DECR2_HUMAN - dbPTM
DECR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DECR2_HUMAN
UniProt AC Q9NUI1
Protein Name Peroxisomal 2,4-dienoyl-CoA reductase
Gene Name DECR2
Organism Homo sapiens (Human).
Sequence Length 292
Subcellular Localization Peroxisome.
Protein Description 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 MAQPPPDVEGDDCLPAYRHLFCPDLLRDKVAFITGGGSGIGFRIAEIFMRHGCHTVIASRSLPRVLTAARKLAGATGRRCLPLSMDVRAPPAVMAAVDQALKEFGRIDILINCAAGNFLCPAGALSFNAFKTVMDIDTSGTFNVSRVLYEKFFRDHGGVIVNITATLGNRGQALQVHAGSAKAAVDAMTRHLAVEWGPQNIRVNSLAPGPISGTEGLRRLGGPQASLSTKVTASPLQRLGNKTEIAHSVLYLASPLASYVTGAVLVADGGAWLTFPNGVKGLPDFASFSAKL
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
2Acetylation------MAQPPPDVE
------CCCCCCCCC
30.5022814378
29UbiquitinationCPDLLRDKVAFITGG
CHHHHCCCEEEEECC
29.09-
292-HydroxyisobutyrylationCPDLLRDKVAFITGG
CHHHHCCCEEEEECC
29.09-
38PhosphorylationAFITGGGSGIGFRIA
EEEECCCCCHHHHHH
30.4322210691
59PhosphorylationGCHTVIASRSLPRVL
CCEEEEECCCHHHHH
15.9820068231
61PhosphorylationHTVIASRSLPRVLTA
EEEEECCCHHHHHHH
39.9820068231
67PhosphorylationRSLPRVLTAARKLAG
CCHHHHHHHHHHHCC
18.53-
94SulfoxidationVRAPPAVMAAVDQAL
CCCCHHHHHHHHHHH
1.8421406390
138PhosphorylationKTVMDIDTSGTFNVS
CEEEEECCCCCCCHH
29.4120068231
139PhosphorylationTVMDIDTSGTFNVSR
EEEEECCCCCCCHHH
31.8920068231
141PhosphorylationMDIDTSGTFNVSRVL
EEECCCCCCCHHHHH
16.2920068231
145PhosphorylationTSGTFNVSRVLYEKF
CCCCCCHHHHHHHHH
20.1320068231
1512-HydroxyisobutyrylationVSRVLYEKFFRDHGG
HHHHHHHHHHHHCCC
35.92-
151AcetylationVSRVLYEKFFRDHGG
HHHHHHHHHHHHCCC
35.9219608861
226PhosphorylationRLGGPQASLSTKVTA
HHCCCCCCCCCCCCC
20.0123312004
228PhosphorylationGGPQASLSTKVTASP
CCCCCCCCCCCCCHH
24.5620068231
229PhosphorylationGPQASLSTKVTASPL
CCCCCCCCCCCCHHH
34.5220068231
230MalonylationPQASLSTKVTASPLQ
CCCCCCCCCCCHHHH
33.9226320211
230AcetylationPQASLSTKVTASPLQ
CCCCCCCCCCCHHHH
33.9225953088
232PhosphorylationASLSTKVTASPLQRL
CCCCCCCCCHHHHHC
23.99-
234PhosphorylationLSTKVTASPLQRLGN
CCCCCCCHHHHHCCC
19.4420068231
287PhosphorylationKGLPDFASFSAKL--
CCCCCHHHHHCCC--
21.5230266825
289PhosphorylationLPDFASFSAKL----
CCCHHHHHCCC----
23.2330266825
291AcetylationDFASFSAKL------
CHHHHHCCC------
54.2319608861

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 DECR2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DECR2_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 DECR2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
EP300_HUMANEP300physical
21988832
SESD1_HUMANSESTD1physical
26186194
SESD1_HUMANSESTD1physical
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 DECR2_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-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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