TRI72_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI72_MOUSE
• UniProt AC: Q1XH17
• Protein Name: Tripartite motif-containing protein 72
• Gene Name: Trim72 {ECO:0000312|MGI:MGI:3612190}
• Organism: Mus musculus (Mouse).
• Sequence Length: 477
• Subcellular Localization: Cell membrane, sarcolemma. Cytoplasmic vesicle membrane. Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine.
• Protein 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..
• Protein Sequence: MSAAPGLLRQELSCPLCLQLFDAPVTAECGHSFCRACLIRVAGEPAADGTVACPCCQAPTRPQALSTNLQLSRLVEGLAQVPQGHCEEHLDPLSIYCEQDRTLVCGVCASLGSHRGHRLLPAAEAQARLKTQLPQQKMQLQEACMRKEKTVAVLEHQLVEVEETVRQFRGAVGEQLGKMRMFLAALESSLDREAERVRGDAGVALRRELSSLNSYLEQLRQMEKVLEEVADKPQTEFLMKFCLVTSRLQKILSESPPPARLDIQLPVISDDFKFQVWKKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSDQKAPPAGEDTRQFDKAVAVVAQQLLSQGEHYWEVEVGDKPRWALGVMAADASRRGRLHAVPSQGLWLLGLRDGKILEAHVEAKEPRALRTPERPPARIGLYLSFADGVLAFYDASNPDVLTPIFSFHERLPGPVYPIFDVCWHDKGKNAQPLLLVGPEQEQA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
137	Ubiquitination	KTQLPQQKMQLQEAC HHHCCHHHHHHHHHH	24.30	22790023
144	S-nitrosocysteine	KMQLQEACMRKEKTV HHHHHHHHHHHHHHH	2.39	-
144	S-nitrosylation	KMQLQEACMRKEKTV HHHHHHHHHHHHHHH	2.39	21278135
178	Acetylation	AVGEQLGKMRMFLAA HHHHHHHHHHHHHHH	31.74	15626469
178	Ubiquitination	AVGEQLGKMRMFLAA HHHHHHHHHHHHHHH	31.74	22790023
242	S-nitrosocysteine	TEFLMKFCLVTSRLQ HHHHHHHHHHHHHHH	2.20	-
242	S-nitrosylation	TEFLMKFCLVTSRLQ HHHHHHHHHHHHHHH	2.20	21278135
253	Phosphorylation	SRLQKILSESPPPAR HHHHHHHHCCCCCCC	39.23	27742792
255	Phosphorylation	LQKILSESPPPARLD HHHHHHCCCCCCCEE	39.05	23737553
313	S-nitrosocysteine	SSGRRVECSDQKAPP CCCCEEECCCCCCCC	5.06	-
313	S-nitrosylation	SSGRRVECSDQKAPP CCCCEEECCCCCCCC	5.06	21278135
341	Phosphorylation	VVAQQLLSQGEHYWE HHHHHHHHCCCCEEE	44.74	-
377	Phosphorylation	GRLHAVPSQGLWLLG CCCEEECCCCEEEEE	30.22	-
398	Ubiquitination	LEAHVEAKEPRALRT EEEEEECCCCCCCCC	55.54	22790023
456	S-nitrosylation	VYPIFDVCWHDKGKN CEECEEEEECCCCCC	2.62	21278135
456	S-nitrosocysteine	VYPIFDVCWHDKGKN CEECEEEEECCCCCC	2.62	-
462	Ubiquitination	VCWHDKGKNAQPLLL EEECCCCCCCCCEEE	55.65	22790023

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of TRI72_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
144	C	Oxidation	S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.	19043407
144	C	S-nitrosylation	S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.	19043407

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TRI72_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE2H_MOUSE	Ube2h	physical	23965929

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.