YI002_YEAST - dbPTM
YI002_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YI002_YEAST
UniProt AC Q3E7Z5
Protein Name Uncharacterized protein YIL002W-A
Gene Name YIL002W-A
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 69
Subcellular Localization
Protein Description
Protein Sequence MTRDTPEDVSTAGAKDILDVLNLLKGGEEKISEVELKLDEMEKKMDSLLVQLEDLHRDNNDLAKSSSQK
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
2Phosphorylation------MTRDTPEDV
------CCCCCHHHH
36.9328889911
5Phosphorylation---MTRDTPEDVSTA
---CCCCCHHHHHHC
25.8622369663
10PhosphorylationRDTPEDVSTAGAKDI
CCCHHHHHHCCHHHH
25.5128132839
11PhosphorylationDTPEDVSTAGAKDIL
CCHHHHHHCCHHHHH
29.0322369663
25UbiquitinationLDVLNLLKGGEEKIS
HHHHHHHHCCCHHHH
68.9524961812
25AcetylationLDVLNLLKGGEEKIS
HHHHHHHHCCCHHHH
68.9524489116
32PhosphorylationKGGEEKISEVELKLD
HCCCHHHHHHHHHHH
46.8128889911
43AcetylationLKLDEMEKKMDSLLV
HHHHHHHHHHHHHHH
52.6824489116
64AcetylationRDNNDLAKSSSQK--
HCCCHHHHHHCCC--
59.1625381059

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 YI002_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YI002_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 YI002_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HPH2_YEASTFRT2physical
22875988
SPC72_YEASTSPC72physical
22875988
FIN1_YEASTFIN1physical
22875988
NBP1_YEASTNBP1physical
22875988
YRA2_YEASTYRA2genetic
27708008
YM14_YEASTYMR130Wgenetic
27708008
DGK1_YEASTDGK1genetic
27708008
SHG1_YEASTSHG1genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
SNT1_YEASTSNT1genetic
27708008
ATG15_YEASTATG15genetic
27708008
IPT1_YEASTIPT1genetic
27708008
PP4C_YEASTPPH3genetic
27708008
VPS41_YEASTVPS41genetic
27708008
FOB1_YEASTFOB1genetic
27708008
SGF73_YEASTSGF73genetic
27708008
HOS2_YEASTHOS2genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
MED20_YEASTSRB2genetic
27708008
STB5_YEASTSTB5genetic
27708008
PTH_YEASTPTH1genetic
27708008
AIM18_YEASTAIM18genetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
DHOM_YEASTHOM6genetic
27708008
RM49_YEASTMRP49genetic
27708008
SET3_YEASTSET3genetic
27708008
NAP1_YEASTNAP1genetic
27708008
PAM17_YEASTPAM17genetic
27708008
HOG1_YEASTHOG1genetic
27708008
MMR1_YEASTMMR1genetic
27708008
VID22_YEASTVID22genetic
27708008
RM39_YEASTMRPL39genetic
27708008
SKY1_YEASTSKY1genetic
27708008
SAP30_YEASTSAP30genetic
27708008
HRB1_YEASTHRB1genetic
27708008
YO036_YEASTYOL036Wgenetic
27708008
PT127_YEASTPET127genetic
27708008
CY1_YEASTCYT1genetic
27708008
RDL2_YEASTRDL2genetic
27708008
MSC6_YEASTMSC6genetic
27708008
RAD1_YEASTRAD1genetic
27708008
TRM44_YEASTTRM44genetic
27708008
FMP30_YEASTFMP30genetic
27708008
PET20_YEASTPET20genetic
27708008
CTI6_YEASTCTI6genetic
27708008
SRO7_YEASTSRO7genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YI002_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-5, AND MASSSPECTROMETRY.

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