TRIM72
entrez
493829
canonical
uniprot
Q6ZMU5
canonical
ensembl
ENSG00000177238
resolver
ensp
ENSP00000312675
resolver
genesymbol
TRIM72
resolver
genesymbol_syn
MG53
resolver
hgnc
HGNC:32671
resolver
uniprot
Q8N4X6
resolver
uniprot
Q8NBD9
resolver
uniprot_entry
TRI72_HUMAN
resolver
uniprot_sec
Q8N4X6
resolver
uniprot_sec
Q8NBD9
resolver
activity_regulation
ACTIVITY REGULATION: Specifically binds phosphatidylserine (PubMed:36944613). The binding to phospholipids enhances ubiquitination activity (By similarity). {ECO:0000250|UniProtKB:Q1XH17, ECO:0000269|PubMed:36944613}.
uniprot
proteins
amino_acid_sequence
MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA
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:36944613). Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (By similarity). 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 (By similarity). This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation (By similarity). Probably acts upstream of the Ca(2+)-dependent membrane resealing process (By similarity). Required for transport of DYSF to sites of cell injury during repair patch formation (By similarity). Regulates membrane budding and exocytosis (By similarity). May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). {ECO:0000250|UniProtKB:Q1XH17, ECO:0000269|PubMed:36944613}.
uniprot
proteins
mass_dalton
52731
uniprot
proteins
mutagenesis
MUTAGEN 95; /note="I->A: Disrupts membrane translocation upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 144; /note="C->S: No decrease in level upon treatment with hydrogen peroxide."; /evidence="ECO:0000269|PubMed:24487118"; MUTAGEN 169; /note="R->A: Reduced cell viability upon peroxide and saponin treatment. Reduced affinity for phospho-L-serine; fails to translocate to membrane and reduced cell viability upon peroxide and saponin treatment; when associated with A-180 and A-198."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 169; /note="R->E: Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 176; /note="L->A: Monomeric; fails to translocate to membrane; reduced cell viability upon peroxide and saponin treatment; when associated with A-179, A-183, A-186 and A-190."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 179; /note="M->A: Monomeric; fails to translocate to membrane; reduced cell viability upon peroxide and saponin treatment; when associated with A-176, A-183, A-186 and A-190."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 179; /note="M->E: Disrupts membrane translocation. Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 180; /note="R->A: Reduced cell viability upon peroxide and saponin treatment. Reduced affinity for phospho-L-serine; fails to translocate to membrane and reduced cell viability upon peroxide and saponin treatment; when associated with A-169 and A-198."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 180; /note="R->E: Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 183; /note="L->A: Monomeric; fails to translocate to membrane; reduced cell viability upon peroxide and saponin treatment; when associated with A-176, A-179, A-186 and A-190."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 186; /note="L->A: Monomeric; fails to translocate to membrane; reduced cell viability upon peroxide and saponin treatment; when associated with A-176, A-179, A-183 and A-190."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 190; /note="L->A: Monomeric; fails to translocate to membrane; reduced cell viability upon peroxide and saponin treatment; when associated with A-176, A-179, A-183 and A-186."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 198; /note="R->A: Reduced cell viability upon peroxide and saponin treatment. Reduced affinity for phospho-L-serine; fails to translocate to membrane and reduced cell viability upon peroxide and saponin treatment; when associated with A-169 and A-180."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 198; /note="R->E: Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 220; /note="R->A: Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 220; /note="R->E: Fails to translocate to membrane and reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 242; /note="C->S: Disrupts oligomerization and membrane translocation upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 272..281; /note="Missing: Abolishes binding to myoblast cell membrane."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 272; /note="F->A: Disrupts membrane translocation. Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 277; /note="W->A,E: Disrupts membrane translocation. Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 279; /note="K->A: Disrupts membrane translocation. Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 279; /note="K->D: Restores membrane translocation and cell viability upon peroxide and saponin treatment; when associated with K-433."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 368..371; /note="RRGR->EEGE: Abolishes binding to myoblast cell membrane."; /evidence="ECO:0000269|PubMed:37770719"; MUTAGEN 433; /note="D->A: Disrupts membrane translocation. Reduced cell viability upon peroxide and saponin treatment."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 433; /note="D->K: Restores membrane translocation and cell viability upon peroxide and saponin treatment; when associated with D-279."; /evidence="ECO:0000269|PubMed:36944613"; MUTAGEN 460..462; /note="KGK->DGD: Abolishes binding to myoblast cell membrane."; /evidence="ECO:0000269|PubMed:37770719
uniprot
proteins
pathway_participation
PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:36944613}.
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. {ECO:0000250}.; PTM: S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death. {ECO:0000269|PubMed:24487118}.
uniprot
proteins
protein_family
TRIM/RBCC family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
19967786
uniprot
proteins
pubmed
24487118
uniprot
proteins
pubmed
36053137
uniprot
proteins
pubmed
36944613
uniprot
proteins
pubmed
37770719
uniprot
proteins
sequence_length
477
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000269|PubMed:36944613}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:36944613, ECO:0000269|PubMed:37770719}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. {ECO:0000250, ECO:0000269|PubMed:36944613, ECO:0000269|PubMed:37770719}.
uniprot
proteins