YP091_YEAST - dbPTM
YP091_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YP091_YEAST
UniProt AC Q06833
Protein Name Uncharacterized PH domain-containing protein YPR091C
Gene Name YPR091C
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 770
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type II membrane protein .
Protein Description
Protein Sequence MASLKVFLAVYLLGGITFLPLVLFTLYKIHLLYSNLKSASKKELDHDTADEIDEKTRLLARDIDPEFKARKLEEQLGVKVFNKGWITVTKQYYYHSSEVAVILKNSNNNKDSDTALQEQILQRTDLKKKQRFFAVLRHGNLFLYKDDSQNANLVHAISLQNRFITIWPRFDELGKEELPDASLFTKRTCIAIFKNDLVSIDSKNHNVILPHFDPLTSAESNNGDISTNDTTHEYQSQFHSSNQFFLYFDNNMDKEDWYYQLINASKNSNSLSTGLLDPNVSANAAHLKTKDMLQLIQDINSTENQLTTKWLNALLGRLFLSLQQTDTLNKFIHEKICKKLNKIKTPGFLDDLVVEKVDVGDSAPLFTSPELLELSPEGSTKIAIDVQYRGNLTIIIATKASINLGSRFKQREVSLQLSIKIKEFSGPLLFLIKPPPSNRIWYAFRTEPIMDFEIEPIVSSSKLSYNVVTNAIKSKFAEAVKESLVVPFMDDIVFYPTPNEVYRGGIWEEQDPEAAARARTAAAASDMNNTSAKEHLEALQEGGMKTQSRIKKALRPERKKENLKDLVDASGVATKTTTQTTVTTATNDDVSSSENSTKSRKYFKNSIKKIGRWYKDNVGNSSDTEDMDEIDVQDKKNDDSADERESDNPILTSNPKMISNRRPVPRRPSQPLNTLSPKLEGRKEKDTENFPVPPSASNMNASKMFANKENRKFSVSSNDSQNSLKNGDPHVKASKLESSQAFVKKTSQNRFNDGFFKQDLEFEEQREPKL
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
55AcetylationTADEIDEKTRLLARD
CHHHHHHHHHHHHHC		34.8924489116
175AcetylationPRFDELGKEELPDAS
CCHHHCCCCCCCCCC		61.7224489116
186AcetylationPDASLFTKRTCIAIF
CCCCCCCCCCEEEEE		38.0724489116
678AcetylationPLNTLSPKLEGRKEK
CCCCCCCCCCCCCCC		56.6524489116
708AcetylationASKMFANKENRKFSV
HHHHHCCCCCCCEEC		53.5924489116
735AcetylationDPHVKASKLESSQAF
CCCCCHHHHHHCHHH		62.2225381059
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 YP091_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YP091_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 YP091_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SAC1_YEASTSAC1genetic
16269340
GPT1_YEASTSCT1physical
22940862
ICS2_YEASTICS2genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
AIM18_YEASTAIM18genetic
27708008
MCR1_YEASTMCR1genetic
27708008
MAK16_YEASTMAK16genetic
27708008
UPPS_YEASTNUS1genetic
27708008
SEC31_YEASTSEC31genetic
27708008
SC61G_YEASTSSS1genetic
27708008
RRP1_YEASTRRP1genetic
27708008
NCS1_YEASTFRQ1genetic
27708008
GPI19_YEASTGPI19genetic
27708008
MOB2_YEASTMOB2genetic
27708008
SAD1_YEASTSAD1genetic
27708008
STT3_YEASTSTT3genetic
27708008
NNF1_YEASTNNF1genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
RRP8_YEASTRRP8genetic
27708008
RM01_YEASTMRPL1genetic
27708008
ATC1_YEASTPMR1genetic
27708008
HUR1_YEASTHUR1genetic
27708008
ADH4_YEASTADH4genetic
27708008
PTH_YEASTPTH1genetic
27708008
FLX1_YEASTFLX1genetic
27708008
YL278_YEASTYLR278Cgenetic
27708008
LIPA_YEASTLIP5genetic
27708008
ARL3_YEASTARL3genetic
27708008
LGE1_YEASTLGE1genetic
27708008
COX10_YEASTCOX10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YP091_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-621; SER-622; SER-640;SER-669; SER-676; SER-714; SER-717; SER-720 AND SER-723, 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 SER-622; SER-640; SER-669AND SER-676, 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-640 AND SER-669, 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-640; SER-669; SER-720AND SER-723, AND MASS SPECTROMETRY.
"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-669 AND SER-676, ANDMASS SPECTROMETRY.

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