dbPTM

PRDX6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRDX6_MOUSE
UniProt AC	O08709
Protein Name	Peroxiredoxin-6
Gene Name	Prdx6
Organism	Mus musculus (Mouse).
Sequence Length	224
Subcellular Localization	Cytoplasm . Lysosome . Also found in lung secretory organelles (lamellar bodies).
Protein Description	Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, and can therefore either reduce the oxidized sn-2 fatty acyl grup of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis..
Protein Sequence	MPGGLLLGDEAPNFEANTTIGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNGETPTEKLPFPIIDDKGRDLAILLGMLDPVEKDDNNMPVTARVVFIFGPDKKLKLSILYPATTGRNFDEILRVVDSLQLTGTKPVATPVDWKKGESVMVVPTLSEEEAKQCFPKGVFTKELPSGKKYLRYTPQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	APNFEANTTIGRIRF CCCCCCCCCEEEEEE	27.17	23984901
19	Phosphorylation	PNFEANTTIGRIRFH CCCCCCCCEEEEEEE	22.65	23984901
44	Phosphorylation	FSHPRDFTPVCTTEL ECCCCCCCCCEEHHH	21.07	25521595
47	S-nitrosocysteine	PRDFTPVCTTELGRA CCCCCCCEEHHHHHH	4.03	-
47	S-palmitoylation	PRDFTPVCTTELGRA CCCCCCCEEHHHHHH	4.03	28526873
47	S-nitrosylation	PRDFTPVCTTELGRA CCCCCCCEEHHHHHH	4.03	24895380
47	Glutathionylation	PRDFTPVCTTELGRA CCCCCCCEEHHHHHH	4.03	24333276
48	Phosphorylation	RDFTPVCTTELGRAA CCCCCCEEHHHHHHH	24.44	25777480
49	Phosphorylation	DFTPVCTTELGRAAK CCCCCEEHHHHHHHH	24.88	25777480
56	Ubiquitination	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	-
56	Malonylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	26320211
63	Succinylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	23954790
63	Malonylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	26320211
63	Acetylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	21728379
63	Ubiquitination	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	-
72	Phosphorylation	NVKLIALSIDSVEDH CCEEEEEECCCHHHH	18.48	23984901
75	Phosphorylation	LIALSIDSVEDHLAW EEEEECCCHHHHHHH	26.24	23984901
83	Phosphorylation	VEDHLAWSKDINAYN HHHHHHHHCCCCCCC	18.16	22817900
89	Phosphorylation	WSKDINAYNGETPTE HHCCCCCCCCCCCCC	21.15	29899451
93	Phosphorylation	INAYNGETPTEKLPF CCCCCCCCCCCCCCC	36.59	25521595
95	Phosphorylation	AYNGETPTEKLPFPI CCCCCCCCCCCCCCE	53.85	23737553
97	Malonylation	NGETPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	26073543
97	Acetylation	NGETPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	22733758
97	Ubiquitination	NGETPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	-
106	Malonylation	PFPIIDDKGRDLAIL CCCEECCCCCCHHHH	52.69	26320211
106	Acetylation	PFPIIDDKGRDLAIL CCCEECCCCCCHHHH	52.69	22826441
106	Ubiquitination	PFPIIDDKGRDLAIL CCCEECCCCCCHHHH	52.69	-
122	Acetylation	GMLDPVEKDDNNMPV CCCCCCCCCCCCCEE	71.29	66728717
141	Acetylation	VFIFGPDKKLKLSIL EEEECCCCCEEEEEE	64.24	22826441
141	Succinylation	VFIFGPDKKLKLSIL EEEECCCCCEEEEEE	64.24	23954790
144	Malonylation	FGPDKKLKLSILYPA ECCCCCEEEEEEEEC	49.41	26320211
144	Ubiquitination	FGPDKKLKLSILYPA ECCCCCEEEEEEEEC	49.41	-
144	Acetylation	FGPDKKLKLSILYPA ECCCCCEEEEEEEEC	49.41	22826441
146	Phosphorylation	PDKKLKLSILYPATT CCCCEEEEEEEECCC	14.68	22871156
152	O-linked_Glycosylation	LSILYPATTGRNFDE EEEEEECCCCCCHHH	25.86	21606357
173	Acetylation	SLQLTGTKPVATPVD HCCCCCCCCCCCCCC	38.55	22733758
173	Malonylation	SLQLTGTKPVATPVD HCCCCCCCCCCCCCC	38.55	26320211
173	Ubiquitination	SLQLTGTKPVATPVD HCCCCCCCCCCCCCC	38.55	-
177	Phosphorylation	TGTKPVATPVDWKKG CCCCCCCCCCCCCCC	24.87	21262967
182	Acetylation	VATPVDWKKGESVMV CCCCCCCCCCCEEEE	46.57	23954790
182	Ubiquitination	VATPVDWKKGESVMV CCCCCCCCCCCEEEE	46.57	-
182	Malonylation	VATPVDWKKGESVMV CCCCCCCCCCCEEEE	46.57	26320211
182	Succinylation	VATPVDWKKGESVMV CCCCCCCCCCCEEEE	46.57	23954790
183	Ubiquitination	ATPVDWKKGESVMVV CCCCCCCCCCEEEEE	64.75	-
183	Malonylation	ATPVDWKKGESVMVV CCCCCCCCCCEEEEE	64.75	26320211
183	Acetylation	ATPVDWKKGESVMVV CCCCCCCCCCEEEEE	64.75	7609747
186	Phosphorylation	VDWKKGESVMVVPTL CCCCCCCEEEEECCC	24.96	23140645
192	Phosphorylation	ESVMVVPTLSEEEAK CEEEEECCCCHHHHH	31.16	25521595
194	Phosphorylation	VMVVPTLSEEEAKQC EEEECCCCHHHHHHH	45.50	25521595
199	Malonylation	TLSEEEAKQCFPKGV CCCHHHHHHHCCCCC	51.37	26320211
199	Acetylation	TLSEEEAKQCFPKGV CCCHHHHHHHCCCCC	51.37	22826441
199	Ubiquitination	TLSEEEAKQCFPKGV CCCHHHHHHHCCCCC	51.37	-
201	S-nitrosocysteine	SEEEAKQCFPKGVFT CHHHHHHHCCCCCEE	6.59	-
201	Glutathionylation	SEEEAKQCFPKGVFT CHHHHHHHCCCCCEE	6.59	24333276
201	S-nitrosylation	SEEEAKQCFPKGVFT CHHHHHHHCCCCCEE	6.59	21278135
204	Malonylation	EAKQCFPKGVFTKEL HHHHHCCCCCEEEEC	47.67	26320211
209	Succinylation	FPKGVFTKELPSGKK CCCCCEEEECCCCCE	45.87	23806337
209	Malonylation	FPKGVFTKELPSGKK CCCCCEEEECCCCCE	45.87	26320211
209	Ubiquitination	FPKGVFTKELPSGKK CCCCCEEEECCCCCE	45.87	-
209	Succinylation	FPKGVFTKELPSGKK CCCCCEEEECCCCCE	45.87	-
209	Acetylation	FPKGVFTKELPSGKK CCCCCEEEECCCCCE	45.87	22826441

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
93	T	Phosphorylation	Kinase	MAPK14	P47811	GPS
177	T	Phosphorylation	Kinase	MAPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
47	C	Oxidation	26830860
Irreversibly inactivated by overoxidation of Cys-47 to sulfinic acid (Cys-SO(2)H) and sulfonic acid (Cys-SO(3)H) forms upon oxidative stress.
177	T	Phosphorylation	-
Phosphorylation at Thr-177 by MAP kinases increases the phospholipase activity of the enzyme (By similarity).

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 PRDX6_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of PRDX6_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of PRDX6_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93, AND MASSSPECTROMETRY.	17203969 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-89, AND MASSSPECTROMETRY.	18034455 [Abstract]

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