dbPTM

PARK7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PARK7_HUMAN
UniProt AC	Q99497
Protein Name	Protein/nucleic acid deglycase DJ-1 {ECO:0000305\|PubMed:25416785, ECO:0000305\|PubMed:28596309}
Gene Name	PARK7 {ECO:0000312\|HGNC:HGNC:16369}
Organism	Homo sapiens (Human).
Sequence Length	189
Subcellular Localization	Cell membrane Lipid-anchor . Cytoplasm . Nucleus . Membrane raft . 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. [PubMed: 25416785]
Protein Sequence	MASKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGPYDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVLKD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MASKRALVI ------CCCCCEEEE	24.61	25944712
17	Sulfoxidation	LAKGAEEMETVIPVD EECCHHHHCCEEEHH	3.83	21406390
19	Phosphorylation	KGAEEMETVIPVDVM CCHHHHCCEEEHHHH	23.56	21406692
26	Sulfoxidation	TVIPVDVMRRAGIKV CEEEHHHHHHCCCEE	1.76	16517609
27	Methylation	VIPVDVMRRAGIKVT EEEHHHHHHCCCEEE	25.75	-
32	Acetylation	VMRRAGIKVTVAGLA HHHHCCCEEEEECCC	30.82	25953088
32	Malonylation	VMRRAGIKVTVAGLA HHHHCCCEEEEECCC	30.82	26320211
32	Ubiquitination	VMRRAGIKVTVAGLA HHHHCCCEEEEECCC	30.82	-
41	Ubiquitination	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	21890473
41	Acetylation	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	26051181
41	Malonylation	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	26320211
41	2-Hydroxyisobutyrylation	TVAGLAGKDPVQCSR EEECCCCCCCCCCCC	53.93	-
46	S-palmitoylation	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	23847046
46	S-nitrosylation	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	24105792
46	Glutathionylation	AGKDPVQCSRDVVIC CCCCCCCCCCCEEEC	3.52	22555962
47	Phosphorylation	GKDPVQCSRDVVICP CCCCCCCCCCEEECC	17.90	29507054
53	S-palmitoylation	CSRDVVICPDASLED CCCCEEECCCCCHHH	1.36	23847046
53	S-nitrosylation	CSRDVVICPDASLED CCCCEEECCCCCHHH	1.36	19483679
53	Glutathionylation	CSRDVVICPDASLED CCCCEEECCCCCHHH	1.36	22555962
53	S-nitrosocysteine	CSRDVVICPDASLED CCCCEEECCCCCHHH	1.36	-
57	Phosphorylation	VVICPDASLEDAKKE EEECCCCCHHHHHHH	39.41	26552605
62	2-Hydroxyisobutyrylation	DASLEDAKKEGPYDV CCCHHHHHHHCCCCE	64.77	-
62	Acetylation	DASLEDAKKEGPYDV CCCHHHHHHHCCCCE	64.77	25953088
62	Ubiquitination	DASLEDAKKEGPYDV CCCHHHHHHHCCCCE	64.77	-
63	Acetylation	ASLEDAKKEGPYDVV CCHHHHHHHCCCCEE	70.40	25038526
63	Ubiquitination	ASLEDAKKEGPYDVV CCHHHHHHHCCCCEE	70.40	-
67	Phosphorylation	DAKKEGPYDVVVLPG HHHHHCCCCEEEECC	32.02	28796482
83	Phosphorylation	NLGAQNLSESAAVKE CCCCCCCCHHHHHHH	36.73	21712546
85	Phosphorylation	GAQNLSESAAVKEIL CCCCCCHHHHHHHHH	20.39	21712546
89	Succinylation	LSESAAVKEILKEQE CCHHHHHHHHHHHHH	34.02	23954790
89	Ubiquitination	LSESAAVKEILKEQE CCHHHHHHHHHHHHH	34.02	-
93	Acetylation	AAVKEILKEQENRKG HHHHHHHHHHHHHCC	64.11	25953088
93	Succinylation	AAVKEILKEQENRKG HHHHHHHHHHHHHCC	64.11	23954790
