ECH1_HUMAN - dbPTM
ECH1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECH1_HUMAN
UniProt AC Q13011
Protein Name Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase, mitochondrial
Gene Name ECH1
Organism Homo sapiens (Human).
Sequence Length 328
Subcellular Localization Mitochondrion. Peroxisome.
Protein Description Isomerization of 3-trans,5-cis-dienoyl-CoA to 2-trans,4-trans-dienoyl-CoA..
Protein Sequence MAAGIVASRRLRDLLTRRLTGSNYPGLSISLRLTGSSAQEEASGVALGEAPDHSYESLRVTSAQKHVLHVQLNRPNKRNAMNKVFWREMVECFNKISRDADCRAVVISGAGKMFTAGIDLMDMASDILQPKGDDVARISWYLRDIITRYQETFNVIERCPKPVIAAVHGGCIGGGVDLVTACDIRYCAQDAFFQVKEVDVGLAADVGTLQRLPKVIGNQSLVNELAFTARKMMADEALGSGLVSRVFPDKEVMLDAALALAAEISSKSPVAVQSTKVNLLYSRDHSVAESLNYVASWNMSMLQTQDLVKSVQATTENKELKTVTFSKL
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
20PhosphorylationDLLTRRLTGSNYPGL
HHHHHHHCCCCCCCE		36.43-
22PhosphorylationLTRRLTGSNYPGLSI
HHHHHCCCCCCCEEE		28.14-
28PhosphorylationGSNYPGLSISLRLTG
CCCCCCEEEEEEEEC		18.9529496963
30PhosphorylationNYPGLSISLRLTGSS
CCCCEEEEEEEECCC		12.2229496963
34PhosphorylationLSISLRLTGSSAQEE
EEEEEEEECCCCCHH		28.6930108239
36PhosphorylationISLRLTGSSAQEEAS
EEEEEECCCCCHHHC		19.7730108239
37PhosphorylationSLRLTGSSAQEEASG
EEEEECCCCCHHHCC		35.0026657352
54PhosphorylationLGEAPDHSYESLRVT
CCCCCCCCHHHCEEC		37.67-
65AcetylationLRVTSAQKHVLHVQL
CEECCCCCEEEEEEC		35.0825825284
65UbiquitinationLRVTSAQKHVLHVQL
CEECCCCCEEEEEEC		35.08-
77AcetylationVQLNRPNKRNAMNKV
EECCCCCCCCHHHHH		50.1123749302
83AcetylationNKRNAMNKVFWREMV
CCCCHHHHHHHHHHH		26.2325825284
832-HydroxyisobutyrylationNKRNAMNKVFWREMV
CCCCHHHHHHHHHHH		26.23-
83UbiquitinationNKRNAMNKVFWREMV
CCCCHHHHHHHHHHH		26.2319608861
95AcetylationEMVECFNKISRDADC
HHHHHHHHHCCCCCC		23.0825825284
952-HydroxyisobutyrylationEMVECFNKISRDADC
HHHHHHHHHCCCCCC		23.08-
108PhosphorylationDCRAVVISGAGKMFT
CCCEEEEECCCHHHH		15.81-
115PhosphorylationSGAGKMFTAGIDLMD
ECCCHHHHCCCCHHH		22.0722210691
139PhosphorylationGDDVARISWYLRDII
CCHHHHHHHHHHHHH		12.2427422710
141PhosphorylationDVARISWYLRDIITR
HHHHHHHHHHHHHHH		5.7628111955
161AcetylationNVIERCPKPVIAAVH
HHHHHCCCCEEEEEC		56.3926051181
186PhosphorylationVTACDIRYCAQDAFF
HHHCCHHHHHCCCCC		7.7728152594
196AcetylationQDAFFQVKEVDVGLA
CCCCCCEEECCCCEE		41.0325038526
214UbiquitinationGTLQRLPKVIGNQSL
HHHHHHCHHHCCHHH		51.5921890473
220PhosphorylationPKVIGNQSLVNELAF
CHHHCCHHHHHHHHH		37.9820068231
228PhosphorylationLVNELAFTARKMMAD
HHHHHHHHHHHHHHH		21.68-
231SuccinylationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.4827452117
2312-HydroxyisobutyrylationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.48-
231UbiquitinationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.48-
231MalonylationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.4826320211
231AcetylationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.4825038526
231SuccinylationELAFTARKMMADEAL
HHHHHHHHHHHHHHH		30.48-
232SulfoxidationLAFTARKMMADEALG
HHHHHHHHHHHHHHH		1.9221406390
240PhosphorylationMADEALGSGLVSRVF
HHHHHHHCCHHHHCC		29.7820068231
244PhosphorylationALGSGLVSRVFPDKE
HHHCCHHHHCCCCHH		27.9820068231
250AcetylationVSRVFPDKEVMLDAA
HHHCCCCHHHHHHHH		53.0725038526
265PhosphorylationLALAAEISSKSPVAV
HHHHHHHHCCCCCEE		24.1828348404
266PhosphorylationALAAEISSKSPVAVQ
HHHHHHHCCCCCEEE		42.7028348404
267AcetylationLAAEISSKSPVAVQS
HHHHHHCCCCCEEEE		52.5712432453
268PhosphorylationAAEISSKSPVAVQST
HHHHHCCCCCEEEEC		26.9325849741
276UbiquitinationPVAVQSTKVNLLYSR
CCEEEECCCEEEECC		34.082190698
281PhosphorylationSTKVNLLYSRDHSVA
ECCCEEEECCCCHHH		12.58-
282PhosphorylationTKVNLLYSRDHSVAE
CCCEEEECCCCHHHH		31.0724719451
318UbiquitinationVQATTENKELKTVTF
HHHHCCCCEEEEEEE		59.1819608861
3182-HydroxyisobutyrylationVQATTENKELKTVTF
HHHHCCCCEEEEEEE		59.18-
318AcetylationVQATTENKELKTVTF
HHHHCCCCEEEEEEE		59.1823749302
3212-HydroxyisobutyrylationTTENKELKTVTFSKL
HCCCCEEEEEEEECC		41.88-
321UbiquitinationTTENKELKTVTFSKL
HCCCCEEEEEEEECC		41.88-
321AcetylationTTENKELKTVTFSKL
HCCCCEEEEEEEECC		41.8825953088
3272-HydroxyisobutyrylationLKTVTFSKL------
EEEEEEECC------		54.76-
327UbiquitinationLKTVTFSKL------
EEEEEEECC------		54.7619608861
327AcetylationLKTVTFSKL------
EEEEEEECC------		54.7619608861
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 ECH1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECH1_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 ECH1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HD_HUMANHTTphysical
15383276
EF1G_HUMANEEF1Gphysical
15383276
A4_HUMANAPPphysical
21832049
OPA1_HUMANOPA1physical
22939629
HNRL1_HUMANHNRNPUL1physical
22939629
STAT3_HUMANSTAT3physical
21988832
EF1D_HUMANEEF1Dphysical
21988832
PEX5_HUMANPEX5physical
21988832
TRAF1_HUMANTRAF1physical
25416956
FAM9B_HUMANFAM9Bphysical
25416956
MCCB_HUMANMCCC2physical
26186194
ECI2_HUMANECI2physical
26186194
TRAF3_HUMANTRAF3physical
26186194
MCCA_HUMANMCCC1physical
26186194
IQGA1_HUMANIQGAP1physical
26186194
EI2BG_HUMANEIF2B3physical
26186194
FHL2_HUMANFHL2physical
26186194
PTGR3_HUMANZADH2physical
26186194
SPS1_HUMANSEPHS1physical
26344197
ECI2_HUMANECI2physical
28514442
TRAF3_HUMANTRAF3physical
28514442
MCCB_HUMANMCCC2physical
28514442
EI2BG_HUMANEIF2B3physical
28514442
MCCA_HUMANMCCC1physical
28514442
FHL2_HUMANFHL2physical
28514442
IQGA1_HUMANIQGAP1physical
28514442
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 ECH1_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-83; LYS-95; LYS-318 ANDLYS-327, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-30, AND MASSSPECTROMETRY.

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