DBF20_YEAST - dbPTM
DBF20_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DBF20_YEAST
UniProt AC P32328
Protein Name Serine/threonine-protein kinase DBF20
Gene Name DBF20
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 564
Subcellular Localization
Protein Description Is probably a Ser/Thr-protein kinase that may function in initiation of DNA synthesis and also in late nuclear division..
Protein Sequence MFSRSDREVDDLAGNMSHLGFYDLNIPKPTSPQAQYRPARKSENGRLTPGLPRSYKPCDSDDQDTFKNRISLNHSPKKLPKDFHERASQSKTQRVVNVCQLYFLDYYCDMFDYVISRRQRTKQVLRYLEQQRSVKNVSNKVLNEEWALYLQREHEVLRKRRLKPKHKDFQILTQVGQGGYGQVYLAKKKDSDEICALKILNKKLLFKLNETNHVLTERDILTTTRSDWLVKLLYAFQDPESLYLAMEFVPGGDFRTLLINTRILKSGHARFYISEMFCAVNALHELGYTHRDLKPENFLIDATGHIKLTDFGLAAGTVSNERIESMKIRLEEVKNLEFPAFTERSIEDRRKIYHNMRKTEINYANSMVGSPDYMALEVLEGKKYDFTVDYWSLGCMLFESLVGYTPFSGSSTNETYENLRYWKKTLRRPRTEDRRAAFSDRTWDLITRLIADPINRVRSFEQVRKMSYFAEINFETLRTSSPPFIPQLDDETDAGYFDDFTNEEDMAKYADVFKRQNKLSAMVDDSAVDSKLVGFTFRHRDGKQGSSGILYNGSEHSDPFSTFY
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
17PhosphorylationDDLAGNMSHLGFYDL
HHHCCCCCCCEEEEC		21.40-
30PhosphorylationDLNIPKPTSPQAQYR
ECCCCCCCCCCHHCC		60.2028889911
31PhosphorylationLNIPKPTSPQAQYRP
CCCCCCCCCCHHCCC		24.4419779198
36PhosphorylationPTSPQAQYRPARKSE
CCCCCHHCCCCCCCC		22.9121440633
42PhosphorylationQYRPARKSENGRLTP
HCCCCCCCCCCCCCC		30.6422369663
48PhosphorylationKSENGRLTPGLPRSY
CCCCCCCCCCCCCCC		17.6022369663
60PhosphorylationRSYKPCDSDDQDTFK
CCCCCCCCCCCHHHH		50.2121551504
65PhosphorylationCDSDDQDTFKNRISL
CCCCCCHHHHHHHHC		30.7621551504
71PhosphorylationDTFKNRISLNHSPKK
HHHHHHHHCCCCCCC		21.6321440633
75PhosphorylationNRISLNHSPKKLPKD
HHHHCCCCCCCCCCC		37.0219823750
303PhosphorylationENFLIDATGHIKLTD
CCEEEECCCCEEECC		26.0828889911
317PhosphorylationDFGLAAGTVSNERIE
CCCEEECCCCHHHHH		18.9428889911
319PhosphorylationGLAAGTVSNERIESM
CEEECCCCHHHHHHH		32.5828889911
325PhosphorylationVSNERIESMKIRLEE
CCHHHHHHHCEEHHH		24.0120377248
359PhosphorylationIYHNMRKTEINYANS
HHHHHHHHHHHHHHH		31.5619779198
363PhosphorylationMRKTEINYANSMVGS
HHHHHHHHHHHCCCC		16.9021440633
366PhosphorylationTEINYANSMVGSPDY
HHHHHHHHCCCCCCE		13.4827821475
467PhosphorylationFEQVRKMSYFAEINF
HHHHHHHHHEEEECH		21.8228889911
536PhosphorylationDSKLVGFTFRHRDGK
CHHHEEEEEECCCCC		17.5222890988
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 DBF20_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DBF20_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 DBF20_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AXL1_YEASTAXL1physical
11805837
MOB1_YEASTMOB1physical
11805837
NACA_YEASTEGD2physical
11805837
RPAB5_YEASTRPB10physical
11805837
IDH2_YEASTIDH2physical
11805837
PHSG_YEASTGPH1physical
11805837
SYA_YEASTALA1physical
11805837
MOB1_YEASTMOB1physical
9528782
NET1_YEASTNET1genetic
11914130
KCS1_YEASTKCS1genetic
19269370
CYK3_YEASTCYK3genetic
20442249
MKT1_YEASTMKT1physical
20489023
MOB1_YEASTMOB1physical
20489023
SA185_YEASTSAP185physical
20489023
YPK1_YEASTYPK1physical
20489023
BUD16_YEASTBUD16physical
21460040
CYK2_YEASTHOF1genetic
21498574
SLX8_YEASTSLX8genetic
21127252
KCS1_YEASTKCS1genetic
21127252
REI1_YEASTREI1genetic
21127252
MET18_YEASTMET18genetic
21127252
BUB1_YEASTBUB1genetic
21127252
UPC2_YEASTUPC2genetic
21127252
CG11_YEASTCLN1genetic
21127252
DYHC_YEASTDYN1genetic
22385961
H1_YEASTHHO1physical
22718910
SSK2_YEASTSSK2genetic
22282571
DBF2_YEASTDBF2genetic
22282571
RV161_YEASTRVS161genetic
22282571
VPS27_YEASTVPS27genetic
22282571
WHI5_YEASTWHI5genetic
22282571
STE50_YEASTSTE50genetic
22282571
UBP3_YEASTUBP3genetic
22282571
NST1_YEASTNST1genetic
22282571
RV161_YEASTRVS161genetic
27708008
INO2_YEASTINO2genetic
27708008
RV167_YEASTRVS167genetic
27708008
UBP3_YEASTUBP3genetic
27708008
DBF2_YEASTDBF2genetic
27708008
LDB18_YEASTLDB18genetic
27708008
CORO_YEASTCRN1genetic
27708008
UBX2_YEASTUBX2genetic
27708008
EOS1_YEASTEOS1genetic
27708008
FAR11_YEASTFAR11genetic
27708008
VPS27_YEASTVPS27genetic
27708008
IRA2_YEASTIRA2genetic
27708008
INO4_YEASTINO4genetic
27708008
MOB1_YEASTMOB1genetic
28450458
ARP8_YEASTARP8genetic
27453043
PBS2_YEASTPBS2genetic
27453043
SWI6_YEASTSWI6genetic
27453043
GCR2_YEASTGCR2genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DBF20_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-366, AND MASSSPECTROMETRY.
"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-75, AND MASSSPECTROMETRY.
"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-536, AND MASSSPECTROMETRY.

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