ECI1_HUMAN - dbPTM
ECI1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECI1_HUMAN
UniProt AC P42126
Protein Name Enoyl-CoA delta isomerase 1, mitochondrial
Gene Name ECI1
Organism Homo sapiens (Human).
Sequence Length 302
Subcellular Localization Mitochondrion 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..
Protein Sequence MALVASVRVPARVLLRAGARLPGAALGRTERAAGGGDGARRFGSQRVLVEPDAGAGVAVMKFKNPPVNSLSLEFLTELVISLEKLENDKSFRGVILTSDRPGVFSAGLDLTEMCGRSPAHYAGYWKAVQELWLRLYQSNLVLVSAINGACPAGGCLVALTCDYRILADNPRYCIGLNETQLGIIAPFWLKDTLENTIGHRAAERALQLGLLFPPAEALQVGIVDQVVPEEQVQSTALSAIAQWMAIPDHARQLTKAMMRKATASRLVTQRDADVQNFVSFISKDSIQKSLQMYLERLKEEKG
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
6Phosphorylation--MALVASVRVPARV
--CCCEEECCCCHHH
11.7224719451
61 (in isoform 1)Ubiquitination-46.7321890473
61SuccinylationGAGVAVMKFKNPPVN
CCCEEEEEECCCCCC
46.7321906983
61SuccinylationGAGVAVMKFKNPPVN
CCCEEEEEECCCCCC
46.73-
61UbiquitinationGAGVAVMKFKNPPVN
CCCEEEEEECCCCCC
46.73-
61 (in isoform 2)Ubiquitination-46.7321890473
61AcetylationGAGVAVMKFKNPPVN
CCCEEEEEECCCCCC
46.7327452117
612-HydroxyisobutyrylationGAGVAVMKFKNPPVN
CCCEEEEEECCCCCC
46.73-
84SuccinylationELVISLEKLENDKSF
HHHHHHHHHHCCCCC
67.41-
84SuccinylationELVISLEKLENDKSF
HHHHHHHHHHCCCCC
67.41-
892-HydroxyisobutyrylationLEKLENDKSFRGVIL
HHHHHCCCCCCEEEE
64.18-
89AcetylationLEKLENDKSFRGVIL
HHHHHCCCCCCEEEE
64.1819608861
89SuccinylationLEKLENDKSFRGVIL
HHHHHCCCCCCEEEE
64.1827452117
171MethylationRILADNPRYCIGLNE
EEECCCCCEEECCCC
45.25-
262PhosphorylationKAMMRKATASRLVTQ
HHHHHHHHHHHHHCH
28.3528842319
266AcetylationRKATASRLVTQRDAD
HHHHHHHHHCHHHHH
4.5319608861
266 (in isoform 2)Ubiquitination-4.5321890473
266UbiquitinationRKATASRLVTQRDAD
HHHHHHHHHCHHHHH
4.5319608861
271 (in isoform 2)Ubiquitination-36.9821890473
279PhosphorylationADVQNFVSFISKDSI
HHHHHHHHHHCHHHH
16.8423663014
282PhosphorylationQNFVSFISKDSIQKS
HHHHHHHCHHHHHHH
28.5328857561
283SuccinylationNFVSFISKDSIQKSL
HHHHHHCHHHHHHHH
51.1627452117
283SuccinylationNFVSFISKDSIQKSL
HHHHHHCHHHHHHHH
51.16-
283UbiquitinationNFVSFISKDSIQKSL
HHHHHHCHHHHHHHH
51.1621890473
283 (in isoform 1)Ubiquitination-51.1621890473
283AcetylationNFVSFISKDSIQKSL
HHHHHHCHHHHHHHH
51.1623954790
285PhosphorylationVSFISKDSIQKSLQM
HHHHCHHHHHHHHHH
30.5621406692
288SuccinylationISKDSIQKSLQMYLE
HCHHHHHHHHHHHHH
52.00-
288SuccinylationISKDSIQKSLQMYLE
HCHHHHHHHHHHHHH
52.0021890473
288UbiquitinationISKDSIQKSLQMYLE
HCHHHHHHHHHHHHH
52.0021890473
288 (in isoform 1)Ubiquitination-52.0021890473
288AcetylationISKDSIQKSLQMYLE
HCHHHHHHHHHHHHH
52.002401759
289PhosphorylationSKDSIQKSLQMYLER
CHHHHHHHHHHHHHH
13.8821406692
293PhosphorylationIQKSLQMYLERLKEE
HHHHHHHHHHHHHHH
7.7621406692

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 ECI1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECI1_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 ECI1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SIN1_HUMANMAPKAP1physical
21988832
POTE1_HUMANPOT1physical
21988832
HIBCH_HUMANHIBCHphysical
26344197

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 ECI1_HUMAN

loading...

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-89 AND LYS-283, AND MASSSPECTROMETRY.

TOP