TRIM72
Tripartite motif-containing protein 72
Also known as: MG53, TRI72_HUMAN
Cross-references: UniProt · Ensembl · Human Protein Atlas · GeneCards · NCBI Gene
Protein identityUniProt · HPA
- UniProt accession
- Q6ZMU5
- Gene
- TRIM72
- Ensembl
- ENSG00000177238
- Chromosome
- 16
- Canonical length
- 477 aa
- Protein class
- Predicted intracellular proteins, Transporters
- Subcellular location
- Nucleoplasm,Vesicles
- Quaternary structure
- Homodimer
OverviewNCBI Gene
Enables identical protein binding activity. Predicted to be involved in several processes, including plasma membrane repair; proteasome-mediated ubiquitin-dependent protein catabolic process; and protein homooligomerization. Predicted to act upstream of or within negative regulation of insulin receptor signaling pathway; negative regulation of insulin-like growth factor receptor signaling pathway; and negative regulation of myotube differentiation. Predicted to be located in cytoplasmic vesicle membrane. Predicted to be active in cytoplasm and sarcolemma. [provided by Alliance of Genome Resources, Jul 2025]
Canonical amino-acid sequenceUniProt
477 residues, UniProt reviewed canonical sequence.
>Q6ZMU5|TRIM72
1 MSAAPGLLHQ ELSCPLCLQL FDAPVTAECG HSFCRACLGR VAGEPAADGT VLCPCCQAPT
61 RPQALSTNLQ LARLVEGLAQ VPQGHCEEHL DPLSIYCEQD RALVCGVCAS LGSHRGHRLL
121 PAAEAHARLK TQLPQQKLQL QEACMRKEKS VAVLEHQLVE VEETVRQFRG AVGEQLGKMR
181 VFLAALEGSL DREAERVRGE AGVALRRELG SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK
241 YCLVTSRLQK ILAESPPPAR LDIQLPIISD DFKFQVWRKM FRALMPALEE LTFDPSSAHP
301 SLVVSSSGRR VECSEQKAPP AGEDPRQFDK AVAVVAHQQL SEGEHYWEVD VGDKPRWALG
361 VIAAEAPRRG RLHAVPSQGL WLLGLREGKI LEAHVEAKEP RALRSPERRP TRIGLYLSFG
421 DGVLSFYDAS DADALVPLFA FHERLPRPVY PFFDVCWHDK GKNAQPLLLV GPEGAEALocalizationUniProt · AlphaFold · HPA
Whether an antibody against TRIM72 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.
- Antibody reachability
- Cell surface
- Secreted
- No
- Transmembrane segments
- 0
- Mean surface accessibility (rSASA)
- 0.34
- Highest tissue expression
- 142 nTPM
Expression across tissuesHPA
Tissue
- skeletal muscle: 142 nTPM
- tongue: 40 nTPM
- cerebellum: 8.8 nTPM
- salivary gland: 2.4 nTPM
- prostate: 1.7 nTPM
- esophagus: 1 nTPM
Single-cell type
- thymic myoid cells: 264 nCPM
- myonuclei: 233 nCPM
- epididymal basal cells: 61 nCPM
- myosatellite cells: 50 nCPM
- pdcs: 48 nCPM
- breast myoepithelial cells: 34 nCPM
Immune cell
- basophil: 1.8 nTPM
- neutrophil: 1.4 nTPM
- plasmacytoid DC: 0.6 nTPM
- eosinophil: 0.5 nTPM
- naive B-cell: 0.5 nTPM
- NK-cell: 0.5 nTPM
Brain region
- cerebellum: 23 nTPM
- pons: 6.9 nTPM
- cerebral cortex: 6.2 nTPM
- white matter: 6.1 nTPM
- amygdala: 5.8 nTPM
- basal ganglia: 5.6 nTPM
ReferencesPubMed · IEDB
Publications for TRIM72 from three distinct lines of evidence, kept separate because they answer different questions: whether antibodies are directed at the protein, whether a B-cell epitope has been mapped on it, and whether a T-cell epitope has. Each is labelled with its source.
Reference: AutoantibodyPubMed
3 publications
- Pathogenic mechanisms of disease in idiopathic inflammatory myopathies: autoantibodies as clues.
2024 · Front Immunol · RCR 3.9 · 17 citations - Autoantibodies targeting TRIM72 compromise membrane repair and contribute to inflammatory myopathy.
2020 · J Clin Invest · RCR 0.9 · 19 citations - Anti-TRIM72 Autoantibodies in Idiopathic Inflammatory Myopathies.
2025 · medRxiv
Sources: PubMed — antigen-level antibody evidence from a custom retrieval. Records matching a controlled set of autoantibody terms (the MeSH descriptors Autoantibodies and Autoantigens, with title and abstract term variants) were obtained through NCBI E-utilities, and their titles and abstracts parsed for constructions that direct an antibody at a named protein rather than for co-occurrence. Captured names were resolved against UniProt nomenclature and each antigen adjudicated individually against the source text. Bibliographic records from PubMed and MeSH, U.S. National Library of Medicine; citation metrics from NIH iCite (Hutchins et al., PLoS Biology 2016). Titles link to PubMed; abstracts are not reproduced here. The NLM does not endorse this analysis.
Genetic constraint and essentialitygnomAD · DepMap
Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.
- gnomAD LOEUF (loss-of-function intolerance)
- 1.05
- gnomAD pLI
- 0
- gnomAD missense Z
- 1.45
- DepMap mean gene effect
- -0.16
- DepMap dependency class
- selective
Cancer expressionTCGA
Across TCGA tumor cohorts, this protein is over-expressed in roughly 3% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).
OntologyGO
Biological processes
- exocytosis
- innate immune response
- muscle organ development
- muscle system process
- negative regulation of insulin receptor signaling pathway
- negative regulation of insulin-like growth factor receptor signaling pathway
- negative regulation of myotube differentiation
- plasma membrane repair
- proteasome-mediated ubiquitin-dependent protein catabolic process
- protein homooligomerization
Molecular functions
- identical protein binding
- mitogen-activated protein kinase kinase kinase binding
- phosphatidylserine binding
- ubiquitin conjugating enzyme binding
- ubiquitin protein ligase activity
- zinc ion binding
Cellular components
Protein domainsUniProt · Pfam · InterPro
- B-box-type zinc finger
- Zinc finger, RING-type
- B30.2/SPRY domain
- SPRY domain
- Butyrophylin-like, SPRY domain
- SPRY-associated
- Zinc finger, RING/FYVE/PHD-type
- Concanavalin A-like lectin/glucanase domain superfamily
- Zinc finger, RING-type, conserved site
- B30.2/SPRY domain superfamily
- Tripartite motif-containing
- SPRY domain
- B-box zinc finger
- SPRY-associated domain
- zinc finger of C3HC4-type, RING
KeywordsUniProt
InteractionsUniProt · HPA
Protein binding partners of TRIM72 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.
Antibody and autoantibody relevanceSeroatlas analysis
Seroatlas reads TRIM72 as an antibody target. Whether an autoantibody or antibody against TRIM72 could matter depends on whether native TRIM72 is physically reachable, whether the body needs it intact, and whether it acts in a disease-relevant tissue.
TRIM72 is annotated at the cell surface, where native TRIM72 is exposed to circulating antibodies and is a prime autoantibody target that could block, deplete, or overstimulate it.
Annotation status
The present source text does not explicitly label TRIM72 as an autoantigen. Seroatlas presents hypothesis context only and does not manufacture a known-serology claim.
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