LGUL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: LGUL_HUMAN
• UniProt AC: Q04760
• Protein Name: Lactoylglutathione lyase
• Gene Name: GLO1
• Organism: Homo sapiens (Human).
• Sequence Length: 184
• Protein Description: Catalyzes the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione. Involved in the regulation of TNF-induced transcriptional activity of NF-kappa-B. Required for normal osteoclastogenesis..
• Protein Sequence: MAEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPDGYWIEILNPNKMATLM

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	------MAEPQPPSG ------CCCCCCCCC	36.86	20454679
8	Phosphorylation	MAEPQPPSGGLTDEA CCCCCCCCCCCCHHH	52.77	27050516
12	Phosphorylation	QPPSGGLTDEAALSC CCCCCCCCHHHHHHH	34.76	24043423
18	Phosphorylation	LTDEAALSCCSDADP CCHHHHHHHCCCCCH	14.35	24043423
21	Phosphorylation	EAALSCCSDADPSTK HHHHHHCCCCCHHHH	39.91	24043423
26	Phosphorylation	CCSDADPSTKDFLLQ HCCCCCHHHHHHHHH	48.95	24043423
27	Phosphorylation	CSDADPSTKDFLLQQ CCCCCHHHHHHHHHH	39.77	24043423
35	Phosphorylation	KDFLLQQTMLRVKDP HHHHHHHHHHHCCCC	12.76	21406692
36	Sulfoxidation	DFLLQQTMLRVKDPK HHHHHHHHHHCCCCC	1.63	21406390
38	Methylation	LLQQTMLRVKDPKKS HHHHHHHHCCCCCCC	23.71	-
44	Ubiquitination	LRVKDPKKSLDFYTR HHCCCCCCCHHHHHH	62.73	-
44	2-Hydroxyisobutyrylation	LRVKDPKKSLDFYTR HHCCCCCCCHHHHHH	62.73	-
45	Phosphorylation	RVKDPKKSLDFYTRV HCCCCCCCHHHHHHH	39.02	20068231
49	Phosphorylation	PKKSLDFYTRVLGMT CCCCHHHHHHHHCCH	8.03	28152594
50	Phosphorylation	KKSLDFYTRVLGMTL CCCHHHHHHHHCCHH	17.81	28152594
55	Sulfoxidation	FYTRVLGMTLIQKCD HHHHHHCCHHHHHCC	2.11	21406390
60	Acetylation	LGMTLIQKCDFPIMK HCCHHHHHCCCCCHH	28.86	26051181
60	Ubiquitination	LGMTLIQKCDFPIMK HCCHHHHHCCCCCHH	28.86	-
61	Glutathionylation	GMTLIQKCDFPIMKF CCHHHHHCCCCCHHE	3.60	22555962
61	S-nitrosylation	GMTLIQKCDFPIMKF CCHHHHHCCCCCHHE	3.60	19483679
61	S-nitrosocysteine	GMTLIQKCDFPIMKF CCHHHHHCCCCCHHE	3.60	-
85	Acetylation	KNDIPKEKDEKIAWA CCCCCHHHHHHHHHH	76.84	25953088
88	Succinylation	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	21890473
88	Succinylation	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	-
88	Ubiquitination	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	21890473
88	Acetylation	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	25953088
88	Ubiquitination	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	21890473
88	Ubiquitination	IPKEKDEKIAWALSR CCHHHHHHHHHHHHC	48.10	21890473
107	Phosphorylation	ELTHNWGTEDDETQS EEEECCCCCCCCCHH	28.05	19199007
136	Phosphorylation	GIAVPDVYSACKRFE EEECHHHHHHHHHHH	9.64	28152594
137	Phosphorylation	IAVPDVYSACKRFEE EECHHHHHHHHHHHH	27.34	28152594
139	S-nitrosylation	VPDVYSACKRFEELG CHHHHHHHHHHHHHC	2.39	25040305
139	S-glutathionyl cysteine	VPDVYSACKRFEELG CHHHHHHHHHHHHHC	2.39	-
139	Glutathionylation	VPDVYSACKRFEELG CHHHHHHHHHHHHHC	2.39	22555962
140	Ubiquitination	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	21890473
140	2-Hydroxyisobutyrylation	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	-
140	Malonylation	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	26320211
140	Acetylation	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	25953088
140	Ubiquitination	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	21890473
140	Ubiquitination	PDVYSACKRFEELGV HHHHHHHHHHHHHCC	60.89	21890473
148	Ubiquitination	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	21890473
148	Ubiquitination	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	21890473
148	Succinylation	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	19608861
148	Acetylation	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	19608861
148	2-Hydroxyisobutyrylation	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	-
148	Succinylation	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	-
148	Ubiquitination	RFEELGVKFVKKPDD HHHHHCCEEEECCCC	42.51	21890473
151	2-Hydroxyisobutyrylation	ELGVKFVKKPDDGKM HHCCEEEECCCCCCE	62.82	-
151	Ubiquitination	ELGVKFVKKPDDGKM HHCCEEEECCCCCCE	62.82	-
157	2-Hydroxyisobutyrylation	VKKPDDGKMKGLAFI EECCCCCCEEEEEEE	44.42	-
157	Acetylation	VKKPDDGKMKGLAFI EECCCCCCEEEEEEE	44.42	26051181
159	Acetylation	KPDDGKMKGLAFIQD CCCCCCEEEEEEEEC	55.01	7705855

