TRIM72 report

I. Expression across cell types

Insufficient scRNA-seq data for expression of TRIM72 at single-cell level.

II. Expression across tissues

sc-RNAseq data

Insufficient scRNA-seq data for expression of TRIM72 at tissue level.

III. Associated gene sets

GO_0001778Biological processplasma membrane repair
GO_0051260Biological processprotein homooligomerization
GO_0016567Biological processprotein ubiquitination
GO_0046627Biological processnegative regulation of insulin receptor signaling pathway
GO_0010832Biological processnegative regulation of myotube differentiation
GO_0003012Biological processmuscle system process
GO_0006887Biological processexocytosis
GO_0007517Biological processmuscle organ development
GO_0043569Biological processnegative regulation of insulin-like growth factor receptor signaling pathway
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0042383Cellular componentsarcolemma
GO_0005737Cellular componentcytoplasm
GO_0030659Cellular componentcytoplasmic vesicle membrane
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0031435Molecular functionmitogen-activated protein kinase kinase kinase binding
GO_0042802Molecular functionidentical protein binding
GO_0001786Molecular functionphosphatidylserine binding
GO_0008270Molecular functionzinc ion binding
GO_0005515Molecular functionprotein binding
GO_0031624Molecular functionubiquitin conjugating enzyme binding

IV. Literature review

[source]
Gene nameTRIM72
Protein nameTripartite motif-containing protein 72 (Mitsugumin-53) (Mg53)
SynonymsMG53
DescriptionFUNCTION: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. 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. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity). .

AccessionsENST00000322122.8 [Q6ZMU5-1]
Q6ZMU5