ENO2_YEAST - dbPTM
ENO2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENO2_YEAST
UniProt AC P00925
Protein Name Enolase 2
Gene Name ENO2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 437
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDEDKSKWMGKGVMNAVNNVNNVIAAAFVKANLDVKDQKAVDDFLLSLDGTANKSKLGANAILGVSMAAARAAAAEKNVPLYQHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTFAEAMRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDGKVKIGLDCASSEFFKDGKYDLDFKNPESDKSKWLTGVELADMYHSLMKRYPIVSIEDPFAEDDWEAWSHFFKTAGIQIVADDLTVTNPARIATAIEKKAADALLLKVNQIGTLSESIKAAQDSFAANWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEELGDKAVYAGENFHHGDKL
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
7Phosphorylation-MAVSKVYARSVYDS
-CCCCEEEEEECCCC
10.4725521595
10PhosphorylationVSKVYARSVYDSRGN
CCEEEEEECCCCCCC
19.5025521595
12PhosphorylationKVYARSVYDSRGNPT
EEEEEECCCCCCCCE
14.9520377248
14PhosphorylationYARSVYDSRGNPTVE
EEEECCCCCCCCEEE
25.1325752575
19PhosphorylationYDSRGNPTVEVELTT
CCCCCCCEEEEEEEC
33.0420377248
25PhosphorylationPTVEVELTTEKGVFR
CEEEEEEECCCCEEE
21.2819823750
26PhosphorylationTVEVELTTEKGVFRS
EEEEEEECCCCEEEE
48.6119823750
28UbiquitinationEVELTTEKGVFRSIV
EEEEECCCCEEEEEC
59.2824961812
33PhosphorylationTEKGVFRSIVPSGAS
CCCCEEEEECCCCCC
19.2420377248
37PhosphorylationVFRSIVPSGASTGVH
EEEEECCCCCCCCHH
35.7819823750
40PhosphorylationSIVPSGASTGVHEAL
EECCCCCCCCHHHHH
29.2617330950
41PhosphorylationIVPSGASTGVHEALE
ECCCCCCCCHHHHHH
42.5620377248
54AcetylationLEMRDEDKSKWMGKG
HHCCCCCHHHHHCHH
52.4624489116
55PhosphorylationEMRDEDKSKWMGKGV
HCCCCCHHHHHCHHH
43.8228889911
56AcetylationMRDEDKSKWMGKGVM
CCCCCHHHHHCHHHH
47.1124489116
56UbiquitinationMRDEDKSKWMGKGVM
CCCCCHHHHHCHHHH
47.1122817900
60AcetylationDKSKWMGKGVMNAVN
CHHHHHCHHHHHHHH
32.0224489116
60UbiquitinationDKSKWMGKGVMNAVN
CHHHHHCHHHHHHHH
32.0223749301
79AcetylationVIAAAFVKANLDVKD
HHHHHHHHCCCCCCC
25.7124489116
79UbiquitinationVIAAAFVKANLDVKD
HHHHHHHHCCCCCCC
25.7123749301
85AcetylationVKANLDVKDQKAVDD
HHCCCCCCCCHHHHH
54.8524489116
85SuccinylationVKANLDVKDQKAVDD
HHCCCCCCCCHHHHH
54.8523954790
85UbiquitinationVKANLDVKDQKAVDD
HHCCCCCCCCHHHHH
54.8522817900
88AcetylationNLDVKDQKAVDDFLL
CCCCCCCHHHHHHHH
61.5824489116
88SuccinylationNLDVKDQKAVDDFLL
CCCCCCCHHHHHHHH
61.5823954790
88UbiquitinationNLDVKDQKAVDDFLL
CCCCCCCHHHHHHHH
61.5822817900
96PhosphorylationAVDDFLLSLDGTANK
HHHHHHHHCCCCCCH
26.9328152593
100PhosphorylationFLLSLDGTANKSKLG
HHHHCCCCCCHHHCC
27.0728152593
103AcetylationSLDGTANKSKLGANA
HCCCCCCHHHCCHHH
46.64-
103UbiquitinationSLDGTANKSKLGANA
HCCCCCCHHHCCHHH
46.6417644757
104PhosphorylationLDGTANKSKLGANAI
CCCCCCHHHCCHHHH
32.6817563356
105AcetylationDGTANKSKLGANAIL
CCCCCHHHCCHHHHH
53.18-
105UbiquitinationDGTANKSKLGANAIL
CCCCCHHHCCHHHHH
53.1817644757
115PhosphorylationANAILGVSMAAARAA
