Q6ZMU5 · TRI72_HUMAN
- ProteinTripartite motif-containing protein 72
- GeneTRIM72
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids477 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 Ca2+-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).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytoplasmic vesicle membrane | |
Cellular Component | sarcolemma | |
Molecular Function | identical protein binding | |
Molecular Function | mitogen-activated protein kinase kinase kinase binding | |
Molecular Function | phosphatidylserine binding | |
Molecular Function | ubiquitin conjugating enzyme binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | exocytosis | |
Biological Process | muscle organ development | |
Biological Process | muscle system process | |
Biological Process | negative regulation of insulin receptor signaling pathway | |
Biological Process | negative regulation of insulin-like growth factor receptor signaling pathway | |
Biological Process | negative regulation of myotube differentiation | |
Biological Process | plasma membrane repair | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein homooligomerization | |
Biological Process | protein ubiquitination |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameTripartite motif-containing protein 72
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6ZMU5
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 144 | No decrease in level upon treatment with hydrogen peroxide. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 637 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), disulfide bond.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000278130 | 1-477 | UniProt | Tripartite motif-containing protein 72 | |||
Sequence: MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA | |||||||
Modified residue | 144 | UniProt | S-nitrosocysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 189 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Disulfide bond | 242 | UniProt | Interchain | ||||
Sequence: C | |||||||
Modified residue | 255 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 255 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
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.
S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homooligomer; disulfide-linked. Interacts with DYSF and CAV3 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6ZMU5 | ABI2 Q9NYB9-2 | 3 | EBI-2341648, EBI-11096309 | |
BINARY | Q6ZMU5 | C1orf216 Q8TAB5 | 3 | EBI-2341648, EBI-747505 | |
BINARY | Q6ZMU5 | MED21 Q13503 | 3 | EBI-2341648, EBI-394678 | |
BINARY | Q6ZMU5 | MZT1 Q08AG7 | 3 | EBI-2341648, EBI-2637198 | |
BINARY | Q6ZMU5 | NMI Q13287 | 3 | EBI-2341648, EBI-372942 | |
BINARY | Q6ZMU5 | PPP3CA Q08209-2 | 3 | EBI-2341648, EBI-11959013 | |
BINARY | Q6ZMU5 | SMARCD1 Q96GM5 | 3 | EBI-2341648, EBI-358489 | |
BINARY | Q6ZMU5 | TCF12 Q99081 | 3 | EBI-2341648, EBI-722877 | |
BINARY | Q6ZMU5 | TCF12 Q99081-3 | 3 | EBI-2341648, EBI-11952764 | |
BINARY | Q6ZMU5 | TRIM72 Q6ZMU5 | 3 | EBI-2341648, EBI-2341648 | |
BINARY | Q6ZMU5 | ZNF655 Q8N720 | 3 | EBI-2341648, EBI-625509 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 14-57 | RING-type | ||||
Sequence: CPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQ | ||||||
Zinc finger | 81-122 | B box-type | ||||
Sequence: VPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPA | ||||||
Coiled coil | 135-169 | |||||
Sequence: QQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFR | ||||||
Domain | 271-475 | B30.2/SPRY | ||||
Sequence: DFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGA |
Sequence similarities
Belongs to the TRIM/RBCC family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q6ZMU5-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length477
- Mass (Da)52,731
- Last updated2007-02-20 v2
- Checksum2B4EE9A00318151F
Q6ZMU5-2
- Name2
- Differences from canonical
- 270-477: Missing
Sequence caution
Features
Showing features for sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 192 | in Ref. 1; BAD18630 | ||||
Sequence: R → C | ||||||
Alternative sequence | VSP_052318 | 270-477 | in isoform 2 | |||
Sequence: Missing | ||||||
Sequence conflict | 315 | in Ref. 1; BAC03506 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK090695 EMBL· GenBank· DDBJ | BAC03506.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK131485 EMBL· GenBank· DDBJ | BAD18630.1 EMBL· GenBank· DDBJ | mRNA | ||
AC009088 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC033211 EMBL· GenBank· DDBJ | AAH33211.1 EMBL· GenBank· DDBJ | mRNA |