ZRG8_YEAST - dbPTM
ZRG8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZRG8_YEAST
UniProt AC P40021
Protein Name Zinc-regulated protein 8
Gene Name ZRG8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1076
Subcellular Localization Cytoplasm. Bud. Bud neck. Bud tip. Localized to the cortex of small and large buds during bud growth, to the bud neck during mitotic exit and to the tips of mating projections in pheromone-treated cells.
Protein Description Involved in the integrity functions of RAM, a conserved signaling network that regulates maintenance of polarized growth and daughter-cell-specific transcription..
Protein Sequence MRSFIKAHKKSTSFDESPKRHSNFSGNTNNSSQRSSDDSLDFLPSTPSQMNYDSIPPPAKHSPGFESFHRLANKTSKLFKKTSNSNLNSHLASTPTTSTNQTTSNSFVLQNPPTKNTGPPPPLPPPLFPSSSTSSFSRHDNESEYTAYKKTSPAKDFNRTTDSLPAIKGTITHSWGDSKVESHVIILNDPASPASNTSEATSSKQFKTPIIGNENLTSTTSPSNLEPAIRILNKNKGKQQENIDDAEDGSSKKEHHVYKALALAKNRNRQARIHSHDDIINLGKASQMDMSLLAAAFSGNSTTTINNDQSSNEQTDEKILDIERVTTTSTLTSSETTSPINKSPCFYSQTLSLSPKIRHGDLQSSPSKVNKNDSQNETLNKKKVRISLNRKEEEKVYSLNNNSDEYSVNEKETHKANDCNDESSENGDGDNDHDDDYDDDDDDDDDDDESEFSFEYAGINVRTSSVKYYSKPEPAANVYIDDLYEDENFDDDMNCIEDDESGNEGNEICGLSTRFEETSLKSNKVKKFNDLFNLSDDDEEEDGKDNSNNGDENESDNLYQKRLENGKETFNGNHGGHHDDASLGETVDNKEQFLINDNVKKPIQKYNDLFDLSDEDDNDDKEMSEAESYMFSDEAPSIESGPANAKSTRGIYSQSNKNIIRDGKPNYSFSLKRNNSDDETEHTSAIKASLTGTTGSTKPTVKSFSDIFNVDDSASDAESDSGTGGNNSNGLVSNDSERQVSLQSSLYETKSESHPPNHPHSQILQTPAKIVITPSVSDAQSQALAITDDDGEDDDDDTSSILRTPFQLIDSSHSQQPHYASPQYTAVLNSPPLPPPARSQSLKYHDLNCDLDSEVPRPMSNLFFIDEAEEDEYNQKSKFFDFDHYDIDEINGIPEDFNFSDSERDDLNRRTLKSPLRGGSKNREVSPFSSVSSSFRSTHSFNGKLTINQGAKELAPMKNKIELTNKTVTFFNSNNWNTYDCNSLSRKTSSQMRDSKYQNHNVGQNVEPSSVLSPQHQISNGLDGKCNDNYVISPNLPTTITPTNSFTKPTPEFSNDYSLSPIQETPSSVQSSPKRA
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
11PhosphorylationFIKAHKKSTSFDESP
HHHHHHCCCCCCCCC		33.8030377154
13PhosphorylationKAHKKSTSFDESPKR
HHHHCCCCCCCCCCC		37.4821440633
17PhosphorylationKSTSFDESPKRHSNF
CCCCCCCCCCCCCCC		37.2523749301
62PhosphorylationIPPPAKHSPGFESFH
CCCCCCCCCCHHHHH		26.4728889911
82PhosphorylationTSKLFKKTSNSNLNS
HHHHHHHCCCCCCHH		33.4620377248
83PhosphorylationSKLFKKTSNSNLNSH
HHHHHHCCCCCCHHH		47.3321440633
85PhosphorylationLFKKTSNSNLNSHLA
HHHHCCCCCCHHHCC		42.3219779198
89PhosphorylationTSNSNLNSHLASTPT
CCCCCCHHHCCCCCC		24.0421440633
93PhosphorylationNLNSHLASTPTTSTN
CCHHHCCCCCCCCCC		41.0819779198
94PhosphorylationLNSHLASTPTTSTNQ
CHHHCCCCCCCCCCC		21.0319823750
96PhosphorylationSHLASTPTTSTNQTT
HHCCCCCCCCCCCCC		33.2019823750
97PhosphorylationHLASTPTTSTNQTTS
HCCCCCCCCCCCCCC		34.4519823750
98PhosphorylationLASTPTTSTNQTTSN
CCCCCCCCCCCCCCC		28.0419823750
99PhosphorylationASTPTTSTNQTTSNS
CCCCCCCCCCCCCCC		29.2919779198
102PhosphorylationPTTSTNQTTSNSFVL
CCCCCCCCCCCCEEE		33.9719779198
103PhosphorylationTTSTNQTTSNSFVLQ
CCCCCCCCCCCEEEC		19.0219823750
104PhosphorylationTSTNQTTSNSFVLQN
CCCCCCCCCCEEECC		33.5919823750
106PhosphorylationTNQTTSNSFVLQNPP
CCCCCCCCEEECCCC		19.2519779198
114PhosphorylationFVLQNPPTKNTGPPP
EEECCCCCCCCCCCC		37.8819823750
131PhosphorylationPPPLFPSSSTSSFSR
CCCCCCCCCCCCCCC		37.5621440633
151PhosphorylationEYTAYKKTSPAKDFN
HEEEEECCCCCCCCC		35.4728889911
152PhosphorylationYTAYKKTSPAKDFNR
EEEEECCCCCCCCCC		31.5725704821
163PhosphorylationDFNRTTDSLPAIKGT
CCCCCCCCCCCCEEE		33.8722369663
182PhosphorylationWGDSKVESHVIILND
CCCCCEEEEEEEECC		26.4922369663
192PhosphorylationIILNDPASPASNTSE
EEECCCCCCCCCCCC		26.7922369663
195PhosphorylationNDPASPASNTSEATS
CCCCCCCCCCCCCCC		43.9822369663
197PhosphorylationPASPASNTSEATSSK
CCCCCCCCCCCCCCC		26.0022369663
198PhosphorylationASPASNTSEATSSKQ
CCCCCCCCCCCCCCC		29.5022369663
201PhosphorylationASNTSEATSSKQFKT
CCCCCCCCCCCCCCC		29.4921440633
202PhosphorylationSNTSEATSSKQFKTP
CCCCCCCCCCCCCCC		42.4522369663
203PhosphorylationNTSEATSSKQFKTPI
CCCCCCCCCCCCCCC		26.5622369663
208PhosphorylationTSSKQFKTPIIGNEN
CCCCCCCCCCCCCCC		22.4721440633
218PhosphorylationIGNENLTSTTSPSNL
CCCCCCCCCCCHHHC		32.6221440633
221PhosphorylationENLTSTTSPSNLEPA
CCCCCCCCHHHCHHH		26.8121551504
275PhosphorylationNRQARIHSHDDIINL
CHHHHCCCHHHHHHH		26.6622369663
343PhosphorylationTTSPINKSPCFYSQT
CCCCCCCCCCCCEEE		23.5528889911
350PhosphorylationSPCFYSQTLSLSPKI
CCCCCEEEECCCCCC		16.6327017623
352PhosphorylationCFYSQTLSLSPKIRH
CCCEEEECCCCCCCC		30.1322369663
354PhosphorylationYSQTLSLSPKIRHGD
CEEEECCCCCCCCCC		22.2922369663
364PhosphorylationIRHGDLQSSPSKVNK
CCCCCCCCCCCCCCC		52.0621440633
365PhosphorylationRHGDLQSSPSKVNKN
CCCCCCCCCCCCCCC		21.8919823750
367PhosphorylationGDLQSSPSKVNKNDS
CCCCCCCCCCCCCCC		51.7021440633
374PhosphorylationSKVNKNDSQNETLNK
CCCCCCCCCCCCCCC		44.2823749301
387PhosphorylationNKKKVRISLNRKEEE
CCCEEEEECCCCCHH		14.7228889911
397PhosphorylationRKEEEKVYSLNNNSD
CCCHHHEEECCCCCC		20.6422369663
398PhosphorylationKEEEKVYSLNNNSDE
CCHHHEEECCCCCCC		27.8422369663
403PhosphorylationVYSLNNNSDEYSVNE
EEECCCCCCCCCCCH		33.6622369663
406PhosphorylationLNNNSDEYSVNEKET
CCCCCCCCCCCHHHC		23.9422369663
407PhosphorylationNNNSDEYSVNEKETH
CCCCCCCCCCHHHCC		19.2022369663
411UbiquitinationDEYSVNEKETHKAND
CCCCCCHHHCCCCCC		63.8123749301
518PhosphorylationLSTRFEETSLKSNKV
CCCCCCHHCCCCCCC		31.9630377154
519PhosphorylationSTRFEETSLKSNKVK
CCCCCHHCCCCCCCE		36.7624930733
522PhosphorylationFEETSLKSNKVKKFN
CCHHCCCCCCCEEHH		47.3723749301
535PhosphorylationFNDLFNLSDDDEEED
HHHHCCCCCCCCCCC		39.8522369663
547PhosphorylationEEDGKDNSNNGDENE
CCCCCCCCCCCCCCH		41.6322369663
555PhosphorylationNNGDENESDNLYQKR
CCCCCCHHHHHHHHH		43.3019779198
569PhosphorylationRLENGKETFNGNHGG
HHHHCCCCCCCCCCC		26.3629136822
582PhosphorylationGGHHDDASLGETVDN
CCCCCCCCCCCCCCC		43.8529136822
586PhosphorylationDDASLGETVDNKEQF
CCCCCCCCCCCHHHE		31.2129136822
613PhosphorylationYNDLFDLSDEDDNDD
CHHHHCCCCCCCCCH		40.5822369663
624PhosphorylationDNDDKEMSEAESYMF
