dbPTM

MGST3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MGST3_HUMAN
UniProt AC	O14880
Protein Name	Microsomal glutathione S-transferase 3
Gene Name	MGST3
Organism	Homo sapiens (Human).
Sequence Length	152
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein . Microsome membrane Multi-pass membrane protein . Microsome membrane Lipid-anchor .
Protein Description	Also functions as a glutathione peroxidase..
Protein Sequence	MAVLSKEYGFVLLTGAASFIMVAHLAINVSKARKKYKVEYPIMYSTDPENGHIFNCIQRAHQNTLEVYPPFLFFLAVGGVYHPRIASGLGLAWIVGRVLYAYGYYTGEPSKRSRGALGSIALLGLVGTTVCSAFQHLGWVKSGLGSGPKCCH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	EYGFVLLTGAASFIM HHCEEEEEHHHHHHH	22.18	-
36	Phosphorylation	VSKARKKYKVEYPIM HHHHHHHCCCCCEEE	24.25	28152594
37	Acetylation	SKARKKYKVEYPIMY HHHHHHCCCCCEEEE	37.15	26051181
40	Phosphorylation	RKKYKVEYPIMYSTD HHHCCCCCEEEEECC	10.88	25884760
44	Phosphorylation	KVEYPIMYSTDPENG CCCCEEEEECCCCCC	14.78	28152594
45	Phosphorylation	VEYPIMYSTDPENGH CCCEEEEECCCCCCC	14.68	28152594
46	Phosphorylation	EYPIMYSTDPENGHI CCEEEEECCCCCCCC	37.78	28152594
81	Phosphorylation	FLAVGGVYHPRIASG HEECCCCCCHHHCHH	14.91	-
100	Phosphorylation	WIVGRVLYAYGYYTG HHHHHHHHHHCCCCC	8.57	21406692
102	Phosphorylation	VGRVLYAYGYYTGEP HHHHHHHHCCCCCCC	7.66	21406692
104	Phosphorylation	RVLYAYGYYTGEPSK HHHHHHCCCCCCCCC	5.79	21406692
105	Phosphorylation	VLYAYGYYTGEPSKR HHHHHCCCCCCCCCC	12.14	21406692
106	Phosphorylation	LYAYGYYTGEPSKRS HHHHCCCCCCCCCCC	26.95	21406692
110	Phosphorylation	GYYTGEPSKRSRGAL CCCCCCCCCCCCCHH	36.08	21406692
111	Ubiquitination	YYTGEPSKRSRGALG CCCCCCCCCCCCHHH	66.17	21890473
111	2-Hydroxyisobutyrylation	YYTGEPSKRSRGALG CCCCCCCCCCCCHHH	66.17	-
111	Acetylation	YYTGEPSKRSRGALG CCCCCCCCCCCCHHH	66.17	26051181
142	Phosphorylation	QHLGWVKSGLGSGPK HHHCCHHHCCCCCCC	29.63	26437602
146	Phosphorylation	WVKSGLGSGPKCCH- CHHHCCCCCCCCCC-	57.89	26437602
149	Ubiquitination	SGLGSGPKCCH---- HCCCCCCCCCC----	53.68	-
149	2-Hydroxyisobutyrylation	SGLGSGPKCCH---- HCCCCCCCCCC----	53.68	-
149	Acetylation	SGLGSGPKCCH---- HCCCCCCCCCC----	53.68	25953088
150	S-palmitoylation	GLGSGPKCCH----- CCCCCCCCCC-----	2.62	21044946
151	S-palmitoylation	LGSGPKCCH------ CCCCCCCCC------	5.50	21044946

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 MGST3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MGST3_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 MGST3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RM49_HUMAN	MRPL49	physical	22939629
RT26_HUMAN	MRPS26	physical	22939629
VATC1_HUMAN	ATP6V1C1	physical	22939629
NDUS4_HUMAN	NDUFS4	physical	22939629
RASH_HUMAN	HRAS	physical	28514442
S10AD_HUMAN	S100A13	physical	28514442
NMT1_HUMAN	NMT1	physical	28514442
GLMN_HUMAN	GLMN	physical	28514442
NMT2_HUMAN	NMT2	physical	28514442
G3PT_HUMAN	GAPDHS	physical	28514442
HS12A_HUMAN	HSPA12A	physical	28514442
BIRC6_HUMAN	BIRC6	physical	28514442
RAP1A_HUMAN	RAP1A	physical	28514442
SVIP_HUMAN	SVIP	physical	28514442
VPP1_HUMAN	ATP6V0A1	physical	28514442

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
There are no disease associations of PTM sites.

Regulatory Network of MGST3_HUMAN

Related Literatures of Post-Translational Modification

Palmitoylation
Reference	PubMed
"Site-specific analysis of protein S-acylation by resin-assistedcapture."; Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A.,Stamler J.S., Casey P.J.; J. Lipid Res. 52:393-398(2011). Cited for: MUTAGENESIS OF CYS-150 AND CYS-151, AND PALMITOYLATION AT CYS-150 ANDCYS-151.	21044946 [Abstract]