dbPTM

RIB3_YEAST - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RIB3_YEAST
UniProt AC	Q99258
Protein Name	3,4-dihydroxy-2-butanone 4-phosphate synthase
Gene Name	RIB3
Organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length	208
Subcellular Localization
Protein Description	Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate..
Protein Sequence	MFTPIDQAIEHFKQNKFVIVMDDAGRENEGDLICAAENVSTEQMAFLVRHSSGYVCAPMTNAIADKLDLPLLRTGMKFESNDDDRHGTAYTITVDVAQGTTTGISAHDRSMTCRALADSSSTPKSFLKPGHICPLRAADGGVLQRRGHTEAGVDLCKLSGLSPVAVIGELVNDDEQGTMMRLNDCQAFGKKHGIPLISIEELAQYLKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Phosphorylation	-----MFTPIDQAIE -----CCCCHHHHHH	20.31	22369663
34	Glutathionylation	ENEGDLICAAENVST CCCCCEEEEEECCCH	3.69	22833525
54	Phosphorylation	LVRHSSGYVCAPMTN HHHCCCCCEEECCCH	8.36	21440633
56	Glutathionylation	RHSSGYVCAPMTNAI HCCCCCEEECCCHHH	2.37	22833525
80	Phosphorylation	RTGMKFESNDDDRHG CCCCCEECCCCCCCC	49.01	24930733
119	Phosphorylation	TCRALADSSSTPKSF HHHHHCCCCCCCHHH	22.15	30377154
120	Phosphorylation	CRALADSSSTPKSFL HHHHCCCCCCCHHHC	38.49	30377154
122	Phosphorylation	ALADSSSTPKSFLKP HHCCCCCCCHHHCCC	36.36	25752575
124	Acetylation	ADSSSTPKSFLKPGH CCCCCCCHHHCCCCC	54.66	24489116
133	Glutathionylation	FLKPGHICPLRAADG HCCCCCCCEEEECCC	1.84	22833525
190	Acetylation	NDCQAFGKKHGIPLI HHHHHHHHHHCCCEE	34.83	22865919
207	Acetylation	EELAQYLKK------ HHHHHHHCC------	52.05	24489116

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 RIB3_YEAST !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
56	C	Glutathionylation		21565288
S-glutathionylation of Cys-56 is reversible and dependent on the cytoplasmic isoform of glutaredoxin-2.

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 RIB3_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ELO3_YEAST	ELO3	genetic	21623372
THDH_YEAST	ILV1	genetic	21623372
TPS2_YEAST	TPS2	genetic	21623372
ERG2_YEAST	ERG2	genetic	21623372

Drug and Disease Associations

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

Regulatory Network of RIB3_YEAST

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-3, AND MASSSPECTROMETRY.	17563356 [Abstract]