Tag | Content |
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CPLM ID | CPLM-012785 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Tripartite motif-containing protein 72 |
Protein Synonyms/Alias | Mitsugumin-53; Mg53 |
Gene Name | Trim72 |
Gene Synonyms/Alias | Mg53 |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
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137 | KTQLPQQKMQLQEAC | ubiquitination | [1] | 178 | AVGEQLGKMRMFLAA | ubiquitination | [1] | 398 | LEAHVEAKEPRALRT | ubiquitination | [1] | 462 | VCWHDKGKNAQPLLL | ubiquitination | [1] |
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Reference | [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | 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. |
Sequence Annotation | DOMAIN 271 475 B30.2/SPRY. ZN_FING 14 57 RING-type. ZN_FING 81 122 B box-type. DISULFID 242 242 Interchain. |
Keyword | Cell membrane; Coiled coil; Complete proteome; Cytoplasmic vesicle; Disulfide bond; Exocytosis; Membrane; Metal-binding; Reference proteome; Transport; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 477 AA |
Protein Sequence | MSAAPGLLRQ ELSCPLCLQL FDAPVTAECG HSFCRACLIR VAGEPAADGT VACPCCQAPT 60 RPQALSTNLQ LSRLVEGLAQ VPQGHCEEHL DPLSIYCEQD RTLVCGVCAS LGSHRGHRLL 120 PAAEAQARLK TQLPQQKMQL QEACMRKEKT VAVLEHQLVE VEETVRQFRG AVGEQLGKMR 180 MFLAALESSL DREAERVRGD AGVALRRELS SLNSYLEQLR QMEKVLEEVA DKPQTEFLMK 240 FCLVTSRLQK ILSESPPPAR LDIQLPVISD DFKFQVWKKM FRALMPALEE LTFDPSSAHP 300 SLVVSSSGRR VECSDQKAPP AGEDTRQFDK AVAVVAQQLL SQGEHYWEVE VGDKPRWALG 360 VMAADASRRG RLHAVPSQGL WLLGLRDGKI LEAHVEAKEP RALRTPERPP ARIGLYLSFA 420 DGVLAFYDAS NPDVLTPIFS FHERLPGPVY PIFDVCWHDK GKNAQPLLLV GPEQEQA 477 |
Gene Ontology | GO:0030659; C:cytoplasmic vesicle membrane; IDA:UniProtKB. GO:0042383; C:sarcolemma; IDA:UniProtKB. GO:0001786; F:phosphatidylserine binding; IDA:UniProtKB. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0006887; P:exocytosis; TAS:UniProtKB. GO:0006900; P:membrane budding; TAS:UniProtKB. GO:0007517; P:muscle organ development; IMP:UniProtKB. GO:0003012; P:muscle system process; IMP:UniProtKB. GO:0001778; P:plasma membrane repair; IMP:UniProtKB. GO:0051260; P:protein homooligomerization; IPI:UniProtKB. |
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