UniProt ID | OPRX_HUMAN | |
---|---|---|
UniProt AC | P41146 | |
Protein Name | Nociceptin receptor | |
Gene Name | OPRL1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 370 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Cytoplasmic vesicle. Ligand binding leads to receptor internalization into cytoplasmic vesicles, decreasing the amount of available receptor at the cell surface. Internalization requires phosphorylation at |
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Protein Description | G-protein coupled opioid receptor that functions as receptor for the endogenous neuropeptide nociceptin. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Signaling via G proteins mediates inhibition of adenylate cyclase activity and calcium channel activity. Arrestins modulate signaling via G proteins and mediate the activation of alternative signaling pathways that lead to the activation of MAP kinases. Plays a role in modulating nociception and the perception of pain. Plays a role in the regulation of locomotor activity by the neuropeptide nociceptin.. | |
Protein Sequence | MEPLFPAPFWEVIYGSHLQGNLSLLSPNHSLLPPHLLLNASHGAFLPLGLKVTIVGLYLAVCVGGLLGNCLVMYVILRHTKMKTATNIYIFNLALADTLVLLTLPFQGTDILLGFWPFGNALCKTVIAIDYYNMFTSTFTLTAMSVDRYVAICHPIRALDVRTSSKAQAVNVAIWALASVVGVPVAIMGSAQVEDEEIECLVEIPTPQDYWGPVFAICIFLFSFIVPVLVISVCYSLMIRRLRGVRLLSGSREKDRNLRRITRLVLVVVAVFVGCWTPVQVFVLAQGLGVQPSSETAVAILRFCTALGYVNSCLNPILYAFLDENFKACFRKFCCASALRRDVQVSDRVRSIAKDVALACKTSETVPRPA | |
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 |
---|---|---|---|---|---|
21 | N-linked_Glycosylation | YGSHLQGNLSLLSPN HCCCCCCCCCCCCCC | 17.31 | UniProtKB CARBOHYD | |
28 | N-linked_Glycosylation | NLSLLSPNHSLLPPH CCCCCCCCCCCCCHH | 33.72 | UniProtKB CARBOHYD | |
39 | N-linked_Glycosylation | LPPHLLLNASHGAFL CCHHHHHHCCCCCCC | 39.09 | UniProtKB CARBOHYD | |
164 | Phosphorylation | RALDVRTSSKAQAVN HHHCCCCCCHHHHHH | 21.19 | 24719451 | |
165 | Phosphorylation | ALDVRTSSKAQAVNV HHCCCCCCHHHHHHH | 31.25 | 24719451 | |
334 | S-palmitoylation | KACFRKFCCASALRR HHHHHHHHHHHHHHH | 1.81 | - | |
346 | Phosphorylation | LRRDVQVSDRVRSIA HHHCCCHHHHHHHHH | 11.56 | - | |
351 | Phosphorylation | QVSDRVRSIAKDVAL CHHHHHHHHHHHHHH | 24.84 | - | |
362 | Phosphorylation | DVALACKTSETVPRP HHHHHCCCCCCCCCC | 31.51 | 25072903 | |
363 | Phosphorylation | VALACKTSETVPRPA HHHHCCCCCCCCCCC | 19.43 | 22596163 | |
365 | Phosphorylation | LACKTSETVPRPA-- HHCCCCCCCCCCC-- | 35.26 | 25072903 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
346 | S | Phosphorylation | Kinase | GRK2 | P25098 | PSP |
346 | S | Phosphorylation | Kinase | GRK3 | P35626 | PSP |
351 | S | Phosphorylation | Kinase | GRK2 | P25098 | PSP |
351 | S | Phosphorylation | Kinase | GRK3 | P35626 | PSP |
362 | T | Phosphorylation | Kinase | GRK2 | P25098 | PSP |
362 | T | Phosphorylation | Kinase | GRK3 | P35626 | PSP |
363 | S | Phosphorylation | Kinase | GRK2 | P25098 | PSP |
363 | S | Phosphorylation | Kinase | GRK3 | P35626 | PSP |
Modified Location | Modified Residue | Modification | Function | Reference |
---|---|---|---|---|
363 | S | Phosphorylation |
| 23086955 |
* 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 OPRX_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
PNOC_HUMAN | PNOC | physical | 10692489 | |
PNOC_HUMAN | PNOC | physical | 11097863 | |
GASP1_HUMAN | GPRASP1 | physical | 15086532 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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