ECHM_HUMAN - dbPTM
ECHM_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ECHM_HUMAN
UniProt AC P30084
Protein Name Enoyl-CoA hydratase, mitochondrial
Gene Name ECHS1
Organism Homo sapiens (Human).
Sequence Length 290
Subcellular Localization Mitochondrion matrix.
Protein Description Straight-chain enoyl-CoA thioesters from C4 up to at least C16 are processed, although with decreasing catalytic rate. Has high substrate specificity for crotonyl-CoA and moderate specificity for acryloyl-CoA, 3-methylcrotonyl-CoA and methacrylyl-CoA. It is noteworthy that binds tiglyl-CoA, but hydrates only a small amount of this substrate..
Protein Sequence MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
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
35PhosphorylationASGANFEYIIAEKRG
CCCCCEEEEEEEECC		8.0921253578
40AcetylationFEYIIAEKRGKNNTV
EEEEEEEECCCCCEE		58.3830585901
43UbiquitinationIIAEKRGKNNTVGLI
EEEEECCCCCEEEEE		51.5727667366
46PhosphorylationEKRGKNNTVGLIQLN
EECCCCCEEEEEECC		25.9120068231
56SuccinylationLIQLNRPKALNALCD
EEECCCHHHHHHHHH		63.3727452117
56UbiquitinationLIQLNRPKALNALCD
EEECCCHHHHHHHHH		63.3729967540
62GlutathionylationPKALNALCDGLIDEL
HHHHHHHHHHHHHHH		3.4722555962
62S-nitrosylationPKALNALCDGLIDEL
HHHHHHHHHHHHHHH		3.4725040305
92AcetylationIVLTGGDKAFAAGAD
EEEECCHHHHHCCCC		48.9923954790
922-HydroxyisobutyrylationIVLTGGDKAFAAGAD
EEEECCHHHHHCCCC		48.99-
92SuccinylationIVLTGGDKAFAAGAD
EEEECCHHHHHCCCC		48.9923954790
92UbiquitinationIVLTGGDKAFAAGAD
EEEECCHHHHHCCCC		48.9929967540
101SuccinylationFAAGADIKEMQNLSF
HHCCCCHHHHHHCCH		47.91-
101SuccinylationFAAGADIKEMQNLSF
HHCCCCHHHHHHCCH		47.91-
101AcetylationFAAGADIKEMQNLSF
HHCCCCHHHHHHCCH		47.9125038526
107PhosphorylationIKEMQNLSFQDCYSS
HHHHHHCCHHHHHCH		28.5428857561
112PhosphorylationNLSFQDCYSSKFLKH
HCCHHHHHCHHHHHH		25.0328857561
113PhosphorylationLSFQDCYSSKFLKHW
CCHHHHHCHHHHHHH		33.1228857561
114PhosphorylationSFQDCYSSKFLKHWD
CHHHHHCHHHHHHHH		10.8428857561
115UbiquitinationFQDCYSSKFLKHWDH
HHHHHCHHHHHHHHH		49.1029967540
115SuccinylationFQDCYSSKFLKHWDH
HHHHHCHHHHHHHHH		49.10-
115SuccinylationFQDCYSSKFLKHWDH
HHHHHCHHHHHHHHH		49.10-
115AcetylationFQDCYSSKFLKHWDH
HHHHHCHHHHHHHHH		49.1023236377
118MalonylationCYSSKFLKHWDHLTQ
HHCHHHHHHHHHHHH		45.8726320211
118AcetylationCYSSKFLKHWDHLTQ
HHCHHHHHHHHHHHH		45.8719608861
118UbiquitinationCYSSKFLKHWDHLTQ
HHCHHHHHHHHHHHH		45.8719608861
1272-HydroxyisobutyrylationWDHLTQVKKPVIAAV
HHHHHHCCCCEEEEE		41.35-
127SuccinylationWDHLTQVKKPVIAAV
HHHHHHCCCCEEEEE		41.3523954790
137PhosphorylationVIAAVNGYAFGGGCE
EEEEECCEEECCHHH		8.1121253578
176PhosphorylationTIPGAGGTQRLTRAV
CCCCCCHHHHHHHHH		15.0328857561
180PhosphorylationAGGTQRLTRAVGKSL
CCHHHHHHHHHHHHH		20.8328857561
185UbiquitinationRLTRAVGKSLAMEMV
HHHHHHHHHHHHHHH		35.3824816145
1852-HydroxyisobutyrylationRLTRAVGKSLAMEMV
HHHHHHHHHHHHHHH		35.38-
186PhosphorylationLTRAVGKSLAMEMVL
HHHHHHHHHHHHHHH		18.5520068231
194PhosphorylationLAMEMVLTGDRISAQ
HHHHHHHHCCCCCHH		26.1420068231
197MethylationEMVLTGDRISAQDAK
HHHHHCCCCCHHHHH		26.55-
199PhosphorylationVLTGDRISAQDAKQA
HHHCCCCCHHHHHHH		22.2924275569
204SuccinylationRISAQDAKQAGLVSK
CCCHHHHHHHCCCCC		49.3123954790
204AcetylationRISAQDAKQAGLVSK
CCCHHHHHHHCCCCC		49.3123236377
204SuccinylationRISAQDAKQAGLVSK
CCCHHHHHHHCCCCC		49.31-
204UbiquitinationRISAQDAKQAGLVSK
CCCHHHHHHHCCCCC		49.3122817900
211UbiquitinationKQAGLVSKICPVETL