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
107	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
107	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
107	T	Phosphorylation	Phosphorylated at Thr-107 in the presence of CaMK2.	19199007
139	C	Glutathionylation	Glutathionylation at Cys-139 inhibits enzyme activity.	20454679

Disease-associated PTM Sites based on SAP

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

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PNPH_HUMAN	PNP	physical	22939629
NEMO_HUMAN	IKBKG	physical	21988832
M3K13_HUMAN	MAP3K13	physical	21988832
MEOX2_HUMAN	MEOX2	physical	24722188
ACY1_HUMAN	ACY1	physical	26344197
ALDR_HUMAN	AKR1B1	physical	26344197
AK1BF_HUMAN	AKR1B15	physical	26344197
PUR9_HUMAN	ATIC	physical	26344197
FABP5_HUMAN	FABP5	physical	26344197
GLOD4_HUMAN	GLOD4	physical	26344197
GRHPR_HUMAN	GRHPR	physical	26344197
ROA1_HUMAN	HNRNPA1	physical	26344197
DHB14_HUMAN	HSD17B14	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
IMPA2_HUMAN	IMPA2	physical	26344197
AGM1_HUMAN	PGM3	physical	26344197
PGP_HUMAN	PGP	physical	26344197
IPYR_HUMAN	PPA1	physical	26344197
PSMG4_HUMAN	PSMG4	physical	26344197
DHPR_HUMAN	QDPR	physical	26344197
STIP1_HUMAN	STIP1	physical	26344197
TKT_HUMAN	TKT	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
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Acetylation

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330

"Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation.";
Birkenmeier G., Stegemann C., Hoffmann R., Gunther R., Huse K.,Birkemeyer C.;
PLoS ONE 5:E10399-E10399(2010).
Cited for: PROTEIN SEQUENCE OF 13-18 AND 128-135, ENZYME REGULATION,BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY, REMOVAL OF INITIATORMETHIONINE, ACETYLATION AT ALA-2, GLUTATHIONYLATION AT CYS-139, ANDDISULFIDE BONDS.
PubMed: 20454679

"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-148, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"Phosphorylation on Thr-106 and NO-modification of glyoxalase Isuppress the TNF-induced transcriptional activity of NF-kappaB.";
de Hemptinne V., Rondas D., Toepoel M., Vancompernolle K.;
Mol. Cell. Biochem. 325:169-178(2009).
Cited for: FUNCTION, PHOSPHORYLATION AT THR-107, AND MUTAGENESIS OF CYS-19;CYS-20; SER-45; SER-69; SER-94; THR-98; THR-102; THR-107 AND CYS-139.
PubMed: 19199007