Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Peroxisomal 2,4-dienoyl-CoA reductase  

UniProtKB / Swiss-Prot ID :  DECR2_HUMAN

Gene Name (Synonyms) : 
DECR2, PDCR  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Peroxisome (By similarity). 

Protein Function :  Auxiliary enzyme of beta-oxidation. Participates in the degradation of unsaturated fatty enoyl-CoA esters having double bonds in both even- and odd-numbered positions in peroxisome. Catalyzes the NADP-dependent reduction of 2,4-dienoyl-CoA to yield trans-3-enoyl-CoA. Has activity towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19- docosaheptaenoyl-CoA, suggesting that it does not constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. 

Protein Sequence MAQPPPDVEGDDCLPAYRHLFCPDLLRDKVAFITGGGSGIGFRIAEIFMRHGCHTVIASRSLPRVLTAAR...
Predicted Secondary Structure CCCCCCCCCCCCCCHHHHHHCCCCCCCCCEEEEEECCCHHHHHHHHHHHHCCCEEEEEECCHHHHHHHHH...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
59PhosphoserineTVIASRSLP
EEEEECCHH
15.98HPRD
Link
59PhosphoserineTVIASRSLP
EEEEECCHH
15.98SysPTM
Link
59Phosphoserine.TVIASRSLP
EEEEECCHH
15.98UniProtKB
Link
61PhosphoserineIASRSLPRV
EEECCHHHH
39.98HPRD
Link
61PhosphoserineIASRSLPRV
EEECCHHHH
39.98SysPTM
Link
61Phosphoserine.IASRSLPRV
EEECCHHHH
39.98UniProtKB
Link
138PhosphothreonineMDIDTSGTF
HHCCCHHHH
29.41HPRD
Link
151N6-acetyllysineVLYEKFFRD
HHHHHHHHC
35.92HPRD
Link
151N6-acetyllysineVLYEKFFRD
HHHHHHHHC
35.92Phosphositeplus
Link
151N6-acetyllysine.VLYEKFFRD
HHHHHHHHC
35.92UniProtKB
Link
291N6-acetyllysineSFSAKL
HHCCCC
54.23HPRD
Link-
291N6-acetyllysineSFSAKL
HHCCCC
54.23Phosphositeplus
Link-
291N6-acetyllysine.SFSAKL
HHCCCC
54.23UniProtKB
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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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-151 AND LYS-291, AND MASSSPECTROMETRY.
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-59 AND SER-61, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures