dbPTM

PRDX6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRDX6_HUMAN
UniProt AC	P30041
Protein Name	Peroxiredoxin-6
Gene Name	PRDX6
Organism	Homo sapiens (Human).
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	MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVDWKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
18	Phosphorylation	APNFEANTTVGRIRF CCCCCCCCCEEEEEE	29.88	28857561
32	Phosphorylation	FHDFLGDSWGILFSH EEHHHCCCEEEEECC	25.96	22673903
44	Phosphorylation	FSHPRDFTPVCTTEL ECCCCCCCCCEEHHH	21.07	19664994
47	S-nitrosylation	PRDFTPVCTTELGRA CCCCCCCEEHHHHHH	4.03	25040305
48	Phosphorylation	RDFTPVCTTELGRAA CCCCCCEEHHHHHHH	24.44	21815630
49	Phosphorylation	DFTPVCTTELGRAAK CCCCCEEHHHHHHHH	24.88	23403867
56	Sumoylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	-
56	Ubiquitination	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	-
56	Sumoylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	-
56	2-Hydroxyisobutyrylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	-
56	Malonylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	26320211
56	Acetylation	TELGRAAKLAPEFAK HHHHHHHHHCHHHHH	44.17	25953088
63	Ubiquitination	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	21890473
63	Methylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	19608861
63	Sumoylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	19608861
63	2-Hydroxyisobutyrylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	-
63	Acetylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	19608861
63	Sumoylation	KLAPEFAKRNVKLIA HHCHHHHHCCCEEEE	50.23	-
72	Phosphorylation	NVKLIALSIDSVEDH CCEEEEEECCCHHHH	18.48	27251275
75	Phosphorylation	LIALSIDSVEDHLAW EEEEECCCHHHHHHH	26.24	28348404
83	Phosphorylation	VEDHLAWSKDINAYN HHHHHHHCCCCCCCC	18.16	-
84	Ubiquitination	EDHLAWSKDINAYNC HHHHHHCCCCCCCCC	52.50	-
84	Acetylation	EDHLAWSKDINAYNC HHHHHHCCCCCCCCC	52.50	26051181
89	Phosphorylation	WSKDINAYNCEEPTE HCCCCCCCCCCCCCC	18.83	21945579
91	S-nitrosocysteine	KDINAYNCEEPTEKL CCCCCCCCCCCCCCC	4.00	-
91	S-nitrosylation	KDINAYNCEEPTEKL CCCCCCCCCCCCCCC	4.00	19483679
91	Glutathionylation	KDINAYNCEEPTEKL CCCCCCCCCCCCCCC	4.00	22555962
95	Phosphorylation	AYNCEEPTEKLPFPI CCCCCCCCCCCCCCE	49.37	21945579
97	Acetylation	NCEEPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	26051181
97	Ubiquitination	NCEEPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	-
97	2-Hydroxyisobutyrylation	NCEEPTEKLPFPIID CCCCCCCCCCCCEEC	65.03	-
106	Methylation	PFPIIDDRNRELAIL CCCEECCCCHHHHHH	40.12	115488765
108	Methylation	PIIDDRNRELAILLG CEECCCCHHHHHHHC	41.00	115488757
122	Acetylation	GMLDPAEKDEKGMPV CCCCHHHCCCCCCCC	73.60	26051181
122	Sumoylation	GMLDPAEKDEKGMPV CCCCHHHCCCCCCCC	73.60	-
122	Ubiquitination	GMLDPAEKDEKGMPV CCCCHHHCCCCCCCC	73.60	-
125	Sumoylation	DPAEKDEKGMPVTAR CHHHCCCCCCCCEEE	71.31	-
125	Ubiquitination	DPAEKDEKGMPVTAR CHHHCCCCCCCCEEE	71.31	21906983
125	Acetylation	DPAEKDEKGMPVTAR CHHHCCCCCCCCEEE	71.31	26051181
125	Sumoylation	DPAEKDEKGMPVTAR CHHHCCCCCCCCEEE	71.31	-
141	Ubiquitination	VFVFGPDKKLKLSIL EEEECCCCCEEEEEE	64.24	-
141	Acetylation	VFVFGPDKKLKLSIL EEEECCCCCEEEEEE	64.24	25953088
142	Acetylation	FVFGPDKKLKLSILY EEECCCCCEEEEEEE	59.23	24887509
142	Sumoylation	FVFGPDKKLKLSILY EEECCCCCEEEEEEE	59.23	-
144	2-Hydroxyisobutyrylation	FGPDKKLKLSILYPA ECCCCCEEEEEEEEC	49.41	-
144	Acetylation	FGPDKKLKLSILYPA ECCCCCEEEEEEEEC	49.41	25953088
146	Phosphorylation	PDKKLKLSILYPATT CCCCEEEEEEEECCC	14.68	20068231
149	Phosphorylation	KLKLSILYPATTGRN CEEEEEEEECCCCCC	6.80	28152594
152	Phosphorylation	LSILYPATTGRNFDE EEEEEECCCCCCHHH	25.86	28152594
153	Phosphorylation	SILYPATTGRNFDEI EEEEECCCCCCHHHH	35.93	28152594
155	Methylation	LYPATTGRNFDEILR EEECCCCCCHHHHHH	38.25	115488773
166	Phosphorylation	EILRVVISLQLTAEK HHHHHHHHHEEECCC	9.84	20068231
170	Phosphorylation	VVISLQLTAEKRVAT HHHHHEEECCCCCCC	21.58	21406692
177	Phosphorylation	TAEKRVATPVDWKDG ECCCCCCCCCCCCCC	22.46	19664994
182	2-Hydroxyisobutyrylation	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	-
182	Sumoylation	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	-
182	Methylation	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	156701
182	Acetylation	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	26051181
182	Sumoylation	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	-
182	Ubiquitination	VATPVDWKDGDSVMV CCCCCCCCCCCEEEE	47.58	21906983
186	Phosphorylation	VDWKDGDSVMVLPTI CCCCCCCEEEEECCC	20.03	21712546
188	Sulfoxidation	WKDGDSVMVLPTIPE CCCCCEEEEECCCCH	2.72	21406390
192	Phosphorylation	DSVMVLPTIPEEEAK CEEEEECCCCHHHHH	45.03	20068231
199	Ubiquitination	TIPEEEAKKLFPKGV CCCHHHHHHHCCCCC	53.97	21906983
199	Sumoylation	TIPEEEAKKLFPKGV CCCHHHHHHHCCCCC	53.97	-
199	Acetylation	TIPEEEAKKLFPKGV CCCHHHHHHHCCCCC	53.97	26051181
199	Sumoylation	TIPEEEAKKLFPKGV CCCHHHHHHHCCCCC	53.97	-
200	Ubiquitination	IPEEEAKKLFPKGVF CCHHHHHHHCCCCCE	63.51	-
204	Sumoylation	EAKKLFPKGVFTKEL HHHHHCCCCCEECCC	61.44	-
204	Ubiquitination	EAKKLFPKGVFTKEL HHHHHCCCCCEECCC	61.44	-
204	Sumoylation	EAKKLFPKGVFTKEL HHHHHCCCCCEECCC	61.44	-
204	Acetylation	EAKKLFPKGVFTKEL HHHHHCCCCCEECCC	61.44	26051181
209	Acetylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	19608861
209	Succinylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	-
209	Malonylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	26320211
209	2-Hydroxyisobutyrylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	-
209	Succinylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	-
209	Ubiquitination	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	21890473
209	Sumoylation	FPKGVFTKELPSGKK CCCCCEECCCCCCCC	45.87	19608861
213	Phosphorylation	VFTKELPSGKKYLRY CEECCCCCCCCEEEE	75.71	24719451
215	2-Hydroxyisobutyrylation	TKELPSGKKYLRYTP ECCCCCCCCEEEECC	42.45	-
215	Acetylation	TKELPSGKKYLRYTP ECCCCCCCCEEEECC	42.45	21339330
216	Acetylation	KELPSGKKYLRYTPQ CCCCCCCCEEEECCC	53.71	21339330
217	Phosphorylation	ELPSGKKYLRYTPQP CCCCCCCEEEECCCC	10.41	22210691

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
177	T	Phosphorylation	Kinase	MAPK1	P28482	GPS
177	T	Phosphorylation	Kinase	MAPK-FAMILY	-	GPS
177	T	Phosphorylation	Kinase	MAPK	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
47	C	Oxidation	9497358
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	26830860
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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
NCF2_HUMAN	NCF2	physical	12121978
PRDX6_HUMAN	PRDX6	physical	9587003
RAGP1_HUMAN	RANGAP1	physical	22939629
TIM9_HUMAN	TIMM9	physical	22939629
SUCB2_HUMAN	SUCLG2	physical	22939629
SMAP_HUMAN	C11orf58	physical	22939629
RHOA_HUMAN	RHOA	physical	22939629
VATA_HUMAN	ATP6V1A	physical	22939629
TPIS_HUMAN	TPI1	physical	22939629
PREP_HUMAN	PITRM1	physical	22939629
TMEDA_HUMAN	TMED10	physical	22939629
TM189_HUMAN	TMEM189	physical	22939629
PUR4_HUMAN	PFAS	physical	22939629
RADI_HUMAN	RDX	physical	22939629
SSU72_HUMAN	SSU72	physical	22939629
PRDX6_HUMAN	PRDX6	physical	21988832
CASPA_HUMAN	CASP10	physical	20829884
CASP8_HUMAN	CASP8	physical	20829884
ALDR_HUMAN	AKR1B1	physical	26344197
ASSY_HUMAN	ASS1	physical	26344197
CD2AP_HUMAN	CD2AP	physical	26344197
ECI1_HUMAN	ECI1	physical	26344197
LGUL_HUMAN	GLO1	physical	26344197
G6PI_HUMAN	GPI	physical	26344197
GRHPR_HUMAN	GRHPR	physical	26344197
SCOT1_HUMAN	OXCT1	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
PRDX5_HUMAN	PRDX5	physical	26344197
STH_HUMAN	STH	physical	16186110
1433E_HUMAN	YWHAE	physical	21346153
SFTA1_HUMAN	SFTPA1	physical	16330552
GSTP1_HUMAN	GSTP1	physical	16401067
PRDX6_HUMAN	PRDX6	physical	16401067

Drug and Disease Associations

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

Regulatory Network of PRDX6_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-63 AND LYS-209, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-44, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-89, AND MASSSPECTROMETRY.	15592455 [Abstract]

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