GSHB_YEAST - dbPTM
GSHB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GSHB_YEAST
UniProt AC Q08220
Protein Name Glutathione synthetase
Gene Name GSH2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 491
Subcellular Localization
Protein Description
Protein Sequence MAHYPPSKDQLNELIQEVNQWAITNGLSMYPPKFEENPSNASVSPVTIYPTPIPRKCFDEAVQIQPVFNELYARITQDMAQPDSYLHKTTEALALSDSEFTGKLWSLYLATLKSAQYKKQNFRLGIFRSDYLIDKKKGTEQIKQVEFNTVSVSFAGLSEKVDRLHSYLNRANKYDPKGPIYNDQNMVISDSGYLLSKALAKAVESYKSQQSSSTTSDPIVAFIVQRNERNVFDQKVLELNLLEKFGTKSVRLTFDDVNDKLFIDDKTGKLFIRDTEQEIAVVYYRTGYTTTDYTSEKDWEARLFLEKSFAIKAPDLLTQLSGSKKIQQLLTDEGVLGKYISDAEKKSSLLKTFVKIYPLDDTKLGREGKRLALSEPSKYVLKPQREGGGNNVYKENIPNFLKGIEERHWDAYILMELIEPELNENNIILRDNKSYNEPIISELGIYGCVLFNDEQVLSNEFSGSLLRSKFNTSNEGGVAAGFGCLDSIILY
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
4Phosphorylation----MAHYPPSKDQL
----CCCCCCCHHHH
13.8030377154
42PhosphorylationEENPSNASVSPVTIY
CCCCCCCCCCCEEEE
27.6428889911
44PhosphorylationNPSNASVSPVTIYPT
CCCCCCCCCEEEECC
15.9121551504
149PhosphorylationIKQVEFNTVSVSFAG
EEEEEEEEEEEEECC
21.3419795423
151PhosphorylationQVEFNTVSVSFAGLS
EEEEEEEEEEECCHH
15.2519823750
153PhosphorylationEFNTVSVSFAGLSEK
EEEEEEEEECCHHHH
11.2419823750
158PhosphorylationSVSFAGLSEKVDRLH
EEEECCHHHHHHHHH
34.1619823750
181PhosphorylationYDPKGPIYNDQNMVI
CCCCCCCCCCCCCEE
18.8019684113
189PhosphorylationNDQNMVISDSGYLLS
CCCCCEECCHHHHHH
17.8319684113
191PhosphorylationQNMVISDSGYLLSKA
CCCEECCHHHHHHHH
23.6519684113
193PhosphorylationMVISDSGYLLSKALA
CEECCHHHHHHHHHH
14.3919684113
244AcetylationLELNLLEKFGTKSVR
HHHHHHHHHCCCEEE
49.4124489116
266AcetylationDKLFIDDKTGKLFIR
CCEEEECCCCCEEEE
56.2724489116
286PhosphorylationIAVVYYRTGYTTTDY
EEEEEEECCCCCCCC
20.5827017623
288PhosphorylationVVYYRTGYTTTDYTS
EEEEECCCCCCCCCC
10.5727017623
289PhosphorylationVYYRTGYTTTDYTSE
EEEECCCCCCCCCCH
25.2727017623
290PhosphorylationYYRTGYTTTDYTSEK
EEECCCCCCCCCCHH
14.8027017623
293PhosphorylationTGYTTTDYTSEKDWE
CCCCCCCCCCHHHHH
15.2927017623
307UbiquitinationEARLFLEKSFAIKAP
HHHHHHHHHHCCCCH
53.6824961812
338AcetylationTDEGVLGKYISDAEK
CCCCCHHHHCCHHHH
34.9424489116
345AcetylationKYISDAEKKSSLLKT
HHCCHHHHHHHHHHH
60.7325381059
351AcetylationEKKSSLLKTFVKIYP
HHHHHHHHHHHEEEE
45.2524489116
363AcetylationIYPLDDTKLGREGKR
EEECCCCCCCHHCCE
56.8124489116
378AcetylationLALSEPSKYVLKPQR
EECCCCCCEEECCCC
50.5224489116
394AcetylationGGGNNVYKENIPNFL
CCCCCHHHCCCCHHH
39.7524489116

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 GSHB_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GSHB_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 GSHB_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSH1_YEASTGSH1genetic
12406228
UBC3_YEASTCDC34genetic
12406228
OPT1_YEASTOPT1genetic
21623372
CEM1_YEASTCEM1genetic
21623372
IDH2_YEASTIDH2genetic
21623372
PDE2_YEASTPDE2genetic
21623372
GSH1_YEASTGSH1genetic
21623372
FOLE_YEASTMET7genetic
21623372
ATPF_YEASTATP4genetic
21623372
COX6_YEASTCOX6genetic
21623372
PDX3_YEASTPDX3genetic
21623372
GPP2_YEASTGPP2genetic
21623372
RAD14_YEASTRAD14genetic
27708008
KPC1_YEASTPKC1genetic
27708008
DPOD_YEASTPOL3genetic
27708008
GPI8_YEASTGPI8genetic
27708008
GPI16_YEASTGPI16genetic
27708008
SSL1_YEASTSSL1genetic
27708008
CDC91_YEASTGAB1genetic
27708008
NSE5_YEASTNSE5genetic
27708008
OST2_YEASTOST2genetic
27708008
GPI2_YEASTGPI2genetic
27708008
BOL3_YEASTAIM1genetic
27708008
PEX22_YEASTPEX22genetic
27708008
TPS1_YEASTTPS1genetic
27708008
ODPB_YEASTPDB1genetic
27708008
SGF29_YEASTSGF29genetic
27708008
GPR1_YEASTGPR1genetic
27708008
RS16A_YEASTRPS16Bgenetic
27708008
RS16B_YEASTRPS16Bgenetic
27708008
HBT1_YEASTHBT1genetic
27708008
TPS2_YEASTTPS2genetic
27708008
GGA1_YEASTGGA1genetic
27708008
STP1_YEASTSTP1genetic
27708008
AST2_YEASTAST2genetic
27708008
RAD4_YEASTRAD4genetic
27708008
FIS1_YEASTFIS1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
PEX2_YEASTPEX2genetic
27708008
OPT1_YEASTOPT1genetic
27708008
DPOD3_YEASTPOL32genetic
27708008
IXR1_YEASTIXR1genetic
27708008
AIM26_YEASTAIM26genetic
27708008
RGT1_YEASTRGT1genetic
27708008
FABG_YEASTOAR1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
DNM1_YEASTDNM1genetic
27708008
BRE2_YEASTBRE2genetic
27708008
SRN2_YEASTSRN2genetic
27708008
CHS5_YEASTCHS5genetic
27708008
RS29A_YEASTRPS29Agenetic
27708008
ATP10_YEASTATP10genetic
27708008
VPS9_YEASTVPS9genetic
27708008
MSC1_YEASTMSC1genetic
27708008
AIM34_YEASTAIM34genetic
27708008
PALI_YEASTRIM9genetic
27708008
RIM13_YEASTRIM13genetic
27708008
YM35_YEASTYMR160Wgenetic
27708008
HFA1_YEASTHFA1genetic
27708008
ATP23_YEASTATP23genetic
27708008
COQ7_YEASTCAT5genetic
27708008
IDH2_YEASTIDH2genetic
27708008
RUP1_YEASTRUP1genetic
27708008
PALA_YEASTRIM20genetic
27708008
RU2A_YEASTLEA1genetic
27708008
EAF3_YEASTEAF3genetic
27708008
MED1_YEASTMED1genetic
27708008

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

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-42, AND MASSSPECTROMETRY.

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