dbPTM

GSTO1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GSTO1_HUMAN
UniProt AC	P78417
Protein Name	Glutathione S-transferase omega-1
Gene Name	GSTO1
Organism	Homo sapiens (Human).
Sequence Length	241
Subcellular Localization	Cytoplasm, cytosol .
Protein Description	Exhibits glutathione-dependent thiol transferase and dehydroascorbate reductase activities. Has S-(phenacyl)glutathione reductase activity. Has also glutathione S-transferase activity. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA) and dimethylarsonic acid..
Protein Sequence	MSGESARSLGKGSAPPGPVPEGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDPYEKACQKMILELFSKVPSLVGSFIRSQNKEDYAGLKEEFRKEFTKLEEVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELYLQNSPEACDYGL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSGESARSL ------CCCHHHHHC	51.79	25849741
2	Acetylation	------MSGESARSL ------CCCHHHHHC	51.79	19413330
5	Phosphorylation	---MSGESARSLGKG ---CCCHHHHHCCCC	32.29	28450419
8	Phosphorylation	MSGESARSLGKGSAP CCCHHHHHCCCCCCC	40.99	28450419
11	Ubiquitination	ESARSLGKGSAPPGP HHHHHCCCCCCCCCC	55.79	21890473
11	Malonylation	ESARSLGKGSAPPGP HHHHHCCCCCCCCCC	55.79	32601280
13	O-linked_Glycosylation	ARSLGKGSAPPGPVP HHHCCCCCCCCCCCC	40.88	28510447
13	Phosphorylation	ARSLGKGSAPPGPVP HHHCCCCCCCCCCCC	40.88	28464451
23	Phosphorylation	PGPVPEGSIRIYSMR CCCCCCCCEEEEEEE	13.66	21712546
29	Acetylation	GSIRIYSMRFCPFAE CCEEEEEEEECCHHH	1.82	19608861
30	Methylation	SIRIYSMRFCPFAER CEEEEEEEECCHHHH	24.87	-
32	Glutathionylation	RIYSMRFCPFAERTR EEEEEEECCHHHHHH	1.59	22833525
37	Ubiquitination	RFCPFAERTRLVLKA EECCHHHHHHHHHHH	23.01	19608861
37	Acetylation	RFCPFAERTRLVLKA EECCHHHHHHHHHHH	23.01	19608861
57	Sumoylation	EVININLKNKPEWFF EEEEEECCCCCHHHC	59.44	19608861
57	Ubiquitination	EVININLKNKPEWFF EEEEEECCCCCHHHC	59.44	-
57	Acetylation	EVININLKNKPEWFF EEEEEECCCCCHHHC	59.44	19608861
57	Malonylation	EVININLKNKPEWFF EEEEEECCCCCHHHC	59.44	26320211
59	Acetylation	ININLKNKPEWFFKK EEEECCCCCHHHCCC	42.60	23749302
59	Malonylation	ININLKNKPEWFFKK EEEECCCCCHHHCCC	42.60	26320211
59	Ubiquitination	ININLKNKPEWFFKK EEEECCCCCHHHCCC	42.60	-
65	Ubiquitination	NKPEWFFKKNPFGLV CCCHHHCCCCCCCCE	42.01	21890473
65	Acetylation	NKPEWFFKKNPFGLV CCCHHHCCCCCCCCE	42.01	19608861
65	2-Hydroxyisobutyrylation	NKPEWFFKKNPFGLV CCCHHHCCCCCCCCE	42.01	-
66	Ubiquitination	KPEWFFKKNPFGLVP CCHHHCCCCCCCCEE	65.77	-
78	Phosphorylation	LVPVLENSQGQLIYE CEEEEECCCCCEEEE	26.72	-
90	Glutathionylation	IYESAITCEYLDEAY EEEEEEEHHCCCHHC	2.37	22833525
92	Nitration	ESAITCEYLDEAYPG EEEEEHHCCCHHCCC	22.92	-
94	Acetylation	AITCEYLDEAYPGKK EEEHHCCCHHCCCCC	37.26	19608861
100	Acetylation	LDEAYPGKKLLPDDP CCHHCCCCCCCCCCH	35.43	11924249
101	Ubiquitination	DEAYPGKKLLPDDPY CHHCCCCCCCCCCHH	62.26	-
108	Phosphorylation	KLLPDDPYEKACQKM CCCCCCHHHHHHHHH	36.74	23917254
108	Nitration	KLLPDDPYEKACQKM CCCCCCHHHHHHHHH	36.74	-
110	Acetylation	LPDDPYEKACQKMIL CCCCHHHHHHHHHHH	48.93	26051181
110	Ubiquitination	LPDDPYEKACQKMIL CCCCHHHHHHHHHHH	48.93	-
112	Glutathionylation	DDPYEKACQKMILEL CCHHHHHHHHHHHHH	6.22	22833525
115	Acetylation	YEKACQKMILELFSK HHHHHHHHHHHHHHC	1.42	19608861
115	Sulfoxidation	YEKACQKMILELFSK HHHHHHHHHHHHHHC	1.42	30846556
120	Acetylation	QKMILELFSKVPSLV HHHHHHHHHCCHHHH	4.92	19608861
121	Phosphorylation	KMILELFSKVPSLVG HHHHHHHHCCHHHHH	45.42	20068231
122	Acetylation	MILELFSKVPSLVGS HHHHHHHCCHHHHHH	51.32	19608861
124	Acetylation	LELFSKVPSLVGSFI HHHHHCCHHHHHHHH	26.19	19608861
125	Phosphorylation	ELFSKVPSLVGSFIR HHHHCCHHHHHHHHH	38.38	20068231
129	Phosphorylation	KVPSLVGSFIRSQNK CCHHHHHHHHHHCCH	15.26	28258704
133	Phosphorylation	LVGSFIRSQNKEDYA HHHHHHHHCCHHHHC	33.03	29514088
136	Malonylation	SFIRSQNKEDYAGLK HHHHHCCHHHHCCCH	44.30	26320211
136	Ubiquitination	SFIRSQNKEDYAGLK HHHHHCCHHHHCCCH	44.30	21890473
136	2-Hydroxyisobutyrylation	SFIRSQNKEDYAGLK HHHHHCCHHHHCCCH	44.30	-
136	Acetylation	SFIRSQNKEDYAGLK HHHHHCCHHHHCCCH	44.30	23236377
139	Phosphorylation	RSQNKEDYAGLKEEF HHCCHHHHCCCHHHH	12.03	27642862
143	Acetylation	KEDYAGLKEEFRKEF HHHHCCCHHHHHHHH	55.04	19608861
143	Ubiquitination	KEDYAGLKEEFRKEF HHHHCCCHHHHHHHH	55.04	19608861
143	Succinylation	KEDYAGLKEEFRKEF HHHHCCCHHHHHHHH	55.04	23954790
148	Acetylation	GLKEEFRKEFTKLEE CCHHHHHHHHHHHHH	63.60	19608861
148	Malonylation	GLKEEFRKEFTKLEE CCHHHHHHHHHHHHH	63.60	26320211
152	Malonylation	EFRKEFTKLEEVLTN HHHHHHHHHHHHHHC	60.26	26320211
152	Acetylation	EFRKEFTKLEEVLTN HHHHHHHHHHHHHHC	60.26	19608861
152	Ubiquitination	EFRKEFTKLEEVLTN HHHHHHHHHHHHHHC	60.26	19608861
160	Acetylation	LEEVLTNKKTTFFGG HHHHHHCCCCCCCCC	46.38	23954790
160	2-Hydroxyisobutyrylation	LEEVLTNKKTTFFGG HHHHHHCCCCCCCCC	46.38	-
160	Ubiquitination	LEEVLTNKKTTFFGG HHHHHHCCCCCCCCC	46.38	21906983
161	Acetylation	EEVLTNKKTTFFGGN HHHHHCCCCCCCCCC	55.67	30583199
188	Ubiquitination	FERLEAMKLNECVDH HHHHHHHCHHHHCCC	56.03	21906983
188	Acetylation	FERLEAMKLNECVDH HHHHHHHCHHHHCCC	56.03	25953088
192	Glutathionylation	EAMKLNECVDHTPKL HHHCHHHHCCCCHHH	4.19	22833525
198	2-Hydroxyisobutyrylation	ECVDHTPKLKLWMAA HHCCCCHHHHHHHHH	60.45	-
198	Acetylation	ECVDHTPKLKLWMAA HHCCCCHHHHHHHHH	60.45	25953088
198	Ubiquitination	ECVDHTPKLKLWMAA HHCCCCHHHHHHHHH	60.45	-
200	Acetylation	VDHTPKLKLWMAAMK CCCCHHHHHHHHHHC	46.35	25953088
207	Ubiquitination	KLWMAAMKEDPTVSA HHHHHHHCCCCCHHH	54.99	21890473
211	Phosphorylation	AAMKEDPTVSALLTS HHHCCCCCHHHHCCC	39.14	20068231
213	Phosphorylation	MKEDPTVSALLTSEK HCCCCCHHHHCCCCC	18.71	20068231
217	Phosphorylation	PTVSALLTSEKDWQG CCHHHHCCCCCCHHH	35.37	23911959
218	Phosphorylation	TVSALLTSEKDWQGF CHHHHCCCCCCHHHH	42.49	20068231
229	Phosphorylation	WQGFLELYLQNSPEA HHHHHHHHHHCCHHH	9.25	22817900
233	Phosphorylation	LELYLQNSPEACDYG HHHHHHCCHHHCCCC	15.91	24275569
237	Glutathionylation	LQNSPEACDYGL--- HHCCHHHCCCCC---	3.84	22833525
239	Phosphorylation	NSPEACDYGL----- CCHHHCCCCC-----	21.88	-

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
Oops, there are no upstream regulatory protein records of GSTO1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GSTO1_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 GSTO1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
KAT5_HUMAN	KAT5	physical	16169070
SETB1_HUMAN	SETDB1	physical	16169070
RBM48_HUMAN	RBM48	physical	16169070
EF1G_HUMAN	EEF1G	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
A4_HUMAN	APP	physical	21832049
GSTT1_HUMAN	GSTT1	physical	22939629
CK054_HUMAN	C11orf54	physical	26344197
CAN1_HUMAN	CAPN1	physical	26344197
CAN9_HUMAN	CAPN9	physical	26344197
DUT_HUMAN	DUT	physical	26344197
ECH1_HUMAN	ECH1	physical	26344197
FKB1B_HUMAN	FKBP1B	physical	26344197
GSTA4_HUMAN	GSTA4	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
LYPA2_HUMAN	LYPLA2	physical	26344197
NUDT9_HUMAN	NUDT9	physical	26344197
PRDX6_HUMAN	PRDX6	physical	26344197
TAGL_HUMAN	TAGLN	physical	26344197
TAGL2_HUMAN	TAGLN2	physical	26344197
TAGL3_HUMAN	TAGLN3	physical	26344197
UCRI_HUMAN	UQCRFS1	physical	26344197
YTDC2_HUMAN	YTHDC2	physical	26344197

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
DB00143	Glutathione
DB00163	Vitamin E

Regulatory Network of GSTO1_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-57; LYS-122; LYS-143;LYS-148 AND LYS-152, AND MASS SPECTROMETRY.	19608861 [Abstract]