KKQ8_YEAST - dbPTM
KKQ8_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KKQ8_YEAST
UniProt AC P36004
Protein Name Probable serine/threonine-protein kinase KKQ8
Gene Name KKQ8
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 724
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MVMQEEKKRQQPVTRRVRSFSESFKNLFRPPRSRDSSPINVTRIPYRSSSTSPKRSSEPPRRSTVSAQILDPKNSPIRQRSYTLKCCTPGLSHPFRQTGSGASNSPTRHRSISGEEQEIVNSLPEYKRSASHTFHGIRRPRSRSSSVSSCDSSNGTTSSSDSQWAMDSLLDDSDNDLTPYRGSNKDILKSKDRAPYNYIDDYNKKALRRATSYPNPLPSKQFYNERLYTRRSHPDEESLESLPRFAGADVQCIIEQNGFKVYEDGSHEHNIKLSGVIAKLEKGNSLPAHRQGSLSRPRLGITLSGLFKHHKNECDIENALSLLPNVEKSQTNHEKRTGQSPNDSNRSSPTQGREDYLKIVNPDASLGSDELKLINSLSSRIHKSLQNYLQEKNLKPAECIGEQAPTFQDNYGHPVGLVGAGAYGEVKLCARLRNEKDSPPFETYHDSKYIYYAVKELKPKPDSDLEKFCTKITSEFIIGHSLSHYHKNGKKPAPNILNVFDILEDSSSFIEVMEFCPAGDLYGMLVGKSKLKGRLHPLEADCFMKQLLHGVKFMHDHGIAHCDLKPENILFYPHGLLKICDFGTSSVFQTAWERRVHAQKGIIGSEPYVAPEEFVDGEYYDPRLIDCWSCGVVYITMILGHYLWKVASREKDMSYDEFYKEMQRKNQFRVFEELKHVNSELATNRKIALYRIFQWEPRKRISVGKLLDMQWMKSTNCCLIYDST
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
19PhosphorylationPVTRRVRSFSESFKN
CCHHHHHHHHHHHHH
30.2121082442
21PhosphorylationTRRVRSFSESFKNLF
HHHHHHHHHHHHHHH
33.3125533186
33PhosphorylationNLFRPPRSRDSSPIN
HHHCCCCCCCCCCCC
46.3322369663
36PhosphorylationRPPRSRDSSPINVTR
CCCCCCCCCCCCCEE
36.5822369663
37PhosphorylationPPRSRDSSPINVTRI
CCCCCCCCCCCCEEC
33.8022369663
42PhosphorylationDSSPINVTRIPYRSS
CCCCCCCEECCCCCC
20.5622369663
46PhosphorylationINVTRIPYRSSSTSP
CCCEECCCCCCCCCC
22.2828889911
48PhosphorylationVTRIPYRSSSTSPKR
CEECCCCCCCCCCCC
23.8528889911
49PhosphorylationTRIPYRSSSTSPKRS
EECCCCCCCCCCCCC
28.7428889911
50PhosphorylationRIPYRSSSTSPKRSS
ECCCCCCCCCCCCCC
33.8628889911
56PhosphorylationSSTSPKRSSEPPRRS
CCCCCCCCCCCCCCC
45.2227017623
57PhosphorylationSTSPKRSSEPPRRST
CCCCCCCCCCCCCCC
59.1528889911
63PhosphorylationSSEPPRRSTVSAQIL
CCCCCCCCCCEEEEC
34.1527017623
75PhosphorylationQILDPKNSPIRQRSY
EECCCCCCCCCCCEE
28.0322369663
81PhosphorylationNSPIRQRSYTLKCCT
CCCCCCCEEEEEEEC
17.7121440633
82PhosphorylationSPIRQRSYTLKCCTP
CCCCCCEEEEEEECC
20.4821440633
83PhosphorylationPIRQRSYTLKCCTPG
CCCCCEEEEEEECCC
22.4619823750
92PhosphorylationKCCTPGLSHPFRQTG
EEECCCCCCCCCCCC
34.7221440633
100PhosphorylationHPFRQTGSGASNSPT
CCCCCCCCCCCCCCC
34.2828889911
103PhosphorylationRQTGSGASNSPTRHR
CCCCCCCCCCCCCCC
41.1721440633
105PhosphorylationTGSGASNSPTRHRSI
CCCCCCCCCCCCCCC
25.7525752575
107PhosphorylationSGASNSPTRHRSISG
CCCCCCCCCCCCCCH
38.6430377154
111PhosphorylationNSPTRHRSISGEEQE
CCCCCCCCCCHHHHH
18.2522369663
113PhosphorylationPTRHRSISGEEQEIV
CCCCCCCCHHHHHHH
41.2022369663
131PhosphorylationPEYKRSASHTFHGIR
HHHHHHHCCCCCCCC
25.0629136822
133PhosphorylationYKRSASHTFHGIRRP
HHHHHCCCCCCCCCC
18.1629136822
211PhosphorylationKKALRRATSYPNPLP
HHHHHHHCCCCCCCC
27.2920377248
212PhosphorylationKALRRATSYPNPLPS
HHHHHHCCCCCCCCC
37.2922369663
213PhosphorylationALRRATSYPNPLPSK
HHHHHCCCCCCCCCH
11.5919779198
220UbiquitinationYPNPLPSKQFYNERL
CCCCCCCHHHHHCCC
42.3523749301
223PhosphorylationPLPSKQFYNERLYTR
CCCCHHHHHCCCCCC
17.3919779198
232PhosphorylationERLYTRRSHPDEESL
CCCCCCCCCCCHHHH
35.7622369663
238PhosphorylationRSHPDEESLESLPRF
CCCCCHHHHHHCCCC
35.0822369663
241PhosphorylationPDEESLESLPRFAGA
CCHHHHHHCCCCCCC
49.3022369663
302PhosphorylationSRPRLGITLSGLFKH
CCCCCEEEHHHHHHH
17.0522369663
304PhosphorylationPRLGITLSGLFKHHK
CCCEEEHHHHHHHCC
25.4622369663
337PhosphorylationQTNHEKRTGQSPNDS
CCCCCCCCCCCCCCC
51.1224961812
340PhosphorylationHEKRTGQSPNDSNRS
CCCCCCCCCCCCCCC
27.3225752575
344PhosphorylationTGQSPNDSNRSSPTQ
CCCCCCCCCCCCCCC
40.5620377248
347PhosphorylationSPNDSNRSSPTQGRE
CCCCCCCCCCCCCCH
44.9420377248
348PhosphorylationPNDSNRSSPTQGRED
CCCCCCCCCCCCCHH
28.8221440633
350PhosphorylationDSNRSSPTQGREDYL
CCCCCCCCCCCHHHH
45.6720377248
356PhosphorylationPTQGREDYLKIVNPD
CCCCCHHHHHHCCCC
12.7321440633
376PhosphorylationDELKLINSLSSRIHK
HHHHHHHHHHHHHHH
23.7228889911
378PhosphorylationLKLINSLSSRIHKSL
HHHHHHHHHHHHHHH
19.8623749301
379PhosphorylationKLINSLSSRIHKSLQ
HHHHHHHHHHHHHHH
40.3123749301

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 KKQ8_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KKQ8_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 KKQ8_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BMH2_YEASTBMH2physical
18719252
BMH1_YEASTBMH1physical
18719252
BMH1_YEASTBMH1physical
20489023
UBC1_YEASTUBC1physical
20489023
PABS_YEASTABZ1physical
21460040
SYA_YEASTALA1physical
21460040
CDC11_YEASTCDC11physical
21460040
CSN9_YEASTCSN9physical
21460040
BUD27_YEASTBUD27physical
21460040
GLNA_YEASTGLN1physical
21460040
PP2C1_YEASTPTC1physical
21460040
UAP1_YEASTQRI1physical
21460040
RIR4_YEASTRNR4physical
21460040
RL39_YEASTRPL39physical
21460040
SHE2_YEASTSHE2physical
21460040
SIP5_YEASTSIP5physical
21460040
IF4A_YEASTTIF2physical
21460040
TDA10_YEASTTDA10physical
21460040
YHY2_YEASTYHR182Wphysical
21460040
YKJ1_YEASTYKL091Cphysical
21460040
YM54_YEASTYMR196Wphysical
21460040
RTG3_YEASTRTG3genetic
21127252
VMS1_YEASTVMS1genetic
21127252
RL6B_YEASTRPL6Bgenetic
22282571
YO163_YEASTYOL163Wgenetic
22282571
KPR5_YEASTPRS5genetic
22282571
SMA2_YEASTSMA2genetic
22282571
YO029_YEASTYOL029Cgenetic
22282571
BUB3_YEASTBUB3genetic
22282571
YO131_YEASTYOL131Wgenetic
22282571
YG35_YEASTYGR125Wgenetic
22282571
PDR15_YEASTPDR15genetic
22282571
CTU2_YEASTNCS2genetic
22282571
YD061_YEASTYDR061Wgenetic
22282571
RAS1_YEASTRAS1genetic
22282571
RS23A_YEASTRPS23Agenetic
22282571
RS23B_YEASTRPS23Agenetic
22282571
GYP1_YEASTGYP1genetic
22282571
VPS68_YEASTVPS68genetic
22282571
RV167_YEASTRVS167genetic
22282571
PTH_YEASTPTH1genetic
22282571
EAF1_YEASTEAF1genetic
22282571
CRD1_YEASTCRD1genetic
22282571
SOL4_YEASTSOL4genetic
22282571
OSH3_YEASTOSH3genetic
22282571
UBA4_YEASTUBA4genetic
22282571
NU133_YEASTNUP133genetic
22282571
APJ1_YEASTAPJ1genetic
22282571
VMA21_YEASTVMA21genetic
22282571
DEP1_YEASTDEP1genetic
22282571
YMD7_YEASTYML037Cgenetic
22282571
PST2_YEASTPST2genetic
22282571
ICS3_YEASTICS3genetic
22282571
PNT1_YEASTPNT1genetic
22282571
VPS74_YEASTVPS74genetic
22282571
ODP2_YEASTLAT1genetic
22282571
PTR2_YEASTPTR2genetic
22282571
SPO11_YEASTSPO11genetic
22282571
SUL1_YEASTSUL1genetic
22282571
YOR1_YEASTYOR1genetic
27708008
MBA1_YEASTMBA1genetic
27708008
CRD1_YEASTCRD1genetic
27708008
YD061_YEASTYDR061Wgenetic
27708008
RV167_YEASTRVS167genetic
27708008
PDR15_YEASTPDR15genetic
27708008
SNF1_YEASTSNF1genetic
27708008
PMD1_YEASTPMD1genetic
27708008
RAD4_YEASTRAD4genetic
27708008
SLX9_YEASTSLX9genetic
27708008
RS23A_YEASTRPS23Agenetic
27708008
RS23B_YEASTRPS23Agenetic
27708008
SOL4_YEASTSOL4genetic
27708008
PTH_YEASTPTH1genetic
27708008
NU133_YEASTNUP133genetic
27708008
YMD7_YEASTYML037Cgenetic
27708008
FMS1_YEASTFMS1genetic
27708008
APJ1_YEASTAPJ1genetic
27708008
CTU2_YEASTNCS2genetic
27708008
COQ2_YEASTCOQ2genetic
27708008
KPR5_YEASTPRS5genetic
27708008
INO4_YEASTINO4genetic
27708008
VPS68_YEASTVPS68genetic
27708008
YO131_YEASTYOL131Wgenetic
27708008
YO163_YEASTYOL163Wgenetic
27708008
RAS1_YEASTRAS1genetic
27708008
YO105_YEASTYOR105Wgenetic
27708008
PNT1_YEASTPNT1genetic
27708008
NACB1_YEASTEGD1genetic
27708008
YP066_YEASTRGL1genetic
27708008
KAR3_YEASTKAR3genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KKQ8_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-21; SER-37; SER-75;SER-111; SER-113; SER-212; SER-232; SER-238 AND SER-241, AND MASSSPECTROMETRY.
"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-19; SER-238 AND SER-241,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-19, 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-232; SER-238 ANDSER-241, 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 SER-21, AND MASSSPECTROMETRY.

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