VHS3_YEAST - dbPTM
VHS3_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VHS3_YEAST
UniProt AC Q08438
Protein Name Phosphopantothenoylcysteine decarboxylase subunit VHS3
Gene Name VHS3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 674
Subcellular Localization
Protein Description Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance..
Protein Sequence MTNKSSLKNNRKGVASNTLSGAEQANIGSSAMPDTNSTGPFSSVSSLDTPVVRKSTSPTGSQTKSIMNASGTSGAVVSNTPEPGLKRIPTVTFSDPKLGSLRSDVEQTPPNQVARQSSEKKATSVHIAAEGANQGRNLKDINTKVPKDGEASASSFSTPTSILSNADMGNNISSLLAKKLSFTGGTDSILNSDNSSDSPRKEHPHFYVEDPLHTPSVRSRSNSTSPRPSVVVNTFNPINIEREGSISKTGEPTLLESVLEEAMSPNAVSNPLKRENIMTNMDPRLPQDDGKLHVLFGATGSLSVFKLKHMIRKLEEIYGRDKICIQVILTNSATKFFAMKYMRKNKKQHNSIDTSFNSTNSNAGNITGNKKKVASLEKFSIQKTSSNSAASQTNNKQEEEKQMASTTGFPSTLGGSRTYSNSSNVVSQHPQIELPAHIQFWTDQDEWDVWRQRTDPVLHIELRRWADILVVAPLTANTLAKIALGLCDNLLTSVIRAWNPTFPIFLAPSMGSGTFNSIMTKKHFRIIQEEMPWVTVFKPSEKVMGINGDIGLSGMMDANEIVGKIVVKLGGYPDVSAGKEEEEDEDNDEEDDNKKNDTGGKDEDNDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDEDDEDEDEDDEGKKKEDKGGLQRS
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
55PhosphorylationDTPVVRKSTSPTGSQ
CCCCCCCCCCCCCCC		24.4528889911
57PhosphorylationPVVRKSTSPTGSQTK
CCCCCCCCCCCCCCC		27.7927214570
65PhosphorylationPTGSQTKSIMNASGT
CCCCCCCEEEECCCC		30.3824961812
78PhosphorylationGTSGAVVSNTPEPGL
CCCCCEECCCCCCCC		28.5224961812
80PhosphorylationSGAVVSNTPEPGLKR
CCCEECCCCCCCCCC		22.8624961812
90PhosphorylationPGLKRIPTVTFSDPK
CCCCCCCEEEECCCC		29.7922369663
92PhosphorylationLKRIPTVTFSDPKLG
CCCCCEEEECCCCCC		21.6522369663
94PhosphorylationRIPTVTFSDPKLGSL
CCCEEEECCCCCCCC		43.5722369663
103PhosphorylationPKLGSLRSDVEQTPP
CCCCCCCCCCCCCCC		51.8322369663
108PhosphorylationLRSDVEQTPPNQVAR
CCCCCCCCCCCHHHC		27.4922369663
117PhosphorylationPNQVARQSSEKKATS
CCHHHCCCCCCCCCE		34.6124961812
118PhosphorylationNQVARQSSEKKATSV
CHHHCCCCCCCCCEE		45.1321440633
143PhosphorylationRNLKDINTKVPKDGE
CCHHHCCCCCCCCCC		33.4822369663
152PhosphorylationVPKDGEASASSFSTP
CCCCCCCCCCCCCCC		25.1230377154
154PhosphorylationKDGEASASSFSTPTS
CCCCCCCCCCCCCHH		29.4430377154
155PhosphorylationDGEASASSFSTPTSI
CCCCCCCCCCCCHHH		23.9621440633
157PhosphorylationEASASSFSTPTSILS
CCCCCCCCCCHHHHH		35.1121551504
158PhosphorylationASASSFSTPTSILSN
CCCCCCCCCHHHHHC		28.6821551504
160PhosphorylationASSFSTPTSILSNAD
CCCCCCCHHHHHCCC		28.6127017623
161PhosphorylationSSFSTPTSILSNADM
CCCCCCHHHHHCCCC		23.8021440633
164PhosphorylationSTPTSILSNADMGNN
CCCHHHHHCCCCCCC		28.4430377154
181PhosphorylationSLLAKKLSFTGGTDS
HHHHHHHCCCCCCCH		29.6422369663
183PhosphorylationLAKKLSFTGGTDSIL
HHHHHCCCCCCCHHC		31.1822369663
186PhosphorylationKLSFTGGTDSILNSD
HHCCCCCCCHHCCCC		28.1122369663
188PhosphorylationSFTGGTDSILNSDNS
CCCCCCCHHCCCCCC		28.9022369663
192PhosphorylationGTDSILNSDNSSDSP
CCCHHCCCCCCCCCC		34.4222369663
195PhosphorylationSILNSDNSSDSPRKE
HHCCCCCCCCCCCCC		40.2822369663
