PAR2_HUMAN - dbPTM
PAR2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PAR2_HUMAN
UniProt AC P55085
Protein Name Proteinase-activated receptor 2
Gene Name F2RL1
Organism Homo sapiens (Human).
Sequence Length 397
Subcellular Localization Cell membrane
Multi-pass membrane protein.
Protein Description Receptor for trypsin and trypsin-like enzymes coupled to G proteins. [PubMed: 28445455 Its function is mediated through the activation of several signaling pathways including phospholipase C (PLC), intracellular calcium, mitogen-activated protein kinase (MAPK), I-kappaB kinase/NF-kappaB and Rho]
Protein Sequence MRSPSAAWLLGAAILLAASLSCSGTIQGTNRSSKGRSLIGKVDGTSHVTGKGVTVETVFSVDEFSASVLTGKLTTVFLPIVYTIVFVVGLPSNGMALWVFLFRTKKKHPAVIYMANLALADLLSVIWFPLKIAYHIHGNNWIYGEALCNVLIGFFYGNMYCSILFMTCLSVQRYWVIVNPMGHSRKKANIAIGISLAIWLLILLVTIPLYVVKQTIFIPALNITTCHDVLPEQLLVGDMFNYFLSLAIGVFLFPAFLTASAYVLMIRMLRSSAMDENSEKKRKRAIKLIVTVLAMYLICFTPSNLLLVVHYFLIKSQGQSHVYALYIVALCLSTLNSCIDPFVYYFVSHDFRDHAKNALLCRSVRTVKQMQVSLTSKKHSRKSSSYSSSSTTVKTSY
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
27UbiquitinationLSCSGTIQGTNRSSK
HHCCCCCCCCCCCCC		53.1222817900
30N-linked_GlycosylationSGTIQGTNRSSKGRS
CCCCCCCCCCCCCCE		48.9712171601
37PhosphorylationNRSSKGRSLIGKVDG
CCCCCCCEEEEEECC		32.7623401153
41UbiquitinationKGRSLIGKVDGTSHV
CCCEEEEEECCCCCC		30.1121906983
45O-linked_GlycosylationLIGKVDGTSHVTGKG
EEEEECCCCCCCCCC		15.9355824547
46O-linked_GlycosylationIGKVDGTSHVTGKGV
EEEECCCCCCCCCCE		22.8455824551
49O-linked_GlycosylationVDGTSHVTGKGVTVE
ECCCCCCCCCCEEEE		27.9655824555
54O-linked_GlycosylationHVTGKGVTVETVFSV
CCCCCCEEEEEEEEH		22.6955824561
222N-linked_GlycosylationTIFIPALNITTCHDV
CCCEECCCCEECCCC		31.5012171601
222N-linked_GlycosylationTIFIPALNITTCHDV
CCCEECCCCEECCCC		31.5012171601
266UbiquitinationASAYVLMIRMLRSSA
HHHHHHHHHHHHHCC		1.7327667366
280UbiquitinationAMDENSEKKRKRAIK
CCCCCCHHHHHHHHH		58.6733845483
342UbiquitinationLNSCIDPFVYYFVSH
HHHCCCHHHHHHHCC		4.9727667366
354UbiquitinationVSHDFRDHAKNALLC
HCCCCHHHHHHHHHH		34.0521890473
356UbiquitinationHDFRDHAKNALLCRS
CCCHHHHHHHHHHCH		39.0627667366
361S-palmitoylationHAKNALLCRSVRTVK
HHHHHHHHCHHHHHH		2.9521627585
363UbiquitinationKNALLCRSVRTVKQM
HHHHHHCHHHHHHEE		18.2422817900
364UbiquitinationNALLCRSVRTVKQMQ
HHHHHCHHHHHHEEE		2.8422817900
366PhosphorylationLLCRSVRTVKQMQVS
HHHCHHHHHHEEEEE		29.8729083192
368UbiquitinationCRSVRTVKQMQVSLT
HCHHHHHHEEEEEEC		39.1721890473
368UbiquitinationCRSVRTVKQMQVSLT
HCHHHHHHEEEEEEC		39.1727667366
373PhosphorylationTVKQMQVSLTSKKHS
HHHEEEEEECCCCCC		14.7223401153
375PhosphorylationKQMQVSLTSKKHSRK
HEEEEEECCCCCCCC		30.8726329039
376PhosphorylationQMQVSLTSKKHSRKS
EEEEEECCCCCCCCC		45.0326329039
