ROD1_YEAST - dbPTM
ROD1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ROD1_YEAST
UniProt AC Q02805
Protein Name Protein ROD1
Gene Name ROD1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 837
Subcellular Localization Membrane
Peripheral membrane protein . Membrane-associated or associated to a complex that cofractionates with plasma membrane.
Protein Description Mediates resistance to o-dinitrobenzene, calcium and zinc..
Protein Sequence MFSSSSRPSKEPLLFDIRLRNLDNDVLLIKGPPDEASSVLLSGTIVLSITEPIQIKSLALRLFGRLRLNIPTVLQTVHGPHKRYSKFERNIYSHFWDDFNIKSYFQNLYDNHNNGKITISSKSSTNLAALPKRKRALSTASLISSNGQTSASKNYHTLVKGNYEFPFSAIIPGSLVESVEGLPNAAVTYALEATIERPKQPDLICKKHLRVIRTLAIDAVELSETVSVDNSWPEKVDYTISIPTKAIAIGSSTMINILIVPILKGLKLGPVRISLVENSQYCGSYGGVINQERMVAKLKLKDPLKHVAQIKKKRSLNEAADEGVDTDTGEFQDKWEVRALLNIPASLTKCSQDCRILSNIKVRHKIKFTISLLNPDGHISELRAALPVQLFISPFVPVNVKTSDVIERTLKTFGPSYQVTSQHDNSFSSKNFVDDSEEDVIFQRSASALQLSSMPTIVSGSTLNINSTDAEATAVADTTMVTSLMVPPNYGNHVYDRVYGEVTNEDETSASASSSAVESQAIHNIQNLYISDSNNSNNPILAPNPQIKIEDDSLNNCDSRGDSVNNSNLNLVNSNLTISENWNNNSPSANRYNNIINAGLNSPSLTPSFAHLSRRNSYSRQTSSTSLKNDLELTDLSRVPSYDKAMKSDMIGEDLPPAYPEEELGVQENKKIELERPQILHHKSTSSLLPLPGSSKSSNNLKRSSSRTHLSHSPLPRNNSGSSVSLQQLARNNTDSSFNLNLSFTSAKSSTGSRHFPFNMTTSFTSNSSSKNNSHFDKTDSTSDANKPREEENYTSATHNRRSRSSSVRSNNSNSPLRQGTGSFANLMEMFTKRDRS
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
121PhosphorylationNGKITISSKSSTNLA
CCEEEEECCCCCCCC		32.4821440633
123PhosphorylationKITISSKSSTNLAAL
EEEEECCCCCCCCCC		44.3225521595
124PhosphorylationITISSKSSTNLAALP
EEEECCCCCCCCCCC		25.6722369663
125PhosphorylationTISSKSSTNLAALPK
EEECCCCCCCCCCCH		41.1522369663
138PhosphorylationPKRKRALSTASLISS
CHHHHHHHHHHHHCC		22.4222369663
139PhosphorylationKRKRALSTASLISSN
HHHHHHHHHHHHCCC		22.5522369663
141PhosphorylationKRALSTASLISSNGQ
HHHHHHHHHHCCCCC		26.7322369663
144PhosphorylationLSTASLISSNGQTSA
HHHHHHHCCCCCCCC		24.0422369663
145PhosphorylationSTASLISSNGQTSAS
HHHHHHCCCCCCCCC		37.6822369663
149PhosphorylationLISSNGQTSASKNYH
HHCCCCCCCCCCCEE		27.8822369663
150PhosphorylationISSNGQTSASKNYHT
HCCCCCCCCCCCEEE		23.7422369663
152PhosphorylationSNGQTSASKNYHTLV
CCCCCCCCCCEEEEE		22.6222369663
315PhosphorylationAQIKKKRSLNEAADE
HHHHHHHCHHHHHHC		44.4128889911
326PhosphorylationAADEGVDTDTGEFQD
HHHCCCCCCCCCCCC		32.8121551504
334UbiquitinationDTGEFQDKWEVRALL
CCCCCCCHHHHHHHH		34.1823749301
401UbiquitinationPFVPVNVKTSDVIER
CCCCCCCCHHHHHHH		36.7922106047
411UbiquitinationDVIERTLKTFGPSYQ
HHHHHHHHHHCCCCE		40.9923749301
416PhosphorylationTLKTFGPSYQVTSQH
HHHHHCCCCEEEECC		28.6930377154
417PhosphorylationLKTFGPSYQVTSQHD
HHHHCCCCEEEECCC		15.3327017623
420PhosphorylationFGPSYQVTSQHDNSF
HCCCCEEEECCCCCC		13.7227017623
426PhosphorylationVTSQHDNSFSSKNFV
EEECCCCCCCCCCCC		32.3421440633
428PhosphorylationSQHDNSFSSKNFVDD
ECCCCCCCCCCCCCC		39.9821440633
436PhosphorylationSKNFVDDSEEDVIFQ
CCCCCCCCHHHCEEE		38.1217330950
447PhosphorylationVIFQRSASALQLSSM
CEEECCHHHHHHHCC		30.6628889911
536PhosphorylationYISDSNNSNNPILAP
EECCCCCCCCCCCCC		42.0828889911
553PhosphorylationQIKIEDDSLNNCDSR
CEECCCCCCCCCCCC		45.3728889911
559PhosphorylationDSLNNCDSRGDSVNN
CCCCCCCCCCCCCCC		40.1228889911
592PhosphorylationNSPSANRYNNIINAG
CCCCHHHCCCHHHCC		16.6222369663
602PhosphorylationIINAGLNSPSLTPSF
HHHCCCCCCCCCHHH		22.4022369663
604PhosphorylationNAGLNSPSLTPSFAH
HCCCCCCCCCHHHHH		44.7022369663
606PhosphorylationGLNSPSLTPSFAHLS
CCCCCCCCHHHHHHH		22.6422369663
608PhosphorylationNSPSLTPSFAHLSRR
CCCCCCHHHHHHHHC		29.8122369663
613PhosphorylationTPSFAHLSRRNSYSR
CHHHHHHHHCCCCCC		21.2322369663
622PhosphorylationRNSYSRQTSSTSLKN
CCCCCCCCCCCCCCC		24.4322369663
623PhosphorylationNSYSRQTSSTSLKND
CCCCCCCCCCCCCCC		24.2322369663
624PhosphorylationSYSRQTSSTSLKNDL
CCCCCCCCCCCCCCH		25.9622369663
625PhosphorylationYSRQTSSTSLKNDLE
CCCCCCCCCCCCCHH		37.5322369663
626PhosphorylationSRQTSSTSLKNDLEL
CCCCCCCCCCCCHHH		39.0222369663
628UbiquitinationQTSSTSLKNDLELTD
CCCCCCCCCCHHHCC		48.4623749301
634PhosphorylationLKNDLELTDLSRVPS
CCCCHHHCCHHCCCC		26.0622369663
637PhosphorylationDLELTDLSRVPSYDK
CHHHCCHHCCCCHHH		33.7622369663
641PhosphorylationTDLSRVPSYDKAMKS
CCHHCCCCHHHHHHC		43.0122369663
642PhosphorylationDLSRVPSYDKAMKSD
CHHCCCCHHHHHHCC		18.5222369663
647UbiquitinationPSYDKAMKSDMIGED
CCHHHHHHCCCCCCC		48.4323749301
670UbiquitinationELGVQENKKIELERP
HHCCCCCCCEEECCC		55.1423749301
684PhosphorylationPQILHHKSTSSLLPL
CCCCCCCCCCCCCCC		29.2122369663
685PhosphorylationQILHHKSTSSLLPLP
CCCCCCCCCCCCCCC		27.4325521595
686PhosphorylationILHHKSTSSLLPLPG
CCCCCCCCCCCCCCC		26.5322890988
687PhosphorylationLHHKSTSSLLPLPGS
CCCCCCCCCCCCCCC		33.7322890988
694PhosphorylationSLLPLPGSSKSSNNL
CCCCCCCCCCCCCCC		32.4322890988
695PhosphorylationLLPLPGSSKSSNNLK
CCCCCCCCCCCCCCC		42.3321440633
697PhosphorylationPLPGSSKSSNNLKRS
CCCCCCCCCCCCCCC		40.0021440633
698PhosphorylationLPGSSKSSNNLKRSS
CCCCCCCCCCCCCCC		33.2121440633
704PhosphorylationSSNNLKRSSSRTHLS
CCCCCCCCCCCCCCC		30.9523749301
705PhosphorylationSNNLKRSSSRTHLSH
CCCCCCCCCCCCCCC		28.0729136822
706PhosphorylationNNLKRSSSRTHLSHS
CCCCCCCCCCCCCCC		42.3123749301
708PhosphorylationLKRSSSRTHLSHSPL
CCCCCCCCCCCCCCC		29.1729136822
711PhosphorylationSSSRTHLSHSPLPRN
CCCCCCCCCCCCCCC		17.8322369663
713PhosphorylationSRTHLSHSPLPRNNS
CCCCCCCCCCCCCCC		25.4222369663
720PhosphorylationSPLPRNNSGSSVSLQ
CCCCCCCCCCCCCHH		43.5322369663
722PhosphorylationLPRNNSGSSVSLQQL
CCCCCCCCCCCHHHH		27.6422369663
723PhosphorylationPRNNSGSSVSLQQLA
CCCCCCCCCCHHHHH		21.1722369663
725PhosphorylationNNSGSSVSLQQLARN
CCCCCCCCHHHHHHC		23.5522369663
736PhosphorylationLARNNTDSSFNLNLS
HHHCCCCCCEEEEEE		34.4923749301
781PhosphorylationSHFDKTDSTSDANKP
CCCCCCCCCCCCCCC		34.7328889911
783PhosphorylationFDKTDSTSDANKPRE
CCCCCCCCCCCCCHH		38.3828889911
805PhosphorylationTHNRRSRSSSVRSNN
CCCCCCCCCCCCCCC		28.3623749301
806PhosphorylationHNRRSRSSSVRSNNS
CCCCCCCCCCCCCCC		31.5721440633
807PhosphorylationNRRSRSSSVRSNNSN
CCCCCCCCCCCCCCC		23.8523749301
810PhosphorylationSRSSSVRSNNSNSPL
CCCCCCCCCCCCCCC		37.9022369663
813PhosphorylationSSVRSNNSNSPLRQG
CCCCCCCCCCCCCCC		42.8222369663
815PhosphorylationVRSNNSNSPLRQGTG
CCCCCCCCCCCCCCC		25.7322369663
821PhosphorylationNSPLRQGTGSFANLM
CCCCCCCCCHHHHHH		22.7022890988
823PhosphorylationPLRQGTGSFANLMEM
CCCCCCCHHHHHHHH		22.4822890988
832PhosphorylationANLMEMFTKRDRS--
HHHHHHHHHHCCC--		24.7022890988
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ROD1_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 ROD1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RSP5_YEASTRSP5physical
12163175
PIS_YEASTPIS1physical
18467557
YOL19_YEASTYOL019Wgenetic
20526336
TAT2_YEASTTAT2genetic
20526336
REG1_YEASTREG1physical
22249293
RSP5_YEASTRSP5physical
22249293
ROG3_YEASTROG3genetic
24820415
LDB19_YEASTLDB19genetic
24820415
BAR1_YEASTBAR1genetic
24820415
SST2_YEASTSST2genetic
24820415
RSP5_YEASTRSP5physical
24820415
ROG3_YEASTROG3genetic
25547292
RHO1_YEASTRHO1physical
26459639
GPR1_YEASTGPR1genetic
27708008
SIF2_YEASTSIF2genetic
27708008
ADPP_YEASTYSA1genetic
27708008
MCFS2_YEASTEHT1genetic
27708008
CS111_YEASTCOS111genetic
27708008
SNT1_YEASTSNT1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
STE23_YEASTSTE23genetic
27708008
VPS9_YEASTVPS9genetic
27708008
YND5_YEASTYNL035Cgenetic
27708008
MSC6_YEASTMSC6genetic
27708008
HXT6_YEASTHXT6physical
27261460
HXT1_YEASTHXT1physical
27261460
RSP5_YEASTRSP5physical
26920760
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ROD1_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-123; SER-124; SER-138;THR-139; SER-141; SER-436; SER-536; SER-602; SER-604; THR-606;SER-626; SER-684; THR-685; SER-720; SER-723; SER-725; SER-813 ANDSER-815, 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-602 AND SER-626, ANDMASS 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-141; SER-436 ANDSER-720, AND MASS SPECTROMETRY.
"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-125, AND MASSSPECTROMETRY.

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