HHHHHHHHHHHHHHH
10.8220377248
126AcetylationARAAAAEKNVPLYQH
HHHHHHHCCCCHHHH
59.5224489116
126SuccinylationARAAAAEKNVPLYQH
HHHHHHHCCCCHHHH
59.5223954790
126UbiquitinationARAAAAEKNVPLYQH
HHHHHHHCCCCHHHH
59.5217644757
131PhosphorylationAEKNVPLYQHLADLS
HHCCCCHHHHHHHHH
6.4421082442
138PhosphorylationYQHLADLSKSKTSPY
HHHHHHHHCCCCCCC
35.1221440633
139AcetylationQHLADLSKSKTSPYV
HHHHHHHCCCCCCCE
64.3724489116
139SuccinylationQHLADLSKSKTSPYV
HHHHHHHCCCCCCCE
64.3723954790
139UbiquitinationQHLADLSKSKTSPYV
HHHHHHHCCCCCCCE
64.3717644757
141UbiquitinationLADLSKSKTSPYVLP
HHHHHCCCCCCCEEC
57.6815699485
143PhosphorylationDLSKSKTSPYVLPVP
HHHCCCCCCCEECCC
20.2628889911
159PhosphorylationLNVLNGGSHAGGALA
EEECCCCCCCHHHHH
16.1525521595
178UbiquitinationMIAPTGAKTFAEAMR
CCCCCCHHHHHHHHH
45.5815699485
179PhosphorylationIAPTGAKTFAEAMRI
CCCCCHHHHHHHHHH
27.7821440633
188PhosphorylationAEAMRIGSEVYHNLK
HHHHHHCHHHHHHHH
22.8617330950
191PhosphorylationMRIGSEVYHNLKSLT
HHHCHHHHHHHHHHC
4.8625521595
195UbiquitinationSEVYHNLKSLTKKRY
HHHHHHHHHHCHHCC
49.0523749301
196PhosphorylationEVYHNLKSLTKKRYG
HHHHHHHHHCHHCCC
44.4221440633
198PhosphorylationYHNLKSLTKKRYGAS
HHHHHHHCHHCCCCC
41.4328889911
199UbiquitinationHNLKSLTKKRYGASA
HHHHHHCHHCCCCCC
40.3122817900
200UbiquitinationNLKSLTKKRYGASAG
HHHHHCHHCCCCCCC
45.6922817900
205PhosphorylationTKKRYGASAGNVGDE
CHHCCCCCCCCCCCC
32.1420377248
221PhosphorylationGVAPNIQTAEEALDL
CCCCCCCCHHHHHHH
32.0417287358
234UbiquitinationDLIVDAIKAAGHDGK
HHHHHHHHHCCCCCC
33.6323749301
241AcetylationKAAGHDGKVKIGLDC
HHCCCCCCEEEEEEC
46.5425381059
241UbiquitinationKAAGHDGKVKIGLDC
HHCCCCCCEEEEEEC
46.5422817900
243AcetylationAGHDGKVKIGLDCAS
CCCCCCEEEEEECCC
34.2424489116
243UbiquitinationAGHDGKVKIGLDCAS
CCCCCCEEEEEECCC
34.2423749301
250PhosphorylationKIGLDCASSEFFKDG
EEEEECCCCHHHHCC
36.4117330950
251PhosphorylationIGLDCASSEFFKDGK
EEEECCCCHHHHCCC
21.6520377248
255UbiquitinationCASSEFFKDGKYDLD
CCCCHHHHCCCCCCC
71.5323749301
258AcetylationSEFFKDGKYDLDFKN
CHHHHCCCCCCCCCC
45.80-
258UbiquitinationSEFFKDGKYDLDFKN
CHHHHCCCCCCCCCC
45.8017644757
259PhosphorylationEFFKDGKYDLDFKNP
HHHHCCCCCCCCCCC
27.5421440633
264AcetylationGKYDLDFKNPESDKS
CCCCCCCCCCCCCHH
71.8624489116
264SuccinylationGKYDLDFKNPESDKS
CCCCCCCCCCCCCHH
71.8623954790
264UbiquitinationGKYDLDFKNPESDKS
CCCCCCCCCCCCCHH
71.8617644757
268PhosphorylationLDFKNPESDKSKWLT
CCCCCCCCCHHHCCC
52.1528889911
270AcetylationFKNPESDKSKWLTGV
CCCCCCCHHHCCCHH
64.3124489116
270UbiquitinationFKNPESDKSKWLTGV
CCCCCCCHHHCCCHH
64.3117644757
272AcetylationNPESDKSKWLTGVEL
CCCCCHHHCCCHHHH
52.5424489116
275PhosphorylationSDKSKWLTGVELADM
CCHHHCCCHHHHHHH
37.7621440633
283PhosphorylationGVELADMYHSLMKRY
HHHHHHHHHHHHHHC
6.7121440633
285PhosphorylationELADMYHSLMKRYPI
HHHHHHHHHHHHCCE
16.8121440633
288AcetylationDMYHSLMKRYPIVSI
HHHHHHHHHCCEEEE
54.8224489116
