PI2R_HUMAN - dbPTM
PI2R_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PI2R_HUMAN
UniProt AC P43119
Protein Name Prostacyclin receptor
Gene Name PTGIR
Organism Homo sapiens (Human).
Sequence Length 386
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Receptor for prostacyclin (prostaglandin I2 or PGI2). The activity of this receptor is mediated by G(s) proteins which activate adenylate cyclase..
Protein Sequence MADSCRNLTYVRGSVGPATSTLMFVAGVVGNGLALGILSARRPARPSAFAVLVTGLAATDLLGTSFLSPAVFVAYARNSSLLGLARGGPALCDAFAFAMTFFGLASMLILFAMAVERCLALSHPYLYAQLDGPRCARLALPAIYAFCVLFCALPLLGLGQHQQYCPGSWCFLRMRWAQPGGAAFSLAYAGLVALLVAAIFLCNGSVTLSLCRMYRQQKRHQGSLGPRPRTGEDEVDHLILLALMTVVMAVCSLPLTIRCFTQAVAPDSSSEMGDLLAFRFYAFNPILDPWVFILFRKAVFQRLKLWVCCLCLGPAHGDSQTPLSQLASGRRDPRAPSAPVGKEGSCVPLSAWGEGQVEPLPPTQQSSGSAVGTSSKAEASVACSLC
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
7N-linked_Glycosylation-MADSCRNLTYVRGS
-CCCCCCCCCEECCC		40.85UniProtKB CARBOHYD
14PhosphorylationNLTYVRGSVGPATST
CCCEECCCCCCCHHH		17.21-
19PhosphorylationRGSVGPATSTLMFVA
CCCCCCCHHHHHHHC		25.94-
20PhosphorylationGSVGPATSTLMFVAG
CCCCCCHHHHHHHCC		22.96-
39PhosphorylationGLALGILSARRPARP
CHHHHHHHCCCCCCH		20.1524719451
78N-linked_GlycosylationVFVAYARNSSLLGLA
HHHHHHCCCHHHHHH		27.9817660510
245PhosphorylationLILLALMTVVMAVCS
HHHHHHHHHHHHHHC		15.7030206219
252PhosphorylationTVVMAVCSLPLTIRC
HHHHHHHCCCHHHHH		26.8230206219
256PhosphorylationAVCSLPLTIRCFTQA
HHHCCCHHHHHHHHC		12.3930206219
308S-palmitoylationQRLKLWVCCLCLGPA
HHHHHHHHHHHHCCC		0.7112488443
311S-palmitoylationKLWVCCLCLGPAHGD
HHHHHHHHHCCCCCC		2.2912488443
328PhosphorylationTPLSQLASGRRDPRA
CCHHHHHCCCCCCCC		41.2322817900
337PhosphorylationRRDPRAPSAPVGKEG
CCCCCCCCCCCCCCC		44.1922798277
363PhosphorylationQVEPLPPTQQSSGSA
CCCCCCCCCCCCCCC		36.9828270605
366PhosphorylationPLPPTQQSSGSAVGT
CCCCCCCCCCCCCCC		27.1828270605
367PhosphorylationLPPTQQSSGSAVGTS
CCCCCCCCCCCCCCC		32.2228270605
369PhosphorylationPTQQSSGSAVGTSSK
CCCCCCCCCCCCCCH		23.0228270605
373PhosphorylationSSGSAVGTSSKAEAS
CCCCCCCCCCHHHHH		24.1928270605
374PhosphorylationSGSAVGTSSKAEASV
CCCCCCCCCHHHHHH		24.7428270605
375PhosphorylationGSAVGTSSKAEASVA
CCCCCCCCHHHHHHH		35.4028270605
383FarnesylationKAEASVACSLC----
HHHHHHHHCCC----		2.7511895442
383MethylationKAEASVACSLC----
HHHHHHHHCCC----		2.75-
383FarnesylationKAEASVACSLC----
HHHHHHHHCCC----		2.7511895442
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
328SPhosphorylationKinasePRKCAP17252
GPS
328SPhosphorylationKinasePKCAP05696
PSP
328SPhosphorylationKinasePKC-FAMILY-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
308CPalmitoylation

12488443
311CPalmitoylation

12488443
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 PI2R_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PDE6D_HUMANPDE6Dphysical
16527812
RB11A_HUMANRAB11Aphysical
18832025
TA2R_HUMANTBXA2Rphysical
15471868
GNAS3_HUMANGNASphysical
16460020
GNAS2_HUMANGNASphysical
16460020
ALEX_HUMANGNASphysical
16460020
GNAS1_HUMANGNASphysical
16460020
NHRF4_HUMANPDZD3physical
22884631
GNAS3_HUMANGNASphysical
11895442
GNAS2_HUMANGNASphysical
11895442
ALEX_HUMANGNASphysical
11895442
GNAS1_HUMANGNASphysical
11895442
GNAQ_HUMANGNAQphysical
11895442
RAB5A_HUMANRAB5Aphysical
18498773
PI2R_HUMANPTGIRphysical
20522800
TA2R_HUMANTBXA2Rphysical
20522800
GNAS3_HUMANGNASphysical
16114876
GNAS2_HUMANGNASphysical
16114876
ALEX_HUMANGNASphysical
16114876
GNAS1_HUMANGNASphysical
16114876
NHRF3_HUMANPDZK1physical
21653824
RB11A_HUMANRAB11Aphysical
21653824
GHRL_HUMANGHRLphysical
18573679
CALX_HUMANCANXphysical
21223948
PI2R_HUMANPTGIRphysical
15194446
RB11A_HUMANRAB11Aphysical
20395296
RAB5A_HUMANRAB5Aphysical
20395296
GNAS3_HUMANGNASphysical
16352729
GNAS2_HUMANGNASphysical
16352729
ALEX_HUMANGNASphysical
16352729
GNAS1_HUMANGNASphysical
16352729
S12A6_HUMANSLC12A6physical
28514442
SC6A8_HUMANSLC6A8physical
28514442
PKD2_HUMANPKD2physical
28514442
CEGT_HUMANUGCGphysical
28514442
PCD10_HUMANPCDH10physical
28514442
FZD2_HUMANFZD2physical
28514442
ZNT1_HUMANSLC30A1physical
28514442
ANO5_HUMANANO5physical
28514442
CXG1_HUMANGJC1physical
28514442
S15A4_HUMANSLC15A4physical
28514442
B3A2_HUMANSLC4A2physical
28514442
GLMN_HUMANGLMNphysical
28514442
SL9A1_HUMANSLC9A1physical
28514442
PDXD1_HUMANPDXDC1physical
28514442
S12A7_HUMANSLC12A7physical
28514442
XKR8_HUMANXKR8physical
28514442
STK39_HUMANSTK39physical
28514442
DJC18_HUMANDNAJC18physical
28514442
S12A9_HUMANSLC12A9physical
28514442
EDA_HUMANEDAphysical
28514442
XPR1_HUMANXPR1physical
28514442
DPH6_HUMANDPH6physical
28514442
MTX3_HUMANMTX3physical
28514442
CTR2_HUMANSLC7A2physical
28514442
S12A2_HUMANSLC12A2physical
28514442
AT11C_HUMANATP11Cphysical
28514442
PIGN_HUMANPIGNphysical
28514442
CSCL1_HUMANTMEM63Aphysical
28514442
HMDH_HUMANHMGCRphysical
28514442
MFSD8_HUMANMFSD8physical
28514442
GLPK_HUMANGKphysical
28514442
AT2B2_HUMANATP2B2physical
28514442
S29A1_HUMANSLC29A1physical
28514442
DAAF5_HUMANDNAAF5physical
28514442
S47A1_HUMANSLC47A1physical
28514442
CSCL2_HUMANTMEM63Bphysical
28514442
COT2_HUMANNR2F2physical
28514442
LRC8E_HUMANLRRC8Ephysical
28514442
TTYH3_HUMANTTYH3physical
28514442
STEA3_HUMANSTEAP3physical
28514442
T179B_HUMANTMEM179Bphysical
28514442
SNX14_HUMANSNX14physical
28514442
FA8A1_HUMANFAM8A1physical
28514442
YIPF4_HUMANYIPF4physical
28514442
S2546_HUMANSLC25A46physical
28514442
MFAP3_HUMANMFAP3physical
28514442
HSP7C_HUMANHSPA8physical
28514442
ATG9A_HUMANATG9Aphysical
28514442
GPAA1_HUMANGPAA1physical
28514442
GP1BB_HUMANGP1BBphysical
28514442
GCP2_HUMANTUBGCP2physical
28514442
ARL5B_HUMANARL5Bphysical
28514442
VPP1_HUMANATP6V0A1physical
28514442
OSBL8_HUMANOSBPL8physical
28514442
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
D00106 Epoprostenol (USAN/INN); Prostaglandin I2; Prostacyclin; Epoprostenol (TN)
D01188 Pimilprost (JAN/INN)
D01337 Epoprostenol sodium (JAN/USAN); Flolan (TN)
D01385 Ibudilast (JP16/INN); Ketas (TN)
D01551 Beraprost sodium (JP16/USAN); Procylin (TN)
D02048 Clinprost (JAN/INN); TEI 9090; Arteron (TN)
D02720 Beraprost (USAN)
D02721 Iloprost (USAN/INN); Ventavis (TN)
D06213 Treprostinil (JAN/USAN/INN); Remodulin (TN)
D08065 Iloprost tromethamine; Ventavis (TN)
D08628 Treprostinil monosodium salt; Treprostinil sodium; Remodulin (TN)
D09994 Selexipag (JAN/USAN/INN)
D10430 Treprostinil diolamine (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PI2R_HUMAN

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Related Literatures of Post-Translational Modification
Palmitoylation
ReferencePubMed
"Palmitoylation of the human prostacyclin receptor. Functionalimplications of palmitoylation and isoprenylation.";
Miggin S.M., Lawler O.A., Kinsella B.T.;
J. Biol. Chem. 278:6947-6958(2003).
Cited for: PALMITOYLATION AT CYS-308 AND CYS-311, LACK OF PALMITOYLATION ATCYS-309, AND MUTAGENESIS OF CYS-308; CYS-309 AND CYS-311.
Prenylation
ReferencePubMed
"Investigation of a functional requirement for isoprenylation by thehuman prostacyclin receptor.";
Miggin S.M., Lawler O.A., Kinsella B.T.;
Eur. J. Biochem. 269:1714-1725(2002).
Cited for: ISOPRENYLATION AT CYS-383, AND MUTAGENESIS OF CYS-383.

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