GRE2_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GRE2_YEAST
• UniProt AC: Q12068
• Protein Name: NADPH-dependent methylglyoxal reductase GRE2
• Gene Name: GRE2
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 342
• Subcellular Localization: Cytoplasm . Nucleus .
• Protein Description: Catalyzes the irreversible reduction of the cytotoxic compound methylglyoxal (MG, 2-oxopropanal) to (S)-lactaldehyde as an alternative to detoxification of MG by glyoxalase I GLO1. MG is synthesized via a bypath of glycolysis from dihydroxyacetone phosphate and is believed to play a role in cell cycle regulation and stress adaptation. Also catalyzes the reduction of 3-methylbutanal to 3-methylbutanol. Acts as a suppressor of 3-methylbutanol-induced filamentation by modulating the levels of 3-methylbutanal, the signal to which cells respond by filamentation. Also involved in ergosterol metabolism..
• Protein Sequence: MSVFVSGANGFIAQHIVDLLLKEDYKVIGSARSQEKAENLTEAFGNNPKFSMEVVPDISKLDAFDHVFQKHGKDIKIVLHTASPFCFDITDSERDLLIPAVNGVKGILHSIKKYAADSVERVVLTSSYAAVFDMAKENDKSLTFNEESWNPATWESCQSDPVNAYCGSKKFAEKAAWEFLEENRDSVKFELTAVNPVYVFGPQMFDKDVKKHLNTSCELVNSLMHLSPEDKIPELFGGYIDVRDVAKAHLVAFQKRETIGQRLIVSEARFTMQDVLDILNEDFPVLKGNIPVGKPGSGATHNTLGATLDNKKSKKLLGFKFRNLKETIDDTASQILKFEGRI

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
36	Acetylation	GSARSQEKAENLTEA CCCCCHHHHHHHHHH	54.05	24489116
36	Ubiquitination	GSARSQEKAENLTEA CCCCCHHHHHHHHHH	54.05	23749301
70	Acetylation	AFDHVFQKHGKDIKI HHHHHHHHHCCEEEE	42.74	24489116
113	Acetylation	GILHSIKKYAADSVE HHHHHHHHHHCCCCC	38.15	25381059
297	Phosphorylation	IPVGKPGSGATHNTL CCCCCCCCCCCCCCC	33.51	27017623
300	Phosphorylation	GKPGSGATHNTLGAT CCCCCCCCCCCCCCC	21.13	27017623
311	Acetylation	LGATLDNKKSKKLLG CCCCCCCHHHHHHHC	59.08	24489116
320	Acetylation	SKKLLGFKFRNLKET HHHHHCCCCCCHHHH	41.43	24489116
327	Phosphorylation	KFRNLKETIDDTASQ CCCCHHHHHCHHHHH	28.28	21126336
331	Phosphorylation	LKETIDDTASQILKF HHHHHCHHHHHHHHH	25.18	22369663
333	Phosphorylation	ETIDDTASQILKFEG HHHCHHHHHHHHHCC	21.61	22369663
337	Acetylation	DTASQILKFEGRI-- HHHHHHHHHCCCC--	42.89	24489116

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

Oops, there are no upstream regulatory protein records of GRE2_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GRE2_YEAST !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of GRE2_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SSB1_YEAST	SSB1	physical	19536198
HAL5_YEAST	HAL5	genetic	20093466
SAC1_YEAST	SAC1	genetic	20093466
VPS24_YEAST	VPS24	genetic	20093466
CAF4_YEAST	CAF4	genetic	20093466
AVO2_YEAST	AVO2	genetic	20093466
MRX11_YEAST	YPL041C	genetic	20093466
SRS2_YEAST	SRS2	genetic	21459050
COX7_YEAST	COX7	genetic	21623372
GRE2_YEAST	GRE2	physical	24879127
RV161_YEAST	RVS161	genetic	27708008
IMG2_YEAST	IMG2	genetic	27708008
GPR1_YEAST	GPR1	genetic	27708008
LRG1_YEAST	LRG1	genetic	27708008
HEL2_YEAST	HEL2	genetic	27708008
SNF6_YEAST	SNF6	genetic	27708008
VPS24_YEAST	VPS24	genetic	27708008
COA4_YEAST	COA4	genetic	27708008
MRX11_YEAST	YPL041C	genetic	27708008

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333, AND MASSSPECTROMETRY.
PubMed: 18407956