377UbiquitinationMQVSLTSKKHSRKSS
EEEEECCCCCCCCCC		49.6327667366
378UbiquitinationQVSLTSKKHSRKSSS
EEEECCCCCCCCCCC		46.7222817900
380UbiquitinationSLTSKKHSRKSSSYS
EECCCCCCCCCCCCC		50.7327667366
380PhosphorylationSLTSKKHSRKSSSYS
EECCCCCCCCCCCCC		50.7322817900
382UbiquitinationTSKKHSRKSSSYSSS
CCCCCCCCCCCCCCC		58.6722817900
383PhosphorylationSKKHSRKSSSYSSSS
CCCCCCCCCCCCCCC		24.3328152594
384PhosphorylationKKHSRKSSSYSSSST
CCCCCCCCCCCCCCC		36.0127273156
385PhosphorylationKHSRKSSSYSSSSTT
CCCCCCCCCCCCCCE		35.8028152594
386PhosphorylationHSRKSSSYSSSSTTV
CCCCCCCCCCCCCEE		17.9628152594
387PhosphorylationSRKSSSYSSSSTTVK
CCCCCCCCCCCCEEE		26.2020363803
388PhosphorylationRKSSSYSSSSTTVKT
CCCCCCCCCCCEEEC		21.7828152594
389PhosphorylationKSSSYSSSSTTVKTS
CCCCCCCCCCEEECC		26.2628152594
390PhosphorylationSSSYSSSSTTVKTSY
CCCCCCCCCEEECCC		30.0020363803
391PhosphorylationSSYSSSSTTVKTSY-
CCCCCCCCEEECCC-		37.2428152594
392PhosphorylationSYSSSSTTVKTSY--
CCCCCCCEEECCC--		23.1928152594
394UbiquitinationSSSSTTVKTSY----
CCCCCEEECCC----		29.6621906983
397PhosphorylationSTTVKTSY-------
CCEEECCC-------		28.01-
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 ligaseCBLP22681
PMID:15708858
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of PAR2_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 PAR2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CSN5_HUMANCOPS5physical
16410250
BIRC5_HUMANBIRC5physical
20826780
GEMI4_HUMANGEMIN4physical
26186194
ZW10_HUMANZW10physical
26186194
SLMAP_HUMANSLMAPphysical
26186194
RINT1_HUMANRINT1physical
26186194
GEMI6_HUMANGEMIN6physical
26186194
SLMAP_HUMANSLMAPphysical
28514442
HSDL2_HUMANHSDL2physical
28514442
INT12_HUMANINTS12physical
28514442
CS025_HUMANC19orf25physical
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
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PAR2_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycosylation of human proteinase-activated receptor-2 (hPAR2): rolein cell surface expression and signalling.";
Compton S.J., Sandhu S., Wijesuriya S.J., Hollenberg M.D.;
Biochem. J. 368:495-505(2002).
Cited for: GLYCOSYLATION AT ASN-30 AND ASN-222, AND MUTAGENESIS OF ASN-30 ANDASN-222.
Palmitoylation
ReferencePubMed
"Palmitoylation of human proteinase-activated receptor-2differentially regulates receptor triggered ERK1/2 activation, calciumsignalling, and endocytosis.";
Botham A., Guo X., Xiao Y.P., Morice A.H., Compton S.J.,Sadofsky L.R.;
Biochem. J. 438:359-367(2011).
Cited for: PALMITOYLATION AT CYS-361.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373, AND MASSSPECTROMETRY.

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