Tgm2
entrez
21817
canonical
uniprot
P21981
canonical
ensembl
ENSMUSG00000037820
resolver
ensp
ENSMUSP00000099411
resolver
enst
ENSMUST00000103122
resolver
genesymbol
Tgm2
resolver
uniprot
O88901
resolver
uniprot
Q3TLV2
resolver
uniprot
Q8C217
resolver
uniprot
Q91VG9
resolver
uniprot
Q9R1F7
resolver
uniprot_entry
TGM2_MOUSE
resolver
uniprot_sec
O88901
resolver
uniprot_sec
Q3TLV2
resolver
uniprot_sec
Q8C217
resolver
uniprot_sec
Q91VG9
resolver
uniprot_sec
Q9R1F7
resolver
activity_regulation
ACTIVITY REGULATION: Acyltransferase activity is regulated by the binding of GTP and Ca(2+): inactivated by GTP, which stabilizes its closed structure, thereby obstructing the accessibility of substrates to the active sites. In contrast, Ca(2+) acts as a cofactor by inducing conformational change to the active open form. In absence of Ca(2+), Mg(2+) may bind Ca(2+)-binding sites, promoting GTP-binding and subsequent inhibition of the acyltransferase activity. Extracellularly reduced and activated by CLIC3. {ECO:0000250|UniProtKB:P21980}.
uniprot
proteins
amino_acid_sequence
MAEELLLERCDLEIQANGRDHHTADLCQEKLVLRRGQRFRLTLYFEGRGYEASVDSLTFGAVTGPDPSEEAGTKARFSLSDNVEEGSWSASVLDQQDNVLSLQLCTPANAPIGLYRLSLEASTGYQGSSFVLGHFILLYNAWCPADDVYLDSEEERREYVLTQQGFIYQGSVKFIKSVPWNFGQFEDGILDTCLMLLDMNPKFLKNRSRDCSRRSSPIYVGRVVSAMVNCNDDQGVLLGRWDNNYGDGISPMAWIGSVDILRRWKEHGCQQVKYGQCWVFAAVACTVLRCLGIPTRVVTNYNSAHDQNSNLLIEYFRNEFGELESNKSEMIWNFHCWVESWMTRPDLQPGYEGWQAIDPTPQEKSEGTYCCGPVSVRAIKEGDLSTKYDAPFVFAEVNADVVDWIRQEDGSVLKSINRSLVVGQKISTKSVGRDDREDITHTYKYPEGSPEEREVFTKANHLNKLAEKEETGVAMRIRVGDSMSMGNDFDVFAHIGNDTSETRECRLLLCARTVSYNGVLGPECGTEDINLTLDPYSENSIPLRILYEKYSGCLTESNLIKVRGLLIEPAANSYLLAERDLYLENPEIKIRVLGEPKQNRKLVAEVSLKNPLSDPLYDCIFTVEGAGLTKEQKSVEVSDPVPAGDLVKARVDLFPTDIGLHKLVVNFQCDKLKSVKGYRNVIIGPA
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.2.13
uniprot
proteins
ec_number
3.4.-.-
uniprot
proteins
ec_number
3.5.1.44
uniprot
proteins
function
FUNCTION: 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 (By similarity). Involved in many biological processes, such as bone development, angiogenesis, wound healing, cellular differentiation, chromatin modification and apoptosis (By similarity). 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:11113189, PubMed:11274171, PubMed:20489165). Under physiological conditions, the protein cross-linking activity is inhibited by GTP; inhibition is relieved by Ca(2+) in response to various stresses (By similarity). When secreted, catalyzes cross-linking of proteins of the extracellular matrix, such as FN1 and SPP1 resulting in the formation of scaffolds (By similarity). 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:12810961, PubMed:15905580). 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:32116663). 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 (By similarity). Catalyzes serotonylation of 'Gln-5' of histone H3 (H3Q5ser) during serotonergic neuron differentiation, thereby facilitating transcription (By similarity). 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 (By similarity). Regulates vein remodeling by mediating serotonylation and subsequent inactivation of ATP2A2/SERCA2 (PubMed:32116663). Also acts as a protein deamidase by mediating the side chain deamidation of specific glutamine residues of proteins to glutamate (By similarity). Catalyzes specific deamidation of protein gliadin, a component of wheat gluten in the diet (By similarity). May also act as an isopeptidase cleaving the previously formed cross-links (By similarity). 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:11274171). {ECO:0000250|UniProtKB:P08587, ECO:0000250|UniProtKB:P21980, ECO:0000269|PubMed:11113189, ECO:0000269|PubMed:11274171, ECO:0000269|PubMed:12810961, ECO:0000269|PubMed:15905580, ECO:0000269|PubMed:20489165, ECO:0000269|PubMed:32116663}.
uniprot
proteins
mass_dalton
77061
uniprot
proteins
post_translational_modification
PTM: Disulfide bond formation inactivates the calcium-dependent acyltransferase activity. 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. May also form interchain disulfids between Cys-230 and Cys-370. Ca(2+) protects against disulfide bond formation and inactivation. {ECO:0000250|UniProtKB:P21980}.; PTM: Auto-transglutaminated: Forms covalent cross-links mediated by transglutaminase between Gln-632 and the epsilon-amino group of a lysine residue of itself or HMGB1, forming homopolymers and heteropolymers, respectively. {ECO:0000250|UniProtKB:P08587}.; PTM: S-nitrosylated, leading to inactivation of the acyltransferase activity. {ECO:0000269|PubMed:20489165}.
uniprot
proteins
protein_family
Transglutaminase family
uniprot
proteins
protein_family
Transglutaminase superfamily
uniprot
proteins
pubmed
10200571
uniprot
proteins
pubmed
10334875
uniprot
proteins
pubmed
11113189
uniprot
proteins
pubmed
11274171
uniprot
proteins
pubmed
12205028
uniprot
proteins
pubmed
12810961
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15905580
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
1670766
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19644512
uniprot
proteins
pubmed
20489165
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
32116663
uniprot
proteins
pubmed
8626785
uniprot
proteins
sequence_length
686
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:19644512}. Nucleus {ECO:0000250|UniProtKB:P21980}. Chromosome {ECO:0000250|UniProtKB:P21980}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:20489165}. Cell membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion {ECO:0000269|PubMed:19644512}. Note=Mainly localizes to the cytosol. Present at much lower level in the nucleus and chromatin. Also secreted via a non-classical secretion pathway to the extracellular matrix. {ECO:0000250|UniProtKB:P21980}.
uniprot
proteins