ENOA_RAT - dbPTM
ENOA_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENOA_RAT
UniProt AC P04764
Protein Name Alpha-enolase
Gene Name Eno1
Organism Rattus norvegicus (Rat).
Sequence Length 434
Subcellular Localization Cytoplasm. Cell membrane. Can translocate to the plasma membrane in either the homodimeric (alpha/alpha) or heterodimeric (alpha/gamma) form.
Protein Description Multifunctional enzyme that, as well as its role in glycolysis, plays a part in various processes such as growth control, hypoxia tolerance and allergic responses. May also function in the intravascular and pericellular fibrinolytic system due to its ability to serve as a receptor and activator of plasminogen on the cell surface of several cell-types such as leukocytes and neurons. Stimulates immunoglobulin production..
Protein Sequence MSILKIHAREIFDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDNDKTRFMGKGVSKAVEHINKTIAPALVSKKLNVVEQEKIDQLMIEMDGTENKSKFGANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNPEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEALELLKSAIAKAGYTDQVVIGMDVAASEFYRAGKYDLDFKSPDDASRYITPDQLADLYKSFIKDYPVVSIEDPFDQDDWDAWQKFTATAGIQVVGDDLTVTNPKRIAKAAGEKSCNCLLLKVNQIGSVTESLQACKLAQSNGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQILRIEEELGSKAKFAGRSFRNPLAK
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
2Acetylation------MSILKIHAR
------CCCEEEEEH
36.31-
5Acetylation---MSILKIHAREIF
---CCCEEEEEHHHH
30.6722902405
25PhosphorylationPTVEVDLYTAKGLFR
CEEEEEEEECCCHHH
10.5322108457
26PhosphorylationTVEVDLYTAKGLFRA
EEEEEEEECCCHHHH
29.2322673903
37PhosphorylationLFRAAVPSGASTGIY
HHHHHCCCCCCCCHH
40.1522108457
40PhosphorylationAAVPSGASTGIYEAL
HHCCCCCCCCHHHHH
30.6021738781
41PhosphorylationAVPSGASTGIYEALE
HCCCCCCCCHHHHHH
27.3722108457
44PhosphorylationSGASTGIYEALELRD
CCCCCCHHHHHHCCC
9.1129779826
54AcetylationLELRDNDKTRFMGKG
HHCCCCCCCCCCCHH
48.1022902405
60AcetylationDKTRFMGKGVSKAVE
CCCCCCCHHHHHHHH
44.3312016721
60SuccinylationDKTRFMGKGVSKAVE
CCCCCCCHHHHHHHH
44.33-
60SuccinylationDKTRFMGKGVSKAVE
CCCCCCCHHHHHHHH
44.33-
64UbiquitinationFMGKGVSKAVEHINK
CCCHHHHHHHHHHHH
54.79-
64AcetylationFMGKGVSKAVEHINK
CCCHHHHHHHHHHHH
54.7922902405
71AcetylationKAVEHINKTIAPALV
HHHHHHHHCHHHHHH
40.4822902405
79PhosphorylationTIAPALVSKKLNVVE
CHHHHHHHHCCCCCC
25.5629779826
80AcetylationIAPALVSKKLNVVEQ
HHHHHHHHCCCCCCH
54.526590955
81SuccinylationAPALVSKKLNVVEQE
HHHHHHHCCCCCCHH
37.4726843850
81UbiquitinationAPALVSKKLNVVEQE
HHHHHHHCCCCCCHH
37.47-
89SuccinylationLNVVEQEKIDQLMIE
CCCCCHHHHHHHHHC
51.80-
89SuccinylationLNVVEQEKIDQLMIE
CCCCCHHHHHHHHHC
51.80-
89AcetylationLNVVEQEKIDQLMIE
CCCCCHHHHHHHHHC
51.8022902405
126AcetylationCKAGAVEKGVPLYRH
HHHCHHHCCCCCHHH
59.62-
131NitrationVEKGVPLYRHIADLA
HHCCCCCHHHHHHHC
8.28-
157PhosphorylationFNVINGGSHAGNKLA
EEEECCCCCCCCCHH
16.1527097102
176PhosphorylationMILPVGASSFREAMR
EEECCCHHHHHHHHH
24.8725403869
177PhosphorylationILPVGASSFREAMRI
EECCCHHHHHHHHHH
27.9925403869
193AcetylationAEVYHNLKNVIKEKY
HHHHHHHHHHHHHHH
55.2622902405
197AcetylationHNLKNVIKEKYGKDA
HHHHHHHHHHHCCCC
43.8222902405
199AcetylationLKNVIKEKYGKDATN
HHHHHHHHHCCCCCC
55.0622902405
202UbiquitinationVIKEKYGKDATNVGD
HHHHHHCCCCCCCCC
40.89-
202AcetylationVIKEKYGKDATNVGD
HHHHHHCCCCCCCCC
40.8922902405
205PhosphorylationEKYGKDATNVGDEGG
HHHCCCCCCCCCCCC
40.3422673903
221AcetylationAPNILENKEALELLK
CCCHHCCHHHHHHHH
34.6822902405
228SuccinylationKEALELLKSAIAKAG
HHHHHHHHHHHHHCC
50.93-
228OtherKEALELLKSAIAKAG
HHHHHHHHHHHHHCC
50.93-
228SuccinylationKEALELLKSAIAKAG
HHHHHHHHHHHHHCC
50.93-
228AcetylationKEALELLKSAIAKAG
HHHHHHHHHHHHHCC
50.9322902405
229PhosphorylationEALELLKSAIAKAGY
HHHHHHHHHHHHCCC
25.5228432305
233N6-malonyllysineLLKSAIAKAGYTDQV
HHHHHHHHCCCCCEE
35.91-
233AcetylationLLKSAIAKAGYTDQV
HHHHHHHHCCCCCEE
35.91-
233MalonylationLLKSAIAKAGYTDQV
HHHHHHHHCCCCCEE
35.91-
236NitrationSAIAKAGYTDQVVIG
HHHHHCCCCCEEEEC
16.41-
256AcetylationSEFYRAGKYDLDFKS
HHHHHCCCCCCCCCC
34.3122902405
257NitrationEFYRAGKYDLDFKSP
HHHHCCCCCCCCCCC
22.33-
257PhosphorylationEFYRAGKYDLDFKSP
HHHHCCCCCCCCCCC
22.3328551015
262AcetylationGKYDLDFKSPDDASR
CCCCCCCCCCCCHHH
61.8226302492
263PhosphorylationKYDLDFKSPDDASRY
CCCCCCCCCCCHHHC
33.2930411139
268PhosphorylationFKSPDDASRYITPDQ
CCCCCCHHHCCCHHH
32.3928551015
270PhosphorylationSPDDASRYITPDQLA
CCCCHHHCCCHHHHH
13.4728432305
272PhosphorylationDDASRYITPDQLADL
CCHHHCCCHHHHHHH
16.3322108457
281AcetylationDQLADLYKSFIKDYP
HHHHHHHHHHHCCCC
46.3022902405
281OtherDQLADLYKSFIKDYP
HHHHHHHHHHHCCCC
46.30-
282PhosphorylationQLADLYKSFIKDYPV
HHHHHHHHHHCCCCE
20.7428432305
285AcetylationDLYKSFIKDYPVVSI
HHHHHHHCCCCEEEC
49.55-
287PhosphorylationYKSFIKDYPVVSIED
HHHHHCCCCEEECCC
7.91-
291PhosphorylationIKDYPVVSIEDPFDQ
HCCCCEEECCCCCCC
22.09-
330UbiquitinationTNPKRIAKAAGEKSC
CCHHHHHHHCCCCCC
36.08-
335AcetylationIAKAAGEKSCNCLLL
HHHHCCCCCCCEEEE
60.43-
343AcetylationSCNCLLLKVNQIGSV
CCCEEEEEHHHCCCH
38.8225786129
362PhosphorylationQACKLAQSNGWGVMV
HHHHHHHHCCCEEEE
31.5322673903
373PhosphorylationGVMVSHRSGETEDTF
EEEEECCCCCCCCCH
35.2422673903
406AcetylationCRSERLAKYNQILRI
CCHHHHHHHHHHHHH
49.692915851
419PhosphorylationRIEEELGSKAKFAGR
HHHHHHHHCHHHCCC
41.9029779826
420UbiquitinationIEEELGSKAKFAGRS
HHHHHHHCHHHCCCC
54.52-
420SuccinylationIEEELGSKAKFAGRS
HHHHHHHCHHHCCCC
54.52-
420MalonylationIEEELGSKAKFAGRS
HHHHHHHCHHHCCCC
54.52-
420AcetylationIEEELGSKAKFAGRS
HHHHHHHCHHHCCCC
54.5222902405
420N6-malonyllysineIEEELGSKAKFAGRS
HHHHHHHCHHHCCCC
54.52-

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 ENOA_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENOA_RAT !!

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 ENOA_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ENOA_RAT !!

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

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Related Literatures of Post-Translational Modification

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