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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Tripartite motif-containing protein 72
UniprotKB/SwissProt ID: Q1XH17 (Q1XH17)

Gene Name: Trim72

Organism: Mus musculus (Mouse)

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:19043407, PubMed:37770719). Its ubiquitination activity is mediated by E2 ubiquitin-conjugating enzymes UBE2D1, UBE2D2 and UBE2D3 (PubMed:37770719). 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 (PubMed:19043407, PubMed:19202355). This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation (PubMed:19043407). Probably acts upstream of the Ca(2+)-dependent membrane resealing process (PubMed:19043407). Required for transport of DYSF to sites of cell injury during repair patch formation (PubMed:19043407). Regulates membrane budding and exocytosis (PubMed:19029292). May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (PubMed:19202355)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Cell membrane, sarcolemma. Cytoplasmic vesicle membrane

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR001870 B30.2/SPRY
IPR043136 B30.2/SPRY_sf
IPR003879 Butyrophylin_SPRY
IPR013320 ConA-like_dom_sf
IPR006574 PRY
IPR003877 SPRY_dom
IPR050143 TRIM/RBCC
IPR027370 Znf-RING_euk
IPR000315 Znf_B-box
IPR001841 Znf_RING
IPR013083 Znf_RING/FYVE/PHD
IPR017907 Znf_RING_CS
The S-nitrosylation sites of Q1XH17
No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 144 PQQKMQLQEA C MRKEKTVAVL  CCCCCCHHHH H CCCCHHHHHC  2.39% 21278135
2 242 KPQTEFLMKF C LVTSRLQKIL  CCCCCCHHHH H CCCCHHHHHC  2.2% 21278135
3 313 VVSSSGRRVE C SDQKAPPAGE  CCCCCCHHHH H CCCCHHHHHC  5.06% 21278135
4 456 PGPVYPIFDV C WHDKGKNAQP  CCCCCCHHHH H CCCCHHHHHC  2.62% 21278135
5 86 EGLAQVPQGH C EEHLDPLSIY  CCCCCCHHHH H CCCCHHHHHC  9.32%
6 97 EEHLDPLSIY C EQDRTLVCGV  CCCCCCHHHH H CCCCHHHHHC  3.45%