RTK1_YEAST - dbPTM
RTK1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RTK1_YEAST
UniProt AC Q12100
Protein Name Probable serine/threonine-protein kinase RTK1
Gene Name RTK1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 620
Subcellular Localization
Protein Description Probable serine/threonine-protein kinase that may be involved in ribosome biogenesis..
Protein Sequence MVKETPLHSSSSTSLSSLFRPTKLKNLSAKIFNGGGNQSYSKTDDVSRSSSRSSKKNTDSDQEDQIKYNKPNDRRSTIGKSPQGNGALSKESHVVASSTLTGISPTSAKKAPIDYSPSRPLPNNHNPVRTGHTVPHLPHSIHNPINYIHQGSKDAFHHPHPVRSTAHSNISTVSSAKSDTPSSNLSYQAHMHPVEILQKQIEDKHFMDSQASTPGSVELQHNSSSGSDDTSSRKKKSLRLTRFFKKIHNDYHDNHHHHHHHNRGSTPTKPKLNLNTNENIVESNGKALYETDNPVELLEKYGIPGRKLGEGASGSVSVVERTDGKLFACKMFRKPHLNNEGTNQSQLANYSKKVTTEFCIGSTLHHENIVETLDMLTEGDTYLLVMEYAPYDFFNLVMSNLMTQDEVNCYFKQLCHGVNYLHSMGLAHRDLKLDNCVVTKDGILKLIDFGSAVVFQYPYEDTIVKSHGIVGSDPYLAPELLKQTSYDPRVADVWSIAIIFYCMVLKRFPWKAPKKSFNSFRLFTEEPEDEDDIVRGPNKILRLLPRHSRTIIGRMLALEPKQRVLMNDVVKDDWLVSVPSCEVDPTSGDLVEKPKNHKHHLVTEEELNELTKQHGNKDSN
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
5Phosphorylation---MVKETPLHSSSS
---CCCCCCCCCCCC		25.9822369663
9PhosphorylationVKETPLHSSSSTSLS
CCCCCCCCCCCCCHH		39.3320377248
10PhosphorylationKETPLHSSSSTSLSS
CCCCCCCCCCCCHHH		19.9822369663
11PhosphorylationETPLHSSSSTSLSSL
CCCCCCCCCCCHHHH		40.4222369663
12PhosphorylationTPLHSSSSTSLSSLF
CCCCCCCCCCHHHHC		24.7822369663
13PhosphorylationPLHSSSSTSLSSLFR
CCCCCCCCCHHHHCC		35.3220377248
14PhosphorylationLHSSSSTSLSSLFRP
CCCCCCCCHHHHCCC		28.3522369663
16PhosphorylationSSSSTSLSSLFRPTK
CCCCCCHHHHCCCHH		25.4322369663
17PhosphorylationSSSTSLSSLFRPTKL
CCCCCHHHHCCCHHH		36.5022369663
22PhosphorylationLSSLFRPTKLKNLSA
HHHHCCCHHHCCCEE		44.7622369663
28PhosphorylationPTKLKNLSAKIFNGG
CHHHCCCEEEEECCC		36.5919795423
30AcetylationKLKNLSAKIFNGGGN
HHCCCEEEEECCCCC		44.4425381059
39PhosphorylationFNGGGNQSYSKTDDV
ECCCCCCCCCCCCCC		35.0622369663
58PhosphorylationSRSSKKNTDSDQEDQ
CCCCCCCCCCCHHHH		45.8422369663
60PhosphorylationSSKKNTDSDQEDQIK
CCCCCCCCCHHHHHH		38.8722369663
76PhosphorylationNKPNDRRSTIGKSPQ
CCCCCCCCCCCCCCC		25.8522369663
77PhosphorylationKPNDRRSTIGKSPQG
CCCCCCCCCCCCCCC		31.7522369663
81PhosphorylationRRSTIGKSPQGNGAL
CCCCCCCCCCCCCCC		19.7622369663
89PhosphorylationPQGNGALSKESHVVA
CCCCCCCCCCCEEEE		33.5722369663
92PhosphorylationNGALSKESHVVASST
CCCCCCCCEEEEEEE		25.8922369663
97PhosphorylationKESHVVASSTLTGIS
CCCEEEEEEECCCCC		16.5522369663
98PhosphorylationESHVVASSTLTGISP
CCEEEEEEECCCCCC		20.0722369663
99PhosphorylationSHVVASSTLTGISPT
CEEEEEEECCCCCCC		26.3322369663
101PhosphorylationVVASSTLTGISPTSA
EEEEEECCCCCCCCC		32.3422369663
104PhosphorylationSSTLTGISPTSAKKA
EEECCCCCCCCCCCC		24.3822369663
106PhosphorylationTLTGISPTSAKKAPI
ECCCCCCCCCCCCCC		34.2322369663
107PhosphorylationLTGISPTSAKKAPID
CCCCCCCCCCCCCCC		41.2822369663
115PhosphorylationAKKAPIDYSPSRPLP
CCCCCCCCCCCCCCC		24.1729688323
116PhosphorylationKKAPIDYSPSRPLPN
CCCCCCCCCCCCCCC		16.8021440633
118PhosphorylationAPIDYSPSRPLPNNH
CCCCCCCCCCCCCCC		40.3619779198
164PhosphorylationHHPHPVRSTAHSNIS
CCCCCCCCCCCCCCC		30.1322369663
165PhosphorylationHPHPVRSTAHSNIST
CCCCCCCCCCCCCCC		20.1622369663
168PhosphorylationPVRSTAHSNISTVSS
CCCCCCCCCCCCCCC		33.1322369663
171PhosphorylationSTAHSNISTVSSAKS
CCCCCCCCCCCCCCC		27.3222369663
172PhosphorylationTAHSNISTVSSAKSD
CCCCCCCCCCCCCCC		22.1722369663
174PhosphorylationHSNISTVSSAKSDTP
CCCCCCCCCCCCCCC		25.3522369663
175PhosphorylationSNISTVSSAKSDTPS
CCCCCCCCCCCCCCC		35.0722369663
178PhosphorylationSTVSSAKSDTPSSNL
CCCCCCCCCCCCCCC		46.5722369663
180PhosphorylationVSSAKSDTPSSNLSY
CCCCCCCCCCCCCHH		31.9620377248
182PhosphorylationSAKSDTPSSNLSYQA
CCCCCCCCCCCHHEE		33.6724961812
209PhosphorylationEDKHFMDSQASTPGS
HCCCCCCCCCCCCCC		18.8319779198
212PhosphorylationHFMDSQASTPGSVEL
CCCCCCCCCCCCEEE		27.7419779198
213PhosphorylationFMDSQASTPGSVELQ
CCCCCCCCCCCEEEE		34.3819779198
216PhosphorylationSQASTPGSVELQHNS
CCCCCCCCEEEECCC		17.3921440633
223PhosphorylationSVELQHNSSSGSDDT
CEEEECCCCCCCCCC		24.6119795423
224PhosphorylationVELQHNSSSGSDDTS
EEEECCCCCCCCCCC		43.9921440633
225PhosphorylationELQHNSSSGSDDTSS
EEECCCCCCCCCCCH		41.9821440633
227PhosphorylationQHNSSSGSDDTSSRK
ECCCCCCCCCCCHHH		33.9721440633
230PhosphorylationSSSGSDDTSSRKKKS
CCCCCCCCCHHHHHH		33.3219795423
231PhosphorylationSSGSDDTSSRKKKSL
CCCCCCCCHHHHHHH		34.8319795423
232PhosphorylationSGSDDTSSRKKKSLR
CCCCCCCHHHHHHHH		50.6519795423
265PhosphorylationHHHHNRGSTPTKPKL
CCCCCCCCCCCCCCC		28.1628889911
266PhosphorylationHHHNRGSTPTKPKLN
CCCCCCCCCCCCCCC		37.4927214570
286UbiquitinationNIVESNGKALYETDN
CHHHCCCEEEEECCC		39.2017644757
300UbiquitinationNPVELLEKYGIPGRK
CHHHHHHHHCCCCCC		49.0617644757
313PhosphorylationRKLGEGASGSVSVVE
CCCCCCCCCCEEEEE		42.3228889911
315PhosphorylationLGEGASGSVSVVERT
CCCCCCCCEEEEECC		14.5528889911
317PhosphorylationEGASGSVSVVERTDG
CCCCCCEEEEECCCC		23.3419779198
334UbiquitinationFACKMFRKPHLNNEG
EEEEECCCCCCCCCC		26.0622106047
342PhosphorylationPHLNNEGTNQSQLAN
CCCCCCCCCHHHHHH		24.7328889911
345PhosphorylationNNEGTNQSQLANYSK
CCCCCCHHHHHHHCC		29.2728889911
351PhosphorylationQSQLANYSKKVTTEF
HHHHHHHCCCEECCC		26.3025704821
352UbiquitinationSQLANYSKKVTTEFC
HHHHHHCCCEECCCC		40.6817644757
353UbiquitinationQLANYSKKVTTEFCI
HHHHHCCCEECCCCC		38.5817644757
445UbiquitinationVTKDGILKLIDFGSA
ECCCCEEEEEECCCE		41.2817644757
465UbiquitinationPYEDTIVKSHGIVGS
CCCCCEEHHCCCCCC		32.6517644757
472PhosphorylationKSHGIVGSDPYLAPE
HHCCCCCCCCCCCHH		25.2321440633
482AcetylationYLAPELLKQTSYDPR
CCCHHHHHCCCCCHH		65.2424489116
482UbiquitinationYLAPELLKQTSYDPR
CCCHHHHHCCCCCHH		65.2417644757
516PhosphorylationPWKAPKKSFNSFRLF
CCCCCCCCCCCEECE		35.4721440633
519PhosphorylationAPKKSFNSFRLFTEE
CCCCCCCCEECEECC		15.1028889911
539UbiquitinationDIVRGPNKILRLLPR
CCCCCHHHHHHHCCC		46.3717644757
580PhosphorylationDWLVSVPSCEVDPTS
CEEEECCCCEECCCC		22.2819779198
598UbiquitinationVEKPKNHKHHLVTEE
CCCCCCCCCCCCCHH		41.9617644757
611PhosphorylationEEELNELTKQHGNKD
HHHHHHHHHHHCCCC		23.6028889911
612UbiquitinationEELNELTKQHGNKDS
HHHHHHHHHHCCCCC		53.5817644757
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 RTK1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RTK1_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 RTK1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AIM2_YEASTAIM2physical
11805837
TDA3_YEASTTDA3physical
11805837
YG1A_YEASTYGR016Wphysical
11805837
IF4E_YEASTCDC33physical
11805837
KHSE_YEASTTHR1genetic
19269370
ARC1_YEASTARC1physical
20489023
BEM2_YEASTBEM2physical
20489023
CDC14_YEASTCDC14physical
20489023
CSK22_YEASTCKA2physical
20489023
ERB1_YEASTERB1physical
20489023
SYEC_YEASTGUS1physical
20489023
HAS1_YEASTHAS1physical
20489023
NET1_YEASTNET1physical
20489023
NOC3_YEASTNOC3physical
20489023
NOG1_YEASTNOG1physical
20489023
NOP12_YEASTNOP12physical
20489023
NOP13_YEASTNOP13physical
20489023
PESC_YEASTNOP7physical
20489023
RRS1_YEASTRRS1physical
20489023
UTP22_YEASTUTP22physical
20489023
YTM1_YEASTYTM1physical
20489023
ARF3_YEASTARF3physical
21460040
MCM4_YEASTMCM4physical
21460040
GSF2_YEASTGSF2physical
21460040
DBP4_YEASTHCA4physical
21460040
HNM1_YEASTHNM1physical
21460040
MPC54_YEASTMPC54physical
21460040
PFKA1_YEASTPFK1physical
21460040
PFKA2_YEASTPFK2physical
21460040
SET4_YEASTSET4physical
21460040
SKY1_YEASTSKY1physical
21460040
YBF5_YEASTYBL055Cphysical
21460040
YD183_YEASTYDL183Cphysical
21460040
YD132_YEASTYDR132Cphysical
21460040
EFM3_YEASTEFM3physical
21460040
YM54_YEASTYMR196Wphysical
21460040
HAL4_YEASTSAT4genetic
21127252
RTG3_YEASTRTG3genetic
21127252
RTK1_YEASTRTK1physical
22940862
HER1_YEASTHER1physical
22940862
RU2A_YEASTLEA1genetic
27708008
ETR1_YEASTETR1genetic
27708008
TCM62_YEASTTCM62genetic
27708008
ADPP_YEASTYSA1genetic
27708008
RV161_YEASTRVS161genetic
27708008
THRC_YEASTTHR4genetic
27708008
RV167_YEASTRVS167genetic
27708008
IES5_YEASTIES5genetic
27708008
SGF73_YEASTSGF73genetic
27708008
ASK10_YEASTASK10genetic
27708008
ELP2_YEASTELP2genetic
27708008
ICE2_YEASTICE2genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
DCOR_YEASTSPE1genetic
27708008
PUR91_YEASTADE16genetic
27708008
UBX2_YEASTUBX2genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
COX7_YEASTCOX7genetic
27708008
ROY1_YEASTROY1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
INO4_YEASTINO4genetic
27708008
RS10A_YEASTRPS10Agenetic
27708008
FUMH_YEASTFUM1genetic
27708008
TRI55_HUMANTRIM55physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RTK1_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 THR-58; SER-60; SER-81;SER-104; THR-106; SER-216 AND SER-516, 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-9; SER-11; SER-12;SER-14; THR-58; SER-60 AND SER-81, AND MASS SPECTROMETRY.
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, AND MASSSPECTROMETRY.

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