93	Ubiquitination	AAVKEILKEQENRKG HHHHHHHHHHHHHCC	64.11	-
93	2-Hydroxyisobutyrylation	AAVKEILKEQENRKG HHHHHHHHHHHHHCC	64.11	-
99	Ubiquitination	LKEQENRKGLIAAIC HHHHHHHCCHHHHHH	70.43	-
106	Cysteine sulfinic acid (-SO2H)	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	-
106	Oxidation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	12939276
106	S-palmitoylation	KGLIAAICAGPTALL CCHHHHHHCCHHHHH	2.84	29575903
130	2-Hydroxyisobutyrylation	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	-
130	Ubiquitination	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	-
130	Sumoylation	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	15976810
130	Succinylation	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	23954790
130	Sumoylation	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	-
130	Acetylation	VTTHPLAKDKMMNGG CCCCCCCCCCCCCCC	66.61	23749302
132	2-Hydroxyisobutyrylation	THPLAKDKMMNGGHY CCCCCCCCCCCCCCC	39.06	-
132	Acetylation	THPLAKDKMMNGGHY CCCCCCCCCCCCCCC	39.06	23954790
133	Sulfoxidation	HPLAKDKMMNGGHYT CCCCCCCCCCCCCCC	3.46	16517609
134	Sulfoxidation	PLAKDKMMNGGHYTY CCCCCCCCCCCCCCC	5.33	16517609
139	Phosphorylation	KMMNGGHYTYSENRV CCCCCCCCCCCCCCE	15.62	21945579
140	Phosphorylation	MMNGGHYTYSENRVE CCCCCCCCCCCCCEE	18.20	21945579
141	Phosphorylation	MNGGHYTYSENRVEK CCCCCCCCCCCCEEE	13.56	21945579
142	Phosphorylation	NGGHYTYSENRVEKD CCCCCCCCCCCEEEC	22.16	21945579
148	Succinylation	YSENRVEKDGLILTS CCCCCEEECEEEEEE	54.99	27452117
148	2-Hydroxyisobutyrylation	YSENRVEKDGLILTS CCCCCEEECEEEEEE	54.99	-
148	Acetylation	YSENRVEKDGLILTS CCCCCEEECEEEEEE	54.99	23954790
148	Ubiquitination	YSENRVEKDGLILTS CCCCCEEECEEEEEE	54.99	21890473
154	Phosphorylation	EKDGLILTSRGPGTS EECEEEEEECCCCCC	14.91	21815630
155	Phosphorylation	KDGLILTSRGPGTSF ECEEEEEECCCCCCH	31.62	21712546
175	Ubiquitination	IVEALNGKEVAAQVK HHHHHCCCHHEEEEE	48.19	-
182	Succinylation	KEVAAQVKAPLVLKD CHHEEEEECCEEECC	32.01	23954790
182	Malonylation	KEVAAQVKAPLVLKD CHHEEEEECCEEECC	32.01	32601280
182	Ubiquitination	KEVAAQVKAPLVLKD CHHEEEEECCEEECC	32.01	-
182	Succinylation	KEVAAQVKAPLVLKD CHHEEEEECCEEECC	32.01	-
182	Acetylation	KEVAAQVKAPLVLKD CHHEEEEECCEEECC	32.01	25953088
188	2-Hydroxyisobutyrylation	VKAPLVLKD------ EECCEEECC------	54.64	-
188	Ubiquitination	VKAPLVLKD------ EECCEEECC------	54.64	-

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	PKACA	P17612	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:15525661
-	K	Ubiquitination	E3 ubiquitin ligase	TRAF6	Q9Y4K3	PMID:20634198

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
130	K	Sumoylation		12851414
Sumoylated on Lys-130 by PIAS2 or PIAS4; which is enhanced after ultraviolet irradiation and 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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EFCB6_HUMAN	EFCAB6	physical	12612053
PIAS2_HUMAN	PIAS2	physical	11477070
SODC_HUMAN	SOD1	physical	20406884
PRKN_HUMAN	PARK2	physical	15525661
PARK7_HUMAN	PARK7	physical	15525661
CHIP_HUMAN	STUB1	physical	15525661
PRKN_HUMAN	PARK2	physical	17846173
MTA1_HUMAN	MTA1	physical	21368136
CHD4_HUMAN	CHD4	physical	20127688
HDAC1_HUMAN	HDAC1	physical	20127688
HDAC2_HUMAN	HDAC2	physical	20127688
MBD3_HUMAN	MBD3	physical	20127688
MTA1_HUMAN	MTA1	physical	20127688
MTA2_HUMAN	MTA2	physical	20127688
P66B_HUMAN	GATAD2B	physical	20127688
RBBP4_HUMAN	RBBP4	physical	20127688
RBBP7_HUMAN	RBBP7	physical	20127688
TRAF6_HUMAN	TRAF6	physical	20634198
BBS1_HUMAN	BBS1	physical	21097510
CLCF1_HUMAN	CLCF1	physical	21097510
RF1M_HUMAN	MTRF1	physical	21097510
OTU7B_HUMAN	OTUD7B	physical	21097510
B2CL1_HUMAN	BCL2L1	physical	21852238
BAX_HUMAN	BAX	physical	21852238
PARK7_HUMAN	PARK7	physical	15894486
PARK7_HUMAN	PARK7	physical	15983381
SAE2_HUMAN	UBA2	physical	15983381
SUMO1_HUMAN	SUMO1	physical	15983381
UBC9_HUMAN	UBE2I	physical	15983381
DAXX_HUMAN	DAXX	physical	15983381
PINK1_HUMAN	PINK1	physical	16632486
PARK7_HUMAN	PARK7	physical	12796482
PARK7_HUMAN	PARK7	physical	12855764
PARK7_HUMAN	PARK7	physical	14665635
PARK7_HUMAN	PARK7	physical	14713311
MAP1B_HUMAN	MAP1B	physical	21645326
NDUA4_HUMAN	NDUFA4	physical	19822128
NU1M_HUMAN	ND1	physical	19822128
NDUS3_HUMAN	NDUFS3	physical	19822128
PRKN_HUMAN	PARK2	physical	19229105
PINK1_HUMAN	PINK1	physical	19229105
PARK7_HUMAN	PARK7	physical	17331951
P53_HUMAN	TP53	physical	18042550
PARK7_HUMAN	PARK7	physical	12761214
PARK7_HUMAN	PARK7	physical	20304780
CASA1_HUMAN	CSN1S1	physical	20304780
VMAT2_HUMAN	SLC18A2	physical	22554508
PTEN_HUMAN	PTEN	physical	21426932
NONO_HUMAN	NONO	physical	15790595
SFPQ_HUMAN	SFPQ	physical	15790595
ANDR_HUMAN	AR	physical	17510388
HIPK1_HUMAN	HIPK1	physical	16390825
PARK7_HUMAN	PARK7	physical	16390825
SYUA_HUMAN	SNCA	physical	15935068
SRBP2_HUMAN	SREBF2	physical	22666465
TYDP2_HUMAN	TDP2	physical	19023331
M3K5_HUMAN	MAP3K5	physical	20213747
PARK7_HUMAN	PARK7	physical	18922803
PTEN_HUMAN	PTEN	physical	19885556
HSP74_HUMAN	HSPA4	physical	20156966
BAG1_HUMAN	BAG1	physical	20156966
PARK7_HUMAN	PARK7	physical	20156966
FADD_HUMAN	FADD	physical	21785459
PRGC1_HUMAN	PPARGC1A	genetic	18689799
PRDX5_HUMAN	PRDX5	physical	22939629
PRDX2_HUMAN	PRDX2	physical	22939629
TALDO_HUMAN	TALDO1	physical	22939629
PARK7_HUMAN	PARK7	physical	12851414
GOPC_HUMAN	GOPC	physical	25416956
PRKN_HUMAN	PARK2	physical	24242043
ANXA7_HUMAN	ANXA7	physical	26344197
ENOA_HUMAN	ENO1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
ITPA_HUMAN	ITPA	physical	26344197
LYPA1_HUMAN	LYPLA1	physical	26344197
MIF_HUMAN	MIF	physical	26344197
E41L5_HUMAN	EPB41L5	physical	26496610
TR150_HUMAN	THRAP3	physical	29128334
THOC4_HUMAN	ALYREF	physical	29128334
CK084_HUMAN	C11orf84	physical	29128334
