dbPTM

GSTP1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GSTP1_HUMAN
UniProt AC	P09211
Protein Name	Glutathione S-transferase P
Gene Name	GSTP1
Organism	Homo sapiens (Human).
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. Regulates negatively CDK5 activity via p25/p35 translocation to prevent neurodegeneration..
Protein Sequence	MPPYTVVYFPVRGRCAALRMLLADQGQSWKEEVVTVETWQEGSLKASCLYGQLPKFQDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYISLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGNGKQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
4	Phosphorylation	----MPPYTVVYFPV ----CCCEEEEEEEC	13.29	28152594
5	Phosphorylation	---MPPYTVVYFPVR ---CCCEEEEEEECC	14.85	26074081
8	Phosphorylation	MPPYTVVYFPVRGRC CCCEEEEEEECCCHH	9.60	27155012
20	Sulfoxidation	GRCAALRMLLADQGQ CHHHHHHHHHHHCCC	3.60	30846556
28	Phosphorylation	LLADQGQSWKEEVVT HHHHCCCCCCEEEEE	47.11	27251275
30	Sumoylation	ADQGQSWKEEVVTVE HHCCCCCCEEEEEEE	49.60	-
35	Phosphorylation	SWKEEVVTVETWQEG CCCEEEEEEEEECCC	20.14	27732954
38	Phosphorylation	EEVVTVETWQEGSLK EEEEEEEEECCCCCC	28.28	30266825
43	Phosphorylation	VETWQEGSLKASCLY EEEECCCCCCHHHHH	26.41	19664994
45	Methylation	TWQEGSLKASCLYGQ EECCCCCCHHHHHCC	39.69	-
47	Phosphorylation	QEGSLKASCLYGQLP CCCCCCHHHHHCCCC	11.76	21712546
48	S-palmitoylation	EGSLKASCLYGQLPK CCCCCHHHHHCCCCC	3.97	29575903
48	S-nitrosylation	EGSLKASCLYGQLPK CCCCCHHHHHCCCCC	3.97	19483679
48	Glutathionylation	EGSLKASCLYGQLPK CCCCCHHHHHCCCCC	3.97	22833525
48	S-nitrosocysteine	EGSLKASCLYGQLPK CCCCCHHHHHCCCCC	3.97	-
50	Phosphorylation	SLKASCLYGQLPKFQ CCCHHHHHCCCCCCC	13.73	28152594
50	Nitration	SLKASCLYGQLPKFQ CCCHHHHHCCCCCCC	13.73	-
55	Acetylation	CLYGQLPKFQDGDLT HHHCCCCCCCCCCEE	65.34	23236377
55	Ubiquitination	CLYGQLPKFQDGDLT HHHCCCCCCCCCCEE	65.34	-
62	Phosphorylation	KFQDGDLTLYQSNTI CCCCCCEEEEECHHH	28.32	28152594
64	Phosphorylation	QDGDLTLYQSNTILR CCCCEEEEECHHHHH	12.50	28152594
66	Phosphorylation	GDLTLYQSNTILRHL CCEEEEECHHHHHHH	23.53	28152594
68	Phosphorylation	LTLYQSNTILRHLGR EEEEECHHHHHHHHH	27.00	28152594
80	Phosphorylation	LGRTLGLYGKDQQEA HHHHHCCCCCCHHHH	21.97	29496907
82	Ubiquitination	RTLGLYGKDQQEAAL HHHCCCCCCHHHHHH	38.51	21906983
82	Sumoylation	RTLGLYGKDQQEAAL HHHCCCCCCHHHHHH	38.51	-
82	Methylation	RTLGLYGKDQQEAAL HHHCCCCCCHHHHHH	38.51	-
92	Sulfoxidation	QEAALVDMVNDGVED HHHHHHHHHCCCHHH	2.06	30846556
102	Glutathionylation	DGVEDLRCKYISLIY CCHHHHHHHEEEEEE	5.22	22833525
103	Acetylation	GVEDLRCKYISLIYT CHHHHHHHEEEEEEE	38.90	30584121
103	Succinylation	GVEDLRCKYISLIYT CHHHHHHHEEEEEEE	38.90	-
103	Succinylation	GVEDLRCKYISLIYT CHHHHHHHEEEEEEE	38.90	-
103	Ubiquitination	GVEDLRCKYISLIYT CHHHHHHHEEEEEEE	38.90	-
106	Phosphorylation	DLRCKYISLIYTNYE HHHHHEEEEEEECCC	12.96	26356563
109	Phosphorylation	CKYISLIYTNYEAGK HHEEEEEEECCCCCC	8.33	20090780
110	Phosphorylation	KYISLIYTNYEAGKD HEEEEEEECCCCCCC	25.08	-
112	Phosphorylation	ISLIYTNYEAGKDDY EEEEEECCCCCCCHH	10.19	-
116	Succinylation	YTNYEAGKDDYVKAL EECCCCCCCHHHHHC	55.25	-
116	Succinylation	YTNYEAGKDDYVKAL EECCCCCCCHHHHHC	55.25	-
116	Acetylation	YTNYEAGKDDYVKAL EECCCCCCCHHHHHC	55.25	20167786
121	2-Hydroxyisobutyrylation	AGKDDYVKALPGQLK CCCCHHHHHCCCCCC	37.67	-
121	Acetylation	AGKDDYVKALPGQLK CCCCHHHHHCCCCCC	37.67	19608861
121	Ubiquitination	AGKDDYVKALPGQLK CCCCHHHHHCCCCCC	37.67	21890473
128	Acetylation	KALPGQLKPFETLLS HHCCCCCCCHHHHHH	39.51	19608861
128	Ubiquitination	KALPGQLKPFETLLS HHCCCCCCCHHHHHH	39.51	21890473
132	Phosphorylation	GQLKPFETLLSQNQG CCCCCHHHHHHCCCC	33.12	26657352
135	Phosphorylation	KPFETLLSQNQGGKT CCHHHHHHCCCCCCE	30.14	26657352
141	Sumoylation	LSQNQGGKTFIVGDQ HHCCCCCCEEEECCC	47.27	-
141	Methylation	LSQNQGGKTFIVGDQ HHCCCCCCEEEECCC	47.27	-
185	Phosphorylation	SAYVGRLSARPKLKA HHHHHHHHCCHHHHH	22.37	15604283
189	Ubiquitination	GRLSARPKLKAFLAS HHHHCCHHHHHHHCC	58.00	-
189	Acetylation	GRLSARPKLKAFLAS HHHHCCHHHHHHHCC	58.00	23749302
191	Ubiquitination	LSARPKLKAFLASPE HHCCHHHHHHHCCCH	43.13	21890473
191	Acetylation	LSARPKLKAFLASPE HHCCHHHHHHHCCCH	43.13	88353
196	Phosphorylation	KLKAFLASPEYVNLP HHHHHHCCCHHCCCC	22.02	21712546
199	Phosphorylation	AFLASPEYVNLPING HHHCCCHHCCCCCCC	9.68	21253578
209	Methylation	LPINGNGKQ------ CCCCCCCCC------	57.76	24129315
209	Ubiquitination	LPINGNGKQ------ CCCCCCCCC------	57.76	-
209	Trimethylation	LPINGNGKQ------ CCCCCCCCC------	57.76	-
209	Acetylation	LPINGNGKQ------ CCCCCCCCC------	57.76	25953088

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	P00533	Uniprot
8	Y	Phosphorylation	Kinase	EGFR	P00533	PSP
43	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
43	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
43	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
185	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
185	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
185	S	Phosphorylation	Kinase	PRKCH	P24723	GPS
185	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
185	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
199	Y	Phosphorylation	Kinase	EGFR	P00533	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	FBXO8	Q9NRD0	PMID:31024008

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GSTP1_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TGM2_HUMAN	TGM2	physical	9973324
PNO1_HUMAN	PNO1	physical	16169070
PTN_HUMAN	PTN	physical	16169070
GSTP1_HUMAN	GSTP1	physical	9398518
FANCC_HUMAN	FANCC	physical	11433346
TRAF2_HUMAN	TRAF2	physical	16636664
SFR19_HUMAN	SCAF1	physical	21988832
K1H1_HUMAN	KRT31	physical	25416956
APBP2_HUMAN	APPBP2	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
KR109_HUMAN	KRTAP10-9	physical	25416956
KR103_HUMAN	KRTAP10-3	physical	25416956
NT2NL_HUMAN	NOTCH2NL	physical	25416956
ACY1_HUMAN	ACY1	physical	26496610
GABP1_HUMAN	GABPB1	physical	26496610
Z518A_HUMAN	ZNF518A	physical	26496610
TXN4A_HUMAN	TXNL4A	physical	26496610
RBMX_HUMAN	RBMX	physical	26496610
UBE2O_HUMAN	UBE2O	physical	26496610
TRAF2_HUMAN	TRAF2	physical	25241761
MK08_HUMAN	MAPK8	physical	25241761
GSTP1_HUMAN	GSTP1	physical	16401067
EGFR_HUMAN	EGFR	physical	19254954

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
DB01008	Busulfan
DB04339	Carbocisteine
DB00958	Carboplatin
DB00291	Chlorambucil
DB00515	Cisplatin
DB01242	Clomipramine
DB00773	Etoposide
DB00143	Glutathione
DB00526	Oxaliplatin
DB00163	Vitamin E

Regulatory Network of GSTP1_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-121 AND LYS-128, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-8, AND MASSSPECTROMETRY.	19534553 [Abstract]
"Tyrosine phosphorylation of the human glutathione S-transferase P1 byepidermal growth factor receptor."; Okamura T., Singh S., Buolamwini J., Haystead T., Friedman H.,Bigner D., Ali-Osman F.; J. Biol. Chem. 284:16979-16989(2009). Cited for: PHOSPHORYLATION AT TYR-4 AND TYR-199.	19254954 [Abstract]