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Entry version 228 (29 Sep 2021)
Sequence version 2 (23 Jan 2002)
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Protein

Protein-glutamine gamma-glutamyltransferase 2

Gene

TGM2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:9252372, PubMed:23941696, PubMed:31991788).

Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (PubMed:1683874, PubMed:7935379, PubMed:9252372, PubMed:27270573).

Acts as a protein-glutamine gamma-glutamyltransferase by mediating the cross-linking of proteins, such as ACO2, HSPB6, FN1, HMGB1, RAP1GDS1, SLC25A4/ANT1, SPP1 and WDR54 (PubMed:23941696, PubMed:24349085, PubMed:29618516, PubMed:30458214).

Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca2+ in response to various stresses (PubMed:7649299, PubMed:7592956, PubMed:18092889).

When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (PubMed:12506096).

Plays a key role during apoptosis, both by (1) promoting the cross-linking of cytoskeletal proteins resulting in condensation of the cytoplasm, and by (2) mediating cross-linking proteins of the extracellular matrix, resulting in the irreversible formation of scaffolds that stabilize the integrity of the dying cells before their clearance by phagocytosis, thereby preventing the leakage of harmful intracellular components (PubMed:7935379, PubMed:9252372).

In addition to protein cross-linking, can use different monoamine substrates to catalyze a vast array of protein post-translational modifications: mediates aminylation of serotonin, dopamine, noradrenaline or histamine into glutamine residues of target proteins to generate protein serotonylation, dopaminylation, noradrenalinylation or histaminylation, respectively (PubMed:23797785, PubMed:30867594).

Mediates protein serotonylation of small GTPases during activation and aggregation of platelets, leading to constitutive activation of these GTPases (By similarity).

Plays a key role in chromatin organization by mediating serotonylation and dopaminylation of histone H3 (PubMed:30867594, PubMed:32273471).

Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (PubMed:30867594).

Acts as a mediator of neurotransmission-independent role of nuclear dopamine in ventral tegmental area (VTA) neurons: catalyzes dopaminylation of 'Gln-5' of histone H3 (H3Q5dop), thereby regulating relapse-related transcriptional plasticity in the reward system (PubMed:32273471).

Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (By similarity).

Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (PubMed:9623982, PubMed:20547769).

Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (PubMed:9623982).

May also act as an isopeptidase cleaving the previously formed cross-links (PubMed:26250429, PubMed:27131890).

Also able to participate in signaling pathways independently of its acyltransferase activity: acts as a signal transducer in alpha-1 adrenergic receptor-mediated stimulation of phospholipase C-delta (PLCD) activity and is required for coupling alpha-1 adrenergic agonists to the stimulation of phosphoinositide lipid metabolism (PubMed:8943303).

1 PublicationBy similarity20 Publications

Has cytotoxic activity: is able to induce apoptosis independently of its acyltransferase activity.

1 Publication

Caution

Initial enzymatic assays were performed with a protein sequence containing a Gly residue instead of a Val at position 224: such protein displays lower Ca2+-binding affinity and reduced transglutaminase activity.2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Ca2+1 Publication1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Acyltransferase activity is regulated by the binding of GTP and Ca2+: inactivated by GTP, which stabilizes its closed structure, thereby obstructing the accessibility of substrates to the active sites (PubMed:2903073, PubMed:7592956, PubMed:18092889, PubMed:31991788). In contrast, Ca2+ acts as a cofactor by inducing conformational change to the active open form (PubMed:2903073, PubMed:18092889, PubMed:31991788). In absence of Ca2+, Mg2+ may bind Ca2+-binding sites, promoting GTP-binding and subsequent inhibition of the acyltransferase activity (PubMed:31991788). Specifically inhibited by compound VA4 ((S)-Benzyl (6-Acrylamido-1-(4-((5-(dimethylamino)naphthalen-1-yl)sulfonyl)piperazin-1-yl)-1-oxohexan-2-yl)carbamate), which specifically abolishes both the transamidation and GTP-binding activities (PubMed:28858494).5 Publications