196PhosphorylationILNSDNSSDSPRKEH
HCCCCCCCCCCCCCC		48.6522369663
198PhosphorylationNSDNSSDSPRKEHPH
CCCCCCCCCCCCCCC		28.6622369663
207PhosphorylationRKEHPHFYVEDPLHT
CCCCCCEEECCCCCC		10.4122369663
214PhosphorylationYVEDPLHTPSVRSRS
EECCCCCCCCCCCCC		25.5822369663
216PhosphorylationEDPLHTPSVRSRSNS
CCCCCCCCCCCCCCC		31.1722369663
219PhosphorylationLHTPSVRSRSNSTSP
CCCCCCCCCCCCCCC		37.5922369663
221PhosphorylationTPSVRSRSNSTSPRP
CCCCCCCCCCCCCCC		36.0622369663
223PhosphorylationSVRSRSNSTSPRPSV
CCCCCCCCCCCCCEE		31.3522369663
224PhosphorylationVRSRSNSTSPRPSVV
CCCCCCCCCCCCEEE		47.1822369663
225PhosphorylationRSRSNSTSPRPSVVV
CCCCCCCCCCCEEEE		20.8022369663
229PhosphorylationNSTSPRPSVVVNTFN
CCCCCCCEEEEECCC		28.9022369663
234PhosphorylationRPSVVVNTFNPINIE
CCEEEEECCCCCEEE		17.1222369663
245PhosphorylationINIEREGSISKTGEP
CEEECCCCCCCCCCC		20.9525752575
253PhosphorylationISKTGEPTLLESVLE
CCCCCCCCHHHHHHH		39.4123607784
257PhosphorylationGEPTLLESVLEEAMS
CCCCHHHHHHHHHCC		31.7822369663
264PhosphorylationSVLEEAMSPNAVSNP
HHHHHHCCCCCCCCC		23.2722369663
269PhosphorylationAMSPNAVSNPLKREN
HCCCCCCCCCCHHHC		30.2522369663
378AcetylationKKVASLEKFSIQKTS
HHEEEEEEEEEEECC		50.1024489116
386PhosphorylationFSIQKTSSNSAASQT
EEEEECCCCCCCHHC		39.7823749301
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 VHS3_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VHS3_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 VHS3_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PPZ1_YEASTPPZ1physical
15192104
CAB3_YEASTCAB3physical
18719252
TRK2_YEASTTRK2genetic
23454581
SIS2_YEASTSIS2genetic
23454581
CG13_YEASTCLN3genetic
27708008
UBP13_YEASTUBP13genetic
27708008
SIF2_YEASTSIF2genetic
27708008
ELO2_YEASTELO2genetic
27708008
BUD31_YEASTBUD31genetic
27708008
GPR1_YEASTGPR1genetic
27708008
ARO1_YEASTARO1genetic
27708008
SAS4_YEASTSAS4genetic
27708008
AROC_YEASTARO2genetic
27708008
MED5_YEASTNUT1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
SSBP1_YEASTSBP1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YJ24_YEASTKCH1genetic
27708008
SIS2_YEASTSIS2genetic
27708008
ENV10_YEASTENV10genetic
27708008
SOK2_YEASTSOK2genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
NAA30_YEASTMAK3genetic
27708008
CHMU_YEASTARO7genetic
27708008
SPEE_YEASTSPE3genetic
27708008
MED1_YEASTMED1genetic
27708008
CAB3_YEASTCAB3physical
26514574
VHS3_YEASTVHS3physical
26514574
COAC_HUMANPPCDCphysical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VHS3_YEAST

loading...

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 THR-90; SER-181; SER-221;SER-223; THR-224 AND SER-225, 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 THR-90; SER-181 AND SER-264,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 THR-90, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-90, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory