YMZ2_YEAST - dbPTM
YMZ2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YMZ2_YEAST
UniProt AC Q03177
Protein Name WD repeat-containing protein YMR102C
Gene Name YMR102C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 834
Subcellular Localization
Protein Description
Protein Sequence MTNMAEDKTSISKVHSEFSNSSNTTGSEEESRSHQESFDGESSSGESKSKSKLNLEYSADIEPLKFRMTKTNNTNDKLKYSNNGNATDSFMRLKEHLQRGNTLNSNLRVNEFYPFNSIDTEQFENYLREPKYIKMLKRRKNLKQFRRLFLAQELMAYEGETVTSTSKSSEPTSKAIWSTKFSRDGKFMATGSKDGKIRIWKVIGSPVERAELDSSAESNKEARAKSMRIKQQVSSLNNPKEKQFLDSATEKYEEKEKLLNLYAPVFHPTPLRLYKEHVQDVLDINWSKNNFILSASMDKTVKLWHPDRKNSLKTFIHPDFVTCVEFHPTDDRFFISGCLDHKCRLWSILDDEVSFEYDCQDLITSVTLSPEEGKYTIIGTFNGYVHILMTRGLTPVSSFHVADRQTQEQNAHVMVTETDSKIRHGPRVTGLQAFRSQLDNSFRLVVTSNDSRIRIFDLEQRKLLEVLKGFHSGSSQHKAQLSIWHGQPIVVNSSDDHWVYGWRLKSSDRENDQDEPKRKPKGLARSGSLRSIFSKSMSRSSSQNNEEKPHHHLKLTNLLPLPHHSNDHYIKNTDYISFHAHNAPVTCVSIAPPETSKTLSLSNDVICELSLEFFQTSDSFDVLSRSNDDGIMSDVESSLGYNSKPGSISNASATSAIPDVVDAIGTILISTDNVGTIRVFRADMPSVIRKRVLLKLEEYNREVRRRFNSSDSLHSLSRSFNSRAKSNLAGQPAAAYTNTGKGYATGRGYSNICPKSSTSLKTLGSNAQPRTPRESMSSIFSNAHGPTTPTSAMNLPIRCNVCNGSRFEAFSGANDQQDRNYYCVDCGTVVNNFR
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
2Phosphorylation------MTNMAEDKT
------CCCCCCCCC
33.4322369663
9PhosphorylationTNMAEDKTSISKVHS
CCCCCCCCCHHHHHH
43.5522369663
10PhosphorylationNMAEDKTSISKVHSE
CCCCCCCCHHHHHHH
30.5222369663
12PhosphorylationAEDKTSISKVHSEFS
CCCCCCHHHHHHHHC
28.5222369663
22PhosphorylationHSEFSNSSNTTGSEE
HHHHCCCCCCCCCHH
42.3122369663
24PhosphorylationEFSNSSNTTGSEEES
HHCCCCCCCCCHHHH
34.1922369663
25PhosphorylationFSNSSNTTGSEEESR
HCCCCCCCCCHHHHH
42.8522369663
27PhosphorylationNSSNTTGSEEESRSH
CCCCCCCCHHHHHHC
39.4822369663
31PhosphorylationTTGSEEESRSHQESF
CCCCHHHHHHCCHHC
42.2222369663
37PhosphorylationESRSHQESFDGESSS
HHHHCCHHCCCCCCC
23.2828889911
42PhosphorylationQESFDGESSSGESKS
CHHCCCCCCCCCCCC
35.0217563356
43PhosphorylationESFDGESSSGESKSK
HHCCCCCCCCCCCCC
37.7517563356
44PhosphorylationSFDGESSSGESKSKS
HCCCCCCCCCCCCCC
56.7229734811
69PhosphorylationEPLKFRMTKTNNTND
CCEEEEEEECCCCCC
30.3828889911
71PhosphorylationLKFRMTKTNNTNDKL
EEEEEEECCCCCCCC
25.2428889911
74PhosphorylationRMTKTNNTNDKLKYS
EEEECCCCCCCCEEC
47.0328889911
87PhosphorylationYSNNGNATDSFMRLK
ECCCCCCCHHHHHHH
35.8522369663
89PhosphorylationNNGNATDSFMRLKEH
CCCCCCHHHHHHHHH
19.3122369663
