ZRG17_YEAST - dbPTM
ZRG17_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRG17_YEAST
UniProt AC P53735
Protein Name Protein ZRG17
Gene Name ZRG17
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 605
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description
Protein Sequence METPQMNAIQEEDNLSPEVAFQTPKLNDSDASSFSLSNMNAVGNVDGIPSQNRTFFASPRPSSLFYSAKEGNNSSSSIIYNPSFTFGENASSNANINEAALMKGKGNEGRRQSLKYIPAPKLVPPPPRTRSPVRGISPDAGSSKRSSMTLDSPFNFTTSTLQPHQQTPPSSAASRTSFRKGHRYKHSSVSMNFFQEPEVKIPLNIAKSLPIPDFNDLLSNLPWPKAYIQLSIAALQIFACLITFQVGHLYSWSNFITLSHFITYDIIGSLVIIFVENLSQFQVWFTGTITFPFGLNRIDVLLSFALAVSLCFVGLDLLFHIIEEFIVLFVESGSSLTNNHDHDEINEQIPHSHIANANDSQNENITLWYSILMINLVLSTLSLYKTFYANKYSNLKTKNPIITITYTAYLFIYPLLLDLLSSISDYLATLVISSLILWHGLTIARWTSTVLLMGFSTTSLSNSALFNNNDSTDTTAHTQQVESKAAKEKPSVRPRSMSSLPIATKNTKIRKTGFLNSAGFTENPTTIKNMIKDQIERLSEFKSRYILNYDDIVISKVNFTLYVVLIKITMKGGSDDDELMLRLAIDKCIQTSIPTCETTIDIDRI
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
3Phosphorylation-----METPQMNAIQ
-----CCCCCCCCCC		19.9528152593
16PhosphorylationIQEEDNLSPEVAFQT
CCCCCCCCHHHHCCC		25.8528152593
23PhosphorylationSPEVAFQTPKLNDSD
CHHHHCCCCCCCCCC		18.8830377154
29PhosphorylationQTPKLNDSDASSFSL
CCCCCCCCCCCCCCC		33.7224961812
32PhosphorylationKLNDSDASSFSLSNM
CCCCCCCCCCCCCCC		36.5924961812
33PhosphorylationLNDSDASSFSLSNMN
CCCCCCCCCCCCCCC		22.1521440633
35PhosphorylationDSDASSFSLSNMNAV
CCCCCCCCCCCCCCC		32.6021440633
37PhosphorylationDASSFSLSNMNAVGN
CCCCCCCCCCCCCCC		32.6024961812
54PhosphorylationGIPSQNRTFFASPRP
CCCCCCCEEEECCCC		30.5622369663
58PhosphorylationQNRTFFASPRPSSLF
CCCEEEECCCCHHHE		19.1122369663
62PhosphorylationFFASPRPSSLFYSAK
EEECCCCHHHEEECC		40.7422369663
63PhosphorylationFASPRPSSLFYSAKE
EECCCCHHHEEECCC		25.7722369663
66PhosphorylationPRPSSLFYSAKEGNN
CCCHHHEEECCCCCC		17.0122369663
67PhosphorylationRPSSLFYSAKEGNNS
CCHHHEEECCCCCCC		26.0622369663
75PhosphorylationAKEGNNSSSSIIYNP
CCCCCCCCCCEEECC		30.1721551504
77PhosphorylationEGNNSSSSIIYNPSF
CCCCCCCCEEECCCC		18.2321551504
115AcetylationEGRRQSLKYIPAPKL
HHHHCCCEEECCCCC		46.5125381059
129PhosphorylationLVPPPPRTRSPVRGI
CCCCCCCCCCCCCCC		41.0721440633
131PhosphorylationPPPPRTRSPVRGISP
CCCCCCCCCCCCCCC		27.4322369663
137PhosphorylationRSPVRGISPDAGSSK
CCCCCCCCCCCCCCC		21.3925752575
142PhosphorylationGISPDAGSSKRSSMT
CCCCCCCCCCCCCCC		34.1124961812
143PhosphorylationISPDAGSSKRSSMTL
CCCCCCCCCCCCCCC		31.0424961812
146PhosphorylationDAGSSKRSSMTLDSP
CCCCCCCCCCCCCCC		28.3528889911
147PhosphorylationAGSSKRSSMTLDSPF
CCCCCCCCCCCCCCC		21.5919779198
149PhosphorylationSSKRSSMTLDSPFNF
CCCCCCCCCCCCCCC		29.3928889911
152PhosphorylationRSSMTLDSPFNFTTS
CCCCCCCCCCCCCCC		34.2119779198
157PhosphorylationLDSPFNFTTSTLQPH
CCCCCCCCCCCCCCC		22.4228889911
167PhosphorylationTLQPHQQTPPSSAAS
CCCCCCCCCCCCCCC		30.5125752575
184PhosphorylationSFRKGHRYKHSSVSM
CCCCCCCCCCCCEEE		13.8428889911
187PhosphorylationKGHRYKHSSVSMNFF
CCCCCCCCCEEECCC		28.4319684113
188PhosphorylationGHRYKHSSVSMNFFQ
CCCCCCCCEEECCCC		20.2419684113
190PhosphorylationRYKHSSVSMNFFQEP
CCCCCCEEECCCCCC		15.2321440633
496PhosphorylationKPSVRPRSMSSLPIA
CCCCCCCCCCCCCCC		26.2125752575
498PhosphorylationSVRPRSMSSLPIATK
CCCCCCCCCCCCCCC		29.9417330950
499PhosphorylationVRPRSMSSLPIATKN
CCCCCCCCCCCCCCC		29.5325752575
539PhosphorylationKDQIERLSEFKSRYI
HHHHHHHHHHHHHEE		47.4030377154
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 ZRG17_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRG17_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 ZRG17_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MSC2_YEASTMSC2physical
15961382
HS150_YEASTHSP150genetic
15961382
ASI3_YEASTASI3genetic
16269340
PDAT_YEASTLRO1genetic
16269340
TSC3_YEASTTSC3genetic
16269340
ECM33_YEASTECM33genetic
20093466
AGP1_YEASTAGP1genetic
20093466
IPT1_YEASTIPT1genetic
20093466
SSD1_YEASTSSD1genetic
20093466
ASG1_YEASTASG1genetic
20093466
ICE2_YEASTICE2genetic
20093466
ECM25_YEASTECM25genetic
20093466
AIM44_YEASTAIM44genetic
20093466
MSC2_YEASTMSC2physical
16093310
MRM2_YEASTMRM2genetic
27708008
FUB1_YEASTFUB1genetic
27708008
GPR1_YEASTGPR1genetic
27708008
MNN10_YEASTMNN10genetic
27708008
ASK10_YEASTASK10genetic
27708008
ASG1_YEASTASG1genetic
27708008
F26_YEASTFBP26genetic
27708008
ECM25_YEASTECM25genetic
27708008
YME2_YEASTYME2genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZRG17_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-16; SER-58; SER-137;SER-496 AND SER-498, AND MASS SPECTROMETRY.
"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-131, AND MASSSPECTROMETRY.
"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-498, AND MASSSPECTROMETRY.

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