MAAI_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MAAI_HUMAN
• UniProt AC: O43708
• Protein Name: Maleylacetoacetate isomerase
• Gene Name: GSTZ1
• Organism: Homo sapiens (Human).
• Sequence Length: 216
• Subcellular Localization: Cytoplasm.
• Protein Description: Bifunctional enzyme showing minimal glutathione-conjugating activity with ethacrynic acid and 7-chloro-4-nitrobenz-2-oxa-1,3-diazole and maleylacetoacetate isomerase activity. Has also low glutathione peroxidase activity with T-butyl and cumene hydroperoxides. Is able to catalyze the glutathione dependent oxygenation of dichloroacetic acid to glyoxylic acid..
• Protein Sequence: MQAGKPILYSYFRSSCSWRVRIALALKGIDYKTVPINLIKDRGQQFSKDFQALNPMKQVPTLKIDGITIHQSLAIIEYLEEMRPTPRLLPQDPKKRASVRMISDLIAGGIQPLQNLSVLKQVGEEMQLTWAQNAITCGFNALEQILQSTAGIYCVGDEVTMADLCLVPQVANAERFKVDLTPYPTISSINKRLLVLEAFQVSHPCRQPDTPTELRA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MQAGKPIL -------CCCCCCCC	5.78	22814378
9	Phosphorylation	QAGKPILYSYFRSSC CCCCCCCHHHHHHHC	11.31	21406692
10	Phosphorylation	AGKPILYSYFRSSCS CCCCCCHHHHHHHCC	17.85	21406692
11	Phosphorylation	GKPILYSYFRSSCSW CCCCCHHHHHHHCCH	6.88	21406692
32	Acetylation	ALKGIDYKTVPINLI HHCCCCCCEEEHHHC	39.02	19608861
32	Succinylation	ALKGIDYKTVPINLI HHCCCCCCEEEHHHC	39.02	23954790
57	Malonylation	FQALNPMKQVPTLKI HHHCCCCCCCCEEEE	49.77	26320211
57	Succinylation	FQALNPMKQVPTLKI HHHCCCCCCCCEEEE	49.77	-
57	Succinylation	FQALNPMKQVPTLKI HHHCCCCCCCCEEEE	49.77	-
57	Acetylation	FQALNPMKQVPTLKI HHHCCCCCCCCEEEE	49.77	25953088
61	Phosphorylation	NPMKQVPTLKIDGIT CCCCCCCEEEECCEE	41.65	24043423
68	Phosphorylation	TLKIDGITIHQSLAI EEEECCEEEHHHHHH	20.24	24043423
72	Phosphorylation	DGITIHQSLAIIEYL CCEEEHHHHHHHHHH	12.95	24043423
78	Phosphorylation	QSLAIIEYLEEMRPT HHHHHHHHHHHHCCC	14.70	24043423
94	2-Hydroxyisobutyrylation	RLLPQDPKKRASVRM CCCCCCHHHHHHHHH	64.28	-
136	Phosphorylation	TWAQNAITCGFNALE HHHHHHHHHCHHHHH	12.26	-
177	Succinylation	VANAERFKVDLTPYP CCCCCCCCCCCCCCC	40.85	-
177	Succinylation	VANAERFKVDLTPYP CCCCCCCCCCCCCCC	40.85	-
181	Phosphorylation	ERFKVDLTPYPTISS CCCCCCCCCCCCHHH	19.13	29083192
183	Phosphorylation	FKVDLTPYPTISSIN CCCCCCCCCCHHHHH	14.05	29083192
185	Phosphorylation	VDLTPYPTISSINKR CCCCCCCCHHHHHHH	27.87	24275569
187	Phosphorylation	LTPYPTISSINKRLL CCCCCCHHHHHHHHH	27.87	24275569
188	Phosphorylation	TPYPTISSINKRLLV CCCCCHHHHHHHHHH	26.74	24275569
191	Acetylation	PTISSINKRLLVLEA CCHHHHHHHHHHEEH	42.63	24888325
212	Phosphorylation	CRQPDTPTELRA--- CCCCCCCCCCCC---	50.14	24719451

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MAAI_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of MAAI_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MAAI_HUMAN	GSTZ1	physical	16189514
MAAI_HUMAN	GSTZ1	physical	25416956
PRDX6_HUMAN	PRDX6	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

Related Literatures of Post-Translational Modification

Acetylation

"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-32, AND MASS SPECTROMETRY.
PubMed: 19608861