OPRX_HUMAN - dbPTM
OPRX_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
21N-linked_GlycosylationYGSHLQGNLSLLSPN
HCCCCCCCCCCCCCC
17.31UniProtKB CARBOHYD
28N-linked_GlycosylationNLSLLSPNHSLLPPH
CCCCCCCCCCCCCHH
33.72UniProtKB CARBOHYD
39N-linked_GlycosylationLPPHLLLNASHGAFL
CCHHHHHHCCCCCCC
39.09UniProtKB CARBOHYD
164PhosphorylationRALDVRTSSKAQAVN
HHHCCCCCCHHHHHH
21.1924719451
165PhosphorylationALDVRTSSKAQAVNV
HHCCCCCCHHHHHHH
31.2524719451
334S-palmitoylationKACFRKFCCASALRR
HHHHHHHHHHHHHHH
1.81-
346PhosphorylationLRRDVQVSDRVRSIA
HHHCCCHHHHHHHHH
11.56-
351PhosphorylationQVSDRVRSIAKDVAL
CHHHHHHHHHHHHHH
24.84-
362PhosphorylationDVALACKTSETVPRP
HHHHHCCCCCCCCCC
31.5125072903
363PhosphorylationVALACKTSETVPRPA
HHHHCCCCCCCCCCC
19.4322596163
365PhosphorylationLACKTSETVPRPA--
HHCCCCCCCCCCC--
35.2625072903

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
346SPhosphorylationKinaseGRK2P25098
PSP
346SPhosphorylationKinaseGRK3P35626
PSP
351SPhosphorylationKinaseGRK2P25098
PSP
351SPhosphorylationKinaseGRK3P35626
PSP
362TPhosphorylationKinaseGRK2P25098
PSP
362TPhosphorylationKinaseGRK3P35626
PSP
363SPhosphorylationKinaseGRK2P25098
PSP
363SPhosphorylationKinaseGRK3P35626
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
363SPhosphorylation

23086955

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 OPRX_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PNOC_HUMANPNOCphysical
10692489
PNOC_HUMANPNOCphysical
11097863
GASP1_HUMANGPRASP1physical
15086532

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OPRX_HUMAN

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Related Literatures of Post-Translational Modification

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