RPH1_YEAST - dbPTM
RPH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RPH1_YEAST
UniProt AC P39956
Protein Name DNA damage-responsive transcriptional repressor RPH1
Gene Name RPH1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 796
Subcellular Localization Nucleus .
Protein Description Transcriptional repressor of photolyase PHR1. Recognizes and binds the sequence AG(4) in the upstream repressing sequence of PHR1. Derepresses PHR1 transcription when phosphorylated..
Protein Sequence MTKLIAPSEIVGGVPVFKPTYEQFEDFYAYCKAINKYGMKSGVVKVIPPKEWKDKLDLPYSAETLQKIKIKSPIQQHISGNKGLFMVQNVEKNKTYNIIQWKDLSKDYVPPEDPKARRNSRKGSVSKSTKLKLKNFESSFNIDDFEQFRTEYTIDLSDFQNTERLKFLEEYYWKTLNFTTPMYGADTPGSIFPEGLNVWNVAKLPNILDHMETKVPGVNDSYLYAGLWKASFSWHLEDQDLYSINYIHFGAPKQWYSIPQEDRFKFYKFMQEQFPEEAKNCPEFLRHKMFLASPKLLQENGIRCNEIVHHEGEFMITYPYGYHAGFNYGYNLAESVNFALEEWLPIGKKAGKCHCISDSVEIDVKKLAKSWRDNNKESKGTPPLNQLPNPAMPLLHRPTLKEMESSSLRSTSPDVGHFSNFKSKSSGVSSPLLSRMKDYSNIVEPTLEDPTLKLKRISSFQEQPLNKLLKRETSQTAMLTDHEDNIVAMSLTSMANSAASSPRLPLSRLNSSNELSNAQPLLDMTNNTLAFPRPNGPSGLNPLLYISNKNISGISHSAPHSPVNPNISLIKRVKSPNIVTLNISRESSRSPIALNYEARQQHSQQHSFSTPSTVSNLSTSVLGPLSDTNDIKTPHPERPNHKTANRILKKESPVETSKSNLILSKVASTRQEDSFTSRNDDLDKEQGSSPLNSKFAPEEIVLSGKNKIYICKECQRKFSSGHHLTRHKKSVHSGEKPHSCPKCGKRFKRRDHVLQHLNKKIPCISNETTVDAPIMNPTVQPQDGKAAINQQSTPLN
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
20PhosphorylationGVPVFKPTYEQFEDF
CEECCCCCHHHHHHH		40.0430377154
21PhosphorylationVPVFKPTYEQFEDFY
EECCCCCHHHHHHHH		19.0930377154
28PhosphorylationYEQFEDFYAYCKAIN
HHHHHHHHHHHHHHH		14.6930377154
30PhosphorylationQFEDFYAYCKAINKY
HHHHHHHHHHHHHHH		5.3230377154
41PhosphorylationINKYGMKSGVVKVIP
HHHHCCCCCCEEECC		28.1130377154
72PhosphorylationLQKIKIKSPIQQHIS
HHHCCCCCCCHHHCC		30.6121440633
138PhosphorylationLKLKNFESSFNIDDF
CEECCCCCCCCCCHH		35.7730377154
139PhosphorylationKLKNFESSFNIDDFE
EECCCCCCCCCCHHH		18.3420190278
256PhosphorylationFGAPKQWYSIPQEDR
ECCCCCCCCCCHHHH		8.3319823750
257PhosphorylationGAPKQWYSIPQEDRF
CCCCCCCCCCHHHHH		25.4919823750
378PhosphorylationWRDNNKESKGTPPLN
HHHCCCCCCCCCCHH		37.6919779198
381PhosphorylationNNKESKGTPPLNQLP
CCCCCCCCCCHHHCC		26.0121440633
399PhosphorylationMPLLHRPTLKEMESS
CCCCCCCCHHHHHHC		50.8725521595
405PhosphorylationPTLKEMESSSLRSTS
CCHHHHHHCCCCCCC		24.7424961812
406PhosphorylationTLKEMESSSLRSTSP
CHHHHHHCCCCCCCC		21.7824961812
407PhosphorylationLKEMESSSLRSTSPD
HHHHHHCCCCCCCCC		36.7621440633
410PhosphorylationMESSSLRSTSPDVGH
HHHCCCCCCCCCCCC		38.2322369663
