UniProt ID | PDE12_MOUSE | |
---|---|---|
UniProt AC | Q3TIU4 | |
Protein Name | 2',5'-phosphodiesterase 12 | |
Gene Name | Pde12 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 608 | |
Subcellular Localization | Mitochondrion matrix. | |
Protein Description | Enzyme that cleaves 2',5'-phosphodiester bond linking adenosines of the 5'-triphosphorylated oligoadenylates, triphosphorylated oligoadenylates referred as 2-5A modulates the 2-5A system. This enzyme degraded triphosphorylated 2-5A to produce AMP and ATP. Also cleaves 3',5'-phosphodiester bond of oligoadenylates. Plays a role as a negative regulator of the 2-5A system that is one of the major pathways for antiviral and antitumor functions induced by interferon (IFNs) (By similarity).. | |
Protein Sequence | MWRLPGRSALRGVRSVVERRSRAEAGTHEAVRAMERAVVRCVPSEPKLSLSFALADGSHKNMQRDQSEPLGRALSRIATNALKGHAKVAAAKKSRKNRAHSSGGAACEATGPEPVATCEPVVKLYYREEAVAEDVLNVDAWQDGAVLQIGDVKYKVERNPPTFTELQLPRYIMAGFPVCPKLGVEFGDPASSVFRWYKEVKPGAAEPGDSGPASSSHSSQPSAWIETGVDERVYTPCNADIGLRLRLHCTPGNGQRFGPSRELESLCPVEAGPGTCTFDHRHLYTKKVTEDSFIRTVSYNILADTYAQTEFSRTVLYPYCAPYALELDYRQNLIQKELTGYNADLICLQEVDRAVFSDSLVPALEAFGLEGVFRIKQHEGLATFYRKSKFRLLSQHDISFQEALKSDPLHKELLEKLALNPLAQEKVLQRSSVLQISVLQSTTDSSKKICVANTHLYWHPKGGYIRLIQMEVALVHIRHVSRDLYPGIPVIFCGDFNSTPSTGMYHFVISGSIAEDHEDWASNGEEERCSMPLSHCFKLKSACGEPAYTNYVGGFHGCLDYIFIDLNTLEVEQVIPLPSHEEVTTHQALPSVSHPSDHIALVCDLKWK | |
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 |
---|---|---|---|---|---|
75 | Phosphorylation | EPLGRALSRIATNAL CHHHHHHHHHHHHHH | 22.21 | 22817900 | |
101 | Phosphorylation | SRKNRAHSSGGAACE HHHCCCCCCCCCCCC | 29.69 | 25266776 | |
102 | Phosphorylation | RKNRAHSSGGAACEA HHCCCCCCCCCCCCC | 31.23 | 25266776 | |
110 | Phosphorylation | GGAACEATGPEPVAT CCCCCCCCCCCCCCC | 30.86 | 25266776 | |
216 | Phosphorylation | DSGPASSSHSSQPSA CCCCCCCCCCCCCCC | 25.54 | - | |
237 | Glutathionylation | DERVYTPCNADIGLR CCCEECCCCCCCCEE | 5.17 | 24333276 | |
289 | Phosphorylation | HLYTKKVTEDSFIRT CEECCCCCCCCCCCC | 42.84 | 28285833 | |
292 | Phosphorylation | TKKVTEDSFIRTVSY CCCCCCCCCCCCEEH | 19.15 | 28285833 | |
426 | Ubiquitination | LNPLAQEKVLQRSSV CCHHHHHHHHHHCCE | 35.84 | 22790023 | |
426 | Acetylation | LNPLAQEKVLQRSSV CCHHHHHHHHHHCCE | 35.84 | 23806337 |
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 PDE12_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of PDE12_MOUSE !! |
* 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 PDE12_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of PDE12_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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