Protein detail

PI2R

Prostacyclin receptor (Prostaglandin I2 receptor) (PGI receptor) (PGI2 receptor) (Prostanoid IP receptor)

Protein symbol
PI2R
UniProt ID
EVMP score
0.25
Frequency
1
Transmembrane count
7
Protein classification
Basic Information
Protein Names
Prostacyclin receptor (Prostaglandin I2 receptor) (PGI receptor) (PGI2 receptor) (Prostanoid IP receptor)
Protein Function
  • FDA approved drug targets:Small molecule drugs
  • Predicted intracellular proteins
  • G-protein coupled receptors:GPCRs excl olfactory receptors
Transmembrane
17..38; Helical; Name=1; 52..76; Helical; Name=2; 95..115; Helical; Name=3; 135..158; Helical; Name=4; 182..208; Helical; Name=5; 236..260; Helical; Name=6; 275..295; Helical; Name=7
Transmembrane Count
7
Entrez Gene Symbol
Frequency
1
EVMP Score
0.25
Fluorescence & Localization
Tissue Specificheart muscleCell SpecificCardiomyocytesSingle-Nuclei Brain Specificdeep-layer corticothalamic and 6b
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

1 record.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
PTGIRPRKCAP17252S328phosphorylationPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPSIGNORProtMapperKEAphosphoELMSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:9722557phosphoELM:9722557KEA:9722557SIGNOR:9722557

Ligand-Receptor Signaling

52 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
receptorreceptorHGNCNoYesNoYesNo
transmembranetransmembrane_predictedPhobiusNoNoNoYesNo
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Regulatory Interaction Network

7 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
PI2RP43119GNAS3O95467YesYesNoSIGNORHPRDHINTBioGRIDLit-BM-17BioGRID:11895442HINT:38335293HPRD:12488443HINT:16460020BioGRID:16114876SIGNOR:31160049HINT:16114876Lit-BM-17:16114876Lit-BM-17:16352729Lit-BM-17:11895442Lit-BM-17:16460020HINT:16352729BioGRID:16352729HINT:12488443BioGRID:16460020
PI2RP43119ALEXP84996YesYesNoSIGNORHPRDHINTBioGRIDLit-BM-17BioGRID:11895442HINT:38335293HPRD:12488443HINT:16460020BioGRID:16114876SIGNOR:31160049HINT:16114876Lit-BM-17:16114876Lit-BM-17:16352729Lit-BM-17:11895442Lit-BM-17:16460020HINT:16352729BioGRID:16352729HINT:12488443BioGRID:16460020
PI2RP43119GNAS2P63092YesYesNoSIGNORHPRDHINTBioGRIDLit-BM-17BioGRID:11895442HINT:38335293HPRD:12488443HINT:16460020BioGRID:16114876SIGNOR:31160049HINT:16114876Lit-BM-17:16114876Lit-BM-17:16352729Lit-BM-17:11895442Lit-BM-17:16460020HINT:16352729BioGRID:16352729HINT:12488443BioGRID:16460020
PI2RP43119GNAS1Q5JWF2YesYesNoSIGNORHPRDHINTBioGRIDLit-BM-17BioGRID:11895442HINT:38335293HPRD:12488443HINT:16460020BioGRID:16114876SIGNOR:31160049HINT:16114876Lit-BM-17:16114876Lit-BM-17:16352729Lit-BM-17:11895442Lit-BM-17:16460020HINT:16352729BioGRID:16352729HINT:12488443BioGRID:16460020
PI2RP43119GNAQP50148YesYesNoHPRDHINTSIGNORSIGNOR:31160049HINT:11443126HPRD:11443126HPRD:10446129HINT:10446129
KPCAP17252PI2RP43119YesNoNoPhosphoNetworksphosphoELM_MIMPPhosphoSite_MIMPMIMPHPRD_MIMPiPTMnetPhosphoPointSIGNORProtMapperHPRDPhosphoSite_KEAKEAphosphoELM_KEAHPRD_KEAphosphoELMSIGNOR_ProtMapperPhosphoSitePhosphoSite_ProtMapperProtMapper:9722557phosphoELM:9722557PhosphoSite:12016224KEA:9722557HPRD:9722557SIGNOR:9722557PhosphoSite:9722557
PI2RP43119GNALP38405YesYesNoSIGNORSIGNOR:31160049

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Size Exclusion ChromatographyMass spectrometry138938674
Sequence, Structure & Domains

Sequences

Length
386
Mass
40,956
Sequence
MADSCRNLTYVRGSVGPATSTLMFVAGVVGNGLALGILSARRPARPSAFAVLVTGLAATDLLGTSFLSPAVFVAYARNSSLLGLARGGPALCDAFAFAMTFFGLASMLILFAMAVERCLALSHPYLYAQLDGPRCARLALPAIYAFCVLFCALPLLGLGQHQQYCPGSWCFLRMRWAQPGGAAFSLAYAGLVALLVAAIFLCNGSVTLSLCRMYRQQKRHQGSLGPRPRTGEDEVDHLILLALMTVVMAVCSLPLTIRCFTQAVAPDSSSEMGDLLAFRFYAFNPILDPWVFILFRKAVFQRLKLWVCCLCLGPAHGDSQTPLSQLASGRRDPRAPSAPVGKEGSCVPLSAWGEGQVEPLPPTQQSSGSAVGTSSKAEASVACSLC

3D Structural Models

Turn
81..87; 293..295
Helix
18..38; 48..77; 90..121; 124..129; 132..152; 154..156; 179..220; 233..264; 275..292; 297..312
Beta Strand
42..44; 161..163; 165..168; 170..172
3D Structure
Electron microscopy (2)

Domain & Motif Annotations

Compositional Bias
363..376; Polar residues
Region
322..376; Disordered
Protein Families
G-protein coupled receptor 1 family
Sequence Similarities
Belongs to the G-protein coupled receptor 1 family.
Clinical Relevance