dbPTM

GSTM1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GSTM1_MOUSE
UniProt AC	P10649
Protein Name	Glutathione S-transferase Mu 1
Gene Name	Gstm1
Organism	Mus musculus (Mouse).
Sequence Length	218
Subcellular Localization	Cytoplasm.
Protein Description	Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles..
Protein Sequence	MPMILGYWNVRGLTHPIRMLLEYTDSSYDEKRYTMGDAPDFDRSQWLNEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLARKHHLDGETEEERIRADIVENQVMDTRMQLIMLCYNPDFEKQKPEFLKTIPEKMKLYSEFLGKRPWFAGDKVTYVDFLAYDILDQYRMFEPKCLDAFPNLRDFLARFEGLKKISAYMKSSRYIATPIFSKMAHWSNK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Nitration	-MPMILGYWNVRGLT -CCCEEEEEECCCCC	7.14	-
19	Oxidation	GLTHPIRMLLEYTDS CCCHHHHHHHHCCCC	5.33	17242355
23	Nitration	PIRMLLEYTDSSYDE HHHHHHHCCCCCCCC	18.80	-
23	Phosphorylation	PIRMLLEYTDSSYDE HHHHHHHCCCCCCCC	18.80	26032504
24	Phosphorylation	IRMLLEYTDSSYDEK HHHHHHCCCCCCCCC	21.74	22324799
26	Phosphorylation	MLLEYTDSSYDEKRY HHHHCCCCCCCCCCC	24.01	22324799
27	Phosphorylation	LLEYTDSSYDEKRYT HHHCCCCCCCCCCCC	39.14	25521595
28	Nitration	LEYTDSSYDEKRYTM HHCCCCCCCCCCCCC	31.88	-
28	Phosphorylation	LEYTDSSYDEKRYTM HHCCCCCCCCCCCCC	31.88	29895711
31	Acetylation	TDSSYDEKRYTMGDA CCCCCCCCCCCCCCC	48.05	23864654
31	Malonylation	TDSSYDEKRYTMGDA CCCCCCCCCCCCCCC	48.05	26320211
31	Ubiquitination	TDSSYDEKRYTMGDA CCCCCCCCCCCCCCC	48.05	-
33	Nitration	SSYDEKRYTMGDAPD CCCCCCCCCCCCCCC	16.49	-
33	Phosphorylation	SSYDEKRYTMGDAPD CCCCCCCCCCCCCCC	16.49	25521595
34	Phosphorylation	SYDEKRYTMGDAPDF CCCCCCCCCCCCCCC	20.79	25521595
35	Oxidation	YDEKRYTMGDAPDFD CCCCCCCCCCCCCCC	3.20	17242355
50	Ubiquitination	RSQWLNEKFKLGLDF HHHHHHHHCCCCCCC	46.88	-
50	Acetylation	RSQWLNEKFKLGLDF HHHHHHHHCCCCCCC	46.88	23806337
50	Malonylation	RSQWLNEKFKLGLDF HHHHHHHHCCCCCCC	46.88	26320211
52	Ubiquitination	QWLNEKFKLGLDFPN HHHHHHCCCCCCCCC	53.35	-
52	Acetylation	QWLNEKFKLGLDFPN HHHHHHCCCCCCCCC	53.35	22733758
52	Malonylation	QWLNEKFKLGLDFPN HHHHHHCCCCCCCCC	53.35	26073543
62	Phosphorylation	LDFPNLPYLIDGSHK CCCCCCCEEECCCCC	21.32	23984901
62	Nitration	LDFPNLPYLIDGSHK CCCCCCCEEECCCCC	21.32	-
67	Phosphorylation	LPYLIDGSHKITQSN CCEEECCCCCCCCHH	20.19	21082442
69	Ubiquitination	YLIDGSHKITQSNAI EEECCCCCCCCHHHH	49.50	-
69	Acetylation	YLIDGSHKITQSNAI EEECCCCCCCCHHHH	49.50	23954790
69	Malonylation	YLIDGSHKITQSNAI EEECCCCCCCCHHHH	49.50	26073543
71	Phosphorylation	IDGSHKITQSNAILR ECCCCCCCCHHHHHH	30.65	23984901
73	Phosphorylation	GSHKITQSNAILRYL CCCCCCCHHHHHHHH	21.41	23984901
79	Nitration	QSNAILRYLARKHHL CHHHHHHHHHHHHCC	10.98	-
83	Ubiquitination	ILRYLARKHHLDGET HHHHHHHHHCCCCCC	29.75	22790023
90	Phosphorylation	KHHLDGETEEERIRA HHCCCCCCHHHHHHH	54.98	25521595
115	S-nitrosylation	RMQLIMLCYNPDFEK HHHHHHHHHCCCHHH	1.38	21278135
115	S-palmitoylation	RMQLIMLCYNPDFEK HHHHHHHHHCCCHHH	1.38	28526873
115	S-nitrosocysteine	RMQLIMLCYNPDFEK HHHHHHHHHCCCHHH	1.38	-
116	Phosphorylation	MQLIMLCYNPDFEKQ HHHHHHHHCCCHHHH	26.26	25195567
122	Ubiquitination	CYNPDFEKQKPEFLK HHCCCHHHHCHHHHH	64.71	-
122	Malonylation	CYNPDFEKQKPEFLK HHCCCHHHHCHHHHH	64.71	26320211
122	Acetylation	CYNPDFEKQKPEFLK HHCCCHHHHCHHHHH	64.71	22733758
124	Ubiquitination	NPDFEKQKPEFLKTI CCCHHHHCHHHHHHH	58.54	-
124	Malonylation	NPDFEKQKPEFLKTI CCCHHHHCHHHHHHH	58.54	26320211
124	Acetylation	NPDFEKQKPEFLKTI CCCHHHHCHHHHHHH	58.54	23201123
129	Ubiquitination	KQKPEFLKTIPEKMK HHCHHHHHHHHHHHH	50.13	-
129	Acetylation	KQKPEFLKTIPEKMK HHCHHHHHHHHHHHH	50.13	23864654
129	Malonylation	KQKPEFLKTIPEKMK HHCHHHHHHHHHHHH	50.13	26320211
134	Malonylation	FLKTIPEKMKLYSEF HHHHHHHHHHHHHHH	35.66	26320211
136	Acetylation	KTIPEKMKLYSEFLG HHHHHHHHHHHHHHC	56.17	22826441
136	Ubiquitination	KTIPEKMKLYSEFLG HHHHHHHHHHHHHHC	56.17	-
136	Malonylation	KTIPEKMKLYSEFLG HHHHHHHHHHHHHHC	56.17	26320211
138	Nitration	IPEKMKLYSEFLGKR HHHHHHHHHHHHCCC	10.71	-
139	Phosphorylation	PEKMKLYSEFLGKRP HHHHHHHHHHHCCCC	32.10	26643407
144	Malonylation	LYSEFLGKRPWFAGD HHHHHHCCCCCCCCC	58.39	26073543
144	Glutarylation	LYSEFLGKRPWFAGD HHHHHHCCCCCCCCC	58.39	24703693
144	Acetylation	LYSEFLGKRPWFAGD HHHHHHCCCCCCCCC	58.39	23864654
144	Ubiquitination	LYSEFLGKRPWFAGD HHHHHHCCCCCCCCC	58.39	-
161	Nitration	TYVDFLAYDILDQYR EEEHHHHHHHHHHHH	12.98	-
173	Malonylation	QYRMFEPKCLDAFPN HHHHHCHHHHHCCCC	39.99	26320211
173	Ubiquitination	QYRMFEPKCLDAFPN HHHHHCHHHHHCCCC	39.99	-
173	Acetylation	QYRMFEPKCLDAFPN HHHHHCHHHHHCCCC	39.99	23864654
174	S-nitrosocysteine	YRMFEPKCLDAFPNL HHHHCHHHHHCCCCH	6.43	-
174	S-palmitoylation	YRMFEPKCLDAFPNL HHHHCHHHHHCCCCH	6.43	28526873
174	S-nitrosylation	YRMFEPKCLDAFPNL HHHHCHHHHHCCCCH	6.43	21278135
192	Acetylation	LARFEGLKKISAYMK HHHHHHHHHHHHHHH	59.94	67967
192	Malonylation	LARFEGLKKISAYMK HHHHHHHHHHHHHHH	59.94	26073543
193	Malonylation	ARFEGLKKISAYMKS HHHHHHHHHHHHHHH	47.11	26320211
195	Phosphorylation	FEGLKKISAYMKSSR HHHHHHHHHHHHHCC	23.40	29472430
199	Acetylation	KKISAYMKSSRYIAT HHHHHHHHHCCCCCH	32.38	23864654
199	Ubiquitination	KKISAYMKSSRYIAT HHHHHHHHHCCCCCH	32.38	-
199	Malonylation	KKISAYMKSSRYIAT HHHHHHHHHCCCCCH	32.38	26320211
200	Phosphorylation	KISAYMKSSRYIATP HHHHHHHHCCCCCHH	11.97	25521595
201	Phosphorylation	ISAYMKSSRYIATPI HHHHHHHCCCCCHHH	24.47	25521595
203	Phosphorylation	AYMKSSRYIATPIFS HHHHHCCCCCHHHHH	9.24	25521595
206	Phosphorylation	KSSRYIATPIFSKMA HHCCCCCHHHHHHHH	13.83	27180971
210	Phosphorylation	YIATPIFSKMAHWSN CCCHHHHHHHHHCCC	23.42	29472430
211	Ubiquitination	IATPIFSKMAHWSNK CCHHHHHHHHHCCCC	29.38	22790023

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 GSTM1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GSTM1_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 GSTM1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of GSTM1_MOUSE !!

Drug and Disease Associations

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

Regulatory Network of GSTM1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-33 AND THR-34, AND MASSSPECTROMETRY.	17242355 [Abstract]
"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-23, AND MASSSPECTROMETRY.	18034455 [Abstract]