DIG2_YEAST - dbPTM
DIG2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIG2_YEAST
UniProt AC Q03373
Protein Name Down-regulator of invasive growth 2
Gene Name DIG2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 323
Subcellular Localization Nucleus.
Protein Description DIG2 and DIG1 are negative regulators of the filamentation and pheromone induced mating program. DIG1 and DIG2 inhibit the transcriptional activity of STE12 by direct protein-protein interaction. DIG2 binds to the DNA binding domain (DBD) of STE12 and thus inhibits transcription when overexpressed..
Protein Sequence MNKEEQEDPQQEQISTVQENDPRNLQQLGMLLVSPGLDEDRLSEKMISKIKKSRDIEKNQKLLISRLSQKEEDHSGKPPTITTSPAEKTVPFKSLNHSLKRKRVPPALNFSDIQASSHLHGSKSAPPNITRFPQHKNSLRVRYMGRMAPTNQDYHPSVANSYMTATYPYPYTGLPPVPCYPYSSTPTQTHAYEGYYSPMYPGPLYNNGIIPADYHAKRKKLAGRSPHLEDLTSRKRTFVSKHHNGDPIISKTDEDIECSVTKNSLSEGASLNDDADDDNDKERIIIGEISLYDDVFKFEVRDDKNDYMKACETIWTEWHNLKK
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
34PhosphorylationQLGMLLVSPGLDEDR
HHHCEEECCCCCHHH		17.1417330950
43PhosphorylationGLDEDRLSEKMISKI
CCCHHHHHHHHHHHH		35.7428132839
68PhosphorylationKLLISRLSQKEEDHS
HHHHHHHHHCCCCCC		37.7922369663
75PhosphorylationSQKEEDHSGKPPTIT
HHCCCCCCCCCCCCC		61.9122890988
80PhosphorylationDHSGKPPTITTSPAE
CCCCCCCCCCCCCCC		39.2122890988
82PhosphorylationSGKPPTITTSPAEKT
CCCCCCCCCCCCCCC		24.5722369663
83PhosphorylationGKPPTITTSPAEKTV
CCCCCCCCCCCCCCC		28.9422369663
84PhosphorylationKPPTITTSPAEKTVP
CCCCCCCCCCCCCCC		17.2925521595
88AcetylationITTSPAEKTVPFKSL
CCCCCCCCCCCCCCC		57.8624489116
124PhosphorylationSHLHGSKSAPPNITR
HHCCCCCCCCCCCCC		47.9422369663
130PhosphorylationKSAPPNITRFPQHKN
CCCCCCCCCCCCCCC		32.6621440633
225PhosphorylationRKKLAGRSPHLEDLT
HHHHCCCCCCHHHHH		18.7622369663
232PhosphorylationSPHLEDLTSRKRTFV
CCCHHHHHHHCCEEE		38.5222369663
233PhosphorylationPHLEDLTSRKRTFVS
CCHHHHHHHCCEEEH		43.0022369663
237PhosphorylationDLTSRKRTFVSKHHN
HHHHHCCEEEHHCCC		31.2724961812
240PhosphorylationSRKRTFVSKHHNGDP
HHCCEEEHHCCCCCC		23.2924961812
241AcetylationRKRTFVSKHHNGDPI
HCCEEEHHCCCCCCC		43.5125381059
259PhosphorylationTDEDIECSVTKNSLS
CCCCCEEEEECCCCC		21.7428889911
261PhosphorylationEDIECSVTKNSLSEG
CCCEEEEECCCCCCC		14.2819779198
264PhosphorylationECSVTKNSLSEGASL
EEEEECCCCCCCCCC		34.5222369663
266PhosphorylationSVTKNSLSEGASLND
EEECCCCCCCCCCCC		33.5322369663
270PhosphorylationNSLSEGASLNDDADD
CCCCCCCCCCCCCCC		38.2621551504
290PhosphorylationRIIIGEISLYDDVFK
EEEEEEEEEECCEEE		19.3028889911
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 DIG2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIG2_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 DIG2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KSS1_YEASTKSS1physical
11805837
IMA1_YEASTSRP1physical
11805837
ACON_YEASTACO1physical
11805837
FUS3_YEASTFUS3physical
14734536
KSS1_YEASTKSS1physical
14734536
FUS3_YEASTFUS3physical
8918885
FUS3_YEASTFUS3physical
9094309
KSS1_YEASTKSS1physical
9094309
STE12_YEASTSTE12physical
9094309
SYEC_YEASTGUS1physical
16554755
HSC82_YEASTHSC82physical
16554755
STE12_YEASTSTE12physical
16782869
DIG1_YEASTDIG1physical
16782869
DIG1_YEASTDIG1physical
18719252
DIG2_YEASTDIG2physical
18719252
STE12_YEASTSTE12physical
18719252
DIG1_YEASTDIG1genetic
22669614
TEC1_YEASTTEC1genetic
22669614
GPR1_YEASTGPR1genetic
27708008
YIA6_YEASTYIA6genetic
27708008
RL37A_YEASTRPL37Agenetic
27708008
EIF3J_YEASTHCR1genetic
27708008
UBX2_YEASTUBX2genetic
27708008
NOP12_YEASTNOP12genetic
27708008
VAM3_YEASTVAM3genetic
27708008
SNF5_YEASTSNF5genetic
27708008
STE50_YEASTSTE50genetic
27708008
RTF1_YEASTRTF1genetic
27708008
RS27B_YEASTRPS27Bgenetic
27708008
SIN3_YEASTSIN3genetic
27708008
MCP1_YEASTMCP1genetic
27708008
MSC6_YEASTMSC6genetic
27708008
YP114_YEASTYPR114Wgenetic
27708008
AXL1_YEASTAXL1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
PP2B1_YEASTCNA1physical
24930733
PP2B2_YEASTCMP2physical
24930733
FUS3_YEASTFUS3physical
24930733
UBC9_HUMANUBE2Iphysical
27107014
1433S_HUMANSFNphysical
27107014
RHXF2_HUMANRHOXF2physical
27107014
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DIG2_YEAST

loading...

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-83; SER-84; SER-225;SER-264; SER-266 AND SER-270, 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-84; SER-225 AND SER-266,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-124 AND SER-225, ANDMASS SPECTROMETRY.
"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-34 AND SER-225, 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 SER-34, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory