Trim72
entrez
434246
canonical
uniprot
Q1XH17
canonical
ensembl
ENSMUSG00000042828
resolver
ensp
ENSMUSP00000079832
resolver
ensp
ENSMUSP00000101855
resolver
enst
ENSMUST00000081042
resolver
enst
ENSMUST00000106248
resolver
genesymbol
Trim72
resolver
genesymbol_syn
Mg53
resolver
uniprot
B2RWH7
resolver
uniprot
Q6NX76
resolver
uniprot_entry
TRI72_MOUSE
resolver
uniprot_sec
B2RWH7
resolver
uniprot_sec
Q6NX76
resolver
activity_regulation
ACTIVITY REGULATION: Specifically binds phosphatidylserine (PubMed:19043407, PubMed:37770719). The binding to phospholipids enhances ubiquitination activity (PubMed:37770719). {ECO:0000269|PubMed:19043407, ECO:0000269|PubMed:37770719}.
uniprot
proteins
amino_acid_sequence
MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA
uniprot
proteins
ec_number
2.3.2.27
uniprot
proteins
function
FUNCTION: Muscle-specific E3 ubiquitin-protein ligase that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites (PubMed:19043407, PubMed:37770719). Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:37770719). Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site (PubMed:19043407, PubMed:19202355). This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation (PubMed:19043407). Probably acts upstream of the Ca(2+)-dependent membrane resealing process (PubMed:19043407). Required for transport of DYSF to sites of cell injury during repair patch formation (PubMed:19043407). Regulates membrane budding and exocytosis (PubMed:19029292). May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (PubMed:19202355). {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407, ECO:0000269|PubMed:19202355, ECO:0000269|PubMed:19380584, ECO:0000269|PubMed:37770719}.
uniprot
proteins
mass_dalton
52817
uniprot
proteins
mutagenesis
MUTAGEN 14; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 17; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 29; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 34; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 37; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 53; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 55; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 56; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 57; /note="Q->R: Enhances ubiquitination activity. Enhances ubiquitination activity; when associated with E-207. Abolishes ubiquitination activity; when associated with R-74."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 74; /note="L->R: Abolishes ubiquitination activity; when associated with R-57."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 86; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 97; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 105; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 106; /note="G->R: Impairs binding to phosphatidylserine liposomes."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 108; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 110; /note="S->R: Impairs binding to phosphatidylserine liposomes."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 144; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 207; /note="R->E: Enhances ubiquitination activity; when associated with E-57."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 242; /note="C->A: Dominant-negative mutant that abolishes homooligomerization and function in membrane repair."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 272..281; /note="Missing: Abolishes binding to phosphatidylserine liposomes."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 313; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 368..371; /note="RRGR->EEGE: Abolishes binding to phosphatidylserine liposomes."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 456; /note="C->A: Does not affect homooligomerization."; /evidence="ECO:0000269|PubMed:19043407"; MUTAGEN 460..462; /note="KGK->DGD: Abolishes binding to phosphatidylserine liposomes."; /evidence="ECO:0000269|PubMed:37770719
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:37770719}.
uniprot
proteins
post_translational_modification
PTM: Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.; PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death. {ECO:0000250|UniProtKB:Q6ZMU5}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
19029292
uniprot
proteins
pubmed
19043407
uniprot
proteins
pubmed
19202355
uniprot
proteins
pubmed
19380584
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
37770719
uniprot
proteins
sequence_length
477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:19029292, ECO:0000269|PubMed:19043407}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
uniprot
proteins