Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Inorganic pyrophosphatase  

UniProtKB / Swiss-Prot ID :  IPYR_YEAST

Gene Name (Synonyms) : 
IPP1, PPA, PPA1 YBR011CYBR0202  

Species :  Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). 

Subcellular Localization :  Cytoplasm. 

Protein Function :   

Protein Sequence MTYTTRQIGAKNTLEYKVYIEKDGKPVSAFHDIPLYADKENNIFNMVVEIPRWTNAKLEITKEETLNPII...
Predicted Secondary Structure CEEEEEECCCCCCCCCEEEEECCCEEECCCCCCCCCCCCCCCEEEEEEEECCCCCEEEEEECCCCCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
61Phosphothreonine.KLEITKEET
EEEEECCCC
24.03UniProtKB
Link
65PhosphothreonineTKEETLNPI
ECCCCCCCC
32.69SysPTM
Link
65Phosphothreonine.TKEETLNPI
ECCCCCCCC
32.69UniProtKB
Link
247PhosphothreonineLTNVTLPDT
EEEEEECCC
34.34SysPTM
Link
247Phosphothreonine.LTNVTLPDT
EEEEEECCC
34.34UniProtKB
Link
251PhosphothreonineTLPDTPTYS
EECCCCCCC
18.65SysPTM
Link
251Phosphothreonine.TLPDTPTYS
EECCCCCCC
18.65UniProtKB
Link
253PhosphothreoninePDTPTYSKA
CCCCCCCHH
42.38SysPTM
Link
253Phosphothreonine.PDTPTYSKA
CCCCCCCHH
42.38UniProtKB
Link
255PhosphoserineTPTYSKAAS
CCCCCHHHH
20.49SysPTM
Link
255Phosphoserine.TPTYSKAAS
CCCCCHHHH
20.49UniProtKB
Link
266PhosphoserineIPPASPKAD
CCCCCCCCC
32.48SysPTM
Link
266Phosphoserine.IPPASPKAD
CCCCCCCCC
32.48UniProtKB
Link
286PhosphoserineFISGSV
EEECCC
20.19SysPTM
Link-
286Phosphoserine.FISGSV
EEECCC
20.19UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-251 AND SER-286, 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 THR-251, 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-61 AND SER-266, AND MASSSPECTROMETRY.
"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-65; THR-247; THR-251;THR-253; SER-255 AND SER-266, AND MASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures