ECI2_HUMAN - dbPTM
ECI2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECI2_HUMAN
UniProt AC O75521
Protein Name Enoyl-CoA delta isomerase 2, mitochondrial
Gene Name ECI2
Organism Homo sapiens (Human).
Sequence Length 394
Subcellular Localization Isoform 1: Mitochondrion.
Isoform 2: Peroxisome matrix.
Protein Description Able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species. Has a preference for 3-trans substrates (By similarity)..
Protein Sequence MAMAYLAWRLARRSCPSSLQVTSFPVVQLHMNRTAMRASQKDFENSMNQVKLLKKDPGNEVKLKLYALYKQATEGPCNMPKPGVFDLINKAKWDAWNALGSLPKEAARQNYVDLVSSLSPSLESSSQVEPGTDRKSTGFETLVVTSEDGITKIMFNRPKKKNAINTEMYHEIMRALKAASKDDSIITVLTGNGDYYSSGNDLTNFTDIPPGGVEEKAKNNAVLLREFVGCFIDFPKPLIAVVNGPAVGISVTLLGLFDAVYASDRATFHTPFSHLGQSPEGCSSYTFPKIMSPAKATEMLIFGKKLTAGEACAQGLVTEVFPDSTFQKEVWTRLKAFAKLPPNALRISKEVIRKREREKLHAVNAEECNVLQGRWLSDECTNAVVNFLSRKSKL
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
5Phosphorylation---MAMAYLAWRLAR
---CHHHHHHHHHHH		5.4924043423
39PhosphorylationNRTAMRASQKDFENS
CHHHHHHHHHHHHHH		27.6524719451
41AcetylationTAMRASQKDFENSMN
HHHHHHHHHHHHHHH		62.9971295
47SulfoxidationQKDFENSMNQVKLLK
HHHHHHHHHHHHHHH		6.4921406390
51AcetylationENSMNQVKLLKKDPG
HHHHHHHHHHHCCCC		38.0419608861
51SuccinylationENSMNQVKLLKKDPG
HHHHHHHHHHHCCCC		38.04-
51SuccinylationENSMNQVKLLKKDPG
HHHHHHHHHHHCCCC		38.04-
51MalonylationENSMNQVKLLKKDPG
HHHHHHHHHHHCCCC		38.0426320211
54AcetylationMNQVKLLKKDPGNEV
HHHHHHHHCCCCCHH		66.6223749302
55SuccinylationNQVKLLKKDPGNEVK
HHHHHHHCCCCCHHH		69.95-
55SuccinylationNQVKLLKKDPGNEVK
HHHHHHHCCCCCHHH		69.95-
60 (in isoform 2)Ubiquitination-47.1221890473
62 (in isoform 2)Ubiquitination-33.4521890473
62SuccinylationKDPGNEVKLKLYALY
CCCCCHHHHHHHHHH		33.45-
62SuccinylationKDPGNEVKLKLYALY
CCCCCHHHHHHHHHH		33.45-
62AcetylationKDPGNEVKLKLYALY
CCCCCHHHHHHHHHH		33.4523749302
622-HydroxyisobutyrylationKDPGNEVKLKLYALY
CCCCCHHHHHHHHHH		33.45-
64AcetylationPGNEVKLKLYALYKQ
CCCHHHHHHHHHHHH		33.4625953088
64MalonylationPGNEVKLKLYALYKQ
CCCHHHHHHHHHHHH		33.4626320211
66PhosphorylationNEVKLKLYALYKQAT
CHHHHHHHHHHHHHC		7.9326356563
69PhosphorylationKLKLYALYKQATEGP
HHHHHHHHHHHCCCC		7.9029496907
70AcetylationLKLYALYKQATEGPC
HHHHHHHHHHCCCCC		34.0225953088
70SuccinylationLKLYALYKQATEGPC
HHHHHHHHHHCCCCC		34.02-
70SuccinylationLKLYALYKQATEGPC
HHHHHHHHHHCCCCC		34.02-
73PhosphorylationYALYKQATEGPCNMP
HHHHHHHCCCCCCCC		38.6928842319
81AcetylationEGPCNMPKPGVFDLI
CCCCCCCCCCHHHHH		43.5726051181
81SuccinylationEGPCNMPKPGVFDLI
CCCCCCCCCCHHHHH		43.57-
81SuccinylationEGPCNMPKPGVFDLI
CCCCCCCCCCHHHHH		43.57-
90AcetylationGVFDLINKAKWDAWN
CHHHHHHHHHHHHHH		44.3325953088
90SuccinylationGVFDLINKAKWDAWN
CHHHHHHHHHHHHHH		44.33-
90SuccinylationGVFDLINKAKWDAWN
CHHHHHHHHHHHHHH		44.33-
90 (in isoform 1)Ubiquitination-44.3321890473
90UbiquitinationGVFDLINKAKWDAWN
CHHHHHHHHHHHHHH		44.3321890473
92SuccinylationFDLINKAKWDAWNAL
HHHHHHHHHHHHHHH		47.41-
92SuccinylationFDLINKAKWDAWNAL
HHHHHHHHHHHHHHH		47.41-
92AcetylationFDLINKAKWDAWNAL
HHHHHHHHHHHHHHH		47.4119608861
92MalonylationFDLINKAKWDAWNAL
HHHHHHHHHHHHHHH		47.4126320211
92 (in isoform 1)Ubiquitination-47.4121890473
92UbiquitinationFDLINKAKWDAWNAL
HHHHHHHHHHHHHHH		47.4119608861
101PhosphorylationDAWNALGSLPKEAAR
HHHHHHCCCCHHHHH		42.2030108239
104AcetylationNALGSLPKEAARQNY
HHHCCCCHHHHHHCH		66.3420167786
116PhosphorylationQNYVDLVSSLSPSLE
HCHHHHHHHCCCCCC		32.6220873877
117PhosphorylationNYVDLVSSLSPSLES
CHHHHHHHCCCCCCC		25.9529116813
119PhosphorylationVDLVSSLSPSLESSS
HHHHHHCCCCCCCCC		17.8729116813
121PhosphorylationLVSSLSPSLESSSQV
HHHHCCCCCCCCCCC		41.2020873877
124PhosphorylationSLSPSLESSSQVEPG
HCCCCCCCCCCCCCC		40.3530576142
125PhosphorylationLSPSLESSSQVEPGT
CCCCCCCCCCCCCCC		18.5326471730
126PhosphorylationSPSLESSSQVEPGTD
CCCCCCCCCCCCCCC		47.7426471730
135UbiquitinationVEPGTDRKSTGFETL
CCCCCCCCCCCCCEE		56.00-
136PhosphorylationEPGTDRKSTGFETLV
CCCCCCCCCCCCEEE		34.3630266825
137PhosphorylationPGTDRKSTGFETLVV
CCCCCCCCCCCEEEE		49.2630266825
141PhosphorylationRKSTGFETLVVTSED
CCCCCCCEEEEECCC		23.6930266825
152AcetylationTSEDGITKIMFNRPK
ECCCCCEEEEECCCC		30.197683033
159AcetylationKIMFNRPKKKNAINT
EEEECCCCCCCCCCH		73.4824886695
159SuccinylationKIMFNRPKKKNAINT
EEEECCCCCCCCCCH		73.4827452117
160AcetylationIMFNRPKKKNAINTE
EEECCCCCCCCCCHH		54.682403911
161SuccinylationMFNRPKKKNAINTEM
EECCCCCCCCCCHHH		58.7127452117
161MalonylationMFNRPKKKNAINTEM
EECCCCCCCCCCHHH		58.7126320211
161AcetylationMFNRPKKKNAINTEM
EECCCCCCCCCCHHH		58.7125038526
161SuccinylationMFNRPKKKNAINTEM
EECCCCCCCCCCHHH		58.71-
166PhosphorylationKKKNAINTEMYHEIM
CCCCCCCHHHHHHHH		18.93-
169PhosphorylationNAINTEMYHEIMRAL
CCCCHHHHHHHHHHH		7.0625219547
218MalonylationGGVEEKAKNNAVLLR
CCHHHHHHHCCCHHH		62.9026320211
278PhosphorylationPFSHLGQSPEGCSSY
CCHHCCCCCCCCCCC		24.1028152594
283PhosphorylationGQSPEGCSSYTFPKI
CCCCCCCCCCCCCCC		36.9228152594
284PhosphorylationQSPEGCSSYTFPKIM
CCCCCCCCCCCCCCC		32.0628152594
285PhosphorylationSPEGCSSYTFPKIMS
CCCCCCCCCCCCCCC		8.9828152594
286PhosphorylationPEGCSSYTFPKIMSP
CCCCCCCCCCCCCCC		35.0928152594
289AcetylationCSSYTFPKIMSPAKA
CCCCCCCCCCCCCCC		47.0226051181
289SuccinylationCSSYTFPKIMSPAKA
CCCCCCCCCCCCCCC		47.02-
289SuccinylationCSSYTFPKIMSPAKA
CCCCCCCCCCCCCCC		47.02-
299SulfoxidationSPAKATEMLIFGKKL
CCCCCCEEEECCCCC		2.7821406390
3042-HydroxyisobutyrylationTEMLIFGKKLTAGEA
CEEEECCCCCHHHHH		33.58-
304AcetylationTEMLIFGKKLTAGEA
CEEEECCCCCHHHHH		33.5825953088
3052-HydroxyisobutyrylationEMLIFGKKLTAGEAC
EEEECCCCCHHHHHH		51.99-
305MalonylationEMLIFGKKLTAGEAC
EEEECCCCCHHHHHH		51.9926320211
305AcetylationEMLIFGKKLTAGEAC
EEEECCCCCHHHHHH		51.9926051181
312GlutathionylationKLTAGEACAQGLVTE
CCHHHHHHHHHCCEE		2.2422555962
328AcetylationFPDSTFQKEVWTRLK
CCCCHHHHHHHHHHH		50.4725038526
339AcetylationTRLKAFAKLPPNALR
HHHHHHHCCCCCHHH		55.8925953088
349UbiquitinationPNALRISKEVIRKRE
CCHHHHCHHHHHHHH		54.34-
359AcetylationIRKREREKLHAVNAE
HHHHHHHHHHCCCHH		52.3623749302
359MalonylationIRKREREKLHAVNAE
HHHHHHHHHHCCCHH		52.3626320211
3592-HydroxyisobutyrylationIRKREREKLHAVNAE
HHHHHHHHHHCCCHH		52.36-
368GlutathionylationHAVNAEECNVLQGRW
HCCCHHHCCCCCCCC		3.0022555962
393AcetylationNFLSRKSKL------
HHHHHHHCC------		62.3418527683
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 ECI2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECI2_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 ECI2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
KDM1A_HUMANKDM1Aphysical
23455924
ECH1_HUMANECH1physical
26344197
ECI2_HUMANECI2physical
27499296
ECH1_HUMANECH1physical
27499296
MCCA_HUMANMCCC1physical
27499296
IDE_HUMANIDEphysical
27499296
ACS2L_HUMANACSS1physical
27499296
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
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 ECI2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51 AND LYS-92, AND MASSSPECTROMETRY.

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