TRPV1_HUMAN - dbPTM
TRPV1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPV1_HUMAN
UniProt AC Q8NER1
Protein Name Transient receptor potential cation channel subfamily V member 1
Gene Name TRPV1
Organism Homo sapiens (Human).
Sequence Length 839
Subcellular Localization Cell junction, synapse, postsynaptic cell membrane
Multi-pass membrane protein . Cell projection, dendritic spine membrane
Multi-pass membrane protein . Cell membrane
Multi-pass membrane protein . Mostly, but not exclusively expressed in postsy
Protein Description Ligand-activated non-selective calcium permeant cation channel involved in detection of noxious chemical and thermal stimuli. Seems to mediate proton influx and may be involved in intracellular acidosis in nociceptive neurons. Involved in mediation of inflammatory pain and hyperalgesia. Sensitized by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases, which involves PKC isozymes and PCL. Activation by vanilloids, like capsaicin, and temperatures higher than 42 degrees Celsius, exhibits a time- and Ca(2+)-dependent outward rectification, followed by a long-lasting refractory state. Mild extracellular acidic pH (6.5) potentiates channel activation by noxious heat and vanilloids, whereas acidic conditions (pH <6) directly activate the channel. Can be activated by endogenous compounds, including 12-hydroperoxytetraenoic acid and bradykinin. Acts as ionotropic endocannabinoid receptor with central neuromodulatory effects. Triggers a form of long-term depression (TRPV1-LTD) mediated by the endocannabinoid anandamine in the hippocampus and nucleus accumbens by affecting AMPA receptors endocytosis..
Protein Sequence MKKWSSTDLGAAADPLQKDTCPDPLDGDPNSRPPPAKPQLSTAKSRTRLFGKGDSEEAFPVDCPHEEGELDSCPTITVSPVITIQRPGDGPTGARLLSQDSVAASTEKTLRLYDRRSIFEAVAQNNCQDLESLLLFLQKSKKHLTDNEFKDPETGKTCLLKAMLNLHDGQNTTIPLLLEIARQTDSLKELVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAAHGDFFKKTKGRPGFYFGELPLSLAACTNQLGIVKFLLQNSWQTADISARDSVGNTVLHALVEVADNTADNTKFVTSMYNEILMLGAKLHPTLKLEELTNKKGMTPLALAAGTGKIGVLAYILQREIQEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFLVYCLYMIIFTMAAYYRPVDGLPPFKMEKTGDYFRVTGEILSVLGGVYFFFRGIQYFLQRRPSMKTLFVDSYSEMLFFLQSLFMLATVVLYFSHLKEYVASMVFSLALGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYIVFLFGFSTAVVTLIEDGKNDSLPSESTSHRWRGPACRPPDSSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGYTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSSRVSGRHWKNFALVPLLREASARDRQSAQPEEVYLRQFSGSLKPEDAEVFKSPAASGEK
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
5Phosphorylation---MKKWSSTDLGAA
---CCCCCCCCCCCC		32.04-
6Phosphorylation--MKKWSSTDLGAAA
--CCCCCCCCCCCCC		25.48-
7Phosphorylation-MKKWSSTDLGAAAD
-CCCCCCCCCCCCCC		29.72-
117PhosphorylationLRLYDRRSIFEAVAQ
HHHHHHHHHHHHHHH		32.3018701070
121 (in isoform 3)Phosphorylation-7.3822210691
122 (in isoform 3)Phosphorylation-4.4222210691
132PhosphorylationNNCQDLESLLLFLQK
CCCCCHHHHHHHHHH		31.4518452278
140PhosphorylationLLLFLQKSKKHLTDN
HHHHHHHHHHCCCCC		33.69-
145PhosphorylationQKSKKHLTDNEFKDP
HHHHHCCCCCCCCCC		36.1814523239
161AcetylationTGKTCLLKAMLNLHD
HHHHHHHHHHHCCCC		20.8520167786
184PhosphorylationLLEIARQTDSLKELV
HHHHHHCCCCHHHHH		23.2323663014
186PhosphorylationEIARQTDSLKELVNA
HHHHCCCCHHHHHHH		44.7423663014
194PhosphorylationLKELVNASYTDSYYK
HHHHHHHHCCCCCCC		24.3023663014
195PhosphorylationKELVNASYTDSYYKG
HHHHHHHCCCCCCCC		16.5023663014
196PhosphorylationELVNASYTDSYYKGQ
HHHHHHCCCCCCCCC		18.9023663014
198PhosphorylationVNASYTDSYYKGQTA
HHHHCCCCCCCCCCH		23.6723663014
199PhosphorylationNASYTDSYYKGQTAL
HHHCCCCCCCCCCHH		16.4123663014
200PhosphorylationASYTDSYYKGQTALH
HHCCCCCCCCCCHHH		16.7623663014
219PhosphorylationRRNMALVTLLVENGA
HHCEEEEEEEHHCCC		18.4127174698
310PhosphorylationTKFVTSMYNEILMLG
CHHHHHHHHHHHHHH		14.9218083107
336PhosphorylationLTNKKGMTPLALAAG
HCCCCCCCHHHHHHC		24.6624719451
371PhosphorylationRHLSRKFTEWAYGPV
HHHHHHHHHHHHCCC		33.3824719451
383PhosphorylationGPVHSSLYDLSCIDT
CCCCCHHHCCCCCCC		19.4524719451
390PhosphorylationYDLSCIDTCEKNSVL
HCCCCCCCCCCCCEE		11.5824719451
495PhosphorylationFFFRGIQYFLQRRPS
HHHHHHHHHHHHCCC		12.3425348772
502PhosphorylationYFLQRRPSMKTLFVD
HHHHHCCCCCEECCC		30.9718701070
565PhosphorylationGFQQMGIYAVMIEKM
CHHHHCHHHHHHHHH		6.3423401153
604N-linked_GlycosylationTLIEDGKNDSLPSES
HHHHCCCCCCCCCCC		50.02UniProtKB CARBOHYD
705PhosphorylationWKLQRAITILDTEKS
HHHHHHHHHHHCHHH		17.9514630912
712PhosphorylationTILDTEKSFLKCMRK
HHHHCHHHHHHHHHH		29.5824719451
773PhosphorylationNCEGVKRTLSFSLRS
CCCCCCEEEEEEECC		22.4929759185
775PhosphorylationEGVKRTLSFSLRSSR
CCCCEEEEEEECCCC		16.5114523239
777PhosphorylationVKRTLSFSLRSSRVS
CCEEEEEEECCCCCC		21.3524719451
780PhosphorylationTLSFSLRSSRVSGRH
EEEEEECCCCCCCCC		27.9929759185
781PhosphorylationLSFSLRSSRVSGRHW
EEEEECCCCCCCCCH		30.2129759185
784PhosphorylationSLRSSRVSGRHWKNF
EECCCCCCCCCHHCE		29.0629759185
801PhosphorylationVPLLREASARDRQSA
HHHHHHHHHHHHHHC		21.0518701070
807PhosphorylationASARDRQSAQPEEVY
HHHHHHHHCCCHHHH		29.75-
814PhosphorylationSAQPEEVYLRQFSGS
HCCCHHHHHHHHCCC		10.23-
821PhosphorylationYLRQFSGSLKPEDAE
HHHHHCCCCCHHHCH		31.8314523239
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
117SPhosphorylationKinasePKA-Uniprot
117SPhosphorylationKinasePKD-Uniprot
145TPhosphorylationKinasePKA-Uniprot
200YPhosphorylationKinaseSRCP12931
PSP
371TPhosphorylationKinasePKA-Uniprot
502SPhosphorylationKinasePRKACAP17612
GPS
502SPhosphorylationKinasePRKCAP17252
GPS
502SPhosphorylationKinasePRKCEQ02156
Uniprot
705TPhosphorylationKinasePRKCBP05771-2
GPS
801SPhosphorylationKinasePRKCAP17252
GPS
801SPhosphorylationKinasePRKCEQ02156
Uniprot
801SPhosphorylationKinasePRKCZQ05513
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
117SPhosphorylation

-
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 TRPV1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYT9_HUMANSYT9physical
15066994
SNAPN_HUMANSNAPINphysical
15066994
TRPV1_HUMANTRPV1physical
11358970
OS9_HUMANOS9physical
17932042
EGFR_HUMANEGFRphysical
19155296
CBL_HUMANCBLphysical
19155296
AKAP5_HUMANAKAP5physical
18701070
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
D00250 Capsaicin (JAN/USP); Zostrix (TN)
D05249 Olvanil (USAN)
D06388 Zucapsaicin (USAN/INN)
D08282 Nonivamide (INN); Nonanoic acid vanillylamide; Hansaplast (TN)
D10370 Mavatrep (USAN)
DrugBank
DB00132Alpha-Linolenic Acid
DB00168Aspartame
DB00159Icosapent
Regulatory Network of TRPV1_HUMAN

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Related Literatures of Post-Translational Modification

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