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Entry version 227 (02 Jun 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%5Fsection">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%5Fsection">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%5Fsection">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%5Fsection">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%5Fsection">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

    More...
    BRENDAi
    2.3.2.13, 2681

    Pathway Commons web resource for biological pathway data

    More...
    PathwayCommonsi
    P21980

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

    More...
    SignaLinki
    P21980

    SIGNOR Signaling Network Open Resource

    More...
    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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

    More...
    HGNCi
    HGNC:11778, TGM2

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    190196, gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_P21980

    Eukaryotic Pathogen, Vector and Host Database Resources

    More...
    VEuPathDBi
    HostDB:ENSG00000198959.11

    <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%5Fand%5Fbiotech%5Fsection">'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

    More...
    DisGeNETi
    7052

    Open Targets

    More...
    OpenTargetsi
    ENSG00000198959

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA36491

    Miscellaneous databases

    Pharos NIH Druggable Genome Knowledgebase

    More...
    Pharosi
    P21980, Tchem

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL2730

    Drug and drug target database

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

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    3015

    Genetic variation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    TGM2

    Domain mapping of disease mutations (DMDM)

    More...
    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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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

    More...
    CPTACi
    CPTAC-1644
    CPTAC-280
    CPTAC-281

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    P21980

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    P21980

    MassIVE - Mass Spectrometry Interactive Virtual Environment

    More...
    MassIVEi
    P21980

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

    More...
    PaxDbi
    P21980

    PeptideAtlas

    More...
    PeptideAtlasi
    P21980

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P21980

    ProteomicsDB: a multi-organism proteome resource

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

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    P21980

    MetOSite database of methionine sulfoxide sites

    More...
    MetOSitei
    P21980

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

    More...
    PhosphoSitePlusi
    P21980

    SwissPalm database of S-palmitoylation events

    More...
    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

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

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    P21980, baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    P21980, HS

    Organism-specific databases

    Human Protein Atlas

    More...
    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%5Fsection">'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%5Fsection">'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%5Fsection">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)

    More...
    BioGRIDi
    112910, 122 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...
    CORUMi
    P21980

    Database of interacting proteins

    More...
    DIPi
    DIP-33557N

    Protein interaction database and analysis system

    More...
    IntActi
    P21980, 79 interactors

    Molecular INTeraction database

    More...
    MINTi
    P21980

    STRING: functional protein association networks

    More...
    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
    ENSGT01010000222350

    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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Freferences%5Fsection">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

    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, 122 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

    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, 1250 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:ENSG00000198959.11

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiENOG502QUSX, Eukaryota
    GeneTreeiENSGT01010000222350
    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 997 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%5Fand%5Fisoforms">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: June 2, 2021
    This is version 227 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
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