ENOG_MOUSE - dbPTM
ENOG_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENOG_MOUSE
UniProt AC P17183
Protein Name Gamma-enolase
Gene Name Eno2
Organism Mus musculus (Mouse).
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 Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity)..
Protein Sequence MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSRIAPALISSGISVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERDLPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKMVIGMDVAASEFYRDGKYDLDFKSPADPSRYITGDQLGALYQDFVRNYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
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------MSIEKIWAR
------CCHHHHHHH		39.18-
2Phosphorylation------MSIEKIWAR
------CCHHHHHHH		39.1822324799
5Acetylation---MSIEKIWAREIL
---CCHHHHHHHHHH		41.71-
14PhosphorylationWAREILDSRGNPTVE
HHHHHHHCCCCCEEE		38.3528059163
19PhosphorylationLDSRGNPTVEVDLYT
HHCCCCCEEEEEEEE		33.0425367039
25PhosphorylationPTVEVDLYTAKGLFR
CEEEEEEEECCCHHH		10.5325177544
26PhosphorylationTVEVDLYTAKGLFRA
EEEEEEEECCCHHHH		29.2325266776
28AcetylationEVDLYTAKGLFRAAV
EEEEEECCCHHHHHC		48.63-
28UbiquitinationEVDLYTAKGLFRAAV
EEEEEECCCHHHHHC		48.63-
37PhosphorylationLFRAAVPSGASTGIY
HHHHHCCCCCCCCHH		40.1528542873
40PhosphorylationAAVPSGASTGIYEAL
HHCCCCCCCCHHHHH		30.6025521595
41PhosphorylationAVPSGASTGIYEALE
HCCCCCCCCHHHHHH		27.3725521595
44NitrationSGASTGIYEALELRD
CCCCCCHHHHHHCCC		9.11-
44PhosphorylationSGASTGIYEALELRD
CCCCCCHHHHHHCCC		9.1125177544
54UbiquitinationLELRDGDKQRYLGKG
HHCCCCCCHHHCCCH		42.0522790023
60AcetylationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.1624062335
60UbiquitinationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.16-
60SuccinylationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.16-
64UbiquitinationYLGKGVLKAVDHINS
HCCCHHHHHHHHCHH		43.9122790023
64AcetylationYLGKGVLKAVDHINS
HCCCHHHHHHHHCHH		43.91-
71PhosphorylationKAVDHINSRIAPALI
HHHHHCHHCHHHHHH		25.1829899451
79PhosphorylationRIAPALISSGISVVE
CHHHHHHHCCCEEEE		24.3022817900
80PhosphorylationIAPALISSGISVVEQ
HHHHHHHCCCEEEEH		32.9020415495
83PhosphorylationALISSGISVVEQEKL
HHHHCCCEEEEHHHH		24.52-
89AcetylationISVVEQEKLDNLMLE
CEEEEHHHHHCCEEE		61.92-
89SuccinylationISVVEQEKLDNLMLE
CEEEEHHHHHCCEEE		61.92-
119S-nitrosylationLGVSLAVCKAGAAER
HHHHHHHHHHCHHHC		1.7624895380
141PhosphorylationIAQLAGNSDLILPVP
HHHHHCCCCEEEEEC		32.6429899451
157PhosphorylationFNVINGGSHAGNKLA
EEEECCCCCCCCCHH		16.15-
193AcetylationAEVYHTLKGVIKDKY
HHHHHHHHHHHHHCC		52.89-
193UbiquitinationAEVYHTLKGVIKDKY
HHHHHHHHHHHHHCC		52.8922790023
197AcetylationHTLKGVIKDKYGKDA
HHHHHHHHHCCCCCC		45.8423576753
199AcetylationLKGVIKDKYGKDATN
HHHHHHHCCCCCCCC		51.4023576753
202AcetylationVIKDKYGKDATNVGD
HHHHCCCCCCCCCCC		40.89-
205PhosphorylationDKYGKDATNVGDEGG
HCCCCCCCCCCCCCC		40.34-
221PhosphorylationAPNILENSEALELVK
CCCHHCCHHHHHHHH		18.1829899451
228AcetylationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.79-
228SuccinylationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.79-
228UbiquitinationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.79-
233OtherLVKEAIDKAGYTEKM
HHHHHHHHCCCCCCE		37.28-
233AcetylationLVKEAIDKAGYTEKM
HHHHHHHHCCCCCCE		37.28-
236PhosphorylationEAIDKAGYTEKMVIG
HHHHHCCCCCCEEEC		19.31-
252NitrationDVAASEFYRDGKYDL
EEHHHHHHCCCCCCC		12.07-
256AcetylationSEFYRDGKYDLDFKS
HHHHCCCCCCCCCCC		39.62-
263PhosphorylationKYDLDFKSPADPSRY
CCCCCCCCCCCHHHC		25.8824925903
268PhosphorylationFKSPADPSRYITGDQ
CCCCCCHHHCCCHHH		37.9624925903
270NitrationSPADPSRYITGDQLG
CCCCHHHCCCHHHHH		13.74-
270PhosphorylationSPADPSRYITGDQLG
CCCCHHHCCCHHHHH		13.7429899451
272PhosphorylationADPSRYITGDQLGAL
CCHHHCCCHHHHHHH		26.2729899451
287PhosphorylationYQDFVRNYPVVSIED
HHHHHHHCCEEEECC		6.19-
291PhosphorylationVRNYPVVSIEDPFDQ
HHHCCEEEECCCCCC		22.09-
326AcetylationDLTVTNPKRIERAVE
CCEECCHHHHHHHHH		68.9930985909
335AcetylationIERAVEEKACNCLLL
HHHHHHHHHHCEEEE		44.74-
337S-nitrosylationRAVEEKACNCLLLKV
HHHHHHHHCEEEEEH		5.6824895380
339S-nitrosylationVEEKACNCLLLKVNQ
HHHHHHCEEEEEHHH		2.5924895380
343AcetylationACNCLLLKVNQIGSV
HHCEEEEEHHHCCCH		38.82-
343UbiquitinationACNCLLLKVNQIGSV
HHCEEEEEHHHCCCH		38.82-
357S-nitrosylationVTEAIQACKLAQENG
HHHHHHHHHHHHHHC		1.8124895380
373PhosphorylationGVMVSHRSGETEDTF
EEEEECCCCCCCCCH		35.2422210690
376PhosphorylationVSHRSGETEDTFIAD
EECCCCCCCCCHHHH		42.5622210690
379PhosphorylationRSGETEDTFIADLVV
CCCCCCCCHHHHHHH		15.6528464351
389S-nitrosylationADLVVGLCTGQIKTG
HHHHHHHHCCCCCCC		3.1024895380
394UbiquitinationGLCTGQIKTGAPCRS
HHHCCCCCCCCCCCH		32.78-
406AcetylationCRSERLAKYNQLMRI
CCHHHHHHHHHHHHH		49.69-
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 ENOG_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENOG_MOUSE !!
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 ENOG_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ENOG_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENOG_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative analysis of both protein expression and serine /threonine post-translational modifications through stable isotopelabeling with dithiothreitol.";
Vosseller K., Hansen K.C., Chalkley R.J., Trinidad J.C., Wells L.,Hart G.W., Burlingame A.L.;
Proteomics 5:388-398(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, AND MASSSPECTROMETRY.
"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-25 AND TYR-44, AND MASSSPECTROMETRY.

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