FPRP_HUMAN - dbPTM
FPRP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FPRP_HUMAN
UniProt AC Q9P2B2
Protein Name Prostaglandin F2 receptor negative regulator
Gene Name PTGFRN
Organism Homo sapiens (Human).
Sequence Length 879
Subcellular Localization Endoplasmic reticulum membrane
Single-pass type I membrane protein. Golgi apparatus, trans-Golgi network membrane
Single-pass type I membrane protein.
Protein Description Inhibits the binding of prostaglandin F2-alpha (PGF2-alpha) to its specific FP receptor, by decreasing the receptor number rather than the affinity constant. Functional coupling with the prostaglandin F2-alpha receptor seems to occur (By similarity)..
Protein Sequence MGRLASRPLLLALLSLALCRGRVVRVPTATLVRVVGTELVIPCNVSDYDGPSEQNFDWSFSSLGSSFVELASTWEVGFPAQLYQERLQRGEILLRRTANDAVELHIKNVQPSDQGHYKCSTPSTDATVQGNYEDTVQVKVLADSLHVGPSARPPPSLSLREGEPFELRCTAASASPLHTHLALLWEVHRGPARRSVLALTHEGRFHPGLGYEQRYHSGDVRLDTVGSDAYRLSVSRALSADQGSYRCIVSEWIAEQGNWQEIQEKAVEVATVVIQPSVLRAAVPKNVSVAEGKELDLTCNITTDRADDVRPEVTWSFSRMPDSTLPGSRVLARLDRDSLVHSSPHVALSHVDARSYHLLVRDVSKENSGYYYCHVSLWAPGHNRSWHKVAEAVSSPAGVGVTWLEPDYQVYLNASKVPGFADDPTELACRVVDTKSGEANVRFTVSWYYRMNRRSDNVVTSELLAVMDGDWTLKYGERSKQRAQDGDFIFSKEHTDTFNFRIQRTTEEDRGNYYCVVSAWTKQRNNSWVKSKDVFSKPVNIFWALEDSVLVVKARQPKPFFAAGNTFEMTCKVSSKNIKSPRYSVLIMAEKPVGDLSSPNETKYIISLDQDSVVKLENWTDASRVDGVVLEKVQEDEFRYRMYQTQVSDAGLYRCMVTAWSPVRGSLWREAATSLSNPIEIDFQTSGPIFNASVHSDTPSVIRGDLIKLFCIITVEGAALDPDDMAFDVSWFAVHSFGLDKAPVLLSSLDRKGIVTTSRRDWKSDLSLERVSVLEFLLQVHGSEDQDFGNYYCSVTPWVKSPTGSWQKEAEIHSKPVFITVKMDVLNAFKYPLLIGVGLSTVIGLLSCLIGYCSSHWCCKKEVQETRRERRRLMSMEMD
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
44N-linked_GlycosylationTELVIPCNVSDYDGP
CEEEEECCCCCCCCC		30.8517960739
150O-linked_GlycosylationDSLHVGPSARPPPSL
CEECCCCCCCCCCCC		30.8655831567
156PhosphorylationPSARPPPSLSLREGE
CCCCCCCCCCCCCCC		36.0417081983
158PhosphorylationARPPPSLSLREGEPF
CCCCCCCCCCCCCCE		29.7117081983
215PhosphorylationGLGYEQRYHSGDVRL
CCCCCCCEECCCEEE		10.46-
233PhosphorylationGSDAYRLSVSRALSA
CCCCEEEEHHHHHCC		14.7324719451
244PhosphorylationALSADQGSYRCIVSE
HHCCCCCCEEEEEEH		12.0824114839
271PhosphorylationEKAVEVATVVIQPSV
HHHHHHEEEEECHHH		22.08-
277PhosphorylationATVVIQPSVLRAAVP
EEEEECHHHHHHHCC		19.8725072903
280MethylationVIQPSVLRAAVPKNV
EECHHHHHHHCCCCE		20.53115489583
286N-linked_GlycosylationLRAAVPKNVSVAEGK
HHHHCCCCEEECCCC		25.8117960739
300N-linked_GlycosylationKELDLTCNITTDRAD
CEEEEEEEEECCCCC		29.4317960739
383N-linked_GlycosylationSLWAPGHNRSWHKVA
EEECCCCCCCHHHHH		45.6717960739
