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Information on EC 2.3.2.13 - protein-glutamine gamma-glutamyltransferase and Organism(s) Mus musculus and UniProt Accession Q8BZH1
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2.3.2.13 protein-glutamine gamma-glutamyltransferaseIUBMB Comments
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
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Word Map
- 2.3.2.13
- celiac
- coagulation
- clot
- fibrinogen
-
crosslinking
- gluten
-
serological
- bleeding
- thrombin
- autoimmune
- children
- autoantibody
- platelet
-
gluten-free
- keratinocytes
-
anti-tissue
- gliadin
- collagen
- duodenal
- igg
- bowel
-
deamidated
- fibronectin
-
villous
- keratin
-
fibrinolysis
- plasminogen
-
isopeptide
- involucrin
- enteropathy
- prothrombin
-
cornified
- plasmin
-
hemostatic
-
endoscopy
-
marsh
-
gelation
-
texture
- ichthyosis
-
fibrinopeptide
-
cryoprecipitate
-
gastroenterology
-
rheological
- leiden
-
malabsorption
- filaggrin
- nutrition
- analysis
- agriculture
- diagnostics
-
antifibrinolytic
- medicine
- synthesis
- food industry
- biotechnology
- histiocytomas
-
sealant
-
2-antiplasmin
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
transglutaminase, factor xiii, tissue transglutaminase, tgase, factor xiiia, transglutaminase 2, microbial transglutaminase, mtgase, tgase 2, protein 4.2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
factor XIIIa
-
-
-
-
fibrin stabilizing factor
-
-
-
-
fibrinoligase
-
-
-
-
glutaminylpeptide gamma-glutamyltransferase
-
-
-
-
glutamyltransferase, glutaminylpeptide gamma-
-
-
-
-
polyamine transglutaminase
-
-
-
-
R-glutaminyl-peptide:amine gamma-glutamyl transferase
-
-
-
-
TG1
TG2
TG6
tissue transglutaminase
transglutaminase
transglutaminase 2
tissue transglutaminase
-
-
-
-
transglutaminase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
structure, function, evolution
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
aminoacyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-glutamine:amine gamma-glutamyltransferase
Requires Ca2+. The gamma-carboxamide groups of peptide-bound glutamine residues act as acyl donors, and the 6-amino-groups of protein- and peptide-bound lysine residues act as acceptors, to give intra- and inter-molecular N6-(5-glutamyl)-lysine crosslinks. Formed by proteolytic cleavage from plasma Factor XIII
CAS REGISTRY NUMBER
COMMENTARY
80146-85-6
-
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
SVS I + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS II + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
SVS III + ?
?
major monomeric protein from mouse seminal secretions
protein is cross-linked by isoform TG4. Both SVS I and SVS III are good substrates, but less active than SVS II
-
?
biotinyl-Aca-DDWDAMDEQIWF + alkylamine
?
a TG6 isozyme specific biotinylated peptide substrate
-
-
?
biotinyl-HQSYVDPWMLDH + alkylamine
?
a TG2 isozyme specific biotinylated peptide substrate
-
-
?
protein-bound gamma-glutamine + methylamine
protein N5-methylglutamine + NH3
-
-
-
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[T26 protein]-L-glutamine + 5-(biotinamido)-pentylamine
[T26 protein]-N5-pentyl-L-glutamine + biotin
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
substrate fibronectin
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
catalyzes post-translational protein modifications by transamidation of glutamine residues
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
forms intramolecular isopeptide bonds between fibrin molecules
resulting bonds are covalent and stable to proteolysis
?
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
additional information
?
-
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
?
additional information
?
-
-
mouse seminal proteins of molecular weight below 14 kDa are nnot substrate for cross-linking
-
-
?
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
?
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
?
additional information
?
-
-
the enzyme uses pepT26-bound gamma-glutamine, vimentin-bound gamma-glutamine, actin-bound gamma-glutamine, heat shock protein 71-bound gamma-glutamine, heat shock protein 90-bound gamma-glutamine, beta-actin-like protein 2-bound gamma-glutamine, serpin H1-bound gamma-glutamine, heat shock protein 60-bound gamma-glutamine, lysozyme C1-bound gamma-glutamine, endoplasmin-bound gamma-glutamine, collagen alpha-1(III) chain-bound gamma-glutamine, elongation factor 1-alpha1-bound gamma-glutamine as substrates
-
-
?
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG2 reactivity is significantly specific (i.e. higher than the cross-reactivity towards TG6-specific peptide) at either the lower and higher enzymatic concentrations used. Usage of a colorimetric assay for theTG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
evaluation of cross-reactivity of biotinylated peptides with recombinant isozymes TG2 and TG6. TG6 reactivity is barely detectable at the lower concentration, and only appears to be measurable and specific at the higher dose. In both cases, reactivity measured against the other peptide is not significantly different than background signal measured in control wells. The used peptides are highly reactive and selective for their corresponding isoform. Usage of a colorimetric assay for the TG-dependent epsilon-(gamma-glutamyl)lysine cross-linking reaction
-
-
-
additional information
?
-
measurement of enzyme-catalyzed hydrolysis reactions of water-soluble fluorogenic acyl donor Z-Glu(HMC)-Gly-OH
-
-
-
NATURAL SUBSTRATE
NATURAL 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
protein-bound gamma-glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
epidermal enzyme involved in formation of cornified envelope
-
?
[amyloid-beta]-L-glutamine + alkylamine
[amyloid-beta]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
[protein]-L-glutamine + alkylamine
[protein]-N5-alkyl-L-glutamine + NH3
-
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
protein glutamine + alkylamine
protein N5-alkylglutamine + NH3
-
-
-
?
additional information
?
-
-
TG2 knockout mice are protected against the development of renal interstitial fibrosis, which is associated with a lesser activation of TGF-beta1 and reduced interstitial inflammation. TG2 plays an important role in the development of renal fibrosis
-
-
?
additional information
?
-
-
tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers. Transglutaminase-mediated oligomerization of soluble ephrin potentially represents a novel mechanism of forward signaling through Eph receptors and may extend the influence of A-type ephrins beyond cell contact mediated signaling
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Ca2+
-
calcium in the putrescine incorporation assay buffer results in activation of previously latent TG2
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(S)-N-(((S)-3-bromo-4,5-dihydroisoxazol-5-yl)methyl)-2-(1-(dimethylamino)naphthalene-5-sulfonamido)-3-(1H-indol-3-yl)propanamide
-
the majority of cellular TG2 cannot be inhibited in intact cells. The inhibitor potently inhibits cell lysate TG2 activity in the presence of calcium
KCC009
-
inhibition of enzyme and subsequent block of fibronectin assembly in the extracellular matrix of glioblastoma cells in vitro and in vivo. KCC009 treatment in mice harboring orthotopic glioblastomas sensitizes the tumors to N,N-bis(2-chloroethyl)-N-nitrosourea chemotherapy
N-[(5S)-6-[4-(6-nitropyridin-2-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
N-[(5S)-6-[4-(6-nitropyridin-3-yl)piperazin-1-yl]-6-oxo-5-(2-phenylacetamido)hexyl]prop-2-enamide
-
Nalpha-[(benzyloxy)carbonyl]-N-[(3-bromo-4,5-dihydroisoxazol-5-yl)methyl]-L-tyrosinamide
-
study on pharmacokinetics, pharmacodynamics, and bioavailability
NC9
potent inhibitor, NC9 inhibiting osteoclastogenesis, also inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
cystamine
-
significant reduction in TG2 activity in NZB/W F1 mice following cystamine administration
cystamine
-
transglutaminase inhibitor cystamine alleviates the abnormality in liver from NZB/W F1 mice
Monodansylcadaverine
treatment of proximal renal tublule cells with inhibitor monodansylcadaverine or siRNA results in decreased proliferation accompanied by activation of signal transducer and activator of transcription, Akt and Stat-3. Treatment with monodansylcadaverine or TGase-1 siRNA decreases Stat-3 but not Akt phosphorylation. TGase-1 interacts with Janus-activated kinase JAK2, and this interaction is inhibited by monodansylcadaverine
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
polyinosinic-polycytidylic acid
-
treatment with 15-30 mg/kg polyinosinic-polycytidylic acid results in villous atrophy and activation of TG2 at the villus tips in small intestine
-
Trypsin
-
3fold activation of epidermal transglutaminase, activation is blocked by trypsin-inhibitors
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetics of Z-Glu(HMC)-Gly-OH hydrolysis
-
0.098 - 0.106
putrescine
-
enzyme induced by 12-O-tetradecanoylphorbol-13-acetate or Ca2+
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the enzyme is secreted into the apical medium of polarized cultures of rabbit connecting tubule and cortical collecting duct cells
-
the enzyme is detected in the apical medium of polarized cultures of rabbit connecting tubule and cortical collecting duct cells
-
primary and MCA3A1-cell line, retinoic acid induced enzyme differs from normal epidermal enzyme
-
isoform TG2 activity is elevated in glioblastomas compared with non-neoplastic brain
-
in the mouse model of coronary ligation, modulation of FXIII activity by therapy impacts myocardial healing
bone resorbing cells, derive from monocyte/macrophage cell lineage
-
vascular smooth muscle, extracellular TG2 interacts with the low density lipoprotein related protein 5 receptor and activates beta-catenin signaling in VSMCs. These results suggest that TG2 may promote vascular calcification by activating the beta-catenin signaling pathway
-
enzyme activity is most pronounced in the duodenum, and decreased progressively in the jejunum and ileum
-
primary cell, extracellular TG2 interacts with the low density lipoprotein related protein 5 receptor and activates beta-catenin signaling in VSMCs. These results suggest that TG2 may promote vascular calcification by activating the beta-catenin signaling pathway
additional information
in situ and in vitro enzymatic activity of transglutaminase isoforms on brain tissue sections and brain extract, monitoring of differences in post-translational protein modifications during neurodegeneration, overview. In situ activity of isoform TG6 varies between BACHD mice in comparison to their wild-type controls. TG6 protein expression is prominent in the brains of mice
cells express isoform TGase-1, but not TGase-2, -5, and -7
additional information
-
not expressed in liver, kidney, lung, instestine, heart, and stomach
additional information
TG6 expression seems to localize to neurons but not to astrocytes or microglia. TG6 shows only a faint vascular signal as compared to a prominent cellular staining in mouse tissue
additional information
TG6 expression seems to localize to neurons but not to astrocytes or microglia. TG6 shows only a faint vascular signal as compared to a prominent cellular staining in mouse tissue
additional information
three TGs are expressed in macrophages and osteoclasts, i.e. TG1, TG2 and factor XIII-A, expression analysis of isozymes
additional information
three TGs are expressed in macrophages and osteoclasts, i.e. TG1, TG2 and factor XIII-A, expression analysis of isozymes
additional information
three TGs are expressed in macrophages and osteoclasts, i.e. TG1, TG2 and factor XIII-A, expression analysis of isozymes
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the majority of extracellular TG2 is inactive under normal physiological conditions in cell culture and in vivo. Physical or certain types of chemical injury can lead to rapid enzymatic activation
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
transglutaminase 2 (TG2) mutations are associated with diabetes type 2. Lack of TG2 reduces glucose-stimulated insulin secretion from the pancreatic islets
malfunction
double-TG1/TG2 knockout mice show epidermal features similar to TG1 knockout mice. Double-FXIII-A/TG2 knockout mice exhibit only a transient delay in bone mineral density and growth relative to wild-type mice
malfunction
effective inhibition of renal interstitial fibrosis by TG inhibitors but only partial reduction of fibrosis in TG2 knockout mice
malfunction
TG1 knockout mice show defective epidermal maturation late in embryonic development, resulting in a drastic increase in skin permeability, but unlike human patients, TG1 knockout mice die from dehydration within a few hours of birth. Double-TG1/TG2 knockout mice show epidermal features similar to TG1 knockout mice
malfunction
transglutaminase (TG) inhibitors are capable of blocking the entire osteoclastogenesis process. The most potent of the inhibitors, NC9 when added to cultures at different phases of osteoclastogenesis, inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect of NC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
malfunction
transglutaminase (TG) inhibitors are capable of blocking the entire osteoclastogenesis process. The most potent of the inhibitors, NC9 when added to cultures at different phases of osteoclastogenesis, inhibits differentiation, migration, and fusion of pre-osteoclasts as well as resorption activity of mature osteoclasts. NC9 increases RhoA levels and blocks podosome belt formation. The number of TRAP+ mononuclear pre-osteoclasts is significantly decreased by NC9 treatment for the first 2 days. The inhibitory effect ofNC9 on osteoclastogenesis as well as podosome belt formation is completely reversed with a Rho-family inhibitor Exoenzyme C3. Microtubule architecture, acetylation, and detyrosination of alpha-tubulin are not affected
physiological function
-
inhibition of TGase activity with monodansylcadervine, or knockdown of TGase-1 with small interference RNA enhances apoptosis and decreased cell survival in hydrogen peroxide-treated renal proximal tubule cells. Overexpression of TGase-1 renders renal proximal tubule cells more resistant to hydrogen peroxide toxicity and monodansylcadaverine treatment blocks this response. Concurrent with renal proximal tubule cells apoptosis, phosphorylation of AKT, signal transducer and activator of transcription-3, and glucogen synthase kinase-3 are observed. Pretreatment of cells with monodansylcadervine or TGase-1 siRNA inhibits phosphorylation of all these molecules
physiological function
treatment of proximal renal tublule cells with inhibitor monodansylcadaverine or siRNA results in decreased proliferation accompanied by activation of signal transducer and activator of transcription, Akt and Stat-3. Treatment with monodansylcadaverine or TGase-1 siRNA decreases Stat-3 but not Akt phosphorylation. Janus-activated kinase JAK2 mediates phosphorylation of Stat-3, and knockdown of either JAK2 or Stat-3 by siRNA decreases cell proliferation. Inhibition of TGase-1 decreases phosphorylation of Stat-3 but not JAK2. JAK2 is indispensable for TGase-1 to induce Stat-3 phosphorylation and TGase-1 potentiates JAK2-induced Stat-3 phosphorylation. Inhibition of TGase-1 and the JAK2-Stat-3 signaling pathway decreases the transcriptional activity of Stat-3 and expression of the Stat-3-targeted genes, cyclin D1 and cyclin E. TGase-1 interacts with JAK2, and this interaction is inhibited by monodansylcadaverine
physiological function
-
phosphorylation of transglutaminase 2 at Ser216 plays a role in transglutaminase 2-mediated activation of nuclear factor-kappaB, Akt and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
physiological function
-
the enzyme reduces the pore diameter and inhibits the activity of transient receptor potential vanilloid 5 in an N-glycosylation-dependent manner
physiological function
-
tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination. The number of melanoma lung foci is more markedly reduced by enzyme overexpression than the metastatic size
physiological function
-
the enzyme has an intrinsic capability to promote cell survival and contributes to oncogenesis
physiological function
-
the enzyme is associated with amyloid-beta deposits and lesion-associated astrocytes in Alzheimer's disease
physiological function
essential role for membrane-bound TG1 in cornified envelope assembly
physiological function
mammalian transglutaminases (TGs) catalyze irreversible posttranslational modifications of proteins, the most prominent of which is the calcium-dependent formation of covalent acyl transfers between the gamma-carboxamide group of glutamine and the epsilon-amino-group of lysine (GGEL-linkage)
physiological function
TG2 is involved in extracellular collagen crosslinking
physiological function
transglutaminase (TG) activity regulates differentiation, migration, and fusion of osteoclasts via affecting actin dynamics. TG activity regulates actin dynamics in pre-osteoclasts. Increased osteoclast activity is responsible for bone destruction in diseases such as osteoporosis, periodontitis and rheumatoid arthritis. Analysis of the role of TG activity in osteoclastogenesis in vitro, overview. TG activity is required for pre-osteoclast migration
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TGM4_MOUSE
670
0
75591
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
-
phosphorylation of transglutaminase 2 (TG2) at serine-216 plays a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of phosphatase and tensin homologue deleted on chromosome 10
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
I331N
-
the mutant is associated with early-onset type 2 diabetes, has no GTP-binding ability and shows 32% of wild type activity
M330R
-
the mutant is associated with early-onset type 2 diabetes, has very weak GTP-binding ability and shows 20% of wild type activity
N333S
-
the mutant is associated with early-onset type 2 diabetes, has elevated GTP-binding ability and shows 7% of wild type activity
additional information
additional information
-
downregulation of enzyme by RNAi in U87MG glioblastoma cells demonstrates decreased assembly of fibronectin in the extracellular matrix
additional information
for analysis of the effect of TG2 deficiency, two independent groups of TG2 knockout mouse models are generated, one a global TG2 knockout fromconception and the other offering the versatility of the Cre/loxP site-specific recombination system to generate, in a temporally specific manner, global knockouts or tissue-specific knockouts
additional information
for analysis of the effect of TG2 deficiency, two independent groups of TG2 knockout mouse models are generated, one a global TG2 knockout fromconception and the other offering the versatility of the Cre/loxP site-specific recombination system to generate, in a temporally specific manner, global knockouts or tissue-specific knockouts
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
thermolabile: t1/2: 3-4 min, 37°C, retinoic acid induced enzyme, 20% loss of activity within 20 min, epidermal enzyme
487851
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
retinoic acid induced transgutaminase, loss of approx. 75% activity after 10 min at pH 9, epidermal transglutaminase, 25% loss of activity after 20 min, pH 9.0
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE-cellulose, CM-cellulose, PO4-cellulose, Sephacryl S-200, Mono-S, cationic dermal isozymes A and B
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression is significantly lower in melanoma cells than in control keratinocytes
-
eposure of renal proximal tubule cells to hydrogen peroxide resultsin apoptosis and an increase in TGase activity
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
KCC009 treatment in mice harboring orthotopic glioblastomas sensitizes the tumors to N,N-bis(2-chloroethyl)-N-nitrosourea chemotherapy
medicine
-
cystamine delays the onset of the neurological symptoms associated with Huntingtons disease when applied to the R6/2 Huntingtons mouse model, and dihydroisoxazoles, when used in tandem with BCNU, are able to decrease tumor size and extend survival in a mouse model of glioblastoma
medicine
-
inhibition of TG2 may provide a new and important therapeutic target against the progression of renal fibrosis
medicine
-
therapeutic potential of the transglutaminase 2 inhibitor cystamine in systemic lupus erythematosus
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Greenberg, C.S.; Birckbichler, P.J.; Rice, R.H.
Transglutaminases: multifunctional cross-linking enzymes that stabilize tissues
FASEB J.
5
3071-3077
1991
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
Nakayama, J.; Osaki, M.; Nagae, S.; Asahi, M.; Urabe, H.
Properties of partially purified mouse epidermal transglutaminase
J. Dermatol.
13
448-455
1986
Mus musculus, Mus musculus BALB/c
Lichti, U.; Ben, T.; Yuspan, S.H.
Retinoic acid-induced transglutaminase in mouse epidermal cells is distinct from epidermal transglutaminase
J. Biol. Chem.
260
1422-1426
1985
Mus musculus, Mus musculus BALB/c
Martinet, N.; Kim, H.C.; Girard, J.E.; Nigra, D.H.; Strong, D.H.; Chung, S.I.; Folk, J.E.
Epidermal and hair follicle transglutaminases. Partial characterization of soluble enzymes in newborn mouse skin
J. Biol. Chem.
263
4236-4241
1988
Mus musculus, Mus musculus CF57
Choi, K.; Siegel, M.; Piper, J.L.; Yuan, L.; Cho, E.; Strnad, P.; Omary, B.; Rich, K.M.; Khosla, C.
Chemistry and biology of dihydroisoxazole derivatives: selective inhibitors of human transglutaminase 2
Chem. Biol.
12
469-475
2005
Homo sapiens, Mus musculus
Yuan, L.; Siegel, M.; Choi, K.; Khosla, C.; Miller, C.R.; Jackson, E.N.; Piwnica-Worms, D.; Rich, K.M.
Transglutaminase 2 inhibitor, KCC009, disrupts fibronectin assembly in the extracellular matrix and sensitizes orthotopic glioblastomas to chemotherapy
Oncogene
26
2563-2573
2007
Homo sapiens, Mus musculus
Shweke, N.; Boulos, N.; Jouanneau, C.; Vandermeersch, S.; Melino, G.; Dussaule, J.C.; Chatziantoniou, C.; Ronco, P.; Boffa, J.J.
Tissue transglutaminase contributes to interstitial renal fibrosis by favoring accumulation of fibrillar collagen through TGF-beta activation and cell infiltration
Am. J. Pathol.
173
631-642
2008
Mus musculus
Nahrendorf, M.; Aikawa, E.; Figueiredo, J.L.; Stangenberg, L.; van den Borne, S.W.; Blankesteijn, W.M.; Sosnovik, D.E.; Jaffer, F.A.; Tung, C.H.; Weissleder, R.
Transglutaminase activity in acute infarcts predicts healing outcome and left ventricular remodelling: implications for FXIII therapy and antithrombin use in myocardial infarction
Eur. Heart J.
29
445-454
2008
Homo sapiens, Mus musculus
Hsu, T.C.; Huang, C.Y.; Chiang, S.Y.; Lai, W.X.; Tsai, C.H.; Tzang, B.S.
Transglutaminase inhibitor cystamine alleviates the abnormality in liver from NZB/W F1 mice
Eur. J. Pharmacol.
579
382-389
2008
Mus musculus
Hsu, T.C.; Chiang, S.Y.; Huang, C.Y.; Tsay, G.J.; Yang, C.W.; Huang, C.N.; Tzang, B.S.
Beneficial effects of treatment with transglutaminase inhibitor cystamine on macrophage response in NZB/W F1 mice
Exp. Biol. Med. (Maywood)
232
195-203
2007
Mus musculus
Alford, S.C.; Bazowski, J.; Lorimer, H.; Elowe, S.; Howard, P.L.
Tissue transglutaminase clusters soluble A-type ephrins into functionally active high molecular weight oligomers
Exp. Cell Res.
313
4170-4179
2007
Mus musculus
Faverman, L.; Mikhaylova, L.; Malmquist, J.; Nurminskaya, M.
Extracellular transglutaminase 2 activates beta-catenin signaling in calcifying vascular smooth muscle cells
FEBS Lett.
582
1552-1557
2008
Mus musculus
Siegel, M.; Khosla, C.
Transglutaminase 2 inhibitors and their therapeutic role in disease states
Pharmacol. Ther.
115
232-245
2007
Cavia porcellus, Homo sapiens, Mus musculus
Siegel, M.; Strnad, P.; Watts, R.E.; Choi, K.; Jabri, B.; Omary, M.B.; Khosla, C.
Extracellular transglutaminase 2 is catalytically inactive, but is transiently activated upon tissue injury
PLoS ONE
3
e1861
2008
Mus musculus
Ponnusamy, M.; Pang, M.; Annamaraju, P.K.; Zhang, Z.; Gong, R.; Chin, Y.E.; Zhuang, S.
Transglutaminase-1 protects renal epithelial cells from hydrogen peroxide-induced apoptosis through activation of STAT3 and AKT signaling pathways
Am. J. Physiol. Renal Physiol.
297
F1361-F1370
2009
Mus musculus
Zhang, Z.; Xing, J.; Ma, L.; Gong, R.; Chin, Y.E.; Zhuang, S.
Transglutaminase-1 regulates renal epithelial cell proliferation through activation of Stat-3
J. Biol. Chem.
284
3345-3353
2009
Mus musculus (Q9JLF6)
Tseng, H.C.; Lin, H.J.; Sudhakar Gandhi, P.S.; Wang, C.Y.; Chen, Y.H.
Purification and identification of transglutaminase from mouse coagulating gland and its cross-linking activity among seminal vesicle secretion proteins
J. Chromatogr. B
876
198-202
2008
Mus musculus (Q8BZH1), Mus musculus
Watanabe, K.; Tsunoda, K.; Itoh, M.; Fukui, M.; Mori, H.; Hitomi, K.
Transglutaminase 2 and Factor XIII catalyze distinct substrates in differentiating osteoblastic cell line: utility of highly reactive substrate peptides
Amino Acids
44
209-214
2013
Mus musculus
Facchiano, F.; DArcangelo, D.; Lentini, A.; Rossi, S.; Senatore, C.; Pannellini, T.; Tabolacci, C.; Facchiano, A.M.; Facchiano, A.; Beninati, S.
Tissue transglutaminase activity protects from cutaneous melanoma metastatic dissemination: an in vivo study
Amino Acids
44
53-61
2013
Homo sapiens, Mus musculus
Wang, Y.; Ande, S.R.; Mishra, S.
Phosphorylation of transglutaminase 2 (TG2) at serine-216 plays a role in TG2 mediated activation of nuclear factor-kappa B and in the downregulation of PTEN
BMC Cancer
12
277
2012
Homo sapiens, Mus musculus
Boros, S.; Xi, Q.; Dimke, H.; van der Kemp, A.W.; Tudpor, K.; Verkaart, S.; Lee, K.P.; Bindels, R.J.; Hoenderop, J.G.
Tissue transglutaminase inhibits the TRPV5-dependent calcium transport in an N-glycosylation-dependent manner
Cell. Mol. Life Sci.
69
981-992
2012
Mus musculus
Salter, N.W.; Ande, S.R.; Nguyen, H.K.; Nyomba, B.L.; Mishra, S.
Functional characterization of naturally occurring transglutaminase 2 mutants implicated in early-onset type 2 diabetes
J. Mol. Endocrinol.
48
203-216
2012
Mus musculus
Dafik, L.; Albertelli, M.; Stamnaes, J.; Sollid, L.M.; Khosla, C.
Activation and inhibition of transglutaminase 2 in mice
PLoS ONE
7
e30642
2012
Mus musculus
Fukui, M.; Kuramoto, K.; Yamasaki, R.; Shimizu, Y.; Itoh, M.; Kawamoto, T.; Hitomi, K.
Identification of a highly reactive substrate peptide for transglutaminase 6 and its use in detecting transglutaminase activity in the skin epidermis
FEBS J.
280
1420-1429
2013
Mus musculus
Boroughs, L.K.; Antonyak, M.A.; Cerione, R.A.
A novel mechanism by which tissue transglutaminase activates signaling events that promote cell survival
J. Biol. Chem.
289
10115-10125
2014
Mus musculus
Wilhelmus, M.M.; de Jager, M.; Smit, A.B.; van der Loo, R.J.; Drukarch, B.
Catalytically active tissue transglutaminase colocalises with Abeta pathology in Alzheimers disease mouse models
Sci. Rep.
6
20569
2016
Mus musculus
Schulze-Krebs, A.; Canneva, F.; Schnepf, R.; Dobner, J.; Dieterich, W.; Von Hoersten, S.
In situ enzymatic activity of transglutaminase isoforms on brain tissue sections of rodents A new approach to monitor differences in post-translational protein modifications during neurodegeneration
Brain Res.
1631
22-33
2016
Rattus norvegicus (F1M4T7), Mus musculus (P21981), Mus musculus (Q8BM11), Rattus norvegicus Sprague-Dawley (F1M4T7), Mus musculus C57BL/6J (P21981), Mus musculus C57BL/6J (Q8BM11)
Lorand, L.; Iismaa, S.E.
Transglutaminase diseases from biochemistry to the bedside
FASEB J.
33
3-12
2019
Homo sapiens (O43548), Homo sapiens (O95932), Homo sapiens (P16452), Homo sapiens (P21980), Homo sapiens (P22735), Homo sapiens (P49221), Homo sapiens (Q08188), Homo sapiens (Q96PF1), Homo sapiens, Mus musculus (P21981), Mus musculus (Q9JLF6)
Sun, H.; Kaartinen, M.T.
Transglutaminase activity regulates differentiation, migration and fusion of osteoclasts via affecting actin dynamics
J. Cell. Physiol.
233
7497-7513
2018
Mus musculus (P21981), Mus musculus (Q8BH61), Mus musculus (Q9JLF6)
Wodtke, R.; Hauser, C.; Ruiz-Gomez, G.; Jaeckel, E.; Bauer, D.; Lohse, M.; Wong, A.; Pufe, J.; Ludwig, F.A.; Fischer, S.; Hauser, S.; Greif, D.; Pisabarro, M.T.; Pietzsch, J.; Pietsch, M.; Loeser, R.
Nepsilon-acryloyllysine piperazides as irreversible inhibitors of transglutaminase 2 synthesis, structure-activity relationships, and pharmacokinetic profiling
J. Med. Chem.
61
4528-4560
2018
Cavia porcellus (H0VXN6), Homo sapiens (O95932), Homo sapiens (P00488), Homo sapiens (P21980), Homo sapiens (P22735), Homo sapiens (Q08188), Mus musculus (P21981)
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