ASG1_YEAST - dbPTM
ASG1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ASG1_YEAST
UniProt AC P40467
Protein Name Activator of stress genes 1
Gene Name ASG1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 964
Subcellular Localization Nucleus .
Protein Description Probable transcription factor involved in the stress response..
Protein Sequence MPEQAQQGEQSVKRRRVTRACDECRKKKVKCDGQQPCIHCTVYSYECTYKKPTKRTQNSGNSGVLTLGNVTTGPSSSTVVAAAASNPNKLLSNIKTERAILPGASTIPASNNPSKPRKYKTKSTRLQSKIDRYKQIFDEVFPQLPDIDNLDIPVFLQIFHNFKRDSQSFLDDTVKEYTLIVNDSSSPIQPVLSSNSKNSTPDEFLPNMKSDSNSASSNREQDSVDTYSNIPVGREIKIILPPKAIALQFVKSTWEHCCVLLRFYHRPSFIRQLDELYETDPNNYTSKQMQFLPLCYAAIAVGALFSKSIVSNDSSREKFLQDEGYKYFIAARKLIDITNARDLNSIQAILMLIIFLQCSARLSTCYTYIGVAMRSALRAGFHRKLSPNSGFSPIEIEMRKRLFYTIYKLDVYINAMLGLPRSISPDDFDQTLPLDLSDENITEVAYLPENQHSVLSSTGISNEHTKLFLILNEIISELYPIKKTSNIISHETVTSLELKLRNWLDSLPKELIPNAENIDPEYERANRLLHLSFLHVQIILYRPFIHYLSRNMNAENVDPLCYRRARNSIAVARTVIKLAKEMVSNNLLTGSYWYACYTIFYSVAGLLFYIHEAQLPDKDSAREYYDILKDAETGRSVLIQLKDSSMAASRTYNLLNQIFEKLNSKTIQLTALHSSPSNESAFLVTNNSSALKPHLGDSLQPPVFFSSQDTKNSFSLAKSEESTNDYAMANYLNNTPISENPLNEAQQQDQVSQGTTNMSNERDPNNFLSIDIRLDNNGQSNILDATDDVFIRNDGDIPTNSAFDFSSSKSNASNNSNPDTINNNYNNVSGKNNNNNNITNNSNNNHNNNNNDNNNNNNNNNNNNNNNNNSGNSSNNNNNNNNNKNNNDFGIKIDNNSPSYEGFPQLQIPLSQDNLNIEDKEEMSPNIEIKNEQNMTDSNDILGVFDQLDAQLFGKYLPLNYPSE
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
92PhosphorylationSNPNKLLSNIKTERA
CCCCHHHHCCCCCCC		47.1221440633
115UbiquitinationPASNNPSKPRKYKTK
CCCCCCCCCCCCCCC		50.5323749301
166PhosphorylationFHNFKRDSQSFLDDT
HHHCCCCCHHHHCCC		31.5820190278
168PhosphorylationNFKRDSQSFLDDTVK
HCCCCCHHHHCCCCC		31.5630377154
177PhosphorylationLDDTVKEYTLIVNDS
HCCCCCEEEEEECCC		10.9219779198
178PhosphorylationDDTVKEYTLIVNDSS
CCCCCEEEEEECCCC		15.8819823750
184PhosphorylationYTLIVNDSSSPIQPV
EEEEECCCCCCCCCC		27.7521440633
185PhosphorylationTLIVNDSSSPIQPVL
EEEECCCCCCCCCCC		42.8925521595
186PhosphorylationLIVNDSSSPIQPVLS
EEECCCCCCCCCCCC		29.9425521595
193PhosphorylationSPIQPVLSSNSKNST
CCCCCCCCCCCCCCC		27.9220377248
194PhosphorylationPIQPVLSSNSKNSTP
CCCCCCCCCCCCCCC		40.7520377248
196PhosphorylationQPVLSSNSKNSTPDE
CCCCCCCCCCCCCCH		34.8521440633
199PhosphorylationLSSNSKNSTPDEFLP
CCCCCCCCCCCHHCC		45.0822369663
200PhosphorylationSSNSKNSTPDEFLPN
CCCCCCCCCCHHCCC		44.1222369663
210PhosphorylationEFLPNMKSDSNSASS
HHCCCCCCCCCCCCC		35.1921551504
212PhosphorylationLPNMKSDSNSASSNR
CCCCCCCCCCCCCCC		39.5127214570
214PhosphorylationNMKSDSNSASSNREQ
CCCCCCCCCCCCCCC		33.2221440633
216PhosphorylationKSDSNSASSNREQDS
CCCCCCCCCCCCCCC		28.1521440633
217PhosphorylationSDSNSASSNREQDSV
CCCCCCCCCCCCCCC		39.3521440633
223PhosphorylationSSNREQDSVDTYSNI
CCCCCCCCCCCCCCC		22.9127214570
226PhosphorylationREQDSVDTYSNIPVG
CCCCCCCCCCCCCCC		27.0528889911
