ESTD_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ESTD_HUMAN
• UniProt AC: P10768
• Protein Name: S-formylglutathione hydrolase
• Gene Name: ESD
• Organism: Homo sapiens (Human).
• Sequence Length: 282
• Subcellular Localization: Cytoplasm. Cytoplasmic vesicle.
• Protein Description: Serine hydrolase involved in the detoxification of formaldehyde..
• Protein Sequence: MALKQISSNKCFGGLQKVFEHDSVELNCKMKFAVYLPPKAETGKCPALYWLSGLTCTEQNFISKSGYHQSASEHGLVVIAPDTSPRGCNIKGEDESWDFGTGAGFYVDATEDPWKTNYRMYSYVTEELPQLINANFPVDPQRMSIFGHSMGGHGALICALKNPGKYKSVSAFAPICNPVLCPWGKKAFSGYLGTDQSKWKAYDATHLVKSYPGSQLDILIDQGKDDQFLLDGQLLPDNFIAACTEKKIPVVFRLQEGYDHSYYFIATFITDHIRHHAKYLNA

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
2	Acetylation	------MALKQISSN ------CCCHHHCCC	24.38	-
4	Acetylation	----MALKQISSNKC ----CCCHHHCCCCC	35.73	23749302
4	Succinylation	----MALKQISSNKC ----CCCHHHCCCCC	35.73	-
4	Ubiquitination	----MALKQISSNKC ----CCCHHHCCCCC	35.73	-
4	Succinylation	----MALKQISSNKC ----CCCHHHCCCCC	35.73	-
7	Phosphorylation	-MALKQISSNKCFGG -CCCHHHCCCCCCCC	25.93	29083192
8	Phosphorylation	MALKQISSNKCFGGL CCCHHHCCCCCCCCH	41.77	29083192
10	Ubiquitination	LKQISSNKCFGGLQK CHHHCCCCCCCCHHH	32.65	-
10	Acetylation	LKQISSNKCFGGLQK CHHHCCCCCCCCHHH	32.65	23749302
11	S-nitrosylation	KQISSNKCFGGLQKV HHHCCCCCCCCHHHH	4.48	24105792
11	S-palmitoylation	KQISSNKCFGGLQKV HHHCCCCCCCCHHHH	4.48	21044946
17	Ubiquitination	KCFGGLQKVFEHDSV CCCCCHHHHHCCCCE	54.67	-
17	Acetylation	KCFGGLQKVFEHDSV CCCCCHHHHHCCCCE	54.67	25953088
28	Glutathionylation	HDSVELNCKMKFAVY CCCEEEEEEEEEEEE	7.72	22555962
29	Ubiquitination	DSVELNCKMKFAVYL CCEEEEEEEEEEEEC	44.01	-
29	Acetylation	DSVELNCKMKFAVYL CCEEEEEEEEEEEEC	44.01	25953088
31	Acetylation	VELNCKMKFAVYLPP EEEEEEEEEEEECCC	18.70	25953088
31	Ubiquitination	VELNCKMKFAVYLPP EEEEEEEEEEEECCC	18.70	21890473
39	Ubiquitination	FAVYLPPKAETGKCP EEEECCCCCCCCCCC	57.84	19608861
39	Acetylation	FAVYLPPKAETGKCP EEEECCCCCCCCCCC	57.84	19608861
65	Phosphorylation	EQNFISKSGYHQSAS CCCEECCCCCCCCCC	37.48	27080861
67	Phosphorylation	NFISKSGYHQSASEH CEECCCCCCCCCCCC	12.08	27080861
70	Phosphorylation	SKSGYHQSASEHGLV CCCCCCCCCCCCCEE	22.05	27080861
72	Phosphorylation	SGYHQSASEHGLVVI CCCCCCCCCCCEEEE	35.06	27080861
83	Phosphorylation	LVVIAPDTSPRGCNI EEEECCCCCCCCCCC	39.30	27080861
84	Phosphorylation	VVIAPDTSPRGCNIK EEECCCCCCCCCCCC	21.71	27080861
120	Sulfoxidation	PWKTNYRMYSYVTEE CCCCCCEEHHHHHHH	1.51	30846556
143	Sulfoxidation	FPVDPQRMSIFGHSM CCCCHHHEEECCCCC	2.80	30846556
144	Phosphorylation	PVDPQRMSIFGHSMG CCCHHHEEECCCCCC	19.56	28348404
149	Phosphorylation	RMSIFGHSMGGHGAL HEEECCCCCCCCCEE	21.36	28348404
150	Sulfoxidation	MSIFGHSMGGHGALI EEECCCCCCCCCEEE	6.55	30846556
166	Phosphorylation	ALKNPGKYKSVSAFA EECCCCCCCEEEEEC	17.89	25693802
167	Ubiquitination	LKNPGKYKSVSAFAP ECCCCCCCEEEEECC	48.11	21890473
168	Phosphorylation	KNPGKYKSVSAFAPI CCCCCCCEEEEECCC	20.43	25693802
170	Phosphorylation	PGKYKSVSAFAPICN CCCCCEEEEECCCCC	25.43	21712546
176	S-nitrosocysteine	VSAFAPICNPVLCPW EEEECCCCCCEECCC	4.60	-
176	S-nitrosylation	VSAFAPICNPVLCPW EEEECCCCCCEECCC	4.60	19483679
176	S-palmitoylation	VSAFAPICNPVLCPW EEEECCCCCCEECCC	4.60	29575903
181	S-palmitoylation	PICNPVLCPWGKKAF CCCCCEECCCCHHCC	2.44	29575903
181	S-nitrosylation	PICNPVLCPWGKKAF CCCCCEECCCCHHCC	2.44	19483679
181	S-nitrosocysteine	PICNPVLCPWGKKAF CCCCCEECCCCHHCC	2.44	-
185	Acetylation	PVLCPWGKKAFSGYL CEECCCCHHCCCCCC	36.74	25953088
185	Ubiquitination	PVLCPWGKKAFSGYL CEECCCCHHCCCCCC	36.74	-
186	Acetylation	VLCPWGKKAFSGYLG EECCCCHHCCCCCCC	51.21	30584241
186	Ubiquitination	VLCPWGKKAFSGYLG EECCCCHHCCCCCCC	51.21	-
186	Malonylation	VLCPWGKKAFSGYLG EECCCCHHCCCCCCC	51.21	26320211
189	Phosphorylation	PWGKKAFSGYLGTDQ CCCHHCCCCCCCCCH	31.24	28152594
191	Phosphorylation	GKKAFSGYLGTDQSK CHHCCCCCCCCCHHH	10.76	28152594
194	Phosphorylation	AFSGYLGTDQSKWKA CCCCCCCCCHHHCEE	28.42	28857561
197	Phosphorylation	GYLGTDQSKWKAYDA CCCCCCHHHCEEEHH	43.20	25159151
198	Acetylation	YLGTDQSKWKAYDAT CCCCCHHHCEEEHHH	47.26	25953088
198	Ubiquitination	YLGTDQSKWKAYDAT CCCCCHHHCEEEHHH	47.26	21890473
200	Malonylation	GTDQSKWKAYDATHL CCCHHHCEEEHHHHH	40.58	26320211
200	Acetylation	GTDQSKWKAYDATHL CCCHHHCEEEHHHHH	40.58	19608861
200	Ubiquitination	GTDQSKWKAYDATHL CCCHHHCEEEHHHHH	40.58	21890473
202	Phosphorylation	DQSKWKAYDATHLVK CHHHCEEEHHHHHHH	11.46	28152594
202	Nitration	DQSKWKAYDATHLVK CHHHCEEEHHHHHHH	11.46	-
209	Ubiquitination	YDATHLVKSYPGSQL EHHHHHHHCCCCCEE	51.11	21890473
210	Phosphorylation	DATHLVKSYPGSQLD HHHHHHHCCCCCEEE	29.13	26657352
211	Nitration	ATHLVKSYPGSQLDI HHHHHHCCCCCEEEE	13.09	-
214	Phosphorylation	LVKSYPGSQLDILID HHHCCCCCEEEEEEE	24.06	27050516
246	Ubiquitination	FIAACTEKKIPVVFR EEHHHCCCCCCEEEE	37.54	-
247	Malonylation	IAACTEKKIPVVFRL EHHHCCCCCCEEEEE	46.11	26320211
247	Ubiquitination	IAACTEKKIPVVFRL EHHHCCCCCCEEEEE	46.11	-
258	Phosphorylation	VFRLQEGYDHSYYFI EEEECCCCCCCEEEE	15.10	-
262	Phosphorylation	QEGYDHSYYFIATFI CCCCCCCEEEEEHHH	10.04	22817900
263	Phosphorylation	EGYDHSYYFIATFIT CCCCCCEEEEEHHHH	7.48	22817900
278	Acetylation	DHIRHHAKYLNA--- HHHHHHHHHHCC---	46.01	19608861

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

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

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ESTD_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 ESTD_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MDHC_HUMAN	MDH1	physical	22939629
ESTD_HUMAN	ESD	physical	25416956
FSD2_HUMAN	FSD2	physical	25416956
FAXC_HUMAN	FAXC	physical	26344197
G6PI_HUMAN	GPI	physical	26344197
PIPNB_HUMAN	PITPNB	physical	26344197
UFM1_HUMAN	UFM1	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-39; LYS-200 AND LYS-278, ANDMASS SPECTROMETRY.
PubMed: 19608861