102PhosphorylationEHLQRGNTLNSNLRV
HHHHCCCCCCCCCCC
30.0930377154
105PhosphorylationQRGNTLNSNLRVNEF
HCCCCCCCCCCCCEE
40.1130377154
168PhosphorylationTVTSTSKSSEPTSKA
CCEECCCCCCCCCCE
39.4419779198
173PhosphorylationSKSSEPTSKAIWSTK
CCCCCCCCCEEEEEE
30.7019779198
178PhosphorylationPTSKAIWSTKFSRDG
CCCCEEEEEEECCCC
18.6619779198
182PhosphorylationAIWSTKFSRDGKFMA
EEEEEEECCCCCEEE
30.9019823750
190PhosphorylationRDGKFMATGSKDGKI
CCCCEEEECCCCCCE
30.1519823750
192PhosphorylationGKFMATGSKDGKIRI
CCEEEECCCCCCEEE
24.1819823750
205PhosphorylationRIWKVIGSPVERAEL
EEEEEECCCCHHHHC
18.0428889911
215PhosphorylationERAELDSSAESNKEA
HHHHCCCCCCCCHHH
35.4030377154
218PhosphorylationELDSSAESNKEARAK
HCCCCCCCCHHHHHH
53.5723749301
234PhosphorylationMRIKQQVSSLNNPKE
HHHHHHHHCCCCHHH
25.4430377154
235PhosphorylationRIKQQVSSLNNPKEK
HHHHHHHCCCCHHHH
35.9423749301
420PhosphorylationVMVTETDSKIRHGPR
EEEECCCCCCCCCCC
37.0827017623
447PhosphorylationNSFRLVVTSNDSRIR
CCEEEEEECCCCCEE
17.8422369663
448PhosphorylationSFRLVVTSNDSRIRI
CEEEEEECCCCCEEE
27.3422369663
451PhosphorylationLVVTSNDSRIRIFDL
EEEECCCCCEEEEEH
33.5822369663
526PhosphorylationKPKGLARSGSLRSIF
CCCHHHCCCCHHHHH
27.4220377248
528PhosphorylationKGLARSGSLRSIFSK
CHHHCCCCHHHHHHH
23.1222369663
531PhosphorylationARSGSLRSIFSKSMS
HCCCCHHHHHHHHCC
33.0222369663
534PhosphorylationGSLRSIFSKSMSRSS
CCHHHHHHHHCCCCC
23.3521440633
536PhosphorylationLRSIFSKSMSRSSSQ
HHHHHHHHCCCCCCC
22.3127717283
538PhosphorylationSIFSKSMSRSSSQNN
HHHHHHCCCCCCCCC
35.7827717283
540PhosphorylationFSKSMSRSSSQNNEE
HHHHCCCCCCCCCCC
27.3428889911
541PhosphorylationSKSMSRSSSQNNEEK
HHHCCCCCCCCCCCC
34.5317287358
542PhosphorylationKSMSRSSSQNNEEKP
HHCCCCCCCCCCCCC
37.8717287358
633PhosphorylationSNDDGIMSDVESSLG
CCCCCHHCHHHHHCC
36.2627017623
638PhosphorylationIMSDVESSLGYNSKP
HHCHHHHHCCCCCCC
16.5928889911
699PhosphorylationVLLKLEEYNREVRRR
HHHHHHHHCHHHHHH
15.3324961812
709PhosphorylationEVRRRFNSSDSLHSL
HHHHHCCCCHHHHHH
32.5822369663
710PhosphorylationVRRRFNSSDSLHSLS
HHHHCCCCHHHHHHH
32.1222369663
712PhosphorylationRRFNSSDSLHSLSRS
HHCCCCHHHHHHHHH
29.9022369663
715PhosphorylationNSSDSLHSLSRSFNS
CCCHHHHHHHHHHHH
33.0822369663
717PhosphorylationSDSLHSLSRSFNSRA
CHHHHHHHHHHHHHH
28.9722369663
719PhosphorylationSLHSLSRSFNSRAKS
HHHHHHHHHHHHHHH
25.9624961812
722PhosphorylationSLSRSFNSRAKSNLA
HHHHHHHHHHHHCCC
31.4424961812
725UbiquitinationRSFNSRAKSNLAGQP
HHHHHHHHHCCCCCC
38.4723749301
726PhosphorylationSFNSRAKSNLAGQPA
HHHHHHHHCCCCCCC
35.7722369663
741UbiquitinationAAYTNTGKGYATGRG
EEECCCCCCCCCCCC
46.8623749301
756PhosphorylationYSNICPKSSTSLKTL
CCCCCCCCCCCCCCC
24.8021440633
757PhosphorylationSNICPKSSTSLKTLG
CCCCCCCCCCCCCCC
28.3021440633
758PhosphorylationNICPKSSTSLKTLGS
CCCCCCCCCCCCCCC
45.2121440633
759PhosphorylationICPKSSTSLKTLGSN
CCCCCCCCCCCCCCC
29.8028152593
761AcetylationPKSSTSLKTLGSNAQ
CCCCCCCCCCCCCCC
41.2825381059
762PhosphorylationKSSTSLKTLGSNAQP
CCCCCCCCCCCCCCC
41.4622369663
765PhosphorylationTSLKTLGSNAQPRTP
CCCCCCCCCCCCCCC
31.9122369663
771PhosphorylationGSNAQPRTPRESMSS
CCCCCCCCCHHHHHH
33.1222369663
775PhosphorylationQPRTPRESMSSIFSN
CCCCCHHHHHHHHCC
25.8322369663
777PhosphorylationRTPRESMSSIFSNAH
CCCHHHHHHHHCCCC
29.5722369663
778PhosphorylationTPRESMSSIFSNAHG
CCHHHHHHHHCCCCC
21.0022369663
781PhosphorylationESMSSIFSNAHGPTT
HHHHHHHCCCCCCCC
31.2822369663
787PhosphorylationFSNAHGPTTPTSAMN
HCCCCCCCCCCCCCC
50.4222369663
788PhosphorylationSNAHGPTTPTSAMNL
CCCCCCCCCCCCCCC
27.9222369663
790PhosphorylationAHGPTTPTSAMNLPI
CCCCCCCCCCCCCCE
27.3322369663
791PhosphorylationHGPTTPTSAMNLPIR
CCCCCCCCCCCCCEE
27.0722369663

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 YMZ2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YMZ2_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 YMZ2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
WRIP1_YEASTMGS1physical
10688190
SEC22_YEASTSEC22genetic
27708008
PRP6_YEASTPRP6genetic
27708008
APC11_YEASTAPC11genetic
27708008
DPOD_YEASTPOL3genetic
27708008
GNA1_YEASTGNA1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC20_YEASTCDC20genetic
27708008
NEP1_YEASTEMG1genetic
27708008
UTP13_YEASTUTP13genetic
27708008
HRP1_YEASTHRP1genetic
27708008
DYR_YEASTDFR1genetic
27708008
APC5_YEASTAPC5genetic
27708008
MOT1_YEASTMOT1genetic
27708008
YPK1_YEASTYPK1genetic
28774891

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YMZ2_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; SER-43; SER-205;SER-709; THR-771 AND THR-788, 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-42; SER-43; SER-709;SER-712 AND THR-788, 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-528; SER-541 ANDSER-542, AND MASS SPECTROMETRY.

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