227PhosphorylationEQDSVDTYSNIPVGR
CCCCCCCCCCCCCCC		8.6823749301
228PhosphorylationQDSVDTYSNIPVGRE
CCCCCCCCCCCCCCE		30.3119779198
400UbiquitinationPIEIEMRKRLFYTIY
CCCHHHHHHHHHHHH		52.7417644757
666PhosphorylationFEKLNSKTIQLTALH
HHHHCCCEEEEEEEE		17.4921551504
675PhosphorylationQLTALHSSPSNESAF
EEEEEECCCCCCCEE		22.9220377248
677PhosphorylationTALHSSPSNESAFLV
EEEECCCCCCCEEEE		56.0021551504
680PhosphorylationHSSPSNESAFLVTNN
ECCCCCCCEEEEECC		28.6820377248
707PhosphorylationQPPVFFSSQDTKNSF
CCCEEECCCCCCCCC		27.2421551504
713PhosphorylationSSQDTKNSFSLAKSE
CCCCCCCCCCCCCCC		20.1228889911
810PhosphorylationFDFSSSKSNASNNSN
CCCCCCCCCCCCCCC		39.3122369663
813PhosphorylationSSSKSNASNNSNPDT
CCCCCCCCCCCCCCC		40.5722369663
816PhosphorylationKSNASNNSNPDTINN
CCCCCCCCCCCCCCC		54.7322369663
820PhosphorylationSNNSNPDTINNNYNN
CCCCCCCCCCCCCCC		27.1923749301
829PhosphorylationNNNYNNVSGKNNNNN
CCCCCCCCCCCCCCC		46.2922369663
897PhosphorylationGIKIDNNSPSYEGFP
CEEECCCCCCCCCCC		22.8321440633
899PhosphorylationKIDNNSPSYEGFPQL
EECCCCCCCCCCCCC		35.3221440633
900PhosphorylationIDNNSPSYEGFPQLQ
ECCCCCCCCCCCCCC		24.3719823750
911PhosphorylationPQLQIPLSQDNLNIE
CCCCCCCCCCCCCCC		30.0819823750
924PhosphorylationIEDKEEMSPNIEIKN
CCCHHHCCCCCEECC		20.3422369663
961PhosphorylationGKYLPLNYPSE----
CCCCCCCCCCC----		18.8022890988
963PhosphorylationYLPLNYPSE------
CCCCCCCCC------		45.6525521595
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
166SPhosphorylationKinaseATMP38110
Uniprot
166SPhosphorylationKinaseATRP38111
Uniprot
166SPhosphorylationKinaseATM/ATR-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ASG1_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 ASG1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YP015_YEASTYPR015Cgenetic
20959818
SAC3_YEASTSAC3genetic
20959818
GCR2_YEASTGCR2genetic
20959818
COG3_YEASTCOG3genetic
27708008
STU1_YEASTSTU1genetic
27708008
KPC1_YEASTPKC1genetic
27708008
PRP6_YEASTPRP6genetic
27708008
APC11_YEASTAPC11genetic
27708008
DPOD_YEASTPOL3genetic
27708008
GNA1_YEASTGNA1genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
FDFT_YEASTERG9genetic
27708008
MET30_YEASTMET30genetic
27708008
SHQ1_YEASTSHQ1genetic
27708008
MOB1_YEASTMOB1genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
PRP19_YEASTPRP19genetic
27708008
UTP13_YEASTUTP13genetic
27708008
BUR1_YEASTSGV1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ASG1_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-166; SER-185; SER-186;THR-200; THR-226; SER-810; SER-813; SER-816; SER-911 AND SER-963, ANDMASS 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-166, 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-963, 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-963, AND MASSSPECTROMETRY.

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