dbPTM

PARK7_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PARK7_RAT
UniProt AC	O88767
Protein Name	Protein/nucleic acid deglycase DJ-1 {ECO:0000250\|UniProtKB:Q99497}
Gene Name	Park7 {ECO:0000312\|RGD:621808}
Organism	Rattus norvegicus (Rat).
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. Also displays an apparent glyoxalase activity that in fact reflects its deglycase activity. 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. It is involved in neuroprotective mechanisms like the stabilization of NFE2L2 and PINK1 proteins, male fertility as a positive regulator of androgen signaling pathway as well as cell growth and transformation through, for instance, the modulation of NF-kappa-B signaling pathway. Eliminates hydrogen peroxide and protects cells against hydrogen peroxide-induced cell death. Required for correct mitochondrial morphology and function as well as for autophagy of dysfunctional mitochondria. Plays a role in regulating expression or stability of the mitochondrial uncoupling proteins SLC25A14 and SLC25A27 in dopaminergic neurons of the substantia nigra pars compacta and attenuates the oxidative stress induced by calcium entry into the neurons via L-type channels during pacemaking. Regulates astrocyte inflammatory responses, may modulate lipid rafts-dependent endocytosis in astrocytes and neuronal cells (By similarity). In pancreatic islets, involved in the maintenance of mitochondrial reactive oxygen species (ROS) levels and glucose homeostasis in an age- and diet dependent manner. Protects pancreatic beta cells from cell death induced by inflammatory and cytotoxic setting (By similarity). Binds to a number of mRNAs containing multiple copies of GG or CC motifs and partially inhibits their translation but dissociates following oxidative stress. Metal-binding protein able to bind copper as well as toxic mercury ions, enhances the cell protection mechanism against induced metal toxicity (By similarity). In macrophages, interacts with the NADPH oxidase subunit NCF1 to direct NADPH oxidase-dependent ROS production, and protects against sepsis (By similarity)..
Protein Sequence	MASKRALVILAKGAEEMETVIPVDIMRRAGIKVTVAGLAGKDPVQCSRDVVICPDTSLEEAKTQGPYDVVVLPGGNLGAQNLSESALVKEILKEQENRKGLIAAICAGPTALLAHEVGFGCKVTSHPLAKDKMMNGSHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEALSGKDMANQVKAPLVLKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASKRALVI ------CCCCCEEEE	24.61	-
34	Phosphorylation	RRAGIKVTVAGLAGK HHCCCEEEEECCCCC	10.31	28689409
46	S-nitrosocysteine	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	-
46	S-palmitoylation	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	-
46	S-nitrosylation	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	22178444
47	Phosphorylation	GKDPVQCSRDVVICP CCCCCCCCCCEEECC	17.90	28689409
53	S-nitrosocysteine	CSRDVVICPDTSLEE CCCCEEECCCCCHHH	1.36	-
53	S-palmitoylation	CSRDVVICPDTSLEE CCCCEEECCCCCHHH	1.36	-
53	S-nitrosylation	CSRDVVICPDTSLEE CCCCEEECCCCCHHH	1.36	22178444
67	Phosphorylation	EAKTQGPYDVVVLPG HHHHCCCCCEEEECC	28.35	-
93	Acetylation	ALVKEILKEQENRKG HHHHHHHHHHHCCCC	64.11	22902405
106	S-palmitoylation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
106	S-nitrosylation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	22178444
106	Oxidation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
106	Cysteine sulfinic acid (-SO2H)	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
121	S-nitrosocysteine	AHEVGFGCKVTSHPL HHHHCCCCEECCCCC	2.75	-
121	S-nitrosylation	AHEVGFGCKVTSHPL HHHHCCCCEECCCCC	2.75	22178444
130	Acetylation	VTSHPLAKDKMMNGS ECCCCCCCCCCCCCC	66.61	22902405
132	Acetylation	SHPLAKDKMMNGSHY CCCCCCCCCCCCCCC	39.06	22902405
137	Phosphorylation	KDKMMNGSHYSYSES CCCCCCCCCCCCCCC	17.78	23984901
139	Phosphorylation	KMMNGSHYSYSESRV CCCCCCCCCCCCCCE	15.82	23984901
140	Phosphorylation	MMNGSHYSYSESRVE CCCCCCCCCCCCCEE	19.43	23984901
141	Phosphorylation	MNGSHYSYSESRVEK CCCCCCCCCCCCEEE	14.86	23984901
142	Phosphorylation	NGSHYSYSESRVEKD CCCCCCCCCCCEEEC	24.13	23984901
144	Phosphorylation	SHYSYSESRVEKDGL CCCCCCCCCEEECCE	35.37	25575281
148	Acetylation	YSESRVEKDGLILTS CCCCCEEECCEEEEE	54.99	22902405
154	Phosphorylation	EKDGLILTSRGPGTS EECCEEEEECCCCCC	14.91	17564427
155	Phosphorylation	KDGLILTSRGPGTSF ECCEEEEECCCCCCH	31.62	17564427
182	Succinylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	-
182	Succinylation	KDMANQVKAPLVLKD CCHHHHCCCCEEECC	34.23	-
188	Acetylation	VKAPLVLKD------ CCCCEEECC------	54.64	22902405
188	Succinylation	VKAPLVLKD------ CCCCEEECC------	54.64	26843850

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

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
154	T	Phosphorylation	Kinase	PRKACA	P00517	GPS
155	S	Phosphorylation	Kinase	PRKACA	P00517	GPS

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.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of PARK7_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SYUA_RAT	Snca	physical	16854843
ENPL_RAT	Hsp90b1	physical	16854843
CALX_RAT	Canx	physical	16854843
CLH1_RAT	Cltc	physical	16854843
1433Z_RAT	Ywhaz	physical	16854843
HAP28_RAT	Pdap1	physical	16854843
CPSF5_RAT	Nudt21	physical	16854843
1433G_RAT	Ywhag	physical	16854843
OSCP1_RAT	Oscp1	physical	16854843
RS3_RAT	Rps3	physical	16854843
CH60_RAT	Hspd1	physical	16854843
RL24_RAT	Rpl24	physical	16854843
RL4_RAT	Rpl4	physical	16854843
ACTS_RAT	Acta1	physical	16854843
ACTC_RAT	Actc1	physical	16854843
ATPB_RAT	Atp5b	physical	16854843
ACLY_RAT	Acly	physical	16854843
COPB2_RAT	Copb2	physical	16854843
BASP1_RAT	Basp1	physical	16854843
CALR_RAT	Calr	physical	16854843
PARK7_RAT	Park7	physical	16854843
CATA_RAT	Cat	physical	16854843
SEPT7_RAT	Sept7	physical	16854843
TCPG_RAT	Cct3	physical	16854843
TCPD_RAT	Cct4	physical	16854843
COF1_RAT	Cfl1	physical	16854843
MDHC_RAT	Mdh1	physical	16854843
DPYL2_RAT	Dpysl2	physical	16854843
EDF1_RAT	Edf1	physical	16854843
EF1A1_RAT	Eef1a1	physical	16854843
EF2_RAT	Eef2	physical	16854843
HMGB1_RAT	Hmgb1	physical	16854843
RL27_RAT	Rpl27	physical	16854843
MYL6_RAT	Myl6l	physical	16854843
RS10_RAT	Rps10	physical	16854843
RS20_RAT	Rps20	physical	16854843
RS25_RAT	Rps25	physical	16854843
RS6_RAT	Rps6	physical	16854843
RL23A_RAT	Rpl23a	physical	16854843
RL32_RAT	Rpl32	physical	16854843
RL8_RAT	Rpl8	physical	16854843
MANF_RAT	Manf	physical	16854843
CYC_RAT	Cycs	physical	16854843
IF2G_RAT	Eif2s3x	physical	16854843
ERF1_RAT	Etf1	physical	16854843
T2FA_RAT	Gtf2f1	physical	16854843
LRC59_RAT	Lrrc59	physical	16854843
MAP1B_RAT	Map1b	physical	16854843
PHB_RAT	Phb	physical	16854843
GDIR1_RAT	Arhgdia	physical	16854843
RL23_RAT	Rpl23	physical	16854843
CC130_RAT	Ccdc130	physical	16854843
RL17_RAT	Rpl17	physical	16854843
SEP11_RAT	Sept11	physical	16854843
SYYC_RAT	Yars	physical	16854843
QCR6_RAT	Uqcrh	physical	16854843
HNRPK_RAT	Hnrnpk	physical	16854843
TCEA1_RAT	Tcea1	physical	16854843
TPM3_RAT	Tpm3	physical	16854843
NPM_RAT	Npm1	physical	16854843
ROA1_RAT	Hnrnpa1	physical	16854843
CLCA_RAT	Clta	physical	16854843
SUCA_RAT	Suclg1	physical	16854843
SODC_RAT	Sod1	physical	16854843
TPIS_RAT	Tpi1	physical	16854843
TBA1A_RAT	Tuba1a	physical	16854843
TBA1B_RAT	Tuba1b	physical	16854843
TBB5_RAT	Tubb5	physical	16854843
TERA_RAT	Vcp	physical	16854843
SEPT2_RAT	Sept2	physical	16854843

Drug and Disease Associations

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

Regulatory Network of PARK7_RAT

Related Literatures of Post-Translational Modification

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