HHHCCCCCCCCHHHH		40.6329967540
211AcetylationKQAGLVSKICPVETL
HHHCCCCCCCCHHHH		40.63-
213GlutathionylationAGLVSKICPVETLVE
HCCCCCCCCHHHHHH		3.3822555962
213S-nitrosylationAGLVSKICPVETLVE
HCCCCCCCCHHHHHH		3.3822178444
225S-nitrosylationLVEEAIQCAEKIASN
HHHHHHHHHHHHHHC		4.2822178444
2342-HydroxyisobutyrylationEKIASNSKIVVAMAK
HHHHHCCCEEEEEEH		43.71-
243PhosphorylationVVAMAKESVNAAFEM
EEEEEHHHHHHHHEE		21.6920068231
251PhosphorylationVNAAFEMTLTEGSKL
HHHHHEEECCCCCHH		24.2720068231
253PhosphorylationAAFEMTLTEGSKLEK
HHHEEECCCCCHHHH		29.1820068231
256PhosphorylationEMTLTEGSKLEKKLF
EEECCCCCHHHHHEE		28.0320068231
257UbiquitinationMTLTEGSKLEKKLFY
EECCCCCHHHHHEEE		72.0923000965
260UbiquitinationTEGSKLEKKLFYSTF
CCCCHHHHHEEEEEE		66.2723000965
261UbiquitinationEGSKLEKKLFYSTFA
CCCHHHHHEEEEEEC		34.1623000965
2612-HydroxyisobutyrylationEGSKLEKKLFYSTFA
CCCHHHHHEEEEEEC		34.16-
261AcetylationEGSKLEKKLFYSTFA
CCCHHHHHEEEEEEC		34.1627452117
264PhosphorylationKLEKKLFYSTFATDD
HHHHHEEEEEECCCC		19.7621945579
265PhosphorylationLEKKLFYSTFATDDR
HHHHEEEEEECCCCC		15.0921945579
266PhosphorylationEKKLFYSTFATDDRK
HHHEEEEEECCCCCC		13.1021945579
269PhosphorylationLFYSTFATDDRKEGM
EEEEEECCCCCCCCC		33.9521406692
2732-HydroxyisobutyrylationTFATDDRKEGMTAFV
EECCCCCCCCCHHHH		66.66-
276SulfoxidationTDDRKEGMTAFVEKR
CCCCCCCCHHHHHHH		2.2821406390
282SuccinylationGMTAFVEKRKANFKD
CCHHHHHHHHHCCCC		54.6323954790
2822-HydroxyisobutyrylationGMTAFVEKRKANFKD
CCHHHHHHHHHCCCC		54.63-
282UbiquitinationGMTAFVEKRKANFKD
CCHHHHHHHHHCCCC		54.6324816145
288UbiquitinationEKRKANFKDQ-----
HHHHHCCCCC-----		55.8424816145
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 ECHM_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ECHM_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 ECHM_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CBWD2_HUMANCBWD2physical
16169070
A1AT_HUMANSERPINA1physical
21988832
UBA1_HUMANUBA1physical
21988832
ECHM_HUMANECHS1physical
21988832
PPM1B_HUMANPPM1Bphysical
21988832
ABHEA_HUMANABHD14Aphysical
22863883
CNDP2_HUMANCNDP2physical
22863883
PSF3_HUMANGINS3physical
22863883
GDS1_HUMANRAP1GDS1physical
22863883
NHRF1_HUMANSLC9A3R1physical
22863883
P4R3B_HUMANSMEK2physical
22863883
TGM2_HUMANTGM2physical
22863883
UB2V1_HUMANUBE2V1physical
22863883
1433T_HUMANYWHAQphysical
22863883
1433Z_HUMANYWHAZphysical
22863883
KCC2D_HUMANCAMK2Dphysical
26186194
KCC2G_HUMANCAMK2Gphysical
26186194
ODB2_HUMANDBTphysical
26186194
UBP15_HUMANUSP15physical
26186194
HERC1_HUMANHERC1physical
26186194
ATPF2_HUMANATPAF2physical
26186194
MTND_HUMANADI1physical
26344197
SAHH2_HUMANAHCYL1physical
26344197
AK1A1_HUMANAKR1A1physical
26344197
ALDOA_HUMANALDOAphysical
26344197
CTBP1_HUMANCTBP1physical
26344197
PCBP1_HUMANPCBP1physical
26344197
TALDO_HUMANTALDO1physical
26344197
ATPF2_HUMANATPAF2physical
28514442
ODB2_HUMANDBTphysical
28514442
HERC1_HUMANHERC1physical
28514442
KCC2D_HUMANCAMK2Dphysical
28514442
YPEL5_HUMANYPEL5physical
27173435
TRAP1_HUMANTRAP1physical
27173435
SND1_HUMANSND1physical
27173435
UBE2N_HUMANUBE2Nphysical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616277Mitochondrial short-chain enoyl-CoA hydratase 1 deficiency (ECHS1D)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ECHM_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-118, AND MASS SPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory