dbPTM

PRDX1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRDX1_HUMAN
UniProt AC	Q06830
Protein Name	Peroxiredoxin-1
Gene Name	PRDX1
Organism	Homo sapiens (Human).
Sequence Length	199
Subcellular Localization	Cytoplasm . Melanosome . Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description	Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H(2)O(2). [PubMed: 9497357 Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation (By similarity]
Protein Sequence	MSSGNAKIGHPAPNFKATAVMPDGQFKDISLSDYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWVNTPKKQGGLGPMNIPLVSDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITVNDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSGNAKIG ------CCCCCCCCC	47.13	25944712
7	Acetylation	-MSSGNAKIGHPAPN -CCCCCCCCCCCCCC	53.90	19608861
7	Sumoylation	-MSSGNAKIGHPAPN -CCCCCCCCCCCCCC	53.90	-
7	Ubiquitination	-MSSGNAKIGHPAPN -CCCCCCCCCCCCCC	53.90	19608861
7	Sumoylation	-MSSGNAKIGHPAPN -CCCCCCCCCCCCCC	53.90	28112733
7	Malonylation	-MSSGNAKIGHPAPN -CCCCCCCCCCCCCC	53.90	26320211
16	Methylation	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	19608861
16	Acetylation	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	19608861
16	Sumoylation	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	-
16	Ubiquitination	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	19608861
16	Sumoylation	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	19608861
16	Malonylation	GHPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	26320211
18	Phosphorylation	PAPNFKATAVMPDGQ CCCCCEEEEECCCCC	22.00	23911959
21	Sulfoxidation	NFKATAVMPDGQFKD CCEEEEECCCCCEEE	2.02	21406390
27	Methylation	VMPDGQFKDISLSDY ECCCCCEEEEECHHC	46.38	19608861
27	Acetylation	VMPDGQFKDISLSDY ECCCCCEEEEECHHC	46.38	19608861
27	Ubiquitination	VMPDGQFKDISLSDY ECCCCCEEEEECHHC	46.38	21890473
27	Malonylation	VMPDGQFKDISLSDY ECCCCCEEEEECHHC	46.38	26320211
27	Ubiquitination	VMPDGQFKDISLSDY ECCCCCEEEEECHHC	46.38	21890473
30	Phosphorylation	DGQFKDISLSDYKGK CCCEEEEECHHCCCC	31.77	25159151
32	Phosphorylation	QFKDISLSDYKGKYV CEEEEECHHCCCCEE	31.91	25159151
34	Phosphorylation	KDISLSDYKGKYVVF EEEECHHCCCCEEEE	20.47	28152594
35	Acetylation	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	19608861
35	Succinylation	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	-
35	Ubiquitination	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	21890473
35	Malonylation	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	26320211
35	Succinylation	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	-
35	Ubiquitination	DISLSDYKGKYVVFF EEECHHCCCCEEEEE	54.65	21890473
37	Acetylation	SLSDYKGKYVVFFFY ECHHCCCCEEEEEEE	30.62	24889089
37	Ubiquitination	SLSDYKGKYVVFFFY ECHHCCCCEEEEEEE	30.62	-
52	S-nitrosocysteine	PLDFTFVCPTEIIAF CCCEEEECCCCEEEE	2.77	-
52	Glutathionylation	PLDFTFVCPTEIIAF CCCEEEECCCCEEEE	2.77	22833525
52	S-nitrosylation	PLDFTFVCPTEIIAF CCCEEEECCCCEEEE	2.77	15683743
67	Acetylation	SDRAEEFKKLNCQVI CHHHHHHHHCCCEEE	60.68	26051181
67	Sumoylation	SDRAEEFKKLNCQVI CHHHHHHHHCCCEEE	60.68	-
67	Ubiquitination	SDRAEEFKKLNCQVI CHHHHHHHHCCCEEE	60.68	-
68	Ubiquitination	DRAEEFKKLNCQVIG HHHHHHHHCCCEEEC	50.70	-
68	Malonylation	DRAEEFKKLNCQVIG HHHHHHHHCCCEEEC	50.70	26320211
68	Acetylation	DRAEEFKKLNCQVIG HHHHHHHHCCCEEEC	50.70	25953088
71	S-palmitoylation	EEFKKLNCQVIGASV HHHHHCCCEEECCEE	5.04	29575903
77	Phosphorylation	NCQVIGASVDSHFCH CCEEECCEECCCCEE	22.65	-
80	Phosphorylation	VIGASVDSHFCHLAW EECCEECCCCEEEEE	19.12	-
83	Glutathionylation	ASVDSHFCHLAWVNT CEECCCCEEEEEECC	1.84	22833525
83	S-palmitoylation	ASVDSHFCHLAWVNT CEECCCCEEEEEECC	1.84	29575903
90	Phosphorylation	CHLAWVNTPKKQGGL EEEEEECCCCCCCCC	27.19	25159151
92	Acetylation	LAWVNTPKKQGGLGP EEEECCCCCCCCCCC	56.54	25953088
92	Ubiquitination	LAWVNTPKKQGGLGP EEEECCCCCCCCCCC	56.54	-
92	Succinylation	LAWVNTPKKQGGLGP EEEECCCCCCCCCCC	56.54	23954790
93	Acetylation	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	26051181
