dbPTM

GSTP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GSTP1_MOUSE
UniProt AC	P19157
Protein Name	Glutathione S-transferase P 1
Gene Name	Gstp1
Organism	Mus musculus (Mouse).
Sequence Length	210
Subcellular Localization	Cytoplasm. Mitochondrion. Nucleus. The 83 N-terminal amino acids function as un uncleaved transit peptide, and arginine residues within it are crucial for mitochondrial localization..
Protein Description	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Can metabolize 1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration (By similarity)..
Protein Sequence	MPPYTIVYFPVRGRCEAMRMLLADQGQSWKEEVVTIDTWMQGLLKPTCLYGQLPKFEDGDLTLYQSNAILRHLGRSLGLYGKNQREAAQMDMVNDGVEDLRGKYVTLIYTNYENGKNDYVKALPGHLKPFETLLSQNQGGKAFIVGDQISFADYNLLDLLLIHQVLAPGCLDNFPLLSAYVARLSARPKIKAFLSSPEHVNRPINGNGKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPPYTIVYFPV ----CCCEEEEEEEC	11.83	29514104
8	Phosphorylation	MPPYTIVYFPVRGRC CCCEEEEEEECCCHH	9.79	20116462
28	Phosphorylation	LLADQGQSWKEEVVT HHHHCCCCHHHEEEE	47.11	22324799
48	S-palmitoylation	QGLLKPTCLYGQLPK HHHCCCHHHCCCCCC	3.60	28526873
48	S-nitrosylation	QGLLKPTCLYGQLPK HHHCCCHHHCCCCCC	3.60	21278135
48	S-nitrosocysteine	QGLLKPTCLYGQLPK HHHCCCHHHCCCCCC	3.60	-
62	Phosphorylation	KFEDGDLTLYQSNAI CCCCCCEEEHHHHHH	28.32	22324799
64	Phosphorylation	EDGDLTLYQSNAILR CCCCEEEHHHHHHHH	12.50	22324799
76	Phosphorylation	ILRHLGRSLGLYGKN HHHHHHHHHCCCCCC	25.62	25521595
80	Phosphorylation	LGRSLGLYGKNQREA HHHHHCCCCCCHHHH	25.02	22324799
82	Ubiquitination	RSLGLYGKNQREAAQ HHHCCCCCCHHHHHH	36.03	27667366
82	Malonylation	RSLGLYGKNQREAAQ HHHCCCCCCHHHHHH	36.03	26320211
82	Succinylation	RSLGLYGKNQREAAQ HHHCCCCCCHHHHHH	36.03	-
82	Acetylation	RSLGLYGKNQREAAQ HHHCCCCCCHHHHHH	36.03	23864654
103	Acetylation	GVEDLRGKYVTLIYT HHHHHCCCEEEEEEE	30.07	23864654
103	Succinylation	GVEDLRGKYVTLIYT HHHHHCCCEEEEEEE	30.07	-
103	Malonylation	GVEDLRGKYVTLIYT HHHHHCCCEEEEEEE	30.07	26320211
103	Ubiquitination	GVEDLRGKYVTLIYT HHHHHCCCEEEEEEE	30.07	-
103	Succinylation	GVEDLRGKYVTLIYT HHHHHCCCEEEEEEE	30.07	23806337
109	Phosphorylation	GKYVTLIYTNYENGK CCEEEEEEECCCCCC	7.64	18563927
110	Phosphorylation	KYVTLIYTNYENGKN CEEEEEEECCCCCCC	25.08	18034455
116	Ubiquitination	YTNYENGKNDYVKAL EECCCCCCCCHHHCC	59.22	-
116	Malonylation	YTNYENGKNDYVKAL EECCCCCCCCHHHCC	59.22	26320211
116	Succinylation	YTNYENGKNDYVKAL EECCCCCCCCHHHCC	59.22	23806337
116	Succinylation	YTNYENGKNDYVKAL EECCCCCCCCHHHCC	59.22	-
116	Acetylation	YTNYENGKNDYVKAL EECCCCCCCCHHHCC	59.22	23954790
119	Phosphorylation	YENGKNDYVKALPGH CCCCCCCHHHCCCCC	17.16	29514104
121	Ubiquitination	NGKNDYVKALPGHLK CCCCCHHHCCCCCCC	37.67	27667366
121	Malonylation	NGKNDYVKALPGHLK CCCCCHHHCCCCCCC	37.67	26320211
121	Succinylation	NGKNDYVKALPGHLK CCCCCHHHCCCCCCC	37.67	-
121	Acetylation	NGKNDYVKALPGHLK CCCCCHHHCCCCCCC	37.67	23954790
128	Malonylation	KALPGHLKPFETLLS HCCCCCCCHHHHHHH	41.82	26320211
128	Succinylation	KALPGHLKPFETLLS HCCCCCCCHHHHHHH	41.82	-
128	Ubiquitination	KALPGHLKPFETLLS HCCCCCCCHHHHHHH	41.82	27667366
128	Acetylation	KALPGHLKPFETLLS HCCCCCCCHHHHHHH	41.82	23864654
132	Phosphorylation	GHLKPFETLLSQNQG CCCCHHHHHHHCCCC	33.12	23984901
135	Phosphorylation	KPFETLLSQNQGGKA CHHHHHHHCCCCCCE	30.14	25521595
191	Malonylation	LSARPKIKAFLSSPE HHCCHHHHHHHCCHH	38.93	26320211
191	Succinylation	LSARPKIKAFLSSPE HHCCHHHHHHHCCHH	38.93	-
191	Ubiquitination	LSARPKIKAFLSSPE HHCCHHHHHHHCCHH	38.93	27667366
191	Acetylation	LSARPKIKAFLSSPE HHCCHHHHHHHCCHH	38.93	23806337
195	Phosphorylation	PKIKAFLSSPEHVNR HHHHHHHCCHHHCCC	37.08	22324799
196	Phosphorylation	KIKAFLSSPEHVNRP HHHHHHCCHHHCCCC	36.13	29899451
209	Ubiquitination	RPINGNGKQ------ CCCCCCCCC------	57.76	-
209	Malonylation	RPINGNGKQ------ CCCCCCCCC------	57.76	26320211
209	Acetylation	RPINGNGKQ------ CCCCCCCCC------	57.76	22902405

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
4	Y	Phosphorylation	Kinase	EGFR	Q01279	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GSTP1_MOUSE !!

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 GSTP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
FANCC_MOUSE	Fancc	physical	11433346

Drug and Disease Associations

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

Regulatory Network of GSTP1_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-109, AND MASSSPECTROMETRY.	18034455 [Abstract]