ENOG_HUMAN - dbPTM
ENOG_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ENOG_HUMAN
UniProt AC P09104
Protein Name Gamma-enolase
Gene Name ENO2
Organism Homo sapiens (Human).
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 MSIEKIWAREILDSRGNPTVEVDLYTAKGLFRAAVPSGASTGIYEALELRDGDKQRYLGKGVLKAVDHINSTIAPALISSGLSVVEQEKLDNLMLELDGTENKSKFGANAILGVSLAVCKAGAAERELPLYRHIAQLAGNSDLILPVPAFNVINGGSHAGNKLAMQEFMILPVGAESFRDAMRLGAEVYHTLKGVIKDKYGKDATNVGDEGGFAPNILENSEALELVKEAIDKAGYTEKIVIGMDVAASEFYRDGKYDLDFKSPTDPSRYITGDQLGALYQDFVRDYPVVSIEDPFDQDDWAAWSKFTANVGIQIVGDDLTVTNPKRIERAVEEKACNCLLLKVNQIGSVTEAIQACKLAQENGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEELGDEARFAGHNFRNPSVL
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-
5Ubiquitination---MSIEKIWAREIL
---CCHHHHHHHHHH		41.71-
5Acetylation---MSIEKIWAREIL
---CCHHHHHHHHHH		41.71-
5Ubiquitination---MSIEKIWAREIL
---CCHHHHHHHHHH		41.71-
19PhosphorylationLDSRGNPTVEVDLYT
HHCCCCCEEEEEEEE		33.0428060719
25PhosphorylationPTVEVDLYTAKGLFR
CEEEEEEEECCCHHH		10.5321082442
26PhosphorylationTVEVDLYTAKGLFRA
EEEEEEEECCCHHHH		29.2320068231
28UbiquitinationEVDLYTAKGLFRAAV
EEEEEECCCHHHHHC		48.63-
28UbiquitinationEVDLYTAKGLFRAAV
EEEEEECCCHHHHHC		48.63-
37PhosphorylationLFRAAVPSGASTGIY
HHHHHCCCCCCCCHH		40.1521945579
40PhosphorylationAAVPSGASTGIYEAL
HHCCCCCCCCHHHHH		30.6029255136
41PhosphorylationAVPSGASTGIYEALE
HCCCCCCCCHHHHHH		27.3721945579
44PhosphorylationSGASTGIYEALELRD
CCCCCCHHHHHHCCC		9.1129255136
50MethylationIYEALELRDGDKQRY
HHHHHHCCCCCCHHH		36.17-
57PhosphorylationRDGDKQRYLGKGVLK
CCCCCHHHCCCHHHH		19.8128387310
60SuccinylationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.16-
60AcetylationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.16-
60UbiquitinationDKQRYLGKGVLKAVD
CCHHHCCCHHHHHHH		43.16-
64AcetylationYLGKGVLKAVDHINS
HCCCHHHHHHHHCCC		43.91-
71PhosphorylationKAVDHINSTIAPALI
HHHHHCCCCHHHHHH		22.1628387310
72PhosphorylationAVDHINSTIAPALIS
HHHHCCCCHHHHHHH		19.37-
79PhosphorylationTIAPALISSGLSVVE
CHHHHHHHCCCCCCC		21.1428387310
80PhosphorylationIAPALISSGLSVVEQ
HHHHHHHCCCCCCCH		36.4421082442
83PhosphorylationALISSGLSVVEQEKL
HHHHCCCCCCCHHHH		27.87-
89SuccinylationLSVVEQEKLDNLMLE
CCCCCHHHHHCCEEE		61.92-
89UbiquitinationLSVVEQEKLDNLMLE
CCCCCHHHHHCCEEE		61.92-
89AcetylationLSVVEQEKLDNLMLE
CCCCCHHHHHCCEEE		61.92-
94SulfoxidationQEKLDNLMLELDGTE
HHHHHCCEEEECCCC		3.2421406390
104PhosphorylationLDGTENKSKFGANAI
ECCCCCCHHHCHHHH		44.81-
105UbiquitinationDGTENKSKFGANAIL
CCCCCCHHHCHHHHH		49.80-
115PhosphorylationANAILGVSLAVCKAG
HHHHHHHHHHHHHHC		14.60-
120UbiquitinationGVSLAVCKAGAAERE
HHHHHHHHHCHHHCC		43.17-
131PhosphorylationAERELPLYRHIAQLA
HHCCCCHHHHHHHHH		9.75-
150UbiquitinationLILPVPAFNVINGGS
EEEEECCEEEECCCC		6.50-
156UbiquitinationAFNVINGGSHAGNKL
CEEEECCCCCCCCCH		16.27-
157PhosphorylationFNVINGGSHAGNKLA
EEEECCCCCCCCCHH		16.1525850435
159AcetylationVINGGSHAGNKLAMQ
EECCCCCCCCCHHCC		25.58-
189PhosphorylationMRLGAEVYHTLKGVI
HHHCHHHHHHHHHHH		4.8027642862
193UbiquitinationAEVYHTLKGVIKDKY
HHHHHHHHHHHHHCC		52.89-
193AcetylationAEVYHTLKGVIKDKY
HHHHHHHHHHHHHCC		52.8920167786
197UbiquitinationHTLKGVIKDKYGKDA
HHHHHHHHHCCCCCC		45.84-
197AcetylationHTLKGVIKDKYGKDA
HHHHHHHHHCCCCCC		45.8420167786
199UbiquitinationLKGVIKDKYGKDATN
HHHHHHHCCCCCCCC		51.40-
199AcetylationLKGVIKDKYGKDATN
HHHHHHHCCCCCCCC		51.40-
202UbiquitinationVIKDKYGKDATNVGD
HHHHCCCCCCCCCCC		40.89-
202AcetylationVIKDKYGKDATNVGD
HHHHCCCCCCCCCCC		40.8923236377
205PhosphorylationDKYGKDATNVGDEGG
HCCCCCCCCCCCCCC		40.34-
213UbiquitinationNVGDEGGFAPNILEN
CCCCCCCCCCCHHCC		17.55-
219UbiquitinationGFAPNILENSEALEL
CCCCCHHCCHHHHHH		55.71-
228UbiquitinationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.79-
228AcetylationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.797851157
228SuccinylationSEALELVKEAIDKAG
HHHHHHHHHHHHHCC		54.79-
233OtherLVKEAIDKAGYTEKI
HHHHHHHHCCCCEEE		37.2829775581
233AcetylationLVKEAIDKAGYTEKI
HHHHHHHHCCCCEEE		37.2825953088
236PhosphorylationEAIDKAGYTEKIVIG
HHHHHCCCCEEEEEC		19.31-
244SulfoxidationTEKIVIGMDVAASEF
CEEEEECEEEEHHHH		2.2930846556
256AcetylationSEFYRDGKYDLDFKS
HHHHHCCCCCCCCCC		39.6225953088
256UbiquitinationSEFYRDGKYDLDFKS
HHHHHCCCCCCCCCC		39.62-
257PhosphorylationEFYRDGKYDLDFKSP
HHHHCCCCCCCCCCC		27.5429691806
262AcetylationGKYDLDFKSPTDPSR
CCCCCCCCCCCCHHH		56.0125953088
262UbiquitinationGKYDLDFKSPTDPSR
CCCCCCCCCCCCHHH		56.01-
263PhosphorylationKYDLDFKSPTDPSRY
CCCCCCCCCCCHHHC		32.7823401153
265PhosphorylationDLDFKSPTDPSRYIT
CCCCCCCCCHHHCCC		68.5830266825
268PhosphorylationFKSPTDPSRYITGDQ
CCCCCCHHHCCCHHH		40.2930266825
280PhosphorylationGDQLGALYQDFVRDY
HHHHHHHHHHHHHCC		12.9027642862
287PhosphorylationYQDFVRDYPVVSIED
HHHHHHCCCEEEECC		6.33-
291PhosphorylationVRDYPVVSIEDPFDQ
HHCCCEEEECCCCCC		22.09-
292UbiquitinationRDYPVVSIEDPFDQD
HCCCEEEECCCCCCC		4.74-
305PhosphorylationQDDWAAWSKFTANVG
CCCHHHHHHHHCCCC		17.1123403867
315UbiquitinationTANVGIQIVGDDLTV
HCCCCEEEECCCCEE		3.36-
326UbiquitinationDLTVTNPKRIERAVE
CCEECCHHHHHHHHH		68.99-
335AcetylationIERAVEEKACNCLLL
HHHHHHHHHHCEEEE		44.7425953088
335UbiquitinationIERAVEEKACNCLLL
HHHHHHHHHHCEEEE		44.74-
343AcetylationACNCLLLKVNQIGSV
HHCEEEEEHHHCCCH		38.8225953088
349PhosphorylationLKVNQIGSVTEAIQA
EEHHHCCCHHHHHHH		27.7421712546
351UbiquitinationVNQIGSVTEAIQACK
HHHCCCHHHHHHHHH		22.77-
351PhosphoglycerylationVNQIGSVTEAIQACK
HHHCCCHHHHHHHHH		22.77-
358UbiquitinationTEAIQACKLAQENGW
HHHHHHHHHHHHHCC		50.28-
363UbiquitinationACKLAQENGWGVMVS
HHHHHHHHCCEEEEE		39.16-
370PhosphorylationNGWGVMVSHRSGETE
HCCEEEEECCCCCCC		8.62-
373PhosphorylationGVMVSHRSGETEDTF
EEEEECCCCCCCCCH		35.2430278072
376PhosphorylationVSHRSGETEDTFIAD
EECCCCCCCCCHHHH		42.5630278072
379PhosphorylationRSGETEDTFIADLVV
CCCCCCCCHHHHHHH		15.6530278072
390PhosphorylationDLVVGLCTGQIKTGA
HHHHHHHCCCCCCCC		36.8428060719
394UbiquitinationGLCTGQIKTGAPCRS
HHHCCCCCCCCCCCH		32.78-
395PhosphorylationLCTGQIKTGAPCRSE
HHCCCCCCCCCCCHH		39.9623882029
406UbiquitinationCRSERLAKYNQLMRI
CCHHHHHHHHHHHHH		49.69-
406AcetylationCRSERLAKYNQLMRI
CCHHHHHHHHHHHHH		49.6925953088
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ENOG_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CF047_HUMANC6orf47physical
16169070
HSF1_HUMANHSF1physical
16169070
IL17B_HUMANIL17Bphysical
16169070
NDUS7_HUMANNDUFS7physical
16169070
SIA4B_HUMANST3GAL2physical
16169070
SIGIR_HUMANSIGIRRphysical
16169070
UBE2C_HUMANUBE2Cphysical
16169070
ANX11_HUMANANXA11physical
16169070
ENSA_HUMANENSAphysical
16169070
HABP4_HUMANHABP4physical
16169070
MAP4_HUMANMAP4physical
16169070
NAT9_HUMANNAT9physical
16169070
HXK1_HUMANHK1physical
16169070
TBA4A_HUMANTUBA4Aphysical
16169070
GUAA_HUMANGMPSphysical
22863883
PNPH_HUMANPNPphysical
22863883
RAB1A_HUMANRAB1Aphysical
22863883
RCN1_HUMANRCN1physical
22863883
EXOC5_HUMANEXOC5physical
25416956
ENOA_HUMANENO1physical
26186194
ENOB_HUMANENO3physical
26186194
ALDR_HUMANAKR1B1physical
26344197
AK1BF_HUMANAKR1B15physical
26344197
GDIR1_HUMANARHGDIAphysical
26344197
CALR_HUMANCALRphysical
26344197
DUT_HUMANDUTphysical
26344197
EF1A1_HUMANEEF1A1physical
26344197
FABP5_HUMANFABP5physical
26344197
FKB1A_HUMANFKBP1Aphysical
26344197
FKB1B_HUMANFKBP1Bphysical
26344197
FKBP7_HUMANFKBP7physical
26344197
CH10_HUMANHSPE1physical
26344197
PGAM1_HUMANPGAM1physical
26344197
PUS7_HUMANPUS7physical
26344197
SUMO2_HUMANSUMO2physical
26344197
SUMO3_HUMANSUMO3physical
26344197
TPIS_HUMANTPI1physical
26344197
THIO_HUMANTXNphysical
26344197
UCHL3_HUMANUCHL3physical
26344197
ENOB_HUMANENO3physical
28514442
ENOA_HUMANENO1physical
28514442
Drug and Disease Associations
Kegg Disease
H00013 Small cell lung cancer
H00043 Neuroblastoma
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ENOG_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASSSPECTROMETRY.
"Time-resolved mass spectrometry of tyrosine phosphorylation sites inthe epidermal growth factor receptor signaling network reveals dynamicmodules.";
Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J.,Lauffenburger D.A., White F.M.;
Mol. Cell. Proteomics 4:1240-1250(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-44, AND MASSSPECTROMETRY.

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