OPRK_HUMAN - dbPTM
OPRK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OPRK_HUMAN
UniProt AC P41145
Protein Name Kappa-type opioid receptor
Gene Name OPRK1
Organism Homo sapiens (Human).
Sequence Length 380
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description G-protein coupled opioid receptor that functions as receptor for endogenous alpha-neoendorphins and dynorphins, but has low affinity for beta-endorphins. Also functions as receptor for various synthetic opioids and for the psychoactive diterpene salvinorin A. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain. Plays a role in mediating reduced physical activity upon treatment with synthetic opioids. Plays a role in the regulation of salivation in response to synthetic opioids. May play a role in arousal and regulation of autonomic and neuroendocrine functions..
Protein Sequence MDSPIQIFRGEPGPTCAPSACLPPNSSAWFPGWAEPDSNGSAGSEDAQLEPAHISPAIPVIITAVYSVVFVVGLVGNSLVMFVIIRYTKMKTATNIYIFNLALADALVTTTMPFQSTVYLMNSWPFGDVLCKIVISIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPLKAKIINICIWLLSSSVGISAIVLGGTKVREDVDVIECSLQFPDDDYSWWDLFMKICVFIFAFVIPVLIIIVCYTLMILRLKSVRLLSGSREKDRNLRRITRLVLVVVAVFVVCWTPIHIFILVEALGSTSHSTAALSSYYFCIALGYTNSSLNPILYAFLDENFKRCFRDFCFPLKMRMERQSTSRVRNTVQDPAYLRDIDGMNKPV
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
25N-linked_GlycosylationPSACLPPNSSAWFPG
CCCCCCCCCCCCCCC		46.8117711303
39N-linked_GlycosylationGWAEPDSNGSAGSED
CCCCCCCCCCCCCCC		56.6817711303
136PhosphorylationVLCKIVISIDYYNMF
HHHHHHEEECHHHCH		9.8625072903
139PhosphorylationKIVISIDYYNMFTSI
HHHEEECHHHCHHHH		8.6225072903
140PhosphorylationIVISIDYYNMFTSIF
HHEEECHHHCHHHHH		9.0825072903
144PhosphorylationIDYYNMFTSIFTLTM
ECHHHCHHHHHHHHC		15.3325072903
145PhosphorylationDYYNMFTSIFTLTMM
CHHHCHHHHHHHHCC		12.3925072903
148PhosphorylationNMFTSIFTLTMMSVD
HCHHHHHHHHCCCCC		21.4625072903
150PhosphorylationFTSIFTLTMMSVDRY
HHHHHHHHCCCCCHH		14.0525072903
153PhosphorylationIFTLTMMSVDRYIAV
HHHHHCCCCCHHHHH		15.2825072903
157PhosphorylationTMMSVDRYIAVCHPV
HCCCCCHHHHHCCCC		6.70-
260PhosphorylationLKSVRLLSGSREKDR
HHHHHHHCCCCHHHH		39.04-
262PhosphorylationSVRLLSGSREKDRNL
HHHHHCCCCHHHHHH		33.61-
338UbiquitinationAFLDENFKRCFRDFC
HHHCHHHHHHHHHHH		60.8918212250
345S-palmitoylationKRCFRDFCFPLKMRM
HHHHHHHHHHHHHHH		3.93-
349UbiquitinationRDFCFPLKMRMERQS
HHHHHHHHHHHHHCC		25.381821225
358PhosphorylationRMERQSTSRVRNTVQ
HHHHCCCHHHHHHCC		33.7418212250
363PhosphorylationSTSRVRNTVQDPAYL
CCHHHHHHCCCHHHH		14.69-
378UbiquitinationRDIDGMNKPV-----
HCCCCCCCCC-----		37.96-
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
358SPhosphorylationKinaseGRK1Q15835
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OPRK_HUMAN !!
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 OPRK_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHRF1_HUMANSLC9A3R1physical
15070904
NHRF1_HUMANSLC9A3R1physical
12004055
GASP1_HUMANGPRASP1physical
15086532
AUP1_HUMANAUP1physical
23840749
CXA4_HUMANGJA4physical
23840749
DOK4_HUMANDOK4physical
23840749
SIAH1_HUMANSIAH1physical
23840749
SIAH2_HUMANSIAH2physical
23840749
VAPA_HUMANVAPAphysical
23840749
WLS_HUMANWLSphysical
23840749
GBRL1_HUMANGABARAPL1physical
19001416
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
D00498 Pentazocine (JP16/USP/INN); Fortral (TN)
D00836 Buprenorphine hydrochloride (JP16/USP); Buprenex (TN)
D00837 Butorphanol tartrate (JAN/USP); Stadol (TN)
D00838 Dezocine (USAN); Dalgan (TN)
D00843 Nalbuphine hydrochloride (USAN); Nubain (TN)
D01340 Naloxone hydrochloride (JP16/USP); Narcan (TN)
D01879 Eptazocine hydrobromide (JAN); Sedapain (TN)
D02095 Naltrexone hydrochloride (USP); ReVia (TN)
D02104 Nalmefene hydrochloride; Revex (TN)
D02111 Pentazocine lactate (USP); Talwin (TN)
D02227 Pentazocine hydrochloride (JAN/USP); Sosegon (TN); Talacen (TN)
D02238 Levallorphan tartrate (JP16); Lorfan (TN)
D03197 Butorphanol (USAN/INN)
D03618 Cyclazocine (USAN/INN)
D04649 Ketazocine (USAN/INN); Ketocyclazocine
D04924 Meptazinol hydrochloride (USAN)
D05111 Nalmefene (USAN/INN); Selincro (TN)
D05113 Naltrexone (USAN/INN); Vivitrol (TN)
D05667 Quadazocine mesylate (USAN)
D05907 Spiradoline mesylate (USAN)
D06395 Enadoline hydrochloride (USAN)
D06405 Nalfurafine hydrochloride (JAN)
D06618 Methylnaltrexone bromide (USAN); Relistor (TN)
D07132 Buprenorphine (JAN/INN); Temgesic (TN)
D07863 Diprenorphine (INN)
D07864 Diprenorphine hydrochloride; Large Animal Revivon (TN)
D07904 Eptazocine (INN)
D07937 Etorphine (INN)
D08182 Meptazinol (INN)
D08246 Nalbuphine (INN); Intapan (TN)
D08249 Naloxone (INN); DBL Naloxone (TN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OPRK_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"N-glycosylation of the human kappa opioid receptor enhances itsstability but slows its trafficking along the biosynthesis pathway.";
Li J.G., Chen C., Liu-Chen L.Y.;
Biochemistry 46:10960-10970(2007).
Cited for: GLYCOSYLATION AT ASN-25 AND ASN-39.

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