PAR1_HUMAN - dbPTM
PAR1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAR1_HUMAN
UniProt AC P25116
Protein Name Proteinase-activated receptor 1
Gene Name F2R
Organism Homo sapiens (Human).
Sequence Length 425
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation and in vascular development..
Protein Sequence MGPRRLLLVAACFSLCGPLLSARTRARRPESKATNATLDPRSFLLRNPNDKYEPFWEDEEKNESGLTEYRLVSINKSSPLQKQLPAFISEDASGYLTSSWLTLFVPSVYTGVFVVSLPLNIMAIVVFILKMKVKKPAVVYMLHLATADVLFVSVLPFKISYYFSGSDWQFGSELCRFVTAAFYCNMYASILLMTVISIDRFLAVVYPMQSLSWRTLGRASFTCLAIWALAIAGVVPLLLKEQTIQVPGLNITTCHDVLNETLLEGYYAYYFSAFSAVFFFVPLIISTVCYVSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIICFGPTNVLLIAHYSFLSHTSTTEAAYFAYLLCVCVSSISCCIDPLIYYYASSECQRYVYSILCCKESSDPSSYNSSGQLMASKMDTCSSNLNNSIYKKLLT
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
21PhosphorylationSLCGPLLSARTRARR
HHHHHHHHHHHHHCC		24.3224719451
31PhosphorylationTRARRPESKATNATL
HHHCCCCCCCCCCCC		30.2122210691
35N-linked_GlycosylationRPESKATNATLDPRS
CCCCCCCCCCCCHHH		35.4719349973
35N-linked_GlycosylationRPESKATNATLDPRS
CCCCCCCCCCCCHHH		35.47UniProtKB CARBOHYD
42PhosphorylationNATLDPRSFLLRNPN
CCCCCHHHHHCCCCC		26.1524719451
51UbiquitinationLLRNPNDKYEPFWED
HCCCCCCCCCCCCCC		59.14-
52PhosphorylationLRNPNDKYEPFWEDE
CCCCCCCCCCCCCCH		31.53-
62N-linked_GlycosylationFWEDEEKNESGLTEY
CCCCHHHCCCCCCEE		52.53UniProtKB CARBOHYD
69PhosphorylationNESGLTEYRLVSINK
CCCCCCEEEEEEECC		12.19-
75N-linked_GlycosylationEYRLVSINKSSPLQK
EEEEEEECCCCHHHH		30.56UniProtKB CARBOHYD
212PhosphorylationVYPMQSLSWRTLGRA
HCCCCCCCCCCCHHH		21.5424719451
250N-linked_GlycosylationTIQVPGLNITTCHDV
EECCCCCCEEEHHHH		35.16UniProtKB CARBOHYD
259N-linked_GlycosylationTTCHDVLNETLLEGY
EEHHHHHCHHHHHHH		39.80UniProtKB CARBOHYD
300PhosphorylationIIRCLSSSAVANRSK
HHHHHCCHHHHCCCH		24.3221888424
306PhosphorylationSSAVANRSKKSRALF
CHHHHCCCHHHHHHH		44.2223911959
375PhosphorylationPLIYYYASSECQRYV
HHHHHHHCHHHHHHH		15.568955127
376PhosphorylationLIYYYASSECQRYVY
HHHHHHCHHHHHHHE		33.938955127
383PhosphorylationSECQRYVYSILCCKE
HHHHHHHEEEEEECC		4.8922817900
384PhosphorylationECQRYVYSILCCKES
HHHHHHEEEEEECCC		10.078955127
387S-palmitoylationRYVYSILCCKESSDP
HHHEEEEEECCCCCC		2.7223580642
388S-palmitoylationYVYSILCCKESSDPS
HHEEEEEECCCCCCC		4.9923580642
391PhosphorylationSILCCKESSDPSSYN
EEEEECCCCCCCCCC		26.0723403867
392PhosphorylationILCCKESSDPSSYNS
EEEECCCCCCCCCCC		55.4123403867
395PhosphorylationCKESSDPSSYNSSGQ
ECCCCCCCCCCCHHC		50.9023403867
396PhosphorylationKESSDPSSYNSSGQL
CCCCCCCCCCCHHCH		33.4523403867
397PhosphorylationESSDPSSYNSSGQLM
CCCCCCCCCCHHCHH		24.3323403867
399PhosphorylationSDPSSYNSSGQLMAS
CCCCCCCCHHCHHHH		27.8410413505
400PhosphorylationDPSSYNSSGQLMASK
CCCCCCCHHCHHHHC		27.2410413505
406PhosphorylationSSGQLMASKMDTCSS
CHHCHHHHCCCCCCH		17.9723403867
407UbiquitinationSGQLMASKMDTCSSN
HHCHHHHCCCCCCHH		31.12-
410PhosphorylationLMASKMDTCSSNLNN
HHHHCCCCCCHHCCC		15.7021945579
412PhosphorylationASKMDTCSSNLNNSI
HHCCCCCCHHCCCHH		25.1021945579
413PhosphorylationSKMDTCSSNLNNSIY
HCCCCCCHHCCCHHH		47.7021945579
418PhosphorylationCSSNLNNSIYKKLLT
CCHHCCCHHHHHHCC		26.6521945579
420PhosphorylationSNLNNSIYKKLLT--
HHCCCHHHHHHCC--		11.2421945579
421UbiquitinationNLNNSIYKKLLT---
HCCCHHHHHHCC---		34.96-
422UbiquitinationLNNSIYKKLLT----
CCCHHHHHHCC----		31.58-
425PhosphorylationSIYKKLLT-------
HHHHHHCC-------		47.188955127
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
-KUbiquitinationE3 ubiquitin ligaseNEDD4P46934
PMID:26391660
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAR1_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 PAR1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SNX1_HUMANSNX1physical
12058063
CHM4A_HUMANCHMP4Aphysical
22547407
PDC6I_HUMANPDCD6IPphysical
22547407
GNAQ_HUMANGNAQphysical
8982657
GNAI2_HUMANGNAI2physical
8982657
FLOT2_HUMANFLOT2physical
15492257
AP3D1_HUMANAP3D1physical
22833563
PDC6I_HUMANPDCD6IPphysical
22833563
CAV1_HUMANCAV1physical
17848177
CAV1_HUMANCAV1physical
20826780
EPCR_HUMANPROCRphysical
20826780
ARRD3_HUMANARRDC3physical
26490116
PDC6I_HUMANPDCD6IPphysical
26490116
MK14_HUMANMAPK14physical
26391660
TAB1_HUMANTAB1physical
26391660
TAB2_HUMANTAB2physical
26391660
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
D09765 Vorapaxar (USAN/INN)
D09766 Vorapaxar sulfate (JAN/USAN)
D09866 Atopaxar (USAN)
D09867 Atopaxar hydrobromide (USAN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAR1_HUMAN

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Related Literatures of Post-Translational Modification

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