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

Kcat is 11.2 min(-1) with benzyloxycarbonyl-Gln-Gly substrate for protein-glutamine deamidase activity.1 Publication
  1. KM=11.2 mM for benzyloxycarbonyl-Gln-Gly (for protein-glutamine deamidase activity)1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei277PROSITE-ProRule annotation2 Publications1
Active sitei335PROSITE-ProRule annotation1
Active sitei358PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi398CalciumBy similarity1
Metal bindingi400CalciumBy similarity1
Metal bindingi437Calcium1 Publication1
Metal bindingi447CalciumBy similarity1
Metal bindingi452CalciumBy similarity1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei516Important for catalytic activityBy similarity1
Metal bindingi539Calcium1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi476 – 483GTPCombined sources2 Publications3 Publications8
Nucleotide bindingi580 – 583GTPCombined sources2 Publications3 Publications4

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAcyltransferase, Hydrolase, Protease, Transferase
LigandCalcium, GTP-binding, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.3.2.13, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P21980

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
P21980

SIGNOR Signaling Network Open Resource

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SIGNORi
P21980

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein-glutamine gamma-glutamyltransferase 2Curated (EC:2.3.2.133 Publications)
Alternative name(s):
Erythrocyte transglutaminase1 Publication
Heart G alpha(h)1 Publication
Short name:
hhG alpha(h)1 Publication
Isopeptidase TGM2Curated (EC:3.4.-.-2 Publications)
Protein G alpha(h)1 Publication
Short name:
G(h)1 Publication
Protein-glutamine deamidase TGM2Curated (EC:3.5.1.442 Publications)
Protein-glutamine dopaminyltransferase TGM2Curated (EC:2.3.1.-1 Publication)
Protein-glutamine histaminyltransferase TGM2Curated (EC:2.3.1.-1 Publication)
Protein-glutamine noradrenalinyltransferase TGM2Curated (EC:2.3.1.-By similarity)
Protein-glutamine serotonyltransferase TGM2Curated (EC:2.3.1.-1 Publication)
Tissue transglutaminase4 Publications
Short name:
tTG2 Publications
Short name:
tTgase2 Publications
Transglutaminase C1 Publication
Short name:
TG(C)1 Publication
Short name:
TGC1 Publication
Short name:
TGase C1 Publication
Transglutaminase H1 Publication
Short name:
TGase H1 Publication
Transglutaminase II1 Publication
Short name:
TGase II1 Publication
Transglutaminase-22 Publications
Short name:
TG22 Publications
Short name:
TGase-2
Short name:
hTG21 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:TGM21 PublicationImported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 20

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:11778, TGM2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
190196, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P21980

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000198959

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cell membrane, Chromosome, Cytoplasm, Extracellular matrix, Membrane, Mitochondrion, Nucleus, Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

TGM2 constitutes the major autoantigen in celiac disease, a multifactorial chronic disorder of the small intestine caused by intolerance to gluten (PubMed:9212111, PubMed:9623982). Celiac disease is characterized by immune-mediated enteropathy associated with failed intestinal absorption and malnutrition: intestinal inflammation is precipitated by ingestion of the protein gliadin, a component of wheat gluten in the diet (PubMed:9212111, PubMed:9623982). TGM2 is the main target for celiac disease-associated anti-endomysium autoantibodies (PubMed:9212111). It mediates its effect by catalyzing specific deamidation of gliadin; this deamidation creates an epitope that binds efficiently to HLA-DQ2 and is recognized by gut-derived T-cells (PubMed:9623982).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi171S → E: Abolishes GTP-binding and transglutaminase activities. Does not have cytotoxic activity when overexpressed. 1 Publication1
Mutagenesisi180W → F: Abolished isopeptidase activity and reduced transamidase activity. 1 Publication1
Mutagenesisi180W → L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi224V → G: Displays lower Ca(2+)-binding affinity and reduced transglutaminase activity. 1 Publication1
Mutagenesisi230C → A: Does not affect the protein-glutamine deamidase activity. 1 Publication1
Mutagenesisi241W → F or L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi277C → S: Abolished protein-glutamine gamma-glutamyltransferase activity without affecting alpha-1 adrenergic receptor signaling. Abolished isopeptidase activity. 4 Publications1
Mutagenesisi277C → V: Dominant negative mutant. Abolishes WDR54 cross-linking. 1 Publication1
Mutagenesisi278W → F in TG2-T; strongly reduced isopeptidase activity without affecting the transamidase activity. 1 Publication1
Mutagenesisi278W → L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi332W → F in TG2-I; strongly reduced transamidase activity without affecting the isopeptidase activity. 1 Publication1
Mutagenesisi332W → L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi334F → L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi337W → F: Reduced isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi337W → L: Abolished isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi370C → A: Impaired substrate recognition for the protein-glutamine deamidase activity. 1 Publication1
Mutagenesisi371C → A: Impaired substrate recognition for the protein-glutamine deamidase activity. 1 Publication1
Mutagenesisi437E → R: Impaired Ca(2+)-binding leading to reduced transglutaminase activity. 1 Publication1
Mutagenesisi516Y → L: No effect on isopeptidase and transamidase activities. 1 Publication1
Mutagenesisi539E → R: Impaired Ca(2+)-binding leading to reduced transglutaminase activity. 1 Publication1
Mutagenesisi665 – 672VVNFESDK → IASMSSDS: Substitution with F13A1 sequence. Abolished interaction with phospholipase C and ability to promote alpha-1 adrenergic receptor signaling. 1 Publication8
Isoform 2 (identifier: P21980-2)
Mutagenesisi277C → V: Abolished protein-glutamine gamma-glutamyltransferase activity without affecting cytotoxic activity. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
7052

