PARK7_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: PARK7_MOUSE
• UniProt AC: Q99LX0
• Protein Name: Protein/nucleic acid deglycase DJ-1 {ECO:0000250|UniProtKB:Q99497}
• Gene Name: Park7 {ECO:0000312|MGI:MGI:2135637}
• Organism: Mus musculus (Mouse).
• Sequence Length: 189
• Subcellular Localization: Cell membrane ; Lipid-anchor . Cytoplasm . Membrane raft . Nucleus . Mitochondrion . Under normal conditions, located predominantly in the cytoplasm and, to a lesser extent, in the nucleus and mitochondrion. Translocates to the mitochondrion and subs
• Protein Description: Protein and nucleotide deglycase that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins or nucleotides and reactive carbonyl groups of glyoxals. Thus, functions as a protein deglycase that repairs methylglyoxal- and glyoxal-glycated proteins, and releases repaired proteins and lactate or glycolate, respectively. Deglycates cysteine, arginine and lysine residues in proteins, and thus reactivates these proteins by reversing glycation by glyoxals. Acts on early glycation intermediates (hemithioacetals and aminocarbinols), preventing the formation of advanced glycation endproducts (AGE) that cause irreversible damage. Also functions as a nucleotide deglycase able to repair glycated guanine in the free nucleotide pool (GTP, GDP, GMP, dGTP) and in DNA and RNA. Is thus involved in a major nucleotide repair system named guanine glycation repair (GG repair), dedicated to reversing methylglyoxal and glyoxal damage via nucleotide sanitization and direct nucleic acid repair (By similarity). Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. [PubMed: 22523093 Plays an important role in cell protection against oxidative stress and cell death acting as oxidative stress sensor and redox-sensitive chaperone and protease; functions probably related to its primary function]
• Protein Sequence: MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVMICPDTSLEDAKTQGPYDVVVLPGGNLGAQNLSESPMVKEILKEQESRKGLIAAICAGPTALLAHEVGFGCKVTTHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAPLVLKD

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
2	Acetylation	------MASKRALVI ------CCCCCEEEE	24.61	-
32	Ubiquitination	VMRRAGIKVTVAGLA HHHHCCCEEEEECCC	30.82	-
32	Malonylation	VMRRAGIKVTVAGLA HHHHCCCEEEEECCC	30.82	26320211
41	Ubiquitination	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	-
41	Acetylation	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	22826441
41	Malonylation	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	26320211
46	S-palmitoylation	AGKDPVQCSRDVMIC CCCCCCCCCCCEEEC	3.52	26165157
46	S-nitrosylation	AGKDPVQCSRDVMIC CCCCCCCCCCCEEEC	3.52	22588120
46	Glutathionylation	AGKDPVQCSRDVMIC CCCCCCCCCCCEEEC	3.52	24333276
46	S-nitrosocysteine	AGKDPVQCSRDVMIC CCCCCCCCCCCEEEC	3.52	-
47	Phosphorylation	GKDPVQCSRDVMICP CCCCCCCCCCEEECC	17.90	25521595
53	S-palmitoylation	CSRDVMICPDTSLED CCCCEEECCCCCHHH	1.03	28526873
53	S-nitrosylation	CSRDVMICPDTSLED CCCCEEECCCCCHHH	1.03	21278135
53	Glutathionylation	CSRDVMICPDTSLED CCCCEEECCCCCHHH	1.03	24333276
53	S-nitrosocysteine	CSRDVMICPDTSLED CCCCEEECCCCCHHH	1.03	-
56	Phosphorylation	DVMICPDTSLEDAKT CEEECCCCCHHHHHH	21.98	23984901
57	Phosphorylation	VMICPDTSLEDAKTQ EEECCCCCHHHHHHC	36.82	23984901
63	Phosphorylation	TSLEDAKTQGPYDVV CCHHHHHHCCCCCEE	40.24	26643407
67	Phosphorylation	DAKTQGPYDVVVLPG HHHHCCCCCEEEECC	28.35	26643407
89	Acetylation	LSESPMVKEILKEQE CCCCHHHHHHHHHHH	32.55	22826441
93	Ubiquitination	PMVKEILKEQESRKG HHHHHHHHHHHHHCC	64.11	27667366
93	Acetylation	PMVKEILKEQESRKG HHHHHHHHHHHHHCC	64.11	22826441
106	S-palmitoylation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	28680068
106	Oxidation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
106	Cysteine sulfinic acid (-SO2H)	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
130	Acetylation	VTTHPLAKDKMMNGS EECCCCCCCCCCCCC	66.61	23806337
132	Ubiquitination	THPLAKDKMMNGSHY CCCCCCCCCCCCCCC	39.06	-
132	Malonylation	THPLAKDKMMNGSHY CCCCCCCCCCCCCCC	39.06	26320211
137	Phosphorylation	KDKMMNGSHYSYSES CCCCCCCCCCCCCCC	17.78	29895711
139	Phosphorylation	KMMNGSHYSYSESRV CCCCCCCCCCCCCCE	15.82	29514104
140	Phosphorylation	MMNGSHYSYSESRVE CCCCCCCCCCCCCEE	19.43	29895711
141	Phosphorylation	MNGSHYSYSESRVEK CCCCCCCCCCCCEEE	14.86	29895711
142	Phosphorylation	NGSHYSYSESRVEKD CCCCCCCCCCCEEEC	24.13	29895711
144	Phosphorylation	SHYSYSESRVEKDGL CCCCCCCCCEEECCE	35.37	23684622
148	Malonylation	YSESRVEKDGLILTS CCCCCEEECCEEEEE	54.99	26320211
148	Ubiquitination	YSESRVEKDGLILTS CCCCCEEECCEEEEE	54.99	-
148	Acetylation	YSESRVEKDGLILTS CCCCCEEECCEEEEE	54.99	23806337
160	Phosphorylation	LTSRGPGTSFEFALA EEECCCCCCHHHHHH	33.12	26643407
161	Phosphorylation	TSRGPGTSFEFALAI EECCCCCCHHHHHHH	28.79	26643407
182	Malonylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	26320211
182	Succinylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	23806337
182	Acetylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	23806337
182	Ubiquitination	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	27667366
182	Succinylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	-

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

Oops, there are no upstream regulatory protein records of PARK7_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
130	K	Sumoylation	Sumoylated on Lys-130 by PIAS2 or PIAS4; which is essential for cell-growth promoting activity and transforming activity.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of PARK7_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB7B_MOUSE	5430435G22Rik	physical	21645620
RAB5B_MOUSE	Rab5b	physical	21645620
RAB4A_MOUSE	Rab4a	physical	21645620
RAB3A_MOUSE	Rab3a	physical	21645620
VAMP2_MOUSE	Vamp2	physical	21645620
SYPH_MOUSE	Syp	physical	21645620
SRBP2_MOUSE	Srebf2	physical	22666465
P53_MOUSE	Trp53	physical	19680261
TENA_MOUSE	Tnc	physical	19885556

Drug and Disease Associations

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