411PhosphorylationESSSLRSTSPDVGHF
HHCCCCCCCCCCCCC		37.5322369663
412PhosphorylationSSSLRSTSPDVGHFS
HCCCCCCCCCCCCCC		21.9822369663
423PhosphorylationGHFSNFKSKSSGVSS
CCCCCCCCCCCCCCH		33.3623749301
425PhosphorylationFSNFKSKSSGVSSPL
CCCCCCCCCCCCHHH		39.1422369663
426PhosphorylationSNFKSKSSGVSSPLL
CCCCCCCCCCCHHHH		47.1222369663
429PhosphorylationKSKSSGVSSPLLSRM
CCCCCCCCHHHHHHC		29.7522369663
430PhosphorylationSKSSGVSSPLLSRMK
CCCCCCCHHHHHHCC		19.7022369663
434PhosphorylationGVSSPLLSRMKDYSN
CCCHHHHHHCCCCCC		37.7022369663
440PhosphorylationLSRMKDYSNIVEPTL
HHHCCCCCCCCCCCC		30.1630377154
458PhosphorylationTLKLKRISSFQEQPL
CCHHEECHHHHHCHH		29.1822369663
459PhosphorylationLKLKRISSFQEQPLN
CHHEECHHHHHCHHH		28.6922369663
473PhosphorylationNKLLKRETSQTAMLT
HHHHCHHHCCCCCCC		30.1219779198
480PhosphorylationTSQTAMLTDHEDNIV
HCCCCCCCCCCCCEE		23.4028889911
492PhosphorylationNIVAMSLTSMANSAA
CEEEEEHHHHHHHHH		14.7819779198
500PhosphorylationSMANSAASSPRLPLS
HHHHHHHCCCCCCHH		40.3619779198
511PhosphorylationLPLSRLNSSNELSNA
CCHHHCCCCCCCCCC		38.8530377154
516PhosphorylationLNSSNELSNAQPLLD
CCCCCCCCCCHHCHH		24.7627017623
552PhosphorylationYISNKNISGISHSAP
EEECCCCCCCCCCCC		39.1922369663
555PhosphorylationNKNISGISHSAPHSP
CCCCCCCCCCCCCCC		18.2122369663
557PhosphorylationNISGISHSAPHSPVN
CCCCCCCCCCCCCCC		36.3822369663
561PhosphorylationISHSAPHSPVNPNIS
CCCCCCCCCCCCCCC		29.5022369663
568PhosphorylationSPVNPNISLIKRVKS
CCCCCCCCHHCCCCC		30.5922369663
575PhosphorylationSLIKRVKSPNIVTLN
CHHCCCCCCCEEEEE		21.9622369663
580PhosphorylationVKSPNIVTLNISRES
CCCCCEEEEEECCCC		15.4122369663
584PhosphorylationNIVTLNISRESSRSP
CEEEEEECCCCCCCC		28.9922369663
587PhosphorylationTLNISRESSRSPIAL
EEEECCCCCCCCEEC		29.9122369663
588PhosphorylationLNISRESSRSPIALN
EEECCCCCCCCEECC		31.8322369663
590PhosphorylationISRESSRSPIALNYE
ECCCCCCCCEECCHH		23.7022369663
596PhosphorylationRSPIALNYEARQQHS
CCCEECCHHHHHHHH		16.3022369663
652PhosphorylationNRILKKESPVETSKS
HHHHHCCCCCCCCHH		43.0322369663
656PhosphorylationKKESPVETSKSNLIL
HCCCCCCCCHHHEEE		41.5119823750
657PhosphorylationKESPVETSKSNLILS
CCCCCCCCHHHEEEH		22.1524961812
659PhosphorylationSPVETSKSNLILSKV
CCCCCCHHHEEEHHH		36.3122369663
664PhosphorylationSKSNLILSKVASTRQ
CHHHEEEHHHHHCCC		20.3524961812
665AcetylationKSNLILSKVASTRQE
HHHEEEHHHHHCCCC		38.0724489116
668PhosphorylationLILSKVASTRQEDSF
EEEHHHHHCCCCCCC		27.4021440633
669PhosphorylationILSKVASTRQEDSFT
EEHHHHHCCCCCCCC		27.0024961812
674PhosphorylationASTRQEDSFTSRNDD
HHCCCCCCCCCCCCC		29.6719779198