Open Targets

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OpenTargetsi
ENSG00000198959

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA36491

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P21980, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2730

Drug and drug target database

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DrugBanki
DB04315, Guanosine-5'-Diphosphate
DB11254, Hexylresorcinol
DB00130, L-Glutamine

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
3015

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
TGM2

Domain mapping of disease mutations (DMDM)

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DMDMi
20141877

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources1 Publication
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002137072 – 687Protein-glutamine gamma-glutamyltransferase 2Add BLAST686

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei60PhosphoserineCombined sources1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi230 ↔ 370Alternate3 Publications
Disulfide bondi370 ↔ 371Alternate1 Publication
Modified residuei468N6-acetyllysineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki633Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Disulfide bond formation inactivates the calcium-dependent acyltransferase activity (PubMed:20547769). Cys-370 can form disulfide bonds with both Cys-230 and Cys-371: formation of a disulfide bond between Cys-230 and Cys-370 facilitates formation of the disulfide between Cys-370 and Cys-371, which promotes inactivation of the acyltransferase activity (PubMed:20547769). May also form interchain disulfids between Cys-230 and Cys-370 (PubMed:25192068). Ca2+ protects against disulfide bond formation and inactivation (PubMed:20547769).2 Publications
Auto-transglutaminated: Forms covalent cross-links mediated by transglutaminase between Gln-633 and the epsilon-amino group of a lysine residue of itself or HMGB1, forming homopolymers and heteropolymers, respectively.By similarity
S-nitrosylated, leading to inactivation of the acyltransferase activity.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Isopeptide bond, Phosphoprotein, S-nitrosylation

Proteomic databases

The CPTAC Assay portal

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CPTACi
CPTAC-1644
CPTAC-280
CPTAC-281

Encyclopedia of Proteome Dynamics

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EPDi
P21980

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P21980

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P21980

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
P21980

PeptideAtlas

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PeptideAtlasi
P21980

PRoteomics IDEntifications database

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PRIDEi
P21980

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
53947 [P21980-1]
53948 [P21980-2]
53949 [P21980-3]

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P21980, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P21980

MetOSite database of methionine sulfoxide sites

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MetOSitei
P21980

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
P21980

SwissPalm database of S-palmitoylation events

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SwissPalmi
P21980

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By retinoic acid.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000198959, Expressed in left coronary artery and 218 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P21980, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P21980, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000198959, Tissue enhanced (liver, placenta)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:25192068).

Interacts with phospholipase C; promoting alpha-1 adrenergic receptor signaling (PubMed:7592956).

Interacts with PLCD1 (By similarity).

By similarity2 Publications

Homooligomer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
112910, 126 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P21980

Database of interacting proteins

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DIPi
DIP-33557N

Protein interaction database and analysis system

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IntActi
P21980, 79 interactors

Molecular INTeraction database

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MINTi
P21980

STRING: functional protein association networks

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STRINGi
9606.ENSP00000355330

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P21980

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P21980, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1687
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P21980

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P21980

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QUSX, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT01040000240412

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013435_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P21980

Identification of Orthologs from Complete Genome Data

More...
OMAi
IKSVPWN

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P21980

TreeFam database of animal gene trees

More...
TreeFami
TF324278

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 3 hits
3.90.260.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR038765, Papain-like_cys_pep_sf
IPR002931, Transglutaminase-like
IPR036985, Transglutaminase-like_sf
IPR023608, Transglutaminase_animal
IPR013808, Transglutaminase_AS
IPR008958, Transglutaminase_C
IPR036238, Transglutaminase_C_sf
IPR001102, Transglutaminase_N

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00927, Transglut_C, 2 hits
PF01841, Transglut_core, 1 hit
PF00868, Transglut_N, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000459, TGM_EBP42, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00460, TGc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49309, SSF49309, 2 hits
SSF54001, SSF54001, 1 hit
SSF81296, SSF81296, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00547, TRANSGLUTAMINASES, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P21980-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MAEELVLERC DLELETNGRD HHTADLCREK LVVRRGQPFW LTLHFEGRNY
60 70 80 90 100
EASVDSLTFS VVTGPAPSQE AGTKARFPLR DAVEEGDWTA TVVDQQDCTL
110 120 130 140 150
SLQLTTPANA PIGLYRLSLE ASTGYQGSSF VLGHFILLFN AWCPADAVYL
160 170 180 190 200
DSEEERQEYV LTQQGFIYQG SAKFIKNIPW NFGQFEDGIL DICLILLDVN
210 220 230 240 250
PKFLKNAGRD CSRRSSPVYV GRVVSGMVNC NDDQGVLLGR WDNNYGDGVS
260 270 280 290 300
PMSWIGSVDI LRRWKNHGCQ RVKYGQCWVF AAVACTVLRC LGIPTRVVTN
310 320 330 340 350
YNSAHDQNSN LLIEYFRNEF GEIQGDKSEM IWNFHCWVES WMTRPDLQPG
360 370 380 390 400
YEGWQALDPT PQEKSEGTYC CGPVPVRAIK EGDLSTKYDA PFVFAEVNAD
410 420 430 440 450
VVDWIQQDDG SVHKSINRSL IVGLKISTKS VGRDEREDIT HTYKYPEGSS
460 470 480 490 500
EEREAFTRAN HLNKLAEKEE TGMAMRIRVG QSMNMGSDFD VFAHITNNTA
510 520 530 540 550
EEYVCRLLLC ARTVSYNGIL GPECGTKYLL NLNLEPFSEK SVPLCILYEK
560 570 580 590 600
YRDCLTESNL IKVRALLVEP VINSYLLAER DLYLENPEIK IRILGEPKQK
610 620 630 640 650
RKLVAEVSLQ NPLPVALEGC TFTVEGAGLT EEQKTVEIPD PVEAGEEVKV
660 670 680
RMDLLPLHMG LHKLVVNFES DKLKAVKGFR NVIIGPA
Length:687
Mass (Da):77,329
Last modified:January 23, 2002 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i7DA33FF335DE7B37
GO
Isoform 2 (identifier: P21980-2) [UniParc]FASTAAdd to basket
Also known as: TGase-S1 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     539-548: EKSVPLCILY → GKALCSWSIC
     549-687: Missing.

Show »
Length:548
Mass (Da):61,678
Checksum:i8C2F43A4D1029AC2
GO
Isoform 3 (identifier: P21980-3) [UniParc]FASTAAdd to basket
Also known as: TGH2

The sequence of this isoform differs from the canonical sequence as follows:
     287-349: VLRCLGIPTR...SWMTRPDLQP → GELHAGMWVM...LSNSHPSSGC
     350-687: Missing.

Show »
Length:349
Mass (Da):38,671
Checksum:i37E1EE27C243CCC5
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A2A299A2A299_HUMAN
Protein-glutamine gamma-glutamyltra...
TGM2
280Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A2A2A0A2A2A0_HUMAN
Protein-glutamine gamma-glutamyltra...
TGM2
159Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti51E → Q in AAA63261 (PubMed:1670766).Curated1
Sequence conflicti186E → Q in AAA63261 (PubMed:1670766).Curated1
Sequence conflicti224V → G in AAA63261 (PubMed:1670766).Curated1
Sequence conflicti533N → T in AAA63261 (PubMed:1670766).Curated1
Sequence conflicti655L → V in AAA63261 (PubMed:1670766).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05255376R → H1 PublicationCorresponds to variant dbSNP:rs41274720EnsemblClinVar.1
Natural variantiVAR_055357214R → H1 PublicationCorresponds to variant dbSNP:rs45530133Ensembl.1
Natural variantiVAR_055358324Q → R1 PublicationCorresponds to variant dbSNP:rs45567334Ensembl.1
Natural variantiVAR_037998330M → R in patients with early-onset diabetes type 2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs141603506Ensembl.1
Natural variantiVAR_037999331I → N in patients with early-onset diabetes type 2; unknown pathological significance. 1 Publication1
Natural variantiVAR_055359436R → W1 PublicationCorresponds to variant dbSNP:rs45629036Ensembl.1
Natural variantiVAR_052554536P → S1 PublicationCorresponds to variant dbSNP:rs45556333Ensembl.1
Natural variantiVAR_036554660G → V in a colorectal cancer sample; somatic mutation. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_006413287 – 349VLRCL…PDLQP → GELHAGMWVMSPGRGHEEHW SRNQDIPALVLPPATNTLNA LCGLEPVTTLSGPLSNSHPS SGC in isoform 3. 1 PublicationAdd BLAST63
Alternative sequenceiVSP_006414350 – 687Missing in isoform 3. 1 PublicationAdd BLAST338
Alternative sequenceiVSP_006411539 – 548EKSVPLCILY → GKALCSWSIC in isoform 2. 2 Publications10
Alternative sequenceiVSP_006412549 – 687Missing in isoform 2. 2 PublicationsAdd BLAST139

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
M55153 mRNA Translation: AAA63261.1
M98478 mRNA Translation: AAA36739.1
S81734 mRNA Translation: AAB36379.1
AY675221 mRNA Translation: AAT79353.1
AK291714 mRNA Translation: BAF84403.1
AK314618 mRNA Translation: BAG37184.1
DQ523828 Genomic DNA Translation: ABF47109.1
AL031651 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW76040.1
CH471077 Genomic DNA Translation: EAW76042.1
CH471077 Genomic DNA Translation: EAW76044.1
BC003551 mRNA Translation: AAH03551.1
AL512703 mRNA Translation: CAC21649.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS13302.1 [P21980-1]

Protein sequence database of the Protein Information Resource

More...
PIRi
A39045
A44302
S68092

NCBI Reference Sequences

More...
RefSeqi
NP_001310245.1, NM_001323316.1 [P21980-1]
NP_004604.2, NM_004613.3 [P21980-1]
NP_945189.1, NM_198951.2 [P21980-2]
XP_011527330.1, XM_011529028.1 [P21980-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000361475; ENSP00000355330; ENSG00000198959 [P21980-1]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7052

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7052

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Wikipedia

Tissue transglutaminase entry

NIEHS-SNPs
Protein Spotlight

Versatile - Issue 236 of May 2021

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M55153 mRNA Translation: AAA63261.1
M98478 mRNA Translation: AAA36739.1
S81734 mRNA Translation: AAB36379.1
AY675221 mRNA Translation: AAT79353.1
AK291714 mRNA Translation: BAF84403.1
AK314618 mRNA Translation: BAG37184.1
DQ523828 Genomic DNA Translation: ABF47109.1
AL031651 Genomic DNA No translation available.
CH471077 Genomic DNA Translation: EAW76040.1
CH471077 Genomic DNA Translation: EAW76042.1
CH471077 Genomic DNA Translation: EAW76044.1
BC003551 mRNA Translation: AAH03551.1
AL512703 mRNA Translation: CAC21649.1
CCDSiCCDS13302.1 [P21980-1]
PIRiA39045
A44302
S68092
RefSeqiNP_001310245.1, NM_001323316.1 [P21980-1]
NP_004604.2, NM_004613.3 [P21980-1]
NP_945189.1, NM_198951.2 [P21980-2]
XP_011527330.1, XM_011529028.1 [P21980-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1FAUmodel-A1-687[»]
1KV3X-ray2.80A/B/C/D/E/F1-687[»]
2Q3ZX-ray2.00A1-687[»]
3LY6X-ray3.14A/B/C1-687[»]
3S3JX-ray2.25A2-687[»]
3S3PX-ray2.50A2-687[»]
3S3SX-ray2.30A2-687[»]
4PYGX-ray2.80A/B/E1-687[»]
6A8PX-ray2.54A/B/C1-687[»]
6KZBX-ray3.35A/B/C1-687[»]
SMRiP21980
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi112910, 126 interactors
CORUMiP21980
DIPiDIP-33557N
IntActiP21980, 79 interactors
MINTiP21980
STRINGi9606.ENSP00000355330

Chemistry databases

BindingDBiP21980
ChEMBLiCHEMBL2730
DrugBankiDB04315, Guanosine-5'-Diphosphate
DB11254, Hexylresorcinol
DB00130, L-Glutamine
GuidetoPHARMACOLOGYi3015

PTM databases

GlyGeniP21980, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP21980
MetOSiteiP21980
PhosphoSitePlusiP21980
SwissPalmiP21980

Genetic variation databases

BioMutaiTGM2
DMDMi20141877

Proteomic databases

CPTACiCPTAC-1644
CPTAC-280
CPTAC-281
EPDiP21980
jPOSTiP21980
MassIVEiP21980
PaxDbiP21980
PeptideAtlasiP21980
PRIDEiP21980
ProteomicsDBi53947 [P21980-1]
53948 [P21980-2]
53949 [P21980-3]

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P21980, 17 sequenced antibodies

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3611, 1263 antibodies

The DNASU plasmid repository

More...
DNASUi
7052

Genome annotation databases

EnsembliENST00000361475; ENSP00000355330; ENSG00000198959 [P21980-1]
GeneIDi7052
KEGGihsa:7052

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7052
DisGeNETi7052

GeneCards: human genes, protein and diseases

More...
GeneCardsi
TGM2
HGNCiHGNC:11778, TGM2
HPAiENSG00000198959, Tissue enhanced (liver, placenta)
MIMi190196, gene
neXtProtiNX_P21980
OpenTargetsiENSG00000198959
PharmGKBiPA36491
VEuPathDBiHostDB:ENSG00000198959

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiENOG502QUSX, Eukaryota
GeneTreeiENSGT01040000240412
HOGENOMiCLU_013435_1_0_1
InParanoidiP21980
OMAiIKSVPWN
PhylomeDBiP21980
TreeFamiTF324278

Enzyme and pathway databases

BRENDAi2.3.2.13, 2681
PathwayCommonsiP21980
SignaLinkiP21980
SIGNORiP21980

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
7052, 5 hits in 1020 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
TGM2, human
EvolutionaryTraceiP21980

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
Tissue_transglutaminase

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
7052
PharosiP21980, Tchem

Protein Ontology

More...
PROi
PR:P21980
RNActiP21980, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000198959, Expressed in left coronary artery and 218 other tissues
ExpressionAtlasiP21980, baseline and differential
GenevisibleiP21980, HS

Family and domain databases

Gene3Di2.60.40.10, 3 hits
3.90.260.10, 1 hit
InterProiView protein in InterPro
IPR013783, Ig-like_fold
IPR014756, Ig_E-set
IPR038765, Papain-like_cys_pep_sf
IPR002931, Transglutaminase-like
IPR036985, Transglutaminase-like_sf
IPR023608, Transglutaminase_animal
IPR013808, Transglutaminase_AS
IPR008958, Transglutaminase_C
IPR036238, Transglutaminase_C_sf
IPR001102, Transglutaminase_N
PfamiView protein in Pfam
PF00927, Transglut_C, 2 hits
PF01841, Transglut_core, 1 hit
PF00868, Transglut_N, 1 hit
PIRSFiPIRSF000459, TGM_EBP42, 1 hit
SMARTiView protein in SMART
SM00460, TGc, 1 hit
SUPFAMiSSF49309, SSF49309, 2 hits
SSF54001, SSF54001, 1 hit
SSF81296, SSF81296, 1 hit
PROSITEiView protein in PROSITE
PS00547, TRANSGLUTAMINASES, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTGM2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P21980
Secondary accession number(s): E1P5V9
, Q16436, Q6B838, Q9BTN7, Q9H035, Q9UH35
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: January 23, 2002
Last modified: September 29, 2021
This is version 228 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
  7. Protein Spotlight
    Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries
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