzyme cleaves the rat consensus substrate (LIETD-SGL) 5-7 times better than the mouse consensus sequence (LIGFD-VGVQ) with almost no cleavage of the human consensus substrate (LIGAD-VLVQ)
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the substrate preference of granzyme B is determined by a positive charge in the specificity pocket
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additional information
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preference for substrates with Glu or Asp as the residue amino-terminal to the scissile bond, little or no activity with oligopeptide substrates for trypsin-like, chymotrypsin-like, and elastase-like proteases
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additional information
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involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
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additional information
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involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
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additional information
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proforms of mCASP-2 and mCASP-1 are not substrates, pro-mCASP-6 is not proteolytically cleaved by granzyme B, mCASP-11 and mCASP-12 are not processed
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requirement for aspartic acid in the substrate P1 position, induces DNA fragmentation in isolated nuclei in the presence of cytosolic factors
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both human or mouse BID are highly resistant to cleavage by mouse GrB
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BID is a poor substrate for mouse GzmB. Fails to cleave caspase-8 and ICAD from either human or murine origin. Cleaves nucleophosmin of human origin very inefficiently, does not cleave nucleophosmin within J774 cell free extracts
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both human or mouse BID are highly resistant to cleavage by mouse GrB. It is unable to cleave BID in cell lysates in which caspases are inactivated but induces BID cleavage, albeit inefficiently, in lysates supporting caspase activity. BID pathway is not a prominent primary mediator of the effects of mouse GrB
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no efficient cleavage of mouse and human Bid by mouse granzyme B
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platelets from septic granzyme B null (-/-) mice show no lymphotoxicity
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involved in cell killing by cytotoxic T lymphocytes, activates the apoptotic death pathway in the target cell
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not able to induce apoptosis on its own
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processing enzyme, requires extended peptide substrates containing an Asp residue
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mediates cell death by cytotoxic lymphocytes
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