BCLF1_HUMAN	BCLAF1	physical	29128334
DREB_HUMAN	DBN1	physical	29128334
PABP1_HUMAN	PABPC1	physical	29128334
RNPS1_HUMAN	RNPS1	physical	29128334
MYCBP_HUMAN	MYCBP	physical	29128334
PAIRB_HUMAN	SERBP1	physical	29128334
THIO_HUMAN	TXN	physical	29128334
TMOD3_HUMAN	TMOD3	physical	29128334
ML12A_HUMAN	MYL12A	physical	29128334
PPM1B_HUMAN	PPM1B	physical	29128334
TPIS_HUMAN	TPI1	physical	29128334
ARF1_HUMAN	ARF1	physical	29128334
1433B_HUMAN	YWHAB	physical	29128334
CHTOP_HUMAN	CHTOP	physical	29128334
LIMA1_HUMAN	LIMA1	physical	29128334
PRDX6_HUMAN	PRDX6	physical	29128334
TRAP1_HUMAN	TRAP1	physical	29128334
TPM1_HUMAN	TPM1	physical	29128334
OAT_HUMAN	OAT	physical	29128334
1433Z_HUMAN	YWHAZ	physical	29128334
PPIA_HUMAN	PPIA	physical	29128334
TAB1_HUMAN	TAB1	physical	29128334
ILF2_HUMAN	ILF2	physical	29128334
HCD2_HUMAN	HSD17B10	physical	29128334
HNRDL_HUMAN	HNRNPDL	physical	29128334
DKC1_HUMAN	DKC1	physical	29128334
EF1G_HUMAN	EEF1G	physical	29128334
MDHM_HUMAN	MDH2	physical	29128334
PRDX3_HUMAN	PRDX3	physical	29128334
TPM3_HUMAN	TPM3	physical	29128334
HORN_HUMAN	HRNR	physical	29128334
TCPQ_HUMAN	CCT8	physical	29128334
IMDH2_HUMAN	IMPDH2	physical	29128334
EIF3B_HUMAN	EIF3B	physical	29128334
RA1L2_HUMAN	HNRNPA1L2	physical	29128334
1433T_HUMAN	YWHAQ	physical	29128334
RT18B_HUMAN	MRPS18B	physical	29128334
HDGR2_HUMAN	HDGFRP2	physical	29128334
ODPA_HUMAN	PDHA1	physical	29128334
SSBP_HUMAN	SSBP1	physical	29128334
ACTN1_HUMAN	ACTN1	physical	29128334
PRP4_HUMAN	PRPF4	physical	29128334
TMOD2_HUMAN	TMOD2	physical	29128334
GEMI4_HUMAN	GEMIN4	physical	29128334
ECHA_HUMAN	HADHA	physical	29128334
PININ_HUMAN	PNN	physical	29128334
SAP18_HUMAN	SAP18	physical	29128334
DLDH_HUMAN	DLD	physical	29128334
ODPB_HUMAN	PDHB	physical	29128334
RAB1A_HUMAN	RAB1A	physical	29128334
PDIA6_HUMAN	PDIA6	physical	29128334
EF2_HUMAN	EEF2	physical	29128334
WBP11_HUMAN	WBP11	physical	29128334
CPSF6_HUMAN	CPSF6	physical	29128334
TIF1B_HUMAN	TRIM28	physical	29128334
RT09_HUMAN	MRPS9	physical	29128334
MYH11_HUMAN	MYH11	physical	29128334
C1TC_HUMAN	MTHFD1	physical	29128334
H2A1B_HUMAN	HIST1H2AE	physical	29128334
BOLA2_HUMAN	BOLA2	physical	29128334

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
606324	Parkinson disease 7 (PARK7)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of PARK7_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-67, AND MASSSPECTROMETRY.	15592455 [Abstract]
Sumoylation
Reference	PubMed
"Proper SUMO-1 conjugation is essential to DJ-1 to exert its fullactivities."; Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C.,Seino C., Iguchi-Ariga S.M.M., Ariga H.; Cell Death Differ. 13:96-108(2006). Cited for: SUMOYLATION AT LYS-130, OXIDATION, SUBCELLULAR LOCATION, INDUCTION,AND FUNCTION.	15976810 [Abstract]

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