TRI72_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TRI72_HUMAN
• UniProt AC: Q6ZMU5
• Protein Name: Tripartite motif-containing protein 72
• Gene Name: TRIM72 {ECO:0000312|HGNC:HGNC:32671}
• Organism: Homo sapiens (Human).
• 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 (By similarity)..
• Protein Sequence: MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA

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
110	Phosphorylation	LVCGVCASLGSHRGH HHHHHHHHCCCCCCC	28.30	27251275
113	Phosphorylation	GVCASLGSHRGHRLL HHHHHCCCCCCCCHH	18.46	27251275
130	Ubiquitination	AEAHARLKTQLPQQK HHHHHHHHHHCCHHH	28.77	27667366
144	S-nitrosocysteine	KLQLQEACMRKEKSV HHHHHHHHHHHHHHH	2.39	-
144	S-nitrosylation	KLQLQEACMRKEKSV HHHHHHHHHHHHHHH	2.39	24487118
150	Phosphorylation	ACMRKEKSVAVLEHQ HHHHHHHHHHHHEEH	19.19	28674151
189	Phosphorylation	FLAALEGSLDREAER HHHHHCCCHHHHHHH	20.09	30624053
232	Acetylation	VLEEVADKPQTEFLM HHHHHCCCHHHHHHH	29.32	26822725
255	Phosphorylation	LQKILAESPPPARLD HHHHHHHCCCCCEEE	36.78	27050516
305	Phosphorylation	AHPSLVVSSSGRRVE CCCEEEECCCCCEEE	16.00	26437602
306	Phosphorylation	HPSLVVSSSGRRVEC CCEEEECCCCCEEEC	25.79	-
307	Phosphorylation	PSLVVSSSGRRVECS CEEEECCCCCEEECC	28.90	26437602
317	Acetylation	RVECSEQKAPPAGED EEECCCCCCCCCCCC	59.83	30593081
405	Phosphorylation	KEPRALRSPERRPTR CCCCCCCCCCCCCCE	31.78	26437602

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

Oops, there are no upstream regulatory protein records of TRI72_HUMAN !!

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.	24487118
144	C	S-nitrosylation	S-nitrosylation at Cys-144 stabilizes TRIM72 and protects against oxidation-induced protein degradation and cell death.	24487118

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CAVN1_HUMAN	PTRF	physical	21343302
MYH9_HUMAN	MYH9	physical	22253476
UBE2H_HUMAN	UBE2H	physical	23965929
UBE2N_HUMAN	UBE2N	physical	23965929
FAK1_HUMAN	PTK2	physical	24344130

Drug and Disease Associations

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