CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001834
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Enolase 1 
Protein Synonyms/Alias
 2-phospho-D-glycerate hydro-lyase 1; 2-phosphoglycerate dehydratase 1 
Gene Name
 ENO1 
Gene Synonyms/Alias
 ENOA; HSP48; YGR254W; G9160 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
5***MAVSKVYARSVYacetylation[1]
28EVELTTEKGVFRSIVacetylation[1]
60DKSKWMGKGVLHAVKacetylation[1]
60DKSKWMGKGVLHAVKubiquitination[2]
67KGVLHAVKNVNDVIAacetylation[1]
79VIAPAFVKANIDVKDacetylation[1]
85VKANIDVKDQKAVDDubiquitination[2]
88NIDVKDQKAVDDFLIubiquitination[2]
126SRAAAAEKNVPLYKHacetylation[1]
132EKNVPLYKHLADLSKacetylation[1]
132EKNVPLYKHLADLSKubiquitination[2]
139KHLADLSKSKTSPYVacetylation[1]
195SEVYHNLKSLTKKRYacetylation[1]
195SEVYHNLKSLTKKRYubiquitination[2, 3]
234DLIVDAIKAAGHDGKubiquitination[2]
255CASSEFFKDGKYDLDacetylation[1]
255CASSEFFKDGKYDLDubiquitination[2]
258SEFFKDGKYDLDFKNacetylation[1]
264GKYDLDFKNPNSDKSacetylation[1]
329DLTVTNPKRIATAIEacetylation[1]
337RIATAIEKKAADALLacetylation[1]
337RIATAIEKKAADALLubiquitination[2]
338IATAIEKKAADALLLacetylation[1]
338IATAIEKKAADALLLubiquitination[2]
346AADALLLKVNQIGTLacetylation[1]
346AADALLLKVNQIGTLubiquitination[2, 3]
358GTLSESIKAAQDSFAubiquitination[2, 3]
397GLRTGQIKTGAPARSacetylation[1]
397GLRTGQIKTGAPARSubiquitination[2]
409ARSERLAKLNQLLRIacetylation[1]
409ARSERLAKLNQLLRIubiquitination[2]
436ENFHHGDKL******acetylation[1]
Reference
 [1] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919]
 [2] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, VillĂ©n J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [3] Sites of ubiquitin attachment in Saccharomyces cerevisiae.
 Starita LM, Lo RS, Eng JK, von Haller PD, Fields S.
 Proteomics. 2012 Jan;12(2):236-40. [PMID: 22106047
Functional Description
  
Sequence Annotation
 REGION 373 376 Substrate binding.
 ACT_SITE 212 212 Proton donor (Probable).
 ACT_SITE 346 346 Proton acceptor.
 METAL 247 247 Magnesium.
 METAL 296 296 Magnesium.
 METAL 321 321 Magnesium.
 BINDING 160 160 Substrate.
 BINDING 169 169 Substrate.
 BINDING 296 296 Substrate.
 BINDING 321 321 Substrate.
 BINDING 397 397 Substrate.
 MOD_RES 96 96 Phosphoserine.
 MOD_RES 104 104 Phosphoserine.
 MOD_RES 119 119 Phosphoserine.
 MOD_RES 138 138 Phosphoserine (By similarity).
 MOD_RES 188 188 Phosphoserine (By similarity).
 MOD_RES 313 313 Phosphothreonine (By similarity).
 MOD_RES 324 324 Phosphothreonine (By similarity).  
Keyword
 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Glycolysis; Lyase; Magnesium; Metal-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 437 AA 
Protein Sequence
MAVSKVYARS VYDSRGNPTV EVELTTEKGV FRSIVPSGAS TGVHEALEMR DGDKSKWMGK 60
GVLHAVKNVN DVIAPAFVKA NIDVKDQKAV DDFLISLDGT ANKSKLGANA ILGVSLAASR 120
AAAAEKNVPL YKHLADLSKS KTSPYVLPVP FLNVLNGGSH AGGALALQEF MIAPTGAKTF 180
AEALRIGSEV YHNLKSLTKK RYGASAGNVG DEGGVAPNIQ TAEEALDLIV DAIKAAGHDG 240
KIKIGLDCAS SEFFKDGKYD LDFKNPNSDK SKWLTGPQLA DLYHSLMKRY PIVSIEDPFA 300
EDDWEAWSHF FKTAGIQIVA DDLTVTNPKR IATAIEKKAA DALLLKVNQI GTLSESIKAA 360
QDSFAAGWGV MVSHRSGETE DTFIADLVVG LRTGQIKTGA PARSERLAKL NQLLRIEEEL 420
GDNAVFAGEN FHHGDKL 437 
Gene Ontology
 GO:0000324; C:fungal-type vacuole; IDA:SGD.
 GO:0005739; C:mitochondrion; IDA:SGD.
 GO:0000015; C:phosphopyruvate hydratase complex; IDA:SGD.
 GO:0005886; C:plasma membrane; IDA:SGD.
 GO:0000287; F:magnesium ion binding; IEA:InterPro.
 GO:0004634; F:phosphopyruvate hydratase activity; IMP:SGD.
 GO:0006094; P:gluconeogenesis; IEP:SGD.
 GO:0006096; P:glycolysis; IMP:SGD.
 GO:0032889; P:regulation of vacuole fusion, non-autophagic; IDA:SGD. 
Interpro
 IPR000941; Enolase.
 IPR020810; Enolase_C.
 IPR020809; Enolase_CS.
 IPR020811; Enolase_N. 
Pfam
 PF00113; Enolase_C
 PF03952; Enolase_N 
SMART
  
PROSITE
 PS00164; ENOLASE 
PRINTS
 PR00148; ENOLASE.