413N-linked_GlycosylationPDYQVYLNASKVPGF
CCEEEEEECCCCCCC		25.2017960739
472PhosphorylationAVMDGDWTLKYGERS
EECCCCCEEECCHHH		20.3620068231
491PhosphorylationQDGDFIFSKEHTDTF
CCCCEEECCCCCCCE		32.1124719451
495PhosphorylationFIFSKEHTDTFNFRI
EEECCCCCCCEEEEE		37.51-
497PhosphorylationFSKEHTDTFNFRIQR
ECCCCCCCEEEEEEE		22.95-
525N-linked_GlycosylationSAWTKQRNNSWVKSK
EEEECCCCCCCCCCH		44.3817960739
531PhosphorylationRNNSWVKSKDVFSKP
CCCCCCCCHHCCCCC		25.19-
566PhosphorylationPFFAAGNTFEMTCKV
CEEECCCEEEEEEEE		21.76-
574PhosphorylationFEMTCKVSSKNIKSP
EEEEEEECCCCCCCC		22.53-
575PhosphorylationEMTCKVSSKNIKSPR
EEEEEECCCCCCCCC		32.48-
580PhosphorylationVSSKNIKSPRYSVLI
ECCCCCCCCCEEEEE		15.7124719451
600N-linked_GlycosylationVGDLSSPNETKYIIS
CCCCCCCCCCEEEEE		72.0817960739
618N-linked_GlycosylationDSVVKLENWTDASRV
CCEEEEECCCCHHHC		58.3417960739
632UbiquitinationVDGVVLEKVQEDEFR
CCCEEEEECCCCCHH		45.0929967540
640PhosphorylationVQEDEFRYRMYQTQV
CCCCCHHHEEECCCC		12.6820068231
643PhosphorylationDEFRYRMYQTQVSDA
CCHHHEEECCCCCCC		10.2220068231
645PhosphorylationFRYRMYQTQVSDAGL
HHHEEECCCCCCCCC		17.2820068231
648PhosphorylationRMYQTQVSDAGLYRC
EEECCCCCCCCCCCH		16.3622210691
653PhosphorylationQVSDAGLYRCMVTAW
CCCCCCCCCHHHEEC		10.8022210691
666PhosphorylationAWSPVRGSLWREAAT
ECCCCCCHHHHHHHH		17.7524719451
691N-linked_GlycosylationQTSGPIFNASVHSDT
ECCCCEEEEEECCCC		31.8317960739
848S-palmitoylationTVIGLLSCLIGYCSS
HHHHHHHHHHHHHHH		3.0329575903
854PhosphorylationSCLIGYCSSHWCCKK
HHHHHHHHHHCHHHH		19.4332142685
875PhosphorylationRERRRLMSMEMD---
HHHHHHHHHCCC---		19.0423927012
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

Oops, there are no upstream regulatory protein records of FPRP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FPRP_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 FPRP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CD82_HUMANCD82physical
11278880
RL6_HUMANRPL6physical
22939629
CD9_HUMANCD9physical
23091066
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FPRP_HUMAN

loading...

Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-286 AND ASN-300, AND MASSSPECTROMETRY.
"Glycosylation status of the membrane protein CD9P-1.";
Andre M., Morelle W., Planchon S., Milhiet P.E., Rubinstein E.,Mollicone R., Chamot-Rooke J., Le Naour F.;
Proteomics 7:3880-3895(2007).
Cited for: GLYCOSYLATION AT ASN-44; ASN-286; ASN-300; ASN-383; ASN-413; ASN-525;ASN-600; ASN-618 AND ASN-691.
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-875, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory