DECR_HUMAN - dbPTM
DECR_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DECR_HUMAN
UniProt AC Q16698
Protein Name 2,4-dienoyl-CoA reductase, mitochondrial
Gene Name DECR1
Organism Homo sapiens (Human).
Sequence Length 335
Subcellular Localization Mitochondrion.
Protein Description Auxiliary enzyme of beta-oxidation. It participates in the metabolism of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA..
Protein Sequence MKLPARVFFTLGSRLPCGLAPRRFFSYGTKILYQNTEALQSKFFSPLQKAMLPPNSFQGKVAFITGGGTGLGKGMTTLLSSLGAQCVIASRKMDVLKATAEQISSQTGNKVHAIQCDVRDPDMVQNTVSELIKVAGHPNIVINNAAGNFISPTERLSPNAWKTITDIVLNGTAFVTLEIGKQLIKAQKGAAFLSITTIYAETGSGFVVPSASAKAGVEAMSKSLAAEWGKYGMRFNVIQPGPIKTKGAFSRLDPTGTFEKEMIGRIPCGRLGTVEELANLAAFLCSDYASWINGAVIKFDGGEEVLISGEFNDLRKVTKEQWDTIEELIRKTKGS
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
29PhosphorylationRRFFSYGTKILYQNT
HHHHHCCCCCEECCH		13.4818491316
33UbiquitinationSYGTKILYQNTEALQ
HCCCCCEECCHHHHH		11.82-
33PhosphorylationSYGTKILYQNTEALQ
HCCCCCEECCHHHHH		11.8229496907
42UbiquitinationNTEALQSKFFSPLQK
CHHHHHHHCCCHHHH		37.15-
42AcetylationNTEALQSKFFSPLQK
CHHHHHHHCCCHHHH		37.15-
42SuccinylationNTEALQSKFFSPLQK
CHHHHHHHCCCHHHH		37.15-
42SuccinylationNTEALQSKFFSPLQK
CHHHHHHHCCCHHHH		37.15-
49SuccinylationKFFSPLQKAMLPPNS
HCCCHHHHHCCCCCC		43.37-
49AcetylationKFFSPLQKAMLPPNS
HCCCHHHHHCCCCCC		43.3725038526
49SuccinylationKFFSPLQKAMLPPNS
HCCCHHHHHCCCCCC		43.37-
51SulfoxidationFSPLQKAMLPPNSFQ
CCHHHHHCCCCCCCC		8.1121406390
65PhosphorylationQGKVAFITGGGTGLG
CCCEEEEECCCCCCH		24.2628857561
69PhosphorylationAFITGGGTGLGKGMT
EEEECCCCCCHHHHH		32.2928857561
73UbiquitinationGGGTGLGKGMTTLLS
CCCCCCHHHHHHHHH		51.02-
73SuccinylationGGGTGLGKGMTTLLS
CCCCCCHHHHHHHHH		51.02-
73SuccinylationGGGTGLGKGMTTLLS
CCCCCCHHHHHHHHH		51.02-
73AcetylationGGGTGLGKGMTTLLS
CCCCCCHHHHHHHHH		51.0225038526
76PhosphorylationTGLGKGMTTLLSSLG
CCCHHHHHHHHHHHC		23.9823312004
77PhosphorylationGLGKGMTTLLSSLGA
CCHHHHHHHHHHHCC		19.4623312004
80PhosphorylationKGMTTLLSSLGAQCV
HHHHHHHHHHCCCEE		26.9923312004
81PhosphorylationGMTTLLSSLGAQCVI
HHHHHHHHHCCCEEH		30.6923312004
90PhosphorylationGAQCVIASRKMDVLK
CCCEEHCCCCHHHHH		22.7028348404
92AcetylationQCVIASRKMDVLKAT
CEEHCCCCHHHHHHH		36.6425038526
97AcetylationSRKMDVLKATAEQIS
CCCHHHHHHHHHHHH		43.4725038526
97SuccinylationSRKMDVLKATAEQIS
CCCHHHHHHHHHHHH		43.47-
97SuccinylationSRKMDVLKATAEQIS
CCCHHHHHHHHHHHH		43.47-
97MalonylationSRKMDVLKATAEQIS
CCCHHHHHHHHHHHH		43.4726320211
99PhosphorylationKMDVLKATAEQISSQ
CHHHHHHHHHHHHHC		29.1925367160
104PhosphorylationKATAEQISSQTGNKV
HHHHHHHHHCCCCCE		18.9828509920
105PhosphorylationATAEQISSQTGNKVH
HHHHHHHHCCCCCEE		33.1328509920
107PhosphorylationAEQISSQTGNKVHAI
HHHHHHCCCCCEEEE		44.6728509920
110AcetylationISSQTGNKVHAIQCD
HHHCCCCCEEEEECC		36.4225038526
110MalonylationISSQTGNKVHAIQCD
HHHCCCCCEEEEECC		36.4226320211
119MethylationHAIQCDVRDPDMVQN
EEEECCCCCHHHHHH		36.17-
123SulfoxidationCDVRDPDMVQNTVSE
CCCCCHHHHHHHHHH		3.9821406390
133AcetylationNTVSELIKVAGHPNI
HHHHHHHHHHCCCCE		38.3625038526
185AcetylationEIGKQLIKAQKGAAF
EHHHHHHHHHHCCEE		54.0525953088
213UbiquitinationFVVPSASAKAGVEAM
EEECCHHHHHHHHHH		12.87-
222UbiquitinationAGVEAMSKSLAAEWG
HHHHHHHHHHHHHHH		36.08-
230AcetylationSLAAEWGKYGMRFNV
HHHHHHHHCCEEEEE		39.4419608861
244MalonylationVIQPGPIKTKGAFSR
EECCCCCCCCCCCCC		47.5226320211
244AcetylationVIQPGPIKTKGAFSR
EECCCCCCCCCCCCC		47.5225038526
244SuccinylationVIQPGPIKTKGAFSR
EECCCCCCCCCCCCC		47.52-
244UbiquitinationVIQPGPIKTKGAFSR
EECCCCCCCCCCCCC		47.52-
244SuccinylationVIQPGPIKTKGAFSR
EECCCCCCCCCCCCC		47.52-
245PhosphorylationIQPGPIKTKGAFSRL
ECCCCCCCCCCCCCC		35.1228857561
246MalonylationQPGPIKTKGAFSRLD
CCCCCCCCCCCCCCC		43.1532601280
246AcetylationQPGPIKTKGAFSRLD
CCCCCCCCCCCCCCC		43.1525038526
246SuccinylationQPGPIKTKGAFSRLD
CCCCCCCCCCCCCCC		43.1527452117
250PhosphorylationIKTKGAFSRLDPTGT
CCCCCCCCCCCCCCC		31.2527251275
251UbiquitinationKTKGAFSRLDPTGTF
CCCCCCCCCCCCCCC		36.33-
2602-HydroxyisobutyrylationDPTGTFEKEMIGRIP
CCCCCCCHHHCCCCC		48.68-
260SuccinylationDPTGTFEKEMIGRIP
CCCCCCCHHHCCCCC		48.68-
260SuccinylationDPTGTFEKEMIGRIP
CCCCCCCHHHCCCCC		48.68-
260UbiquitinationDPTGTFEKEMIGRIP
CCCCCCCHHHCCCCC		48.68-
260AcetylationDPTGTFEKEMIGRIP
CCCCCCCHHHCCCCC		48.6820167786
310UbiquitinationEEVLISGEFNDLRKV
CEEEEEEECCHHHHC		34.19-
316AcetylationGEFNDLRKVTKEQWD
EECCHHHHCCHHHHH		62.6525038526
319SuccinylationNDLRKVTKEQWDTIE
CHHHHCCHHHHHHHH		51.39-
319SuccinylationNDLRKVTKEQWDTIE
CHHHHCCHHHHHHHH		51.39-
319UbiquitinationNDLRKVTKEQWDTIE
CHHHHCCHHHHHHHH		51.39-
319AcetylationNDLRKVTKEQWDTIE
CHHHHCCHHHHHHHH		51.3925038526
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 DECR_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DECR_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 DECR_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
DHB4_HUMANHSD17B4physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
6160342,4-dienoyl-CoA reductase deficiency (DECRD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DECR_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-230, AND MASS SPECTROMETRY.

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