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Tissue transglutaminase

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these disorders have been found to be in vivo and in vitro substrates of tTG. Although tTG is up regulated in the areas of the brain affected by Huntington's disease, a recent study showed that increasing levels of tTG do not affect the onset and/or progression of the disease in mice. Recent studies show that tTG may not be involved in AD as studies show it is associated with erythrocyte lysis and is a consequence of the disease rather than a cause.
2029: 602: 595: 609: 350: 249: 4354: 1664:-1 has been shown to activate extracellular tTG by reducing the disulfide bond. Another disuplhide bond can form in tTG, between the residues Cys-230 and Cys-370. While this bond does not exist in the enzyme's native state, it appears when the enzyme is inactivated via oxidation. The presence of calcium protects against the formation of both disulfide bonds, thus making the enzyme more resistant to oxidation. 5057: 2088:
cultured human umbilical vein endothelial cells (HUVECs). ERp57 oxidized TG2 with a rate constant that was 400-2000-fold higher than those of the aforementioned small molecule oxidants. Moreover, its specificity for TG2 was also markedly higher than those of other secreted redox proteins, including protein disulfide isomerase (PDI), ERp72, TRX, and quiescin sulfhydryl oxidase 1 (QSOX1).
1696: 1668: 1461:, GTP-binding/hydrolyzing, and isopeptidase activities. Unlike other members of the transglutaminase family, tTG can be found both in the intracellular and the extracellular spaces of various types of tissues and is found in many different organs including the heart, the liver, and the small intestine. Intracellular tTG is abundant in the 1751:. Evidence shows that intracellular tTG crosslinks itself to myosin. It is also believed that tTG may stabilize the structure of the dying cells during apoptosis by polymerizing the components of the cytoskeleton, therefore preventing the leakage of the cellular contents into the extracellular space. 1838:
and tumor biology. tTG expression is elevated in multiple cancer cell types and is implicated in drug resistance and metastasis due to its ability to promote mesenchymal transition and stem cell like properties. In its GTP bound form, tTG contributes to cancer cell survival and appears to be a cancer
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activity: In the presence of GTP, it suggested to function as a G protein participating in signaling processes. Besides its transglutaminase activity, tTG is proposed to also act as kinase, and protein disulfide isomerase, and deamidase. This latter activity is important in the deamidation of gliadin
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residues, namely Cys 370 and Cys 371. When this disulfide bond forms, the enzyme remains in an open confirmation but becomes catalytically inactive. The, oxidation/reduction of the disulfide bond serves as a third allosteric regulatory mechanism (along with GTP/GDP and Ca) for the activation of tTG.
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Endoplasmic reticulum (ER)-resident protein 57 (ERp57), a protein in the ER that promotes folding of nascent proteins and is also present in the extracellular environment, has the cellular and biochemical characteristics for inactivating TG2. We found that ERp57 colocalizes with extracellular TG2 in
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Crosslinking activity by tTG requires the binding of Ca ions. Multiple Ca can bind to a single tTG molecule. Specifically, tTG binds up to 6 calcium ions at 5 different binding sites. Mutations to these binding sites causing lower calcium affinity, decrease the enzyme's transglutaminase activity. In
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diseases by affecting transcription, differentiation and migration and adhesion . Such neurological diseases are characterized in part by the abnormal aggregation of proteins due to the increased activity of protein crosslinking in the affected brain. Additionally, specific proteins associated with
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Recent studies have suggested that interferon-Îł may serve as an activator of extracellular tTG in the small intestine; these studies have a direct implication to the pathogenesis of celiac disease. Activation of tTG has been shown to be accompanied by large conformational changes, switching from a
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tTG is the most comprehensively studied transglutaminase and has been associated with many diseases. However, none of these diseases are related to an enzyme deficiency. Indeed, thus far no disease has been attributed to the lack of tTG activity and this has been attested through the study of tTG
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of TG2 are known to affect TG2 activity, which enables it to subsequently execute diverse biological functions in the cell. However, the importance of non-enzymatic interactions in regulating TG2 activities is yet to be revealed. Recent studies indicate that non-enzymatic interactions play
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have demonstrated that these forms of TG2 adopt a "closed" conformation, whereas TG2 with the active site occupied by an inhibitory gluten peptide mimic or other similar inhibitors adopts an "open" conformation. In the open conformation the four domains of TG2 are arranged in an extended
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inhibits the crosslinking activity of the enzyme. Therefore, intracellular tTG is mostly inactive due to the relatively high concentration of GTP/GDP and the low levels of calcium inside the cell. Although extracellular tTG is expected to be active due to the low concentration of
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Figure 2: Cystein residues relevant in tTG activity. The disulfide bond between Cys 370 and Cys 371 has formed, therefore the enzyme is in an active conformation. The distance between Cys 370 and Cys 230 is 11.3 Ă…. Cys 277 is the cystein located within the active site of the
73: 47: 1602:(i.e. deamidation). The deamidation of glutamine residues catalyzed by tTG is thought to be linked to the pathological immune response to gluten in celiac disease. A schematic for the crosslinking and the deamidation reactions is provided in Figure 1. 3634:
Rossin F, Villella VR, D'Eletto M, Farrace MG, Esposito S, Ferrari E, Monzani R, Occhigrossi L, Pagliarini V, Sette C, Cozza G, Barlev NA, Falasca L, Fimia GM, Kroemer G, Raia V, Maiuri L, Piacentini M (July 2018).
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Sblattero D, Berti I, Trevisiol C, Marzari R, Tommasini A, Bradbury A, Fasano A, Ventura A, Not T (May 2000). "Human recombinant tissue transglutaminase ELISA: an innovative diagnostic assay for celiac disease".
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Martin A, Giuliano A, Collaro D, De Vivo G, Sedia C, Serretiello E, Gentile V (January 2013). "Possible involvement of transglutaminase-catalyzed reactions in the physiopathology of neurodegenerative diseases".
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have showed promise in using tTG inhibitors as anti-cancer therapeutic agents. However, other studies have noted that tTG transamidation activity could be linked to the inhibition of tumor cell invasiveness.
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and the high levels of calcium in the extracellular space, evidence has shown that extracellular tTG is mostly inactive. Recent studies suggest that extracellular tTG is kept inactive by the formation of a
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which catalyze the crosslinking of proteins by epsilon-(gamma-glutamyl)lysine isopeptide bonds. Similarly to other transglutaminases, tTG consists of a GTP/ GDP binding site, a
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bond between the two substrates (i.e. crosslinking). Alternatively, the thioester intermediate can be hydrolyzed, resulting in the net conversion of the glutamine residue to
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Dieterich W, Ehnis T, Bauer M, Donner P, Volta U, Riecken EO, Schuppan D (July 1997). "Identification of tissue transglutaminase as the autoantigen of celiac disease".
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These Mutant ES Cells can be studied directly or used to generate mice with this gene knocked out. Study of these mice can shed light on the function of Tgm2: see
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atrophy. It has also been implicated in the pathophysiology of many other diseases, including such as many different cancers and neurogenerative diseases.
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Han BG, Cho JW, Cho YD, Jeong KC, Kim SY, Lee BI (August 2010). "Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate".
917: 3440:"Tissue transglutaminase has intrinsic kinase activity: identification of transglutaminase 2 as an insulin-like growth factor-binding protein-3 kinase" 898: 179: 1708:
tTG is expressed ubiquitously and is present in various cellular compartments, such as the cytosol, the nucleus, and the plasma membrane. It requires
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Di Sabatino A, Vanoli A, Giuffrida P, Luinetti O, Solcia E, Corazza GR (August 2012). "The function of tissue transglutaminase in celiac disease".
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tTG is thought to be involved in the regulation of the cytoskeleton by crosslinking various cytoskeletal proteins including myosin, actin, and
5089: 4583: 5337: 4333: 2164: 2146: 4571: 3889:"Presence of tissue transglutaminase in granular endoplasmic reticulum is characteristic of melanized neurons in Parkinson's disease brain" 1766:
tTG also presents PDI (Protein Disulfide Isomerase) activity. Based on its PDI activity, tTG plays an important role in the regulation of
3246:"Cytosolic guanine nucledotide binding deficient form of transglutaminase 2 (R580a) potentiates cell death in oxygen glucose deprivation" 4743: 4353: 2660:"Functional significance of five noncanonical Ca2+-binding sites of human transglutaminase 2 characterized by site-directed mutagenesis" 2566:"Interferon-Îł activates transglutaminase 2 via a phosphatidylinositol-3-kinase-dependent pathway: implications for celiac sprue therapy" 1622:. Once synthesized, most of the protein is found in the cytoplasm, plasma membrane and ECM, but a small fraction is translocated to the 2824:"Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity" 1699:
Figure 4: The proteins that allosterically regulate tTG. On the left Erp57 which oxidizes tTG and on the right TRX-1 which reduces tTG.
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positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G protein-coupled signaling pathway
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responses that eventually result in the production of anti-transglutaminase antibodies IgA and IgG. tTG specifically deamidates the
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diseases. This indicates that tTG inhibitors could also serve as a tool to mitigate the progression of tTG brain related diseases.
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Transglutaminase 2 (TG2) is a ubiquitously expressed (intracellular as well as extracellular) protein, with multiple modes of
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Király R, Csosz E, Kurtán T, Antus S, Szigeti K, Simon-Vecsei Z, Korponay-Szabó IR, Keresztessy Z, Fésüs L (December 2009).
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intermediate. The thioester intermediate can then be attacked by the surface amine of a second substrate (typically from a
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Lortat-Jacob H, Burhan I, Scarpellini A, Thomas A, Imberty A, Vivès RR, Johnson T, Gutierrez A, Verderio EA (May 2012).
159: 3832:"Transglutaminase 2 takes center stage as a cancer cell survival factor and therapy target: Transglutaminase in cancer" 1477:. In the extracellular space, tTG binds to proteins of the extracellular matrix (ECM), binding particularly tightly to 4723: 4497: 2187:"Protein transamidation by transglutaminase 2 in cells: a disputed Ca2+-dependent action of a multifunctional protein" 1968: 1935:(>90%) for identifying celiac disease. Modern anti-tTG assays rely on a human recombinant protein as an antigen. 356: 255: 5119: 5082: 5047: 4733: 4566: 4440: 4917: 5033: 5020: 5007: 4994: 4981: 4968: 4955: 4681: 4657: 4608: 4492: 4445: 4420: 4380: 4326: 349: 248: 4927: 1328: 4881: 4824: 4686: 4411: 1908:. Specifically, in kidney fibrosis, tTG contributes to the stabilization and accumulation of the ECM affecting 1729: 1423: 1221: 962: 167: 31: 1457:(protein degradation). Aside from its crosslinking function, tTG catalyzes other types of reactions including 1315: 4829: 4728: 1943:
It's still experimental to use tTG as a form of surgical glue. It is also being studied as an attenuator of
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has superseded older serological tests (anti-endomysium, anti-gliadin, and anti-reticulin) and has a strong
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Mutant Mouse Embryonic Stem Cell Clones. These are the known targeted mutations for this gene in a mouse.
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causes a pathological immune response resulting in the inflammation of the small intestine and subsequent
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Fesus L, Piacentini M (October 2002). "Transglutaminase 2: an enigmatic enzyme with diverse functions".
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Chen X, Hnida K, Graewert MA, Andersen JT, Iversen R, Tuukkanen A, Svergun D, Sollid LM (August 2015).
1736:. It has been noted that tTG may have very different activity in different cell types. For example, in 1238: 4738: 4625: 4612: 4512: 4319: 3257: 2835: 2059: 1725: 1689: 1627: 146: 3887:
Wilhelmus MM, Verhaar R, Andringa G, Bol JG, Cras P, Shan L, Hoozemans JJ, Drukarch B (March 2011).
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group from a Cys residue in the active site of tTG. The thiol group attacks the carboxamide of a
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Kumar A, Kneynsberg A, Tucholski J, Perry G, van Groen T, Detloff PJ, Lesort M (September 2012).
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Hasegawa G, Suwa M, Ichikawa Y, Ohtsuka T, Kumagai S, Kikuchi M, Sato Y, Saito Y (August 2003).
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McConkey DJ, Orrenius S (October 1997). "The role of calcium in the regulation of apoptosis".
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Figure 1: Transamidation (crosslinking) and deamidation mechanisms of tissue transglutaminase
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configuration, allowing for catalytic activity, whereas in the closed conformation the two
1291: 5255: 5250: 5240: 5235: 5230: 5225: 5220: 5215: 4912: 4896: 4809: 4706: 4407: 4372: 4299: 3025:"Spotlight on the transglutaminase 2 gene: a focus on genomic and transcriptional aspects" 1971:. Enzymatic interactions are formed between TG2 and its substrate proteins containing the 1856: 1848: 1760: 608: 411: 187: 3582:"The Role of Tissue Transglutaminase in Cancer Cell Initiation, Survival and Progression" 2726:
Transglutaminases : multiple functional modifiers and targets for new drug discovery
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driver. tTG is upregulated in cancer cells and tissues in many cancer types, including
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The expression of tTG is regulated at the transcriptional level depending on complex
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physiological roles and enable diverse TG2 functions in a context-specific manner.
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are folded in on the catalytic core domain which includes the residue Cys-277. The
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Marker Symbol for Mouse Gene. This symbol is assigned to the genomic locus by the
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A collection of substrates and interaction partners of TG2 is accessible in the
3481:"A novel function of tissue-type transglutaminase: protein disulphide isomerase" 2169:
National Center for Biotechnology Information, U.S. National Library of Medicine
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National Center for Biotechnology Information, U.S. National Library of Medicine
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in certain tumors. tTG shows promise as a potential therapeutic target to treat
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Tabolacci C, De Martino A, Mischiati C, Feriotto G, Beninati S (January 2019).
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Jin X, Stamnaes J, Klöck C, DiRaimondo TR, Sollid LM, Khosla C (October 2011).
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Proceedings of the National Academy of Sciences of the United States of America
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tTG is believed to contribute to several neurodegenerative disorders including
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residue, creating an inter- or intramolecular bond that is highly resistant to
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Wang Z, Stuckey DJ, Murdoch CE, Camelliti P, Lip GY, Griffin M (April 2018).
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only shows minor structural changes between the two different conformations.
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that are crosslinked to tTG are able to stimulate transglutaminase specific
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Stamnaes J, Pinkas DM, Fleckenstein B, Khosla C, Sollid LM (August 2010).
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knocking out the gene expression for tTG is beneficial to cell survival.
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as a cofactor for transamidation activity. Transcription is increased by
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compact (inactive) to an extended (active) conformation. (see Figure 3)
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Figure 3: Compact (inactive) and extended (active) conformations of tTG
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phospholipase C-activating G protein-coupled receptor signaling pathway
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Example structure of targeted conditional mutant allele for this gene
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negative regulation of endoplasmic reticulum calcium ion concentration
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residues creating epitopes that increase the binding affinity of the
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residue on the surface of a protein or peptide substrate, releasing
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Colak G, Keillor JW, Johnson GV (January 2011). Polymenis M (ed.).
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The catalytic mechanism for crosslinking in human tTG involves the
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Akimov SS, Krylov D, Fleischman LF, Belkin AM (February 2000).
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positive regulation of mitochondrial calcium ion concentration
3691:"Transglutaminase diseases: from biochemistry to the bedside" 2000: 1473:. Intracellular tTG is thought to play an important role in 2251:"Role of transglutaminase 2 in celiac disease pathogenesis" 4754: 3193:
Pinkas DM, Strop P, Brunger AT, Khosla C (December 2007).
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Pinkas DM, Strop P, Brunger AT, Khosla C (December 2007).
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peptides, thus playing important role in the pathology of
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positive regulation of I-kappaB kinase/NF-kappaB signaling
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Sakly W, Thomas V, Quash G, El Alaoui S (December 2006).
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Yi MC, Melkonian AV, Ousey JA, Khosla C (February 2018).
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The Journal of Pharmacology and Experimental Therapeutics
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isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysine
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positive regulation of smooth muscle cell proliferation
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Ricotta M, Iannuzzi M, Vivo GD, Gentile V (May 2010).
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residue). The end product of the reaction is a stable
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TG2 participates in both enzymatic and non-enzymatic
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Recent studies suggest that tTG also plays a role in
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family). Like other transglutaminases, it crosslinks
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Branched-chain alpha-keto acid dehydrogenase complex
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Griffin M, Casadio R, Bergamini CM (December 2002).
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protein-glutamine gamma-glutamyltransferase activity
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Biochemical and Biophysical Research Communications
2303:Facchiano F, Facchiano A, Facchiano AM (May 2006). 1389: 1377: 1365: 1360: 1340: 1321: 1309: 1297: 1285: 1273: 1261: 1249: 1244: 1232: 1220: 1215: 1210: 1125: 1088: 1062: 1025: 3303:Quinn BR, Yunes-Medina L, Johnson GV (July 2018). 2883:International Journal of Biological Macromolecules 2125: 2123: 2121: 2104: 2102: 2100: 793:branching involved in salivary gland morphogenesis 4362:: HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM 3575: 3573: 2923:"Redox regulation of transglutaminase 2 activity" 1951:, through the activity of a highly selective tTG 366: 265: 3781:Murray JA, Frey MR, Oliva-Hemker M (June 2018). 3023:Bianchi N, Beninati S, Bergamini CM (May 2018). 2916: 2914: 2912: 1896:tTG has also been linked to the pathogenesis of 1525:TG2 is a multifunctional enzyme that belongs to 30:"TGM2" redirects here. For the Tetris game, see 4233:Kanchan K, Fuxreiter M, FĂ©sĂĽs L (August 2015). 2564:Diraimondo TR, Klöck C, Khosla C (April 2012). 2050:Endoplasmic reticulum protein 57 (Erp57), is a 27:Protein-coding gene in the species Homo sapiens 3684: 3682: 3680: 3629: 3627: 2719: 2717: 2653: 2651: 2649: 2647: 2506:"Transglutaminases: nature's biological glues" 2249:Klöck C, Diraimondo TR, Khosla C (July 2012). 2130:GRCm38: Ensembl release 89: ENSMUSG00000037820 2080:bond between Cys-370-Cys-371 that renders the 5083: 4770: 4388: 4327: 3354:Cellular functions of tissue transglutaminase 2559: 2557: 2555: 2553: 2551: 2549: 2185:Király R, DemĂ©ny M, FĂ©sĂĽs L (December 2011). 1465:but smaller amounts can also be found in the 8: 4594:2-acylglycerol-3-phosphate O-acyltransferase 4589:1-acylglycerol-3-phosphate O-acyltransferase 798:positive regulation of inflammatory response 4179: 4177: 2611: 2609: 2298: 2296: 2294: 2109:GRCh38: Ensembl release 89: ENSG00000198959 1211:Protein-glutamine gamma-glutamyltransferase 5090: 5076: 5068: 4777: 4763: 4755: 4395: 4381: 4373: 4334: 4320: 4312: 3137: 3135: 3133: 3131: 3129: 2822:Liu S, Cerione RA, Clardy J (March 2002). 2756:: CS1 maint: location missing publisher ( 2499: 2497: 2495: 2493: 1826:, initiating an adaptive immune response. 1357: 858: 633: 407: 306: 203: 81: 4258: 4209: 4157: 4064: 3971: 3961: 3912: 3855: 3806: 3706: 3660: 3607: 3597: 3553: 3504: 3455: 3379: 3328: 3279: 3269: 3220: 3210: 3169: 3159: 3109: 3099: 2999: 2989: 2948: 2938: 2857: 2847: 2798: 2788: 2675: 2589: 2529: 2473: 2424: 2414: 2357: 2320: 2274: 2202: 1634:contrast, the binding of one molecule of 4091:The American Journal of Gastroenterology 2180: 2178: 1990: 818:positive regulation of apoptotic process 742:collagen-containing extracellular matrix 5052: 4349: 2244: 2242: 2240: 2238: 2236: 2234: 2232: 2230: 2096: 4584:Glycerol-3-phosphate O-acyltransferase 3077: 3075: 3073: 3071: 3069: 2749: 2708:"Entrez Gene: TGM2 transglutaminase 2" 2084:inactive in the extracellular matrix. 1207: 702:intrinsic component of plasma membrane 36: 4577:Lecithin—cholesterol acyltransferase 3950:World Journal of Biological Chemistry 1770:, by catalyzing the trimerization of 1513:The human tTG gene is located on the 371: 332: 327: 270: 229: 224: 7: 4572:Glyceronephosphate O-acyltransferase 4239:Cellular and Molecular Life Sciences 3689:Lorand L, Iismaa SE (January 2019). 3534:Clinical and Experimental Immunology 2724:Hitomi K, Kojima S, Fesus L (2015). 1791:tTG is best known for its link with 788:positive regulation of cell adhesion 4744:Sulfoacetaldehyde acetyltransferase 4436:Acetyl-Coenzyme A acetyltransferase 3444:The Journal of Biological Chemistry 3148:The Journal of Biological Chemistry 3088:The Journal of Biological Chemistry 2978:The Journal of Biological Chemistry 2927:The Journal of Biological Chemistry 2403:The Journal of Biological Chemistry 4660:: converted into alkyl on transfer 3362:10.1016/B978-0-12-394305-7.00001-X 3352:Nurminskaya MV, Belkin AM (2012). 1822:peptide to the antigen presenting 1122: 1085: 1059: 1022: 998: 979: 953: 934: 908: 889: 589: 507: 445: 424: 25: 4466:Chloramphenicol acetyltransferase 3830:Eckert, Richard L. (2019-01-29). 3438:Mishra S, Murphy LJ (June 2004). 1418:) is a 78-kDa, calcium-dependent 5055: 4518:Carnitine O-palmitoyltransferase 4352: 4184:Min B, Chung KC (January 2018). 4103:10.1111/j.1572-0241.2000.02018.x 3905:10.1111/j.1750-3639.2010.00429.x 3546:10.1111/j.1365-2249.2006.03236.x 3309:Journal of Neuroscience Research 2677:10.1111/j.1742-4658.2009.07420.x 2204:10.1111/j.1742-4658.2011.08345.x 2027: 1979:donor groups in the presence of 1900:in various organs including the 1803:in which a cellular response to 1797:Anti-transglutaminase antibodies 607: 600: 593: 355: 348: 342: 319: 254: 247: 241: 216: 45: 4461:Beta-galactoside transacetylase 4057:10.1016/j.expneurol.2012.05.015 681:protein domain specific binding 4476:Serotonin N-acetyl transferase 4423:: other than amino-acyl groups 3405:Trends in Biochemical Sciences 2895:10.1016/j.ijbiomac.2010.04.023 1994:Mouse Mutant Alleles for Tgm2 618:More reference expression data 573:More reference expression data 1: 4641:Keratinocyte transglutaminase 4621:Gamma-glutamyl transpeptidase 4535:Serine C-palmitoyltransferase 3417:10.1016/S0968-0004(02)02182-5 2071:Post-translational regulation 2054:molecule involved in loading 531:tunica media of zone of aorta 340: 239: 5338:Genes on human chromosome 20 4562:Aminolevulinic acid synthase 4456:Acetyl-CoA C-acyltransferase 4451:Dihydrolipoyl transacetylase 4202:10.5483/BMBRep.2018.51.1.227 3799:10.1053/j.gastro.2017.12.026 3271:10.1371/journal.pone.0016665 3212:10.1371/journal.pbio.0050327 2790:10.1371/journal.pbio.0050327 2630:10.1016/j.autrev.2012.01.007 4724:2-hydroxyglutarate synthase 2454:The Journal of Cell Biology 2255:Seminars in Immunopathology 823:protein homooligomerization 5364: 5143:Epidermal transglutaminase 5120:Oxoglutarate dehydrogenase 4734:2-isopropylmalate synthase 4567:Beta-ketoacyl-ACP synthase 4441:N-Acetylglutamate synthase 29: 4933:Michaelis–Menten kinetics 4682:Decylhomocitrate synthase 4493:Histone acetyltransferase 4446:Choline acetyltransferase 4347: 4251:10.1007/s00018-015-1909-z 4150:10.1038/s41419-018-0573-2 4010:10.1007/s00726-011-1081-1 2267:10.1007/s00281-012-0305-0 2165:"Mouse PubMed Reference:" 2147:"Human PubMed Reference:" 2035: 2026: 2021: 1993: 1655:bond between two vicinal 1356: 1195: 1190: 1186: 1179: 1163: 1157:Chr 2: 157.96 – 157.99 Mb 1144: 1129: 1092: 1081: 1066: 1029: 1018: 1005: 1001: 986: 982: 973: 960: 956: 941: 937: 928: 915: 911: 896: 892: 883: 868: 861: 857: 841: 768:salivary gland cavitation 636: 632: 615: 592: 583: 570: 519: 510: 457: 448: 418: 410: 406: 389: 376: 339: 318: 309: 305: 288: 275: 238: 215: 206: 202: 157: 154: 144: 137: 132: 89: 84: 67: 62: 57: 53: 44: 39: 5297:Filaggrin (Citrullinate) 4825:Diffusion-limited enzyme 4687:2-methylcitrate synthase 4138:Cell Death & Disease 3836:Molecular Carcinogenesis 3161:10.1074/jbc.RA117.001382 1150:Chr 20: 38.13 – 38.17 Mb 758:apoptotic cell clearance 656:acyltransferase activity 32:Tetris: The Grand Master 5148:Tissue transglutaminase 4729:3-propylmalate synthase 4636:Tissue transglutaminase 3653:10.15252/embr.201745067 3485:The Biochemical Journal 3101:10.1074/jbc.M111.287490 3032:The Biochemical Journal 2991:10.1074/jbc.M115.669895 2940:10.1074/jbc.M109.097162 2582:10.1124/jpet.111.187385 2510:The Biochemical Journal 2416:10.1074/jbc.M111.337089 2309:Frontiers in Bioscience 1865:chemotherapy resistance 1728:development as well as 1408:Tissue transglutaminase 833:blood vessel remodeling 559:external carotid artery 493:upper lobe of left lung 5272:Acetylcholine receptor 5125:Pyruvate dehydrogenase 4697:3-ethylmalate synthase 4692:2-ethylmalate synthase 4557:Acyltransferase like 2 4045:Experimental Neurology 3963:10.4331/wjbc.v1.i5.181 3457:10.1074/jbc.M311919200 2849:10.1073/pnas.042454899 2368:10.1006/bbrc.1997.7409 1700: 1685: 1673: 1610: 547:mesenteric lymph nodes 5307:Sp100 nuclear antigen 4918:Eadie–Hofstee diagram 4851:Allosteric regulation 4677:Citrate (Re)-synthase 4672:Decylcitrate synthase 4613:Aminoacyltransferases 4513:palmitoyltransferases 4293:Endomysial antibodies 3708:10.1096/fj.201801544R 3599:10.3390/medsci7020019 2466:10.1083/jcb.148.4.825 2064:endoplasmic reticulum 2060:MHC class I molecules 1778:Clinical significance 1698: 1683: 1670: 1628:transcription factors 1608: 783:peptide cross-linking 727:endoplasmic reticulum 712:extracellular exosome 465:right coronary artery 232:Chromosome 20 (human) 4928:Lineweaver–Burk plot 4739:Homocitrate synthase 4626:Peptidyl transferase 2618:Autoimmunity Reviews 1799:result in a form of 1726:extracellular matrix 1690:extracellular matrix 737:extracellular matrix 651:transferase activity 469:left coronary artery 373:2 H1|2 78.72 cM 334:Chromosome 2 (mouse) 85:List of PDB id codes 58:Available structures 4471:N-acetyltransferase 3262:2011PLoSO...616665C 3044:10.1042/BCJ20170601 2840:2002PNAS...99.2743L 523:conjunctival fornix 473:canal of the cervix 4887:Enzyme superfamily 4820:Enzyme promiscuity 4431:acetyltransferases 4298:2021-05-12 at the 3752:10.1038/nm0797-797 3497:10.1042/BJ20021084 2522:10.1042/BJ20021234 1869:Preclinical trials 1801:gluten sensitivity 1701: 1686: 1674: 1611: 1586:, and producing a 1560:C-terminal domains 1545:of TG2 with bound 1543:Crystal structures 963:ENSMUSG00000037820 751:Biological process 690:Cellular component 644:Molecular function 489:right uterine tube 18:Transglutaminase 2 5325: 5324: 5043: 5042: 4752: 4751: 4702:ATP citrate lyase 4370: 4369: 3491:(Pt 3): 793–803. 3321:10.1002/jnr.24239 2043: 2042: 1957:neurodegenerative 1853:pancreatic cancer 1564:N-terminal domain 1527:transglutaminases 1405: 1404: 1401: 1400: 1304:metabolic pathway 1206: 1205: 1202: 1201: 1175: 1174: 1140: 1139: 1119: 1118: 1077: 1076: 1056: 1055: 1014: 1013: 995: 994: 969: 968: 950: 949: 924: 923: 905: 904: 853: 852: 671:metal ion binding 628: 627: 624: 623: 579: 578: 566: 565: 504: 503: 402: 401: 301: 300: 128: 127: 124: 123: 68:Ortholog search: 16:(Redirected from 5355: 5282:Apolipoprotein H 5135:Transglutaminase 5092: 5085: 5078: 5069: 5060: 5059: 5051: 4923:Hanes–Woolf plot 4866:Enzyme activator 4861:Enzyme inhibitor 4835:Enzyme catalysis 4779: 4772: 4765: 4756: 4712:HMG-CoA synthase 4667:Citrate synthase 4631:Transglutaminase 4408:acyltransferases 4397: 4390: 4383: 4374: 4356: 4336: 4329: 4322: 4313: 4281: 4280: 4262: 4230: 4224: 4223: 4213: 4181: 4172: 4171: 4161: 4129: 4123: 4122: 4085: 4079: 4078: 4068: 4036: 4030: 4029: 3992: 3986: 3985: 3975: 3965: 3941: 3935: 3934: 3916: 3884: 3878: 3877: 3859: 3848:10.1002/mc.22986 3827: 3821: 3820: 3810: 3793:(8): 2005–2008. 3787:Gastroenterology 3783:"Celiac Disease" 3778: 3772: 3771: 3735: 3729: 3728: 3710: 3686: 3675: 3674: 3664: 3631: 3622: 3621: 3611: 3601: 3586:Medical Sciences 3577: 3568: 3567: 3557: 3525: 3519: 3518: 3508: 3476: 3470: 3469: 3459: 3435: 3429: 3428: 3400: 3394: 3393: 3383: 3349: 3343: 3342: 3332: 3315:(7): 1150–1158. 3300: 3294: 3293: 3283: 3273: 3241: 3235: 3234: 3224: 3214: 3190: 3184: 3183: 3173: 3163: 3154:(8): 2640–2649. 3139: 3124: 3123: 3113: 3103: 3094:(43): 37866–73. 3079: 3064: 3063: 3038:(9): 1643–1667. 3029: 3020: 3014: 3013: 3003: 2993: 2984:(35): 21365–75. 2969: 2963: 2962: 2952: 2942: 2918: 2907: 2906: 2878: 2872: 2871: 2861: 2851: 2819: 2813: 2812: 2802: 2792: 2768: 2762: 2761: 2755: 2747: 2721: 2712: 2711: 2704: 2698: 2697: 2679: 2664:The FEBS Journal 2655: 2642: 2641: 2613: 2604: 2603: 2593: 2561: 2544: 2543: 2533: 2516:(Pt 2): 377–96. 2501: 2488: 2487: 2477: 2445: 2439: 2438: 2428: 2418: 2409:(22): 18005–17. 2394: 2388: 2387: 2361: 2341: 2335: 2334: 2324: 2300: 2289: 2288: 2278: 2246: 2225: 2224: 2206: 2191:The FEBS Journal 2182: 2173: 2172: 2161: 2155: 2154: 2143: 2137: 2127: 2116: 2106: 2031: 1991: 1949:cardiac fibrosis 1531:catalytic domain 1445:residue and a Îł- 1431:transglutaminase 1410:(abbreviated as 1358: 1208: 1188: 1187: 1159: 1152: 1135: 1123: 1114: 1086: 1082:RefSeq (protein) 1072: 1060: 1051: 1023: 999: 980: 954: 935: 909: 890: 859: 634: 620: 611: 604: 597: 590: 575: 551:efferent ductule 515: 513:Top expressed in 508: 477:popliteal artery 453: 451:Top expressed in 446: 425: 408: 398: 385: 374: 359: 352: 346: 335: 323: 307: 297: 284: 273: 258: 251: 245: 234: 220: 204: 198: 196:TGM2 - orthologs 149: 142: 119: 82: 76: 55: 54: 49: 37: 21: 5363: 5362: 5358: 5357: 5356: 5354: 5353: 5352: 5328: 5327: 5326: 5321: 5260: 5152: 5129: 5101: 5096: 5066: 5054: 5046: 5044: 5039: 4951:Oxidoreductases 4937: 4913:Enzyme kinetics 4901: 4897:List of enzymes 4870: 4839: 4810:Catalytic triad 4788: 4783: 4753: 4748: 4707:Malate synthase 4652: 4603: 4415: 4401: 4371: 4366: 4363: 4357: 4343: 4340: 4300:Wayback Machine 4289: 4284: 4245:(16): 3009–35. 4232: 4231: 4227: 4183: 4182: 4175: 4131: 4130: 4126: 4087: 4086: 4082: 4038: 4037: 4033: 3994: 3993: 3989: 3943: 3942: 3938: 3893:Brain Pathology 3886: 3885: 3881: 3829: 3828: 3824: 3780: 3779: 3775: 3740:Nature Medicine 3737: 3736: 3732: 3688: 3687: 3678: 3633: 3632: 3625: 3579: 3578: 3571: 3527: 3526: 3522: 3478: 3477: 3473: 3450:(23): 23863–8. 3437: 3436: 3432: 3402: 3401: 3397: 3372: 3351: 3350: 3346: 3302: 3301: 3297: 3243: 3242: 3238: 3192: 3191: 3187: 3141: 3140: 3127: 3081: 3080: 3067: 3027: 3022: 3021: 3017: 2971: 2970: 2966: 2933:(33): 25402–9. 2920: 2919: 2910: 2880: 2879: 2875: 2821: 2820: 2816: 2770: 2769: 2765: 2748: 2736: 2723: 2722: 2715: 2706: 2705: 2701: 2670:(23): 7083–96. 2657: 2656: 2645: 2615: 2614: 2607: 2563: 2562: 2547: 2503: 2502: 2491: 2447: 2446: 2442: 2396: 2395: 2391: 2359:10.1.1.483.2738 2343: 2342: 2338: 2302: 2301: 2292: 2248: 2247: 2228: 2197:(24): 4717–39. 2184: 2183: 2176: 2163: 2162: 2158: 2145: 2144: 2140: 2128: 2119: 2107: 2098: 2094: 2073:, including an 2048: 1965: 1941: 1918: 1878: 1857:cervical cancer 1849:prostate cancer 1832: 1789: 1783:knockout mice. 1780: 1761:coeliac disease 1730:differentiation 1706: 1620:signal cascades 1616: 1572: 1523: 1517:(20q11.2-q12). 1515:20th chromosome 1511: 1506: 1197:View/Edit Mouse 1192:View/Edit Human 1155: 1148: 1145:Location (UCSC) 1131: 1110: 1106: 1102: 1098: 1094: 1068: 1047: 1043: 1039: 1035: 1031: 944:ENSG00000198959 837: 746: 732:plasma membrane 685: 666:protein binding 616: 606: 605: 599: 598: 571: 562: 557: 553: 549: 545: 541: 539:right lung lobe 537: 535:ascending aorta 533: 529: 525: 511: 500: 495: 491: 487: 483: 481:tibial arteries 479: 475: 471: 467: 463: 449: 393: 380: 372: 362: 361: 360: 353: 333: 310:Gene location ( 292: 279: 271: 261: 260: 259: 252: 230: 207:Gene location ( 158: 145: 138: 91: 69: 35: 28: 23: 22: 15: 12: 11: 5: 5361: 5359: 5351: 5350: 5345: 5340: 5330: 5329: 5323: 5322: 5320: 5319: 5314: 5309: 5304: 5299: 5294: 5289: 5284: 5279: 5274: 5268: 5266: 5262: 5261: 5259: 5258: 5253: 5248: 5243: 5238: 5233: 5228: 5223: 5218: 5213: 5208: 5203: 5198: 5193: 5188: 5183: 5178: 5173: 5168: 5162: 5160: 5154: 5153: 5151: 5150: 5145: 5139: 5137: 5131: 5130: 5128: 5127: 5122: 5117: 5111: 5109: 5103: 5102: 5097: 5095: 5094: 5087: 5080: 5072: 5065: 5064: 5041: 5040: 5038: 5037: 5024: 5011: 4998: 4985: 4972: 4959: 4945: 4943: 4939: 4938: 4936: 4935: 4930: 4925: 4920: 4915: 4909: 4907: 4903: 4902: 4900: 4899: 4894: 4889: 4884: 4878: 4876: 4875:Classification 4872: 4871: 4869: 4868: 4863: 4858: 4853: 4847: 4845: 4841: 4840: 4838: 4837: 4832: 4827: 4822: 4817: 4812: 4807: 4802: 4796: 4794: 4790: 4789: 4784: 4782: 4781: 4774: 4767: 4759: 4750: 4749: 4747: 4746: 4741: 4736: 4731: 4726: 4721: 4720: 4719: 4709: 4704: 4699: 4694: 4689: 4684: 4679: 4674: 4669: 4663: 4661: 4654: 4653: 4651: 4650: 4649: 4648: 4643: 4638: 4628: 4623: 4617: 4615: 4605: 4604: 4602: 4601: 4596: 4591: 4586: 4580: 4579: 4574: 4569: 4564: 4559: 4550: 4549: 4548: 4547: 4542: 4532: 4531: 4530: 4525: 4508: 4507: 4506: 4505: 4500: 4490: 4489: 4488: 4483: 4478: 4468: 4463: 4458: 4453: 4448: 4443: 4438: 4426: 4424: 4417: 4416: 4402: 4400: 4399: 4392: 4385: 4377: 4368: 4367: 4365: 4364: 4358: 4351: 4348: 4345: 4344: 4341: 4339: 4338: 4331: 4324: 4316: 4310: 4309: 4302: 4288: 4287:External links 4285: 4283: 4282: 4225: 4173: 4124: 4080: 4031: 3987: 3936: 3879: 3842:(6): 837–853. 3822: 3773: 3746:(7): 797–801. 3730: 3676: 3623: 3569: 3520: 3471: 3430: 3395: 3370: 3344: 3295: 3236: 3185: 3125: 3065: 3015: 2964: 2908: 2873: 2814: 2763: 2734: 2713: 2699: 2643: 2624:(10): 746–53. 2605: 2545: 2489: 2440: 2389: 2336: 2290: 2226: 2174: 2156: 2138: 2117: 2095: 2093: 2090: 2047: 2044: 2041: 2040: 2038:Knockout mouse 2033: 2032: 2024: 2023: 2019: 2018: 2013: 2009: 2008: 2003: 1996: 1995: 1964: 1961: 1940: 1937: 1917: 1914: 1877: 1876:Other Diseases 1874: 1831: 1828: 1793:celiac disease 1788: 1787:Celiac Disease 1785: 1779: 1776: 1705: 1702: 1615: 1612: 1571: 1568: 1522: 1519: 1510: 1507: 1505: 1502: 1490:celiac disease 1403: 1402: 1399: 1398: 1393: 1387: 1386: 1381: 1375: 1374: 1369: 1363: 1362: 1354: 1353: 1344: 1338: 1337: 1326: 1319: 1318: 1313: 1307: 1306: 1301: 1295: 1294: 1289: 1283: 1282: 1277: 1271: 1270: 1265: 1259: 1258: 1253: 1247: 1246: 1242: 1241: 1236: 1230: 1229: 1224: 1218: 1217: 1213: 1212: 1204: 1203: 1200: 1199: 1194: 1184: 1183: 1177: 1176: 1173: 1172: 1170: 1168: 1161: 1160: 1153: 1146: 1142: 1141: 1138: 1137: 1127: 1126: 1120: 1117: 1116: 1090: 1089: 1083: 1079: 1078: 1075: 1074: 1064: 1063: 1057: 1054: 1053: 1027: 1026: 1020: 1016: 1015: 1012: 1011: 1003: 1002: 996: 993: 992: 984: 983: 977: 971: 970: 967: 966: 958: 957: 951: 948: 947: 939: 938: 932: 926: 925: 922: 921: 913: 912: 906: 903: 902: 894: 893: 887: 881: 880: 875: 870: 866: 865: 855: 854: 851: 850: 839: 838: 836: 835: 830: 825: 820: 815: 810: 805: 800: 795: 790: 785: 780: 775: 770: 765: 760: 754: 752: 748: 747: 745: 744: 739: 734: 729: 724: 719: 717:focal adhesion 714: 709: 704: 699: 693: 691: 687: 686: 684: 683: 678: 673: 668: 663: 658: 653: 647: 645: 641: 640: 630: 629: 626: 625: 622: 621: 613: 612: 587: 581: 580: 577: 576: 568: 567: 564: 563: 561: 560: 556: 552: 548: 544: 540: 536: 532: 528: 524: 520: 517: 516: 505: 502: 501: 499: 498: 494: 490: 486: 482: 478: 474: 470: 466: 462: 458: 455: 454: 442: 441: 433: 422: 416: 415: 412:RNA expression 404: 403: 400: 399: 391: 387: 386: 378: 375: 370: 364: 363: 354: 347: 341: 337: 336: 331: 325: 324: 316: 315: 303: 302: 299: 298: 290: 286: 285: 277: 274: 269: 263: 262: 253: 246: 240: 236: 235: 228: 222: 221: 213: 212: 200: 199: 156: 152: 151: 143: 135: 134: 130: 129: 126: 125: 122: 121: 87: 86: 78: 77: 66: 60: 59: 51: 50: 42: 41: 26: 24: 14: 13: 10: 9: 6: 4: 3: 2: 5360: 5349: 5346: 5344: 5341: 5339: 5336: 5335: 5333: 5318: 5317:Topoisomerase 5315: 5313: 5310: 5308: 5305: 5303: 5300: 5298: 5295: 5293: 5290: 5288: 5285: 5283: 5280: 5278: 5275: 5273: 5270: 5269: 5267: 5263: 5257: 5254: 5252: 5249: 5247: 5244: 5242: 5239: 5237: 5234: 5232: 5229: 5227: 5224: 5222: 5219: 5217: 5214: 5212: 5209: 5207: 5204: 5202: 5199: 5197: 5194: 5192: 5189: 5187: 5184: 5182: 5179: 5177: 5174: 5172: 5169: 5167: 5164: 5163: 5161: 5159: 5155: 5149: 5146: 5144: 5141: 5140: 5138: 5136: 5132: 5126: 5123: 5121: 5118: 5116: 5113: 5112: 5110: 5108: 5107:Dehydrogenase 5104: 5100: 5093: 5088: 5086: 5081: 5079: 5074: 5073: 5070: 5063: 5058: 5053: 5049: 5035: 5031: 5030: 5025: 5022: 5018: 5017: 5012: 5009: 5005: 5004: 4999: 4996: 4992: 4991: 4986: 4983: 4979: 4978: 4973: 4970: 4966: 4965: 4960: 4957: 4953: 4952: 4947: 4946: 4944: 4940: 4934: 4931: 4929: 4926: 4924: 4921: 4919: 4916: 4914: 4911: 4910: 4908: 4904: 4898: 4895: 4893: 4892:Enzyme family 4890: 4888: 4885: 4883: 4880: 4879: 4877: 4873: 4867: 4864: 4862: 4859: 4857: 4856:Cooperativity 4854: 4852: 4849: 4848: 4846: 4842: 4836: 4833: 4831: 4828: 4826: 4823: 4821: 4818: 4816: 4815:Oxyanion hole 4813: 4811: 4808: 4806: 4803: 4801: 4798: 4797: 4795: 4791: 4787: 4780: 4775: 4773: 4768: 4766: 4761: 4760: 4757: 4745: 4742: 4740: 4737: 4735: 4732: 4730: 4727: 4725: 4722: 4718: 4715: 4714: 4713: 4710: 4708: 4705: 4703: 4700: 4698: 4695: 4693: 4690: 4688: 4685: 4683: 4680: 4678: 4675: 4673: 4670: 4668: 4665: 4664: 4662: 4659: 4655: 4647: 4644: 4642: 4639: 4637: 4634: 4633: 4632: 4629: 4627: 4624: 4622: 4619: 4618: 4616: 4614: 4610: 4606: 4600: 4597: 4595: 4592: 4590: 4587: 4585: 4582: 4581: 4578: 4575: 4573: 4570: 4568: 4565: 4563: 4560: 4558: 4555: 4552: 4551: 4546: 4543: 4541: 4538: 4537: 4536: 4533: 4529: 4526: 4524: 4521: 4520: 4519: 4516: 4514: 4510: 4509: 4504: 4501: 4499: 4496: 4495: 4494: 4491: 4487: 4484: 4482: 4479: 4477: 4474: 4473: 4472: 4469: 4467: 4464: 4462: 4459: 4457: 4454: 4452: 4449: 4447: 4444: 4442: 4439: 4437: 4434: 4432: 4428: 4427: 4425: 4422: 4418: 4413: 4409: 4405: 4398: 4393: 4391: 4386: 4384: 4379: 4378: 4375: 4361: 4355: 4350: 4346: 4337: 4332: 4330: 4325: 4323: 4318: 4317: 4314: 4307: 4303: 4301: 4297: 4294: 4291: 4290: 4286: 4278: 4274: 4270: 4266: 4261: 4256: 4252: 4248: 4244: 4240: 4236: 4229: 4226: 4221: 4217: 4212: 4207: 4203: 4199: 4195: 4191: 4187: 4180: 4178: 4174: 4169: 4165: 4160: 4155: 4151: 4147: 4143: 4139: 4135: 4128: 4125: 4120: 4116: 4112: 4108: 4104: 4100: 4097:(5): 1253–7. 4096: 4092: 4084: 4081: 4076: 4072: 4067: 4062: 4058: 4054: 4050: 4046: 4042: 4035: 4032: 4027: 4023: 4019: 4015: 4011: 4007: 4003: 3999: 3991: 3988: 3983: 3979: 3974: 3969: 3964: 3959: 3955: 3951: 3947: 3940: 3937: 3932: 3928: 3924: 3920: 3915: 3910: 3906: 3902: 3898: 3894: 3890: 3883: 3880: 3875: 3871: 3867: 3863: 3858: 3853: 3849: 3845: 3841: 3837: 3833: 3826: 3823: 3818: 3814: 3809: 3804: 3800: 3796: 3792: 3788: 3784: 3777: 3774: 3769: 3765: 3761: 3757: 3753: 3749: 3745: 3741: 3734: 3731: 3726: 3722: 3718: 3714: 3709: 3704: 3700: 3696: 3695:FASEB Journal 3692: 3685: 3683: 3681: 3677: 3672: 3668: 3663: 3658: 3654: 3650: 3647:(7): e45067. 3646: 3642: 3638: 3630: 3628: 3624: 3619: 3615: 3610: 3605: 3600: 3595: 3591: 3587: 3583: 3576: 3574: 3570: 3565: 3561: 3556: 3551: 3547: 3543: 3539: 3535: 3531: 3524: 3521: 3516: 3512: 3507: 3502: 3498: 3494: 3490: 3486: 3482: 3475: 3472: 3467: 3463: 3458: 3453: 3449: 3445: 3441: 3434: 3431: 3426: 3422: 3418: 3414: 3411:(10): 534–9. 3410: 3406: 3399: 3396: 3391: 3387: 3382: 3377: 3373: 3371:9780123943057 3367: 3363: 3359: 3355: 3348: 3345: 3340: 3336: 3331: 3326: 3322: 3318: 3314: 3310: 3306: 3299: 3296: 3291: 3287: 3282: 3277: 3272: 3267: 3263: 3259: 3256:(1): e16665. 3255: 3251: 3247: 3240: 3237: 3232: 3228: 3223: 3218: 3213: 3208: 3204: 3200: 3196: 3189: 3186: 3181: 3177: 3172: 3167: 3162: 3157: 3153: 3149: 3145: 3138: 3136: 3134: 3132: 3130: 3126: 3121: 3117: 3112: 3107: 3102: 3097: 3093: 3089: 3085: 3078: 3076: 3074: 3072: 3070: 3066: 3061: 3057: 3053: 3052:11392/2388638 3049: 3045: 3041: 3037: 3033: 3026: 3019: 3016: 3011: 3007: 3002: 2997: 2992: 2987: 2983: 2979: 2975: 2968: 2965: 2960: 2956: 2951: 2946: 2941: 2936: 2932: 2928: 2924: 2917: 2915: 2913: 2909: 2904: 2900: 2896: 2892: 2888: 2884: 2877: 2874: 2869: 2865: 2860: 2855: 2850: 2845: 2841: 2837: 2834:(5): 2743–7. 2833: 2829: 2825: 2818: 2815: 2810: 2806: 2801: 2796: 2791: 2786: 2782: 2778: 2774: 2767: 2764: 2759: 2753: 2745: 2741: 2737: 2735:9784431558255 2731: 2727: 2720: 2718: 2714: 2709: 2703: 2700: 2695: 2691: 2687: 2683: 2678: 2673: 2669: 2665: 2661: 2654: 2652: 2650: 2648: 2644: 2639: 2635: 2631: 2627: 2623: 2619: 2612: 2610: 2606: 2601: 2597: 2592: 2587: 2583: 2579: 2576:(1): 104–14. 2575: 2571: 2567: 2560: 2558: 2556: 2554: 2552: 2550: 2546: 2541: 2537: 2532: 2527: 2523: 2519: 2515: 2511: 2507: 2500: 2498: 2496: 2494: 2490: 2485: 2481: 2476: 2471: 2467: 2463: 2460:(4): 825–38. 2459: 2455: 2451: 2444: 2441: 2436: 2432: 2427: 2422: 2417: 2412: 2408: 2404: 2400: 2393: 2390: 2385: 2381: 2377: 2373: 2369: 2365: 2360: 2355: 2352:(2): 357–66. 2351: 2347: 2340: 2337: 2332: 2328: 2323: 2318: 2314: 2310: 2306: 2299: 2297: 2295: 2291: 2286: 2282: 2277: 2272: 2268: 2264: 2261:(4): 513–22. 2260: 2256: 2252: 2245: 2243: 2241: 2239: 2237: 2235: 2233: 2231: 2227: 2222: 2218: 2214: 2210: 2205: 2200: 2196: 2192: 2188: 2181: 2179: 2175: 2170: 2166: 2160: 2157: 2152: 2148: 2142: 2139: 2135: 2131: 2126: 2124: 2122: 2118: 2114: 2110: 2105: 2103: 2101: 2097: 2091: 2089: 2085: 2083: 2079: 2076: 2072: 2067: 2065: 2061: 2057: 2053: 2045: 2039: 2034: 2030: 2025: 2020: 2017: 2014: 2011: 2010: 2007: 2004: 2002: 1998: 1997: 1992: 1989: 1986: 1982: 1978: 1974: 1970: 1962: 1960: 1958: 1954: 1950: 1946: 1938: 1936: 1934: 1930: 1926: 1923:for anti-tTG 1922: 1915: 1913: 1911: 1907: 1903: 1899: 1894: 1891: 1887: 1883: 1875: 1873: 1870: 1866: 1862: 1858: 1854: 1850: 1846: 1845:breast cancer 1842: 1837: 1829: 1827: 1825: 1821: 1817: 1813: 1809: 1807: 1802: 1798: 1794: 1786: 1784: 1777: 1775: 1773: 1769: 1764: 1762: 1757: 1754:tTG also has 1752: 1750: 1745: 1743: 1739: 1735: 1734:cell adhesion 1731: 1727: 1723: 1719: 1718:wound healing 1715: 1714:retinoic acid 1711: 1703: 1697: 1693: 1691: 1682: 1678: 1669: 1665: 1663: 1658: 1654: 1649: 1646: 1641: 1637: 1631: 1629: 1625: 1621: 1613: 1607: 1603: 1601: 1600:glutamic acid 1597: 1593: 1589: 1585: 1581: 1577: 1569: 1567: 1565: 1561: 1556: 1552: 1548: 1544: 1540: 1539:beta-sandwich 1536: 1532: 1528: 1520: 1518: 1516: 1508: 1503: 1501: 1499: 1495: 1491: 1487: 1482: 1480: 1476: 1472: 1468: 1464: 1460: 1456: 1452: 1448: 1444: 1440: 1437:between an ε- 1436: 1432: 1428: 1425: 1421: 1417: 1413: 1409: 1397: 1394: 1392: 1388: 1385: 1382: 1380: 1376: 1373: 1370: 1368: 1364: 1359: 1355: 1352: 1348: 1345: 1343: 1342:Gene Ontology 1339: 1336: 1333: 1330: 1327: 1324: 1320: 1317: 1314: 1312: 1308: 1305: 1302: 1300: 1296: 1293: 1290: 1288: 1284: 1281: 1280:NiceZyme view 1278: 1276: 1272: 1269: 1266: 1264: 1260: 1257: 1254: 1252: 1248: 1243: 1240: 1237: 1235: 1231: 1228: 1225: 1223: 1219: 1214: 1209: 1198: 1193: 1189: 1185: 1182: 1178: 1171: 1169: 1166: 1162: 1158: 1154: 1151: 1147: 1143: 1136: 1134: 1128: 1124: 1121: 1115: 1113: 1109: 1105: 1101: 1097: 1091: 1087: 1084: 1080: 1073: 1071: 1065: 1061: 1058: 1052: 1050: 1046: 1042: 1038: 1034: 1028: 1024: 1021: 1019:RefSeq (mRNA) 1017: 1010: 1009: 1004: 1000: 997: 991: 990: 985: 981: 978: 976: 972: 965: 964: 959: 955: 952: 946: 945: 940: 936: 933: 931: 927: 920: 919: 914: 910: 907: 901: 900: 895: 891: 888: 886: 882: 879: 876: 874: 871: 867: 864: 860: 856: 849: 845: 840: 834: 831: 829: 826: 824: 821: 819: 816: 814: 811: 809: 806: 804: 801: 799: 796: 794: 791: 789: 786: 784: 781: 779: 776: 774: 771: 769: 766: 764: 761: 759: 756: 755: 753: 750: 749: 743: 740: 738: 735: 733: 730: 728: 725: 723: 722:mitochondrion 720: 718: 715: 713: 710: 708: 705: 703: 700: 698: 695: 694: 692: 689: 688: 682: 679: 677: 674: 672: 669: 667: 664: 662: 659: 657: 654: 652: 649: 648: 646: 643: 642: 639: 638:Gene ontology 635: 631: 619: 614: 610: 603: 596: 591: 588: 586: 582: 574: 569: 558: 554: 550: 546: 542: 538: 534: 530: 526: 522: 521: 518: 514: 509: 506: 496: 492: 488: 485:right auricle 484: 480: 476: 472: 468: 464: 460: 459: 456: 452: 447: 444: 443: 440: 438: 434: 432: 431: 427: 426: 423: 421: 417: 413: 409: 405: 397: 392: 388: 384: 379: 369: 365: 358: 351: 345: 338: 330: 326: 322: 317: 313: 308: 304: 296: 291: 287: 283: 278: 268: 264: 257: 250: 244: 237: 233: 227: 223: 219: 214: 210: 205: 201: 197: 193: 189: 185: 181: 177: 173: 169: 165: 161: 153: 148: 141: 136: 131: 120: 118: 114: 110: 106: 102: 98: 94: 88: 83: 80: 79: 75: 72: 65: 61: 56: 52: 48: 43: 38: 33: 19: 5348:Autoantigens 5302:Gangliosides 5158:Nucleoporins 5147: 5099:Autoantigens 5029:Translocases 5026: 5013: 5000: 4987: 4974: 4964:Transferases 4961: 4948: 4805:Binding site 4635: 4553: 4511: 4429: 4404:Transferases 4359: 4242: 4238: 4228: 4193: 4189: 4141: 4137: 4127: 4094: 4090: 4083: 4051:(1): 78–89. 4048: 4044: 4034: 4004:(1): 111–8. 4001: 3997: 3990: 3956:(5): 181–7. 3953: 3949: 3939: 3899:(2): 130–9. 3896: 3892: 3882: 3839: 3835: 3825: 3790: 3786: 3776: 3743: 3739: 3733: 3698: 3694: 3644: 3641:EMBO Reports 3640: 3589: 3585: 3540:(3): 550–8. 3537: 3533: 3523: 3488: 3484: 3474: 3447: 3443: 3433: 3408: 3404: 3398: 3353: 3347: 3312: 3308: 3298: 3253: 3249: 3239: 3205:(12): e327. 3202: 3199:PLOS Biology 3198: 3188: 3151: 3147: 3091: 3087: 3035: 3031: 3018: 2981: 2977: 2967: 2930: 2926: 2889:(2): 190–5. 2886: 2882: 2876: 2831: 2827: 2817: 2783:(12): e327. 