676PhosphorylationTRQEDSFTSRNDDLD
CCCCCCCCCCCCCCC		30.6321440633
677PhosphorylationRQEDSFTSRNDDLDK
CCCCCCCCCCCCCCC		27.3824961812
684AcetylationSRNDDLDKEQGSSPL
CCCCCCCCCCCCCCC		60.2724489116
688PhosphorylationDLDKEQGSSPLNSKF
CCCCCCCCCCCCCCC		28.6024961812
689PhosphorylationLDKEQGSSPLNSKFA
CCCCCCCCCCCCCCC		39.9825521595
693PhosphorylationQGSSPLNSKFAPEEI
CCCCCCCCCCCCCEE		36.5124961812
694AcetylationGSSPLNSKFAPEEIV
CCCCCCCCCCCCEEE		44.4624489116
703PhosphorylationAPEEIVLSGKNKIYI
CCCEEEECCCCEEEE		36.5130377154
725PhosphorylationFSSGHHLTRHKKSVH
CCCCCCCCCCCCCCC		26.7728889911
759AcetylationHVLQHLNKKIPCISN
HHHHHHHHCCCCCCC		59.4425381059
793PhosphorylationAAINQQSTPLN----
CCCCCCCCCCC----		27.7028889911
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 RPH1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RPH1_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 RPH1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
H2A1_YEASTHTA1genetic
17314980
SWD1_YEASTSWD1genetic
17314980
H3_YEASTHHT1physical
17525156
SSB1_YEASTSSB1physical
19536198
YPT6_YEASTYPT6genetic
20959818
GLN3_YEASTGLN3genetic
21127252
ADA2_YEASTADA2genetic
21127252
RAD51_YEASTRAD51genetic
21127252
UME6_YEASTUME6genetic
21127252
H3_YEASTHHT1physical
21067515
JHD1_YEASTJHD1genetic
25774516
GIS1_YEASTGIS1genetic
25774516
STU1_YEASTSTU1genetic
27708008
PP2C3_YEASTPTC3genetic
27708008
SNF5_YEASTSNF5genetic
27708008
STE50_YEASTSTE50genetic
27708008
YKF0_YEASTYKL050Cgenetic
27708008
TDA1_YEASTTDA1genetic
27708008
INO4_YEASTINO4genetic
27708008
CY1_YEASTCYT1genetic
27708008
MDM36_YEASTMDM36genetic
27708008
POP7_YEASTPOP7genetic
27708008
CDC48_YEASTCDC48genetic
27708008
CDC4_YEASTCDC4genetic
27708008
SMD1_YEASTSMD1genetic
27708008
PTI1_YEASTPTI1genetic
27708008
MED6_YEASTMED6genetic
27708008
STS1_YEASTSTS1genetic
27708008
PSF2_YEASTPSF2genetic
27708008
HACD_YEASTPHS1genetic
27708008
BET3_YEASTBET3genetic
27708008
MED14_YEASTRGR1genetic
27708008
SMC4_YEASTSMC4genetic
27708008
PWP1_YEASTPWP1genetic
27708008
TAD3_YEASTTAD3genetic
27708008
ORC1_YEASTORC1genetic
27708008
POB3_YEASTPOB3genetic
27708008
RSC9_YEASTRSC9genetic
27708008
RNA1_YEASTRNA1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
MED4_YEASTMED4genetic
27708008
IWS1_YEASTSPN1genetic
27708008
MED10_YEASTNUT2genetic
27708008
ATC3_YEASTDRS2genetic
27708008
ECM1_YEASTECM1genetic
27708008
RCR1_YEASTRCR1genetic
27708008
RL4A_YEASTRPL4Agenetic
27708008
ICS2_YEASTICS2genetic
27708008
SHG1_YEASTSHG1genetic
27708008
TAH1_YEASTTAH1genetic
27708008
BRE1_YEASTBRE1genetic
27708008
CYK3_YEASTCYK3genetic
27708008
YD121_YEASTYDL121Cgenetic
27708008
VPS41_YEASTVPS41genetic
27708008
NBP2_YEASTNBP2genetic
27708008
BL1S4_YEASTCNL1genetic
27708008
SAC7_YEASTSAC7genetic
27708008
DOT1_YEASTDOT1genetic
27708008
SDC1_YEASTSDC1genetic
27708008
FAB1_YEASTFAB1genetic
27708008
MAN1_YEASTAMS1genetic
27708008
GCN1_YEASTGCN1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RTF1_YEASTRTF1genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
CGS6_YEASTCLB6genetic
27708008
YG51_YEASTYGR237Cgenetic
27708008
YPT35_YEASTYPT35genetic
27708008
AIM18_YEASTAIM18genetic
27708008
ICE2_YEASTICE2genetic
27708008
SWE1_YEASTSWE1genetic
27708008
TUL1_YEASTTUL1genetic
27708008
YKH7_YEASTYKL077Wgenetic
27708008
MBR1_YEASTMBR1genetic
27708008
FEN1_YEASTRAD27genetic
27708008
MRP8_YEASTMRP8genetic
27708008
OSH6_YEASTOSH6genetic
27708008
IRS4_YEASTIRS4genetic
27708008
YK03_YEASTYKR023Wgenetic
27708008
SHB17_YEASTSHB17genetic
27708008
SRL3_YEASTSRL3genetic
27708008
BRE2_YEASTBRE2genetic
27708008
PUR91_YEASTADE16genetic
27708008
HOG1_YEASTHOG1genetic
27708008
STM1_YEASTSTM1genetic
27708008
ELO3_YEASTELO3genetic
27708008
SEI1_YEASTFLD1genetic
27708008
SRR1L_YEASTBER1genetic
27708008
PUN1_YEASTPUN1genetic
27708008
TDA5_YEASTTDA5genetic
27708008
PML39_YEASTPML39genetic
27708008
MSC1_YEASTMSC1genetic
27708008
MAC1_YEASTMAC1genetic
27708008
CSI1_YEASTCSI1genetic
27708008
RCO1_YEASTRCO1genetic
27708008
PET8_YEASTPET8genetic
27708008
PMS1_YEASTPMS1genetic
27708008
TOP1_YEASTTOP1genetic
27708008
MET22_YEASTMET22genetic
27708008
RTC1_YEASTRTC1genetic
27708008
ASE1_YEASTASE1genetic
27708008
HAP5_YEASTHAP5genetic
27708008
RAD1_YEASTRAD1genetic
27708008
LGE1_YEASTLGE1genetic
27708008
TGS1_YEASTTGS1genetic
27708008
RU2A_YEASTLEA1genetic
27708008
XPO1_YEASTCRM1physical
28334815
NUP1_YEASTNUP1physical
28334815
H3_YEASTHHT1genetic
26159996
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RPH1_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-412; SER-429; SER-430;SER-459; SER-557; SER-561; SER-575; SER-652; SER-688 AND SER-689, ANDMASS 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-412; SER-459; SER-557;SER-561; SER-652 AND SER-689, 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-652, 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-561 AND SER-689, ANDMASS SPECTROMETRY.

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