YGK3_YEAST - dbPTM
YGK3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YGK3_YEAST
UniProt AC Q12222
Protein Name Glycogen synthase kinase-3 homolog YGK3
Gene Name YGK3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 375
Subcellular Localization
Protein Description Required for heat stress-instigated phosphorylation of BCY1 which is involved in cell wall integrity signaling. Regulates activity of MSN2, a transcription factor that binds to the stress-response element (STRE). Probably promotes formation of a complex between MSN2 and DNA. Regulates the stability of ROG1..
Protein Sequence MLKVNNVFGSNPNRMTKLEDEHYFIDDIVSIKNRQKSKMYVREGKRIGHGSFGTVTQSILSSNSIEWLGPYAIKRVVKSPKVQSLELEILQNIRHPNLVTLEFFFESHCTTKDGGHLYQKNFVMEYIPQTLSSEIHEYFDNGSKMPTKHIKLYTFQILRALLTLHSMSICHGDLKPSNILIIPSSGIAKVCDFGSAQRLDDNTELKTYFCSRFYRAPELLLNSKDYTTQIDIWSLGCIIGEMIKGQPLFKGDSANSQLEEIAKLLGRFPKSSIKNSQELQDSLNDQKFKKFMHWFPSIEFFDVEFLLKVLTYDATERCDARQLMAHEFFDALRNETYFLPRGSSMPVHLPDLFNFSASEKRALGEYYNLIVPSLD
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 Orthologous
Protein Cluster
208PhosphorylationDNTELKTYFCSRFYR
CCHHHHHHHHHHHHC
10.8620377248
211PhosphorylationELKTYFCSRFYRAPE
HHHHHHHHHHHCCHH
18.6117287358
276PhosphorylationPKSSIKNSQELQDSL
CHHHCCCHHHHHHHH
21.7428889911
282PhosphorylationNSQELQDSLNDQKFK
CHHHHHHHHCHHHHH
18.9928889911

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 YGK3_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YGK3_YEAST !!

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 YGK3_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSP2_YEASTGSP2physical
11805837
TRXB1_YEASTTRR1physical
11805837
OYE2_YEASTOYE2physical
11805837
MDHM_YEASTMDH1physical
11805837
MSN2_YEASTMSN2genetic
12529445
MCK1_YEASTMCK1genetic
12529445
KAPR_YEASTBCY1physical
16319894
KCC2_YEASTCMK2physical
16319894
CYSD_YEASTMET17physical
16319894
RHO4_YEASTRHO4physical
16319894
PTK2_YEASTPTK2physical
16319894
PGM1_YEASTPGM1genetic
12529445
KHSE_YEASTTHR1genetic
19269370
SKI7_YEASTSKI7genetic
19269370
EI2BE_YEASTGCD6physical
20489023
LSM12_YEASTLSM12physical
20489023
MTC1_YEASTMTC1physical
20489023
PUF3_YEASTPUF3physical
20489023
METK1_YEASTSAM1physical
20489023
SPT16_YEASTSPT16physical
20489023
SYPM_YEASTAIM10physical
21460040
IF5A2_YEASTANB1physical
21460040
ARA2_YEASTARA2physical
21460040
CARB_YEASTCPA2physical
21460040
CRZ1_YEASTCRZ1physical
21460040
GLRX4_YEASTGRX4physical
21460040
GYS2_YEASTGSY2physical
21460040
NTF2_YEASTNTF2physical
21460040
KPR1_YEASTPRS1physical
21460040
RIM11_YEASTRIM11physical
21460040
UBX1_YEASTSHP1physical
21460040
YIG1_YEASTYIG1physical
21460040
CG11_YEASTCLN1genetic
21127252
REI1_YEASTREI1genetic
21127252
MET18_YEASTMET18genetic
21127252
MMS22_YEASTMMS22genetic
21127252
MET32_YEASTMET32genetic
21127252

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YGK3_YEAST

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND MASSSPECTROMETRY.
"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 TYR-208, AND MASSSPECTROMETRY.

TOP