93	Sumoylation	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	-
93	Ubiquitination	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	21890473
93	Sumoylation	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	-
93	Malonylation	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	26320211
93	Ubiquitination	AWVNTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	21890473
106	Phosphorylation	PMNIPLVSDPKRTIA CCCCCCCCCCCCCHH	56.74	20860994
109	Acetylation	IPLVSDPKRTIAQDY CCCCCCCCCCHHHHC	68.14	23954790
109	Ubiquitination	IPLVSDPKRTIAQDY CCCCCCCCCCHHHHC	68.14	-
109	Malonylation	IPLVSDPKRTIAQDY CCCCCCCCCCHHHHC	68.14	26320211
111	Phosphorylation	LVSDPKRTIAQDYGV CCCCCCCCHHHHCCE	27.13	28152594
116	Phosphorylation	KRTIAQDYGVLKADE CCCHHHHCCEEECCC	9.32	28152594
120	Ubiquitination	AQDYGVLKADEGISF HHHCCEEECCCCCCE	51.92	21906983
120	Acetylation	AQDYGVLKADEGISF HHHCCEEECCCCCCE	51.92	25953088
120	Sumoylation	AQDYGVLKADEGISF HHHCCEEECCCCCCE	51.92	28112733
126	Phosphorylation	LKADEGISFRGLFII EECCCCCCEEEEEEE	21.54	21815630
136	Acetylation	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	23954790
136	Ubiquitination	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	21890473
136	Ubiquitination	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	21890473
136	Succinylation	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	23954790
143	Phosphorylation	KGILRQITVNDLPVG CCEEEEEEECCCCCC	12.62	28450419
151	Methylation	VNDLPVGRSVDETLR ECCCCCCCCHHHHHH	33.47	-
152	Phosphorylation	NDLPVGRSVDETLRL CCCCCCCCHHHHHHH	28.17	21815630
156	Phosphorylation	VGRSVDETLRLVQAF CCCCHHHHHHHHHHH	16.83	-
158	Methylation	RSVDETLRLVQAFQF CCHHHHHHHHHHHCC	39.99	115488689
166	Phosphorylation	LVQAFQFTDKHGEVC HHHHHCCCCCCCCCC	33.10	21712546
168	Acetylation	QAFQFTDKHGEVCPA HHHCCCCCCCCCCCC	50.91	23954790
168	Ubiquitination	QAFQFTDKHGEVCPA HHHCCCCCCCCCCCC	50.91	-
173	S-nitrosocysteine	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	-
173	Glutathionylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	22833525
173	S-nitrosylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	15683743
173	S-palmitoylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	29575903
178	Methylation	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	51082937
178	Acetylation	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	25953088
178	Ubiquitination	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	21890473
178	Malonylation	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	26320211
178	Ubiquitination	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	21890473
181	Phosphorylation	PAGWKPGSDTIKPDV CCCCCCCCCCCCCCH	39.86	25159151
183	Phosphorylation	GWKPGSDTIKPDVQK CCCCCCCCCCCCHHH	32.37	25159151
183	O-linked_Glycosylation	GWKPGSDTIKPDVQK CCCCCCCCCCCCHHH	32.37	OGP
185	Acetylation	KPGSDTIKPDVQKSK CCCCCCCCCCHHHHH	36.94	23954790
185	Ubiquitination	KPGSDTIKPDVQKSK CCCCCCCCCCHHHHH	36.94	-
185	Sumoylation	KPGSDTIKPDVQKSK CCCCCCCCCCHHHHH	36.94	25114211
185	Malonylation	KPGSDTIKPDVQKSK CCCCCCCCCCHHHHH	36.94	26320211
190	Ubiquitination	TIKPDVQKSKEYFSK CCCCCHHHHHHHHHC	64.44	-
191	Phosphorylation	IKPDVQKSKEYFSKQ CCCCHHHHHHHHHCC	17.39	28152594
192	Sumoylation	KPDVQKSKEYFSKQK CCCHHHHHHHHHCCC	64.57	-
192	Ubiquitination	KPDVQKSKEYFSKQK CCCHHHHHHHHHCCC	64.57	-
192	Sumoylation	KPDVQKSKEYFSKQK CCCHHHHHHHHHCCC	64.57	-
192	Malonylation	KPDVQKSKEYFSKQK CCCHHHHHHHHHCCC	64.57	26320211
192	Acetylation	KPDVQKSKEYFSKQK CCCHHHHHHHHHCCC	64.57	26051181
194	Phosphorylation	DVQKSKEYFSKQK-- CHHHHHHHHHCCC--	19.52	27273156
194	Nitration	DVQKSKEYFSKQK-- CHHHHHHHHHCCC--	19.52	-
196	Phosphorylation	QKSKEYFSKQK---- HHHHHHHHCCC----	33.02	28152594
197	Acetylation	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	19608861
197	Ubiquitination	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	21890473
197	Malonylation	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	26320211
197	Ubiquitination	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	21890473

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
18	T	Phosphorylation	Kinase	STK4	Q13043	GPS
32	S	Phosphorylation	Kinase	PBK	Q96KB5	PSP
90	T	Phosphorylation	Kinase	CDK1	P06493	Uniprot
90	T	Phosphorylation	Kinase	STK4	Q13043	GPS
183	T	Phosphorylation	Kinase	STK4	Q13043	GPS
194	Y	Phosphorylation	Kinase	LCK	P06239	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:20589759

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
90	T	Phosphorylation		11986303
Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic 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 PRDX1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
G3P_HUMAN	GAPDH	physical	16169070
PRDX1_HUMAN	PRDX1	physical	9388242
PRDX4_HUMAN	PRDX4	physical	9388242
UBE3A_HUMAN	UBE3A	physical	20589759
PRDX2_HUMAN	PRDX2	physical	22939629
THIM_HUMAN	ACAA2	physical	22939629
PRDX5_HUMAN	PRDX5	physical	22939629
SODC_HUMAN	SOD1	physical	22939629
URM1_HUMAN	URM1	physical	22939629
YAP1_HUMAN	YAP1	physical	22939629
TPM3_HUMAN	TPM3	physical	22939629
RINI_HUMAN	RNH1	physical	22939629
UBP5_HUMAN	USP5	physical	22939629
TIPRL_HUMAN	TIPRL	physical	22939629
DNPH1_HUMAN	DNPH1	physical	22939629
ZFR_HUMAN	ZFR	physical	22939629
PRDX6_HUMAN	PRDX6	physical	22939629
RD23A_HUMAN	RAD23A	physical	22939629
UBE2H_HUMAN	UBE2H	physical	22939629
TKT_HUMAN	TKT	physical	22939629
SH3L2_HUMAN	SH3BGRL2	physical	22939629
TIPIN_HUMAN	TIPIN	physical	17141802
SMRD1_HUMAN	SMARCD1	physical	21988832
PRDX4_HUMAN	PRDX4	physical	21988832
SH21B_HUMAN	SH2D1B	physical	21988832
ASSY_HUMAN	ASS1	physical	26344197
MSH6_HUMAN	MSH6	physical	26344197
PRDX2_HUMAN	PRDX2	physical	26344197
PRDX3_HUMAN	PRDX3	physical	26344197
THIO_HUMAN	TXN	physical	26344197
UBC12_HUMAN	UBE2M	physical	26344197
TRIM4_HUMAN	TRIM4	physical	26524401

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 PRDX1_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-7; LYS-16; LYS-27; LYS-35AND LYS-197, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-183, AND MASSSPECTROMETRY.	17287340 [Abstract]
"Regulation of peroxiredoxin I activity by Cdc2-mediatedphosphorylation."; Chang T.-S., Jeong W., Choi S.Y., Yu S., Kang S.W., Rhee S.G.; J. Biol. Chem. 277:25370-25376(2002). Cited for: PHOSPHORYLATION AT THR-90, AND MUTAGENESIS OF THR-90.	11986303 [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-194, AND MASSSPECTROMETRY.	15592455 [Abstract]

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