Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Pyruvate kinase 1  

UniProtKB / Swiss-Prot ID :  KPYK1_YEAST

Gene Name (Synonyms) : 
CDC19, PYK1 YAL038W  

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

Subcellular Localization :   

Protein Function :   

Protein Sequence MSRLERLTSLNVVAGSDLRRTSIIGTIGPKTNNPETLVALRKAGLNIVRMNFSHGSYEYHKSVIDNARKS...
Predicted Secondary Structure CCHHHHHHCCCCCCCHHHCCCEEEEEECCCCCCHHHHHHHHHCCCCEEEEECCCCCHHHHHHHHHHHHHH...
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
8PhosphothreonineLERLTSLNV
HHHHHCCCC
37.07SysPTM
Link
8Phosphothreonine.LERLTSLNV
HHHHHCCCC
37.07UniProtKB
Link
9PhosphoserineERLTSLNVV
HHHHCCCCC
23.65SysPTM
Link
9Phosphoserine.ERLTSLNVV
HHHHCCCCC
23.65UniProtKB
Link
16PhosphoserineVVAGSDLRR
CCCCHHHCC
24.59SysPTM
Link
16Phosphoserine.VVAGSDLRR
CCCCHHHCC
24.59UniProtKB
Link
21Phosphothreonine.DLRRTSIIG
HHCCCEEEE
20.17UniProtKB
Link
22PhosphoserineLRRTSIIGT
HCCCEEEEE
15.48SysPTM
Link
22Phosphoserine.LRRTSIIGT
HCCCEEEEE
15.48UniProtKB
Link
26PhosphothreonineSIIGTIGPK
EEEEEECCC
16.62SysPTM
Link
26Phosphothreonine.SIIGTIGPK
EEEEEECCC
16.62UniProtKB
Link
53PhosphoserineRMNFSHGSY
EEECCCCCH
23.18SysPTM
Link
53Phosphoserine.RMNFSHGSY
EEECCCCCH
23.18UniProtKB
Link
56PhosphoserineFSHGSYEYH
CCCCCHHHH
14.90SysPTM
Link
56Phosphoserine.FSHGSYEYH
CCCCCHHHH
14.90UniProtKB
Link
213PhosphoserineMVFASFIRT
EEEEECCCC
15.11SysPTM
Link
213Phosphoserine.MVFASFIRT
EEEEECCCC
15.11UniProtKB
Link
332PhosphoserineCVMLSGETA
EEEEECCCC
19.25SysPTM
Link
332Phosphoserine.CVMLSGETA
EEEEECCCC
19.25UniProtKB
Link
372PhosphothreonineMRNCTPKPT
HHCCCCCCC
37.59SysPTM
Link
372Phosphothreonine.MRNCTPKPT
HHCCCCCCC
37.59UniProtKB
Link
376PhosphothreonineTPKPTSTTE
CCCCCCHHH
44.85SysPTM
Link
377PhosphoserinePKPTSTTET
CCCCCHHHH
41.69SysPTM
Link
385PhosphoserineTVAASAVAA
HHHHHHHHH
17.34SysPTM
Link
402PhosphoserineIIVLSTSGT
EEEEECCCC
15.05SysPTM
Link
402Phosphoserine.IIVLSTSGT
EEEEECCCC
15.05UniProtKB
Link
403PhosphothreonineIVLSTSGTT
EEEECCCCH
27.32SysPTM
Link
403Phosphothreonine.IVLSTSGTT
EEEECCCCH
27.32UniProtKB
Link
407PhosphothreonineTSGTTPRLV
CCCCHHHHH
15.22SysPTM
Link
407Phosphothreonine.TSGTTPRLV
CCCCHHHHH
15.22UniProtKB
Link
450PhosphoserineKEPVSDWTD
CCCCCCCHH
37.84SysPTM
Link
450Phosphoserine.KEPVSDWTD
CCCCCCCHH
37.84UniProtKB
Link
478PhosphothreonineKKGDTYVSI
CCCCEEEEE
34.20SysPTM
Link
478Phosphothreonine.KKGDTYVSI
CCCCEEEEE
34.20UniProtKB
Link
479PhosphotyrosineKGDTYVSIQ
CCCEEEEEE
9.28SysPTM
Link
479Phosphotyrosine.KGDTYVSIQ
CCCEEEEEE
9.28UniProtKB
Link
498PhosphoserineTLQVSTV
EEEEEEC
15.53SysPTM
Link
498Phosphoserine.TLQVSTV
EEEEEEC
15.53UniProtKB
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
"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 THR-8; SER-9; SER-53; SER-56AND SER-213, 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-9; THR-21 AND SER-22,AND MASS SPECTROMETRY.
"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-8; SER-9; SER-16;SER-22; THR-26; SER-53; SER-332; SER-402; THR-403; THR-407; SER-450;THR-478 AND TYR-479, 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-9; SER-22; THR-372;SER-402; THR-478 AND SER-498, AND MASS 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-9; SER-22 AND THR-478,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