dbPTM

GGT1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	GGT1_HUMAN
UniProt AC	P19440
Protein Name	Glutathione hydrolase 1 proenzyme
Gene Name	GGT1
Organism	Homo sapiens (Human).
Sequence Length	569
Subcellular Localization	Cell membrane Single-pass type II membrane protein .
Protein Description	Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates, and other gamma-glutamyl compounds. The metabolism of glutathione releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases. In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound. Initiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracellular GSH level. It is part of the cell antioxidant defense mechanism. Isoform 3 seems to be inactive..
Protein Sequence	MKKKLVVLGLLAVVLVLVIVGLCLWLPSASKEPDNHVYTRAAVAADAKQCSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTRKAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDRKVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVTAEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFSRESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEFFAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAVEEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVRTAGGWAAASDSRKGGEPAGY

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
48	2-Hydroxyisobutyrylation	AAVAADAKQCSKIGR HHHHHCHHHHHHHCH	53.00	-
95	N-linked_Glycosylation	GLFLTIYNSTTRKAE EEEEEEEECCCCCEE	29.09	20622017
120	N-linked_Glycosylation	LAFATMFNSSEQSQK HHHHHCCCCCHHHHC	33.53	24047895
172	Ubiquitination	RQGFPVGKGLAAALE HCCCCCCHHHHHHHH	51.49	-
181	Ubiquitination	LAAALENKRTVIEQQ HHHHHHCCCCHHHCC	39.82	-
181	2-Hydroxyisobutyrylation	LAAALENKRTVIEQQ HHHHHHCCCCHHHCC	39.82	-
230	N-linked_Glycosylation	EGAQAFYNGSLTAQI HCCHHHHCCCHHHHH	27.42	24047895
266	N-linked_Glycosylation	ELIEHPLNISLGDVV HHHHCCCCCCCCCEE	26.67	24047895
296	Phosphorylation	ILNILKGYNFSRESV HHHHHCCCCCCHHHC	16.08	-
297	N-linked_Glycosylation	LNILKGYNFSRESVE HHHHCCCCCCHHHCC	36.77	20622017
334	Ubiquitination	RTLLGDPKFVDVTEV HHHHCCCCCCCHHHH	63.86	-
344	N-linked_Glycosylation	DVTEVVRNMTSEFFA CHHHHHHHHCHHHHH	26.86	24047895
438	O-linked_Glycosylation	NEFGVPPSPANFIQP CCCCCCCCCCCCCCC	30.49	OGP
511	N-linked_Glycosylation	LHNQLLPNVTTVERN HHHCCCCCCEEEECC	43.68	15084671
550	Phosphorylation	VVQAIVRTAGGWAAA HHHHHHHHCCCHHCC	20.82	-

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 GGT1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of GGT1_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 GGT1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GGT1_HUMAN	GGT1	physical	4442
GGT1_HUMAN	GGT1	physical	18197
GGT1_HUMAN	GGT1	physical	7816801
GGT1_HUMAN	GGT1	physical	8827453
GGT1_HUMAN	GGT1	physical	1978610
GGT1_HUMAN	GGT1	physical	6112969

Drug and Disease Associations

Kegg Disease
H00048	Hepatocellular carcinoma
OMIM Disease
231950	Glutathionuria (GLUTH)
Kegg Drug
D02755	Acivicin (USAN/INN)
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of GGT1_HUMAN

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Analysis of site-specific glycosylation of renal and hepatic gamma-glutamyl transpeptidase from normal human tissue."; West M.B., Segu Z.M., Feasley C.L., Kang P., Klouckova I., Li C.,Novotny M.V., West C.M., Mechref Y., Hanigan M.H.; J. Biol. Chem. 285:29511-29524(2010). Cited for: FUNCTION, CATALYTIC ACTIVITY, AND GLYCOSYLATION AT ASN-95; ASN-120;ASN-230; ASN-266; ASN-297; ASN-344 AND ASN-511.	20622017 [Abstract]
"Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."; Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,Schiess R., Aebersold R., Watts J.D.; Nat. Biotechnol. 27:378-386(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120, AND MASSSPECTROMETRY.	19349973 [Abstract]
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-120; ASN-230 AND ASN-511,AND MASS SPECTROMETRY.	19159218 [Abstract]
"A proteomic analysis of human bile."; Kristiansen T.Z., Bunkenborg J., Gronborg M., Molina H.,Thuluvath P.J., Argani P., Goggins M.G., Maitra A., Pandey A.; Mol. Cell. Proteomics 3:715-728(2004). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-511, AND MASSSPECTROMETRY.	15084671 [Abstract]