GCH1_YEAST - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: GCH1_YEAST
• UniProt AC: P51601
• Protein Name: GTP cyclohydrolase 1
• Gene Name: FOL2
• Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
• Sequence Length: 243
• Protein Description: GTP cyclohydrolase 1 is the first enzyme in the biosynthetic pathway leading to folic acid..
• Protein Sequence: MHNIQLVQEIERHETPLNIRPTSPYTLNPPVERDGFSWPSVGTRQRAEETEEEEKERIQRISGAIKTILTELGEDVNREGLLDTPQRYAKAMLYFTKGYQTNIMDDVIKNAVFEEDHDEMVIVRDIEIYSLCEHHLVPFFGKVHIGYIPNKKVIGLSKLARLAEMYARRLQVQERLTKQIAMALSDILKPLGVAVVMEASHMCMVSRGIQKTGSSTVTSCMLGGFRAHKTREEFLTLLGRRSI

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
15	Phosphorylation	QEIERHETPLNIRPT HHHHHCCCCCCCCCC	27.27	22369663
22	Phosphorylation	TPLNIRPTSPYTLNP CCCCCCCCCCCCCCC	32.27	22369663
23	Phosphorylation	PLNIRPTSPYTLNPP CCCCCCCCCCCCCCC	20.70	22369663
25	Phosphorylation	NIRPTSPYTLNPPVE CCCCCCCCCCCCCCC	24.51	22369663
26	Phosphorylation	IRPTSPYTLNPPVER CCCCCCCCCCCCCCC	24.36	22890988
37	Phosphorylation	PVERDGFSWPSVGTR CCCCCCCCCCCCCCC	43.54	22369663
40	Phosphorylation	RDGFSWPSVGTRQRA CCCCCCCCCCCCHHH	27.24	22369663
43	Phosphorylation	FSWPSVGTRQRAEET CCCCCCCCCHHHHHC	22.82	22369663
55	Acetylation	EETEEEEKERIQRIS HHCHHHHHHHHHHHH	56.42	22865919
66	Acetylation	QRISGAIKTILTELG HHHHHHHHHHHHHHC	29.04	24489116
84	Phosphorylation	NREGLLDTPQRYAKA CCCCCCCCHHHHHHH	22.69	22369663
90	Ubiquitination	DTPQRYAKAMLYFTK CCHHHHHHHHHHHCC	25.95	23749301
90	Acetylation	DTPQRYAKAMLYFTK CCHHHHHHHHHHHCC	25.95	24489116
158	Acetylation	KKVIGLSKLARLAEM CCEECHHHHHHHHHH	51.73	24489116
242	Phosphorylation	LTLLGRRSI------ HHHHCCCCC------	31.15	21440633

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

Oops, there are no upstream regulatory protein records of GCH1_YEAST !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of GCH1_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 GCH1_YEAST !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GCH1_YEAST	FOL2	physical	10688190
SSB1_YEAST	SSB1	physical	19536198
ATPO_YEAST	ATP5	genetic	21623372
METE_YEAST	MET6	genetic	21623372
MDHP_YEAST	MDH3	genetic	21623372
FOLE_YEAST	MET7	genetic	21623372
CYS3_YEAST	CYS3	genetic	21623372
ALAT_YEAST	ALT2	genetic	21623372
TPS2_YEAST	TPS2	genetic	21623372
ARGJ_YEAST	ARG7	genetic	21623372
ATP5E_YEAST	ATP15	genetic	21623372
PDX3_YEAST	PDX3	genetic	21623372
PYC2_YEAST	PYC2	genetic	21623372
COQ7_YEAST	CAT5	genetic	21623372
ACON2_YEAST	ACO2	genetic	21623372
6PGD1_YEAST	GND1	genetic	21623372

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 THR-15; THR-22; SER-23 ANDTYR-25, AND MASS SPECTROMETRY.
PubMed: 18407956

"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-15; THR-22 AND SER-23,AND MASS SPECTROMETRY.
PubMed: 17563356

"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-15 AND SER-23, AND MASSSPECTROMETRY.
PubMed: 17330950