GLC8_YEAST - dbPTM
GLC8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLC8_YEAST
UniProt AC P41818
Protein Name Protein GLC8
Gene Name GLC8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 229
Subcellular Localization
Protein Description Modulator of GLC7 type-1 protein phosphatase..
Protein Sequence MGGILKNPLALSPEQLAQQDPETLEEFRRQVYENTQKNAKLTSHKRNIPGLDNTKEEGEIIGTSSTFLPKDTLSLKHEQDMLAKMTPEERVQWNQRNLAENEITKKQFQDIHIDEPKTPYQGAVDPHGEYYRVDDDEDEDNSDKKPCQVANDDIDDLSLGEPEFEIKENKQPDFETNDENDEDSPEARHKKFEEMRKKHYDVRAIFNKKSREALKDEDEDEDDSTTKEP
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
12PhosphorylationLKNPLALSPEQLAQQ
CCCCCCCCHHHHHHC		22.3022369663
23PhosphorylationLAQQDPETLEEFRRQ
HHHCCHHHHHHHHHH		44.8722890988
40AcetylationENTQKNAKLTSHKRN
HHHHHHHHCCCCCCC		62.7925381059
63PhosphorylationEEGEIIGTSSTFLPK
CCCCEEEECCCCCCC		14.7527017623
64PhosphorylationEGEIIGTSSTFLPKD
CCCEEEECCCCCCCC		23.3621551504
65PhosphorylationGEIIGTSSTFLPKDT
CCEEEECCCCCCCCC		24.0219779198
66PhosphorylationEIIGTSSTFLPKDTL
CEEEECCCCCCCCCC		29.0327017623
74PhosphorylationFLPKDTLSLKHEQDM
CCCCCCCCCCHHHHH		37.1521440633
76AcetylationPKDTLSLKHEQDMLA
CCCCCCCCHHHHHHH		41.5424489116
105AcetylationLAENEITKKQFQDIH
HHHCCCCHHHHCCCC		50.6825381059
118PhosphorylationIHIDEPKTPYQGAVD
CCCCCCCCCCCCCCC		37.6325521595
120PhosphorylationIDEPKTPYQGAVDPH
CCCCCCCCCCCCCCC		25.4725521595
142PhosphorylationDDEDEDNSDKKPCQV
CCCCCCCCCCCCCEE		64.2329136822
158PhosphorylationNDDIDDLSLGEPEFE
CCCCCCCCCCCCCCC		41.1222369663
170UbiquitinationEFEIKENKQPDFETN
CCCCCCCCCCCCCCC		65.3823749301
176PhosphorylationNKQPDFETNDENDED
CCCCCCCCCCCCCCC		48.2222369663
184PhosphorylationNDENDEDSPEARHKK
CCCCCCCCHHHHHHH		23.6922369663
198AcetylationKFEEMRKKHYDVRAI
HHHHHHHHHHHHHHH		36.7125381059
210PhosphorylationRAIFNKKSREALKDE
HHHHCHHHHHHHCCC		36.6421551504
224PhosphorylationEDEDEDDSTTKEP--
CCCCCCCCCCCCC--		50.7417563356
225PhosphorylationDEDEDDSTTKEP---
CCCCCCCCCCCC---		49.2128132839
226PhosphorylationEDEDDSTTKEP----
CCCCCCCCCCC----		37.0425752575
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
118TPhosphorylationKinasePHO85P17157
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
118TPhosphorylation

12407105
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 GLC8_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PP12_YEASTGLC7physical
11805837
PPZ2_YEASTPPZ2physical
11805837
PHO85_YEASTPHO85physical
11805837
PCL6_YEASTPCL6physical
17634282
PP12_YEASTGLC7physical
17634282
SLT2_YEASTSLT2genetic
19269370
CKS1_YEASTCKS1genetic
19269370
SSD1_YEASTSSD1genetic
19269370
PFD2_YEASTGIM4genetic
19269370
UBP3_YEASTUBP3genetic
19269370
SKN7_YEASTSKN7genetic
19269370
CUL8_YEASTRTT101genetic
19269370
BCK1_YEASTBCK1genetic
19269370
CTK1_YEASTCTK1genetic
19269370
SDS22_YEASTSDS22genetic
19269370
VAC14_YEASTVAC14genetic
19269370
TCO89_YEASTTCO89genetic
21368139
UBX1_YEASTSHP1genetic
23418575
PP12_YEASTGLC7physical
23418575
SNX4_YEASTSNX4genetic
24586198
REG1_YEASTREG1genetic
24586198
SNF1_YEASTSNF1genetic
24586198
EFM2_YEASTEFM2genetic
27708008
ILV6_YEASTILV6genetic
27708008
AGP1_YEASTAGP1genetic
27708008
RNQ1_YEASTRNQ1genetic
27708008
LSB5_YEASTLSB5genetic
27708008
YCR3_YEASTYCR023Cgenetic
27708008
BPH1_YEASTBPH1genetic
27708008
HCM1_YEASTHCM1genetic
27708008
RS29B_YEASTRPS29Bgenetic
27708008
VAM7_YEASTVAM7genetic
27708008
ICE2_YEASTICE2genetic
27708008
ALLA_YEASTDAL3genetic
27708008
YRA2_YEASTYRA2genetic
27708008
RAD10_YEASTRAD10genetic
27708008
VAM3_YEASTVAM3genetic
27708008
AXL1_YEASTAXL1genetic
27708008
LTE1_YEASTLTE1genetic
27708008
RL23A_YEASTRPL23Agenetic
27708008
RL23B_YEASTRPL23Agenetic
27708008
H4_YEASTHHF1genetic
27708008
H3_YEASTHHT1genetic
27708008
SHG1_YEASTSHG1genetic
27708008
TXTP_YEASTCTP1genetic
27708008
POF1_YEASTPOF1genetic
27708008
PAT1_YEASTPAT1genetic
27708008
YCZ2_YEASTYCR102Cgenetic
27708008
YD012_YEASTYDL012Cgenetic
27708008
RPN4_YEASTRPN4genetic
27708008
RTK1_YEASTRTK1genetic
27708008
MRX9_YEASTYDL027Cgenetic
27708008
PEX19_YEASTPEX19genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
CYK3_YEASTCYK3genetic
27708008
RLA3_YEASTRPP1Bgenetic
27708008
RL35A_YEASTRPL35Agenetic
27708008
RL35B_YEASTRPL35Agenetic
27708008
RAD57_YEASTRAD57genetic
27708008
YD286_YEASTYDR286Cgenetic
27708008
INM2_YEASTINM2genetic
27708008
CEM1_YEASTCEM1genetic
27708008
AIM11_YEASTAIM11genetic
27708008
HUR1_YEASTHUR1genetic
27708008
SLT2_YEASTSLT2genetic
27708008
PIH1_YEASTPIH1genetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
PRY3_YEASTPRY3genetic
27708008
BCK1_YEASTBCK1genetic
27708008
CYP7_YEASTCPR7genetic
27708008
RL43A_YEASTRPL43Bgenetic
27708008
RL43B_YEASTRPL43Bgenetic
27708008
ELM1_YEASTELM1genetic
27708008
KDX1_YEASTKDX1genetic
27708008
FPS1_YEASTFPS1genetic
27708008
RSSA2_YEASTRPS0Bgenetic
27708008
SWI6_YEASTSWI6genetic
27708008
VIP1_YEASTVIP1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
YP034_YEASTYPL034Wgenetic
27708008
ISU1_YEASTISU1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
THP3_YEASTTHP3genetic
27708008
SPEE_YEASTSPE3genetic
27708008
SYT1_YEASTSYT1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLC8_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-12; SER-158 AND SER-184,AND MASS SPECTROMETRY.
"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 SER-12; SER-184 AND SER-224,AND MASS SPECTROMETRY.
"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 SER-158, AND MASSSPECTROMETRY.
"Pho85 phosphorylates the Glc7 protein phosphatase regulator Glc8 invivo.";
Tan Y.S.H., Morcos P.A., Cannon J.F.;
J. Biol. Chem. 278:147-153(2003).
Cited for: PHOSPHORYLATION AT THR-118.

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