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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MAQPPPDVE ------CCCCCCCCC | 30.50 | 22814378 | |
29 | Ubiquitination | CPDLLRDKVAFITGG CHHHHCCCEEEEECC | 29.09 | - | |
29 | 2-Hydroxyisobutyrylation | CPDLLRDKVAFITGG CHHHHCCCEEEEECC | 29.09 | - | |
38 | Phosphorylation | AFITGGGSGIGFRIA EEEECCCCCHHHHHH | 30.43 | 22210691 | |
59 | Phosphorylation | GCHTVIASRSLPRVL CCEEEEECCCHHHHH | 15.98 | 20068231 | |
61 | Phosphorylation | HTVIASRSLPRVLTA EEEEECCCHHHHHHH | 39.98 | 20068231 | |
67 | Phosphorylation | RSLPRVLTAARKLAG CCHHHHHHHHHHHCC | 18.53 | - | |
94 | Sulfoxidation | VRAPPAVMAAVDQAL CCCCHHHHHHHHHHH | 1.84 | 21406390 | |
138 | Phosphorylation | KTVMDIDTSGTFNVS CEEEEECCCCCCCHH | 29.41 | 20068231 | |
139 | Phosphorylation | TVMDIDTSGTFNVSR EEEEECCCCCCCHHH | 31.89 | 20068231 | |
141 | Phosphorylation | MDIDTSGTFNVSRVL EEECCCCCCCHHHHH | 16.29 | 20068231 | |
145 | Phosphorylation | TSGTFNVSRVLYEKF CCCCCCHHHHHHHHH | 20.13 | 20068231 | |
151 | 2-Hydroxyisobutyrylation | VSRVLYEKFFRDHGG HHHHHHHHHHHHCCC | 35.92 | - | |
151 | Acetylation | VSRVLYEKFFRDHGG HHHHHHHHHHHHCCC | 35.92 | 19608861 | |
226 | Phosphorylation | RLGGPQASLSTKVTA HHCCCCCCCCCCCCC | 20.01 | 23312004 | |
228 | Phosphorylation | GGPQASLSTKVTASP CCCCCCCCCCCCCHH | 24.56 | 20068231 | |
229 | Phosphorylation | GPQASLSTKVTASPL CCCCCCCCCCCCHHH | 34.52 | 20068231 | |
230 | Malonylation | PQASLSTKVTASPLQ CCCCCCCCCCCHHHH | 33.92 | 26320211 | |
230 | Acetylation | PQASLSTKVTASPLQ CCCCCCCCCCCHHHH | 33.92 | 25953088 | |
232 | Phosphorylation | ASLSTKVTASPLQRL CCCCCCCCCHHHHHC | 23.99 | - | |
234 | Phosphorylation | LSTKVTASPLQRLGN CCCCCCCHHHHHCCC | 19.44 | 20068231 | |
287 | Phosphorylation | KGLPDFASFSAKL-- CCCCCHHHHHCCC-- | 21.52 | 30266825 | |
289 | Phosphorylation | LPDFASFSAKL---- CCCHHHHHCCC---- | 23.23 | 30266825 | |
291 | Acetylation | DFASFSAKL------ CHHHHHCCC------ | 54.23 | 19608861 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DECR2_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
A4_HUMAN | APP | physical | 21832049 | |
EP300_HUMAN | EP300 | physical | 21988832 | |
SESD1_HUMAN | SESTD1 | physical | 26186194 | |
SESD1_HUMAN | SESTD1 | physical | 28514442 |
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. |
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Acetylation | |
Reference | PubMed |
"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 | |
Reference | PubMed |
"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. |