288UbiquitinationDMYHSLMKRYPIVSI
HHHHHHHHHCCEEEE
54.8223749301
308PhosphorylationEDDWEAWSHFFKTAG
CCCHHHHHHHHHHCC
19.9124961812
312UbiquitinationEAWSHFFKTAGIQIV
HHHHHHHHHCCCEEE
36.2017644757
313PhosphorylationAWSHFFKTAGIQIVA
HHHHHHHHCCCEEEE
25.5921440633
324PhosphorylationQIVADDLTVTNPARI
EEEECCCCCCCHHHH
32.0721440633
326PhosphorylationVADDLTVTNPARIAT
EECCCCCCCHHHHHH
30.1928889911
333PhosphorylationTNPARIATAIEKKAA
CCHHHHHHHHHHHHH
26.2923749301
337UbiquitinationRIATAIEKKAADALL
HHHHHHHHHHHHHHH
41.4123749301
338UbiquitinationIATAIEKKAADALLL
HHHHHHHHHHHHHHH
35.7023749301
346UbiquitinationAADALLLKVNQIGTL
HHHHHHHHHHHHCCH
38.8223749301
352PhosphorylationLKVNQIGTLSESIKA
HHHHHHCCHHHHHHH
28.8328152593
354PhosphorylationVNQIGTLSESIKAAQ
HHHHCCHHHHHHHHH
29.1828152593
356PhosphorylationQIGTLSESIKAAQDS
HHCCHHHHHHHHHHH
26.4728152593
358UbiquitinationGTLSESIKAAQDSFA
CCHHHHHHHHHHHHH
47.1223749301
373PhosphorylationANWGVMVSHRSGETE
HCCEEEEECCCCCCC
8.6217287358
376PhosphorylationGVMVSHRSGETEDTF
EEEEECCCCCCCCCE
35.2424909858
379PhosphorylationVSHRSGETEDTFIAD
EECCCCCCCCCEEEH
42.5628889911
397UbiquitinationGLRTGQIKTGAPARS
HHCCCCCCCCCCCHH
32.7823749301
398PhosphorylationLRTGQIKTGAPARSE
HCCCCCCCCCCCHHH
39.9623749301
404PhosphorylationKTGAPARSERLAKLN
CCCCCCHHHHHHHHH
29.2225521595
409UbiquitinationARSERLAKLNQLLRI
CHHHHHHHHHHHHHH
53.1923749301
423AcetylationIEEELGDKAVYAGEN
HHHHHCCCEEECCCC
37.6424489116
423SuccinylationIEEELGDKAVYAGEN
HHHHHCCCEEECCCC
37.6423954790
423UbiquitinationIEEELGDKAVYAGEN
HHHHHCCCEEECCCC
37.6423749301
426PhosphorylationELGDKAVYAGENFHH
HHCCCEEECCCCCCC
17.4721082442
436AcetylationENFHHGDKL------
CCCCCCCCC------
61.77-
436UbiquitinationENFHHGDKL------
CCCCCCCCC------
61.7717644757

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 ENO2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENO2_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 ENO2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SSB1_YEASTSSB1physical
19536198
ENO1_YEASTENO1genetic
18408719
ERR1_YEASTERR1genetic
16941010
ERR2_YEASTERR1genetic
16941010
SEO1_YEASTSEO1genetic
20093466
CALX_YEASTCNE1genetic
20093466
HSP71_YEASTSSA1genetic
20093466
KMO_YEASTBNA4genetic
20093466
RS8A_YEASTRPS8Agenetic
20093466
RS8B_YEASTRPS8Agenetic
20093466
SHE1_YEASTSHE1genetic
20093466
QOR_YEASTZTA1genetic
20093466
TEC1_YEASTTEC1genetic
20093466
RU1A_YEASTMUD1genetic
20093466
MRC1_YEASTMRC1genetic
20093466
MGR1_YEASTMGR1genetic
20093466
FRM2_YEASTFRM2genetic
20093466
YD218_YEASTYDL218Wgenetic
20093466
THI3_YEASTTHI3genetic
20093466
PP4C_YEASTPPH3genetic
20093466
SWF1_YEASTSWF1genetic
20093466
HEL2_YEASTHEL2genetic
20093466
SNX41_YEASTSNX41genetic
20093466
FIT1_YEASTFIT1genetic
20093466
UBP5_YEASTUBP5genetic
20093466
UBP3_YEASTUBP3genetic
20093466
SPT2_YEASTSPT2genetic
20093466
RTG2_YEASTRTG2genetic
20093466
CLG1_YEASTCLG1genetic
20093466
DBF2_YEASTDBF2genetic
20093466
DRN1_YEASTDRN1genetic
20093466
ASK10_YEASTASK10genetic
20093466
ENO1_YEASTENO1genetic
20093466
RS21B_YEASTRPS21Bgenetic
20093466
PBS2_YEASTPBS2genetic
20093466
IML2_YEASTIML2genetic
20093466
DPOD3_YEASTPOL32genetic
20093466
NAP1_YEASTNAP1genetic
20093466
HOG1_YEASTHOG1genetic
20093466
LEUR_YEASTLEU3genetic
20093466
SUB1_YEASTSUB1genetic
20093466
IOC4_YEASTIOC4genetic
20093466
CSM3_YEASTCSM3genetic
20093466
MOT3_YEASTMOT3genetic
20093466
ROY1_YEASTROY1genetic
20093466
LSM7_YEASTLSM7genetic
20093466
CPT1_YEASTCPT1genetic
20093466
PHO23_YEASTPHO23genetic
20093466
EOS1_YEASTEOS1genetic
20093466
BRE5_YEASTBRE5genetic
20093466
HPF1_YEASTHPF1genetic
20093466
TRM10_YEASTTRM10genetic
20093466
ADH1_YEASTADH1genetic
20093466
IRA2_YEASTIRA2genetic
20093466
RTG1_YEASTRTG1genetic
20093466
CSK2C_YEASTCKB2genetic
20093466
ASE1_YEASTASE1genetic
20093466
ELG1_YEASTELG1genetic
20093466
FABD_YEASTMCT1genetic
20093466
PALA_YEASTRIM20genetic
20093466
TYE7_YEASTTYE7genetic
20093466
GPB1_YEASTGPB1genetic
20093466
NEW1_YEASTNEW1genetic
20093466
ELP3_YEASTELP3genetic
20093466
GGPPS_YEASTBTS1genetic
20093466
CTF19_YEASTCTF19genetic
20093466
ROX1_YEASTROX1genetic
20093466
PHSG_YEASTGPH1genetic
20093466
ENO2_YEASTENO2physical
15373835
ERR3_YEASTERR3genetic
23359425
HOG1_YEASTHOG1genetic
22282571
PBS2_YEASTPBS2genetic
22282571
YL224_YEASTYLR224Wphysical
26297823
ASK10_YEASTASK10genetic
27708008
SIN3_YEASTSIN3genetic
27708008
RU1A_YEASTMUD1genetic
27708008
MRC1_YEASTMRC1genetic
27708008
THI3_YEASTTHI3genetic
27708008
PP4C_YEASTPPH3genetic
27708008
SWF1_YEASTSWF1genetic
27708008
HEL2_YEASTHEL2genetic
27708008
UBP5_YEASTUBP5genetic
27708008
UBP3_YEASTUBP3genetic
27708008
MRM2_YEASTMRM2genetic
27708008
ENO1_YEASTENO1genetic
27708008
PBS2_YEASTPBS2genetic
27708008
RS21B_YEASTRPS21Bgenetic
27708008
DPOD3_YEASTPOL32genetic
27708008
HOG1_YEASTHOG1genetic
27708008
ORM2_YEASTORM2genetic
27708008
SUB1_YEASTSUB1genetic
27708008
CSM3_YEASTCSM3genetic
27708008
MOT3_YEASTMOT3genetic
27708008
BRE5_YEASTBRE5genetic
27708008
RTG1_YEASTRTG1genetic
27708008
ELG1_YEASTELG1genetic
27708008
LIPA_YEASTLIP5genetic
27708008
FABD_YEASTMCT1genetic
27708008
TYE7_YEASTTYE7genetic
27708008
GGPPS_YEASTBTS1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENO2_YEAST

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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 SER-40; SER-188; SER-205;THR-221 AND SER-373, 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-10 AND SER-188, AND MASSSPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, 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-324 AND THR-326, ANDMASS SPECTROMETRY.

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