CCCHHHHHHHHHHHH		34.4428889911
632PhosphorylationEAESYMFSDEAPSIE
HHHHHHHCCCCCCCC		20.2928889911
655PhosphorylationTRGIYSQSNKNIIRD
CCCCCCCCCCCEECC		43.7823749301
657AcetylationGIYSQSNKNIIRDGK
CCCCCCCCCEECCCC		55.5625381059
667PhosphorylationIRDGKPNYSFSLKRN
ECCCCCCCEEEEECC		21.4421440633
668PhosphorylationRDGKPNYSFSLKRNN
CCCCCCCEEEEECCC		18.2624961812
670PhosphorylationGKPNYSFSLKRNNSD
CCCCCEEEEECCCCC		27.3424961812
676PhosphorylationFSLKRNNSDDETEHT
EEEECCCCCCCCHHH		50.4122369663
680PhosphorylationRNNSDDETEHTSAIK
CCCCCCCCHHHHHHH		39.8119823750
683PhosphorylationSDDETEHTSAIKASL
CCCCCHHHHHHHHHH		17.3929734811
684PhosphorylationDDETEHTSAIKASLT
CCCCHHHHHHHHHHH		29.8819823750
691PhosphorylationSAIKASLTGTTGSTK
HHHHHHHHCCCCCCC		29.9528889911
766PhosphorylationPHSQILQTPAKIVIT
CCHHHCCCCCEEEEC		23.0528889911
914PhosphorylationLNRRTLKSPLRGGSK
HHHHHHCCCCCCCCC		32.0725704821
926PhosphorylationGSKNREVSPFSSVSS
CCCCCCCCCCCCCCC		18.5722369663
929PhosphorylationNREVSPFSSVSSSFR
CCCCCCCCCCCCHHC		32.9622369663
930PhosphorylationREVSPFSSVSSSFRS
CCCCCCCCCCCHHCC		26.8022369663
934PhosphorylationPFSSVSSSFRSTHSF
CCCCCCCHHCCCCCC		19.7128889911
940PhosphorylationSSFRSTHSFNGKLTI
CHHCCCCCCCCEEEE		22.0930377154
1013PhosphorylationVEPSSVLSPQHQISN
CCHHHHCCCCCCCCC		21.9928889911
1060PhosphorylationFSNDYSLSPIQETPS
CCCCCCCCCCCCCCC		17.6421551504
1071PhosphorylationETPSSVQSSPKRA--
CCCCCHHCCCCCC--		46.5921551504
1072PhosphorylationTPSSVQSSPKRA---
CCCCHHCCCCCC---		19.8321551504
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 ZRG8_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZRG8_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 ZRG8_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSD1_YEASTSSD1physical
15972461
SSB1_YEASTSSB1physical
19536198
RTG3_YEASTRTG3genetic
20093466
HAP3_YEASTHAP3genetic
20093466
BRE1_YEASTBRE1genetic
20093466
HAP2_YEASTHAP2genetic
20093466
VMA21_YEASTVMA21genetic
20093466
PLMT_YEASTOPI3genetic
20093466
CBT1_YEASTCBT1genetic
20093466
ATP10_YEASTATP10genetic
20093466
HAP3_YEASTHAP3genetic
27708008
RV161_YEASTRVS161genetic
27708008
IMG2_YEASTIMG2genetic
27708008
RV167_YEASTRVS167genetic
27708008
MUP1_YEASTMUP1genetic
27708008
VMA21_YEASTVMA21genetic
27708008
CBT1_YEASTCBT1genetic
27708008
HIR2_YEASTHIR2genetic
27708008
WDR6_YEASTRTT10genetic
27708008
YME1_YEASTYME1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ZRG8_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-275; SER-354; SER-403;SER-407; SER-632 AND SER-676, 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-403; SER-407 ANDSER-676, 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-275; SER-365 ANDSER-676, 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-275, 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 SER-221 AND SER-354, ANDMASS SPECTROMETRY.

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