dbPTM

PRDX1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	PRDX1_MOUSE
UniProt AC	P35700
Protein Name	Peroxiredoxin-1
Gene Name	Prdx1
Organism	Mus musculus (Mouse).
Sequence Length	199
Subcellular Localization	Cytoplasm .
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) (By similarity). Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation. [PubMed: 19766572]
Protein Sequence	MSSGNAKIGYPAPNFKATAVMPDGQFKDISLSEYKGKYVVFFFYPLDFTFVCPTEIIAFSDRADEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLISDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDEIIRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVNKSKEYFSKQK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSGNAKIG ------CCCCCCCCC	47.13	-
2	Phosphorylation	------MSSGNAKIG ------CCCCCCCCC	47.13	19854140
3	Phosphorylation	-----MSSGNAKIGY -----CCCCCCCCCC	34.47	19854140
7	Acetylation	-MSSGNAKIGYPAPN -CCCCCCCCCCCCCC	40.44	23806337
7	Malonylation	-MSSGNAKIGYPAPN -CCCCCCCCCCCCCC	40.44	26320211
7	Succinylation	-MSSGNAKIGYPAPN -CCCCCCCCCCCCCC	40.44	23806337
7	Ubiquitination	-MSSGNAKIGYPAPN -CCCCCCCCCCCCCC	40.44	-
10	Phosphorylation	SGNAKIGYPAPNFKA CCCCCCCCCCCCCEE	10.33	25521595
16	Malonylation	GYPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	26320211
16	Ubiquitination	GYPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	27667366
16	Acetylation	GYPAPNFKATAVMPD CCCCCCCEEEEECCC	52.01	23864654
27	Succinylation	VMPDGQFKDISLSEY ECCCCCEEEEEHHHC	46.38	23806337
27	Ubiquitination	VMPDGQFKDISLSEY ECCCCCEEEEEHHHC	46.38	27667366
27	Acetylation	VMPDGQFKDISLSEY ECCCCCEEEEEHHHC	46.38	22826441
27	Malonylation	VMPDGQFKDISLSEY ECCCCCEEEEEHHHC	46.38	26320211
30	Phosphorylation	DGQFKDISLSEYKGK CCCEEEEEHHHCCCE	35.66	25521595
32	Phosphorylation	QFKDISLSEYKGKYV CEEEEEHHHCCCEEE	31.89	25521595
35	Succinylation	DISLSEYKGKYVVFF EEEHHHCCCEEEEEE	44.89	-
35	Succinylation	DISLSEYKGKYVVFF EEEHHHCCCEEEEEE	44.89	23806337
35	Ubiquitination	DISLSEYKGKYVVFF EEEHHHCCCEEEEEE	44.89	27667366
35	Malonylation	DISLSEYKGKYVVFF EEEHHHCCCEEEEEE	44.89	26320211
35	Acetylation	DISLSEYKGKYVVFF EEEHHHCCCEEEEEE	44.89	23864654
67	Acetylation	SDRADEFKKLNCQVI CCCHHHHHHCCCEEE	55.06	2389719
67	Malonylation	SDRADEFKKLNCQVI CCCHHHHHHCCCEEE	55.06	26073543
68	Acetylation	DRADEFKKLNCQVIG CCHHHHHHCCCEEEC	50.70	22826441
68	Malonylation	DRADEFKKLNCQVIG CCHHHHHHCCCEEEC	50.70	26073543
71	S-palmitoylation	DEFKKLNCQVIGASV HHHHHCCCEEECCEE	5.04	28526873
83	S-palmitoylation	ASVDSHFCHLAWINT CEECCCEEEEEEECC	1.84	28526873
90	Phosphorylation	CHLAWINTPKKQGGL EEEEEECCCCCCCCC	27.61	-
93	Succinylation	AWINTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	23806337
93	Ubiquitination	AWINTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	27667366
93	Malonylation	AWINTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	26320211
93	Acetylation	AWINTPKKQGGLGPM EEECCCCCCCCCCCC	56.21	23806337
106	Phosphorylation	PMNIPLISDPKRTIA CCCCCCCCCCCCCHH	56.39	24759943
109	Malonylation	IPLISDPKRTIAQDY CCCCCCCCCCHHHHH	68.14	26320211
109	Acetylation	IPLISDPKRTIAQDY CCCCCCCCCCHHHHH	68.14	23864654
109	Ubiquitination	IPLISDPKRTIAQDY CCCCCCCCCCHHHHH	68.14	27667366
109	Succinylation	IPLISDPKRTIAQDY CCCCCCCCCCHHHHH	68.14	23954790
120	Acetylation	AQDYGVLKADEGISF HHHHCEEECCCCCCE	51.92	22826441
120	Ubiquitination	AQDYGVLKADEGISF HHHHCEEECCCCCCE	51.92	-
136	Acetylation	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	23806337
136	Succinylation	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	23806337
136	Ubiquitination	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	-
136	Malonylation	GLFIIDDKGILRQIT EEEEECCCCEEEEEE	44.07	26073543
152	Phosphorylation	NDLPVGRSVDEIIRL CCCCCCCCHHHHHHH	28.17	20469934
168	Acetylation	QAFQFTDKHGEVCPA HHHHCCCCCCCCCCC	50.91	23864654
168	Ubiquitination	QAFQFTDKHGEVCPA HHHHCCCCCCCCCCC	50.91	-
168	Malonylation	QAFQFTDKHGEVCPA HHHHCCCCCCCCCCC	50.91	26320211
173	S-nitrosylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	22588120
173	S-palmitoylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	28526873
173	S-nitrosocysteine	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	-
173	Glutathionylation	TDKHGEVCPAGWKPG CCCCCCCCCCCCCCC	1.34	24333276
178	Ubiquitination	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	-
178	Acetylation	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	22826441
178	Malonylation	EVCPAGWKPGSDTIK CCCCCCCCCCCCCCC	38.29	26320211
181	Phosphorylation	PAGWKPGSDTIKPDV CCCCCCCCCCCCCCC	39.86	21743459
183	Phosphorylation	GWKPGSDTIKPDVNK CCCCCCCCCCCCCCH	32.37	23684622
185	Malonylation	KPGSDTIKPDVNKSK CCCCCCCCCCCCHHH	36.94	26320211
185	Acetylation	KPGSDTIKPDVNKSK CCCCCCCCCCCCHHH	36.94	23864654
185	Ubiquitination	KPGSDTIKPDVNKSK CCCCCCCCCCCCHHH	36.94	-
190	Malonylation	TIKPDVNKSKEYFSK CCCCCCCHHHHHHHC	63.85	26073543
190	Acetylation	TIKPDVNKSKEYFSK CCCCCCCHHHHHHHC	63.85	23864654
190	Ubiquitination	TIKPDVNKSKEYFSK CCCCCCCHHHHHHHC	63.85	-
192	Malonylation	KPDVNKSKEYFSKQK CCCCCHHHHHHHCCC	59.03	26320211
192	Acetylation	KPDVNKSKEYFSKQK CCCCCHHHHHHHCCC	59.03	22826441
192	Ubiquitination	KPDVNKSKEYFSKQK CCCCCHHHHHHHCCC	59.03	27667366
194	Phosphorylation	DVNKSKEYFSKQK-- CCCHHHHHHHCCC--	19.52	22499769
196	Phosphorylation	NKSKEYFSKQK---- CHHHHHHHCCC----	33.02	22499769
197	Malonylation	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	26320211
197	Ubiquitination	KSKEYFSKQK----- HHHHHHHCCC-----	52.81	27667366

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
194	Y	Phosphorylation	Kinase	SRC	P05480	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
90	T	Phosphorylation		-
Phosphorylated on Thr-90 during the M-phase, which leads to a 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_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ADX_HUMAN	FDX1	physical	26496610
RAD51_HUMAN	RAD51	physical	26496610
PRDX2_HUMAN	PRDX2	physical	26496610
TRIO_HUMAN	TRIO	physical	26496610
ZMYM1_HUMAN	ZMYM1	physical	26496610
TXND5_HUMAN	TXNDC5	physical	26496610

Drug and Disease Associations

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

Regulatory Network of PRDX1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-10, AND MASSSPECTROMETRY.	18034455 [Abstract]

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