UniProt ID | OARD1_HUMAN | |
---|---|---|
UniProt AC | Q9Y530 | |
Protein Name | O-acetyl-ADP-ribose deacetylase 1 | |
Gene Name | OARD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 152 | |
Subcellular Localization | ||
Protein Description | Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.. | |
Protein Sequence | MASSLNEDPEGSRITYVKGDLFACPKTDSLAHCISEDCRMGAGIAVLFKKKFGGVQELLNQQKKSGEVAVLKRDGRYIYYLITKKRASHKPTYENLQKSLEAMKSHCLKNGVTDLSMPRIGCGLDRLQWENVSAMIEEVFEATDIKITVYTL | |
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 | ------MASSLNEDP ------CCCCCCCCC | 22223895 | ||
3 | Phosphorylation | -----MASSLNEDPE -----CCCCCCCCCC | 23401153 | ||
4 | Phosphorylation | ----MASSLNEDPEG ----CCCCCCCCCCC | 25159151 | ||
12 | Phosphorylation | LNEDPEGSRITYVKG CCCCCCCCCEEEEEC | 22199227 | ||
15 | Phosphorylation | DPEGSRITYVKGDLF CCCCCCEEEEECCEE | 23186163 | ||
18 | Acetylation | GSRITYVKGDLFACP CCCEEEEECCEEECC | 26051181 | ||
18 | Ubiquitination | GSRITYVKGDLFACP CCCEEEEECCEEECC | - | ||
26 | Acetylation | GDLFACPKTDSLAHC CCEEECCCCCCHHHH | 26051181 | ||
26 | Ubiquitination | GDLFACPKTDSLAHC CCEEECCCCCCHHHH | - | ||
50 | Acetylation | GIAVLFKKKFGGVQE CEEEEEHHHHCCHHH | 25953088 | ||
51 | Acetylation | IAVLFKKKFGGVQEL EEEEEHHHHCCHHHH | 25953088 | ||
51 | Malonylation | IAVLFKKKFGGVQEL EEEEEHHHHCCHHHH | 26320211 | ||
51 | Ubiquitination | IAVLFKKKFGGVQEL EEEEEHHHHCCHHHH | - | ||
63 | Ubiquitination | QELLNQQKKSGEVAV HHHHHHHCCCCCEEE | - | ||
64 | Ubiquitination | ELLNQQKKSGEVAVL HHHHHHCCCCCEEEE | - | ||
72 | Ubiquitination | SGEVAVLKRDGRYIY CCCEEEEEECCCEEE | - | ||
72 | Acetylation | SGEVAVLKRDGRYIY CCCEEEEEECCCEEE | 25953088 | ||
79 | Phosphorylation | KRDGRYIYYLITKKR EECCCEEEEEEECCC | 21406692 | ||
80 | Phosphorylation | RDGRYIYYLITKKRA ECCCEEEEEEECCCC | 21406692 | ||
83 | Phosphorylation | RYIYYLITKKRASHK CEEEEEEECCCCCCC | 21406692 | ||
84 | Acetylation | YIYYLITKKRASHKP EEEEEEECCCCCCCC | 25953088 | ||
90 | Ubiquitination | TKKRASHKPTYENLQ ECCCCCCCCCHHHHH | - | ||
92 | Phosphorylation | KRASHKPTYENLQKS CCCCCCCCHHHHHHH | 29496907 | ||
93 | Phosphorylation | RASHKPTYENLQKSL CCCCCCCHHHHHHHH | 27642862 | ||
98 | Ubiquitination | PTYENLQKSLEAMKS CCHHHHHHHHHHHHH | - | ||
104 | Ubiquitination | QKSLEAMKSHCLKNG HHHHHHHHHHHHHCC | - | ||
109 | Ubiquitination | AMKSHCLKNGVTDLS HHHHHHHHCCCCCCC | - | ||
109 | Acetylation | AMKSHCLKNGVTDLS HHHHHHHHCCCCCCC | 25953088 |
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 OARD1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of OARD1_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 OARD1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
A4_HUMAN | APP | physical | 21832049 | |
OXSR1_HUMAN | OXSR1 | physical | 26344197 |
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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