2780: 2777:PLOS Biology 2776: 2766: 2725: 2702: 2667: 2663: 2621: 2617: 2573: 2569: 2513: 2509: 2457: 2453: 2443: 2406: 2402: 2392: 2349: 2345: 2339: 2322:10.2741/1921 2312: 2308: 2258: 2254: 2194: 2190: 2168: 2159: 2150: 2141: 2086: 2068: 2049: 1969:interactions 1966: 1963:Interactions 1942: 1919: 1895: 1879: 1836:inflammation 1833: 1805: 1790: 1781: 1768:proteostasis 1765: 1753: 1746: 1707: 1687: 1675: 1632: 1617: 1573: 1524: 1512: 1483: 1471:mitochondria 1415: 1411: 1407: 1406: 1268:BRENDA entry 1130: 1104:NP_001310247 1100:NP_001310246 1096:NP_001310245 1093: 1067: 1049:NM_001323318 1045:NM_001323317 1041:NM_001323316 1030: 1006: 987: 961: 942: 916: 897: 877: 872: 555:carotid body 543:ciliary body 435: 428: 394:157,988,356 381:157,958,322 155:External IDs 90: 5287:Cardiolipin 4800:Active site 4646:Factor XIII 4342:PDB gallery 4196:(1): 5–13. 4190:BMB Reports 3998:Amino Acids 3701:(1): 3–12. 2315:: 1758–73. 1939:Therapeutic 1933:specificity 1929:sensitivity 1662:Thioredoxin 1648:nucleotides 1535:beta barrel 1486:autoantigen 1484:tTG is the 1479:fibronectin 1459:deamidation 1455:proteolysis 1447:carboxamide 1441:group of a 1256:IntEnz view 1239:80146-85-6 1216:Identifiers 676:GTP binding 527:Paneth cell 293:38,166,578 280:38,127,385 133:Identifiers 5332:Categories 5292:Centromere 5003:Isomerases 4977:Hydrolases 4844:Regulation 4144:(6): 613. 2136:, May 2017 2115:, May 2017 2092:References 2075:allosteric 1985:Substrates 1975:donor and 1945:metastasis 1931:(99%) and 1925:antibodies 1916:Diagnostic 1912:activity. 1890:Huntington 1861:metastasis 1742:astrocytes 1614:Regulation 1596:isopeptide 1325:structures 1292:KEGG entry 439:(ortholog) 176:HomoloGene 4882:EC number 3592:(2): 19. 2752:cite book 2744:937392418 2728:. Tokyo. 2354:CiteSeerX 2078:disulfide 2052:chaperone 1973:glutamine 1953:inhibitor 1886:Parkinson 1882:Alzheimer 1816:glutamine 1806:Triticeae 1722:apoptosis 1653:disulfide 1588:thioester 1580:glutamine 1570:Mechanism 1504:Structure 1475:apoptosis 1451:glutamine 1449:group of 1245:Databases 1133:NP_033399 1112:NP_945189 1108:NP_004604 1070:NM_009373 1037:NM_198951 1033:NM_004613 863:Orthologs 697:cytoplasm 461:beta cell 184:GeneCards 5343:EC 2.3.2 5312:Thrombin 4906:Kinetics 4830:Cofactor 4793:Activity 4498:P300/CBP 4306:TRANSDAB 4296:Archived 4277:14849506 4269:25943306 4260:11113818 4220:29187283 4168:29795262 4119:11018740 4111:10811336 4075:22698685 4026:16143202 4018:21938398 3982:21541002 3923:20731657 3874:59341070 3866:30693974 3817:29550590 3768:20033968 3725:58551851 3717:30593123 3671:29752334 3618:30691081 3564:17100777 3515:12737632 3466:15069073 3425:12368090 3390:22364871 3339:29570839 3290:21304968 3250:PLOS ONE 3231:18092889 3180:29305423 3120:21908620 3060:29764956 3010:26160175 2959:20547769 2903:20450932 2868:11867708 2809:18092889 2694:21883387 2686:19878304 2638:22326684 2600:22228808 2540:12366374 2484:10684262 2435:22442151 2384:11242870 2331:16368554 2285:22437759 2221:19217277 2213:21902809 2132:– 2111:– 1921:Serology 1910:TGF beta 1904:and the 1898:fibrosis 1841:leukemia 1749:spectrin 1704:Function 1657:cysteine 1469:and the 1435:proteins 1427:2.3.2.13 1396:proteins 1384:articles 1372:articles 1329:RCSB PDB 1227:2.3.2.13 1181:Wikidata 842:Sources: 272:20q11.23 5062:Biology 5016:Ligases 4786:Enzymes 4211:5796628 4159:5966415 4066:3418489 3973:3083958 3914:8094245 3857:7754084 3808:6203336 3760:9212111 3662:6030705 3609:6409630 3555:1810403 3506:1223550 3381:3746560 3330:5980740 3281:3031627 3258:Bibcode 3222:2140088 3171:5827427 3111:3199528 3001:4571865 2950:2919103 2836:Bibcode 2800:2140088 2591:3310700 2531:1223021 2475:2169362 2426:3365763 2376:9344835 2276:3712867 2134:Ensembl 2113:Ensembl 2062:in the 2056:peptide 1981:calcium 1824:T cells 1808:glutens 1738:neurons 1710:calcium 1688:In the 1672:enzyme. 1645:guanine 1624:nucleus 1584:ammonia 1521:Protein 1498:villous 1467:nucleus 1463:cytosol 1351:QuickGO 1316:profile 1299:MetaCyc 1234:CAS no. 975:UniProt 930:Ensembl 869:Species 848:QuickGO 707:cytosol 497:decidua 414:pattern 140:Aliases 5256:NUP214 5251:NUP205 5246:NUP210 5241:NUP188 5236:NUP160 5231:NUP155 5226:NUP153 5221:NUP133 5216:NUP107 5048:Portal 4990:Lyases 4717:HMGCS2 4554:other: 4545:SPTLC2 4540:SPTLC1 4481:HGSNAT 4275:  4267:  4257:  4218:  4208:  4166:  4156:  4117:  4109:  4073:  4063:  4024:  4016:  3980:  3970:  3931:586174 3929:  3921:  3911:  3872:  3864:  3854:  3815:  3805:  3766:  3758:  3723:  3715:  3669:  3659:  3616:  3606:  3562:  3552:  3513:  3503:  3464:  3423:  3388:  3378:  3368:  3337:  3327:  3288:  3278:  3229:  3219:  3178:  3168:  3118:  3108:  3058:  3008:  2998:  2957:  2947:  2901:  2866:  2859:122418 2856:  2807:  2797:  2742:  2732:  2692:  2684:  2636:  2598:  2588:  2538:  2528:  2482:  2472:  2433:  2423:  2382:  2374:  2356:  2329:  2283:  2273:  2219:  2211:  2082:enzyme 1977:lysine 1906:kidney 1830:Cancer 1820:gluten 1812:B-cell 1756:GTPase 1724:, and 1592:lysine 1537:and a 1533:, two 1494:gluten 1443:lysine 1420:enzyme 1379:PubMed 1361:Search 1347:AmiGO 1335:PDBsum 1275:ExPASy 1263:BRENDA 1251:IntEnz 1222:EC no. 1167:search 1165:PubMed 1008:P21981 989:P21980 885:Entrez 585:BioGPS 164:190196 5277:Actin 5265:Other 5211:NUP98 5206:NUP93 5201:NUP88 5196:NUP85 5191:NUP62 5186:NUP54 5181:NUP50 5176:NUP43 5171:NUP37 5166:NUP35 4942:Types 4658:2.3.3 4609:2.3.2 4599:ABHD5 4486:ARD1A 4421:2.3.1 4273:S2CID 4115:S2CID 4022:S2CID 3927:S2CID 3870:S2CID 3764:S2CID 3721:S2CID 3028:(PDF) 2690:S2CID 2380:S2CID 2217:S2CID 2058:onto 2046:Erp57 1576:thiol 1553:, or 1439:amino 1311:PRIAM 918:21817 878:Mouse 873:Human 844:Amigo 437:Mouse 430:Human 377:Start 312:Mouse 276:Start 209:Human 172:98731 5034:list 5027:EC7 5021:list 5014:EC6 5008:list 5001:EC5 4995:list 4988:EC4 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Index

Transglutaminase 2
Tetris: The Grand Master

PDB
PDBe
RCSB
4PYG
1KV3
2Q3Z
3LY6
3S3J
3S3P
3S3S
Aliases
TGM2
OMIM
190196
MGI
98731
HomoloGene
3391
GeneCards
TGM2
OMA
TGM2 - orthologs
Human
Chromosome 20 (human)
Chr.
Chromosome 20 (human)
Chromosome 20 (human)

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