YDR09_YEAST - dbPTM
YDR09_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YDR09_YEAST
UniProt AC Q04585
Protein Name Uncharacterized sugar kinase YDR109C
Gene Name YDR109C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 715
Subcellular Localization
Protein Description
Protein Sequence MKSRKRQNNMQNETREPAVLSSQETSISRISPQDPEAKFYVGVDVGTGSARACVIDQSGNMLSLAEKPIKREQLISNFITQSSREIWNAVCYCVRTVVEESGVDPERVRGIGFDATCSLVVVSATNFEEIAVGPDFTNNDQNIILWMDHRAMKETEEINSSGDKCLKYVGGQMSVEMEIPKIKWLKNNLEAGIFQDCKFFDLPDYLTFKATGKENRSFCSAVCKQGFLPVGVEGSDIGWSKEFLNSIGLSELTKNDFERLGGSLREKKNFLTAGECISPLDKKAACQLGLTEHCVVSSGIIDAYAGWVGTVAAKPESAVKGLAETENYKKDFNGAIGRLAAVAGTSTCHILLSKNPIFVHGVWGPYRDVLARGFWAAEGGQSCTGVLLDHLITTHPAFTELSHMANLAGVSKFEYLNKILETLVEKRKVRSVISLAKHLFFYGDYHGNRSPIADPNMRACIIGQSMDNSIEDLAVMYLSACEFISQQTRQIIEVMLKSGHEINAIFMSGGQCRNSLLMRLLADCTGLPIVIPRYVDAAVVFGSALLGAAASEDFDYTREKRTLKGQKSSQTKTERFNDSYSSIQKLSMEDRNSTNGFVSPHNLQLSTPSAPAKINNYSLPICTQQPLDKTSEESSKDASLTVGQESLGEGRYNGTSFLWKVMQELTGNARIVNPNEKTHPDRILLDTKYQIFLDMIETQRKYRRMVDKVEGSFSR
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
22PhosphorylationREPAVLSSQETSISR
CCCHHHCCCCCCCCC
28.0728889911
31PhosphorylationETSISRISPQDPEAK
CCCCCCCCCCCCCCC
18.5228889911
450PhosphorylationGDYHGNRSPIADPNM
CCCCCCCCCCCCCCC
25.3428889911
465PhosphorylationRACIIGQSMDNSIED
CEEEECCCCCCCHHH
23.9228889911
469PhosphorylationIGQSMDNSIEDLAVM
ECCCCCCCHHHHHHH
24.0828889911
525PhosphorylationMRLLADCTGLPIVIP
HHHHHHHHCCCEEEC
42.1517563356
573PhosphorylationQKSSQTKTERFNDSY
CCCCCCCHHHCCCCH
35.4622369663
579PhosphorylationKTERFNDSYSSIQKL
CHHHCCCCHHHHHHH
28.1922369663
580PhosphorylationTERFNDSYSSIQKLS
HHHCCCCHHHHHHHC
14.8622369663
581PhosphorylationERFNDSYSSIQKLSM
HHCCCCHHHHHHHCC
25.5622369663
582PhosphorylationRFNDSYSSIQKLSME
HCCCCHHHHHHHCCC
22.3222369663
656PhosphorylationEGRYNGTSFLWKVMQ
CCCCCHHHHHHHHHH
21.5328889911

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 YDR09_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YDR09_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 YDR09_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SED5_YEASTSED5genetic
27708008
SEC22_YEASTSEC22genetic
27708008
MCM1_YEASTMCM1genetic
27708008
CDC24_YEASTCDC24genetic
27708008
STU1_YEASTSTU1genetic
27708008
PRP9_YEASTPRP9genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SMD1_YEASTSMD1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
RPC6_YEASTRPC34genetic
27708008
ASA1_YEASTASA1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YDR09_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-22 AND SER-579, 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 THR-525, AND MASSSPECTROMETRY.

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