dbPTM

TRPV1_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRPV1_RAT
UniProt AC	O35433
Protein Name	Transient receptor potential cation channel subfamily V member 1
Gene Name	Trpv1
Organism	Rattus norvegicus (Rat).
Sequence Length	838
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.; Isoform 3: Does not display channel activity in response to noxious chemical compounds, such as capsaicin and the vanilloid resiniferatoxin. Channel activity is not elicited by mildly acidic extracellular pH, and only slight channel activity is observed in response to noxiuos heat stimuli..
Protein Sequence	MEQRASLDSEESESPPQENSCLDPPDRDPNCKPPPVKPHIFTTRSRTRLFGKGDSEEASPLDCPYEEGGLASCPIITVSSVLTIQRPGDGPASVRPSSQDSVSAGEKPPRLYDRRSIFDAVAQSNCQELESLLPFLQRSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDVARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMTLVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTVDNTKFVTSMYNEILILGAKLHPTLKLEEITNRKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTAAAYYRPVEGLPPYKLKNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSQRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPMESTPHKCRGSACKPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDYRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHATQQEEVQLKHYTGSLKPEDAEVFKDSMVPGEK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
6	Phosphorylation	--MEQRASLDSEESE --CCCCCCCCCCCCC	34.59	12194871
116	Phosphorylation	PRLYDRRSIFDAVAQ CCCCCHHHHHHHHHH	28.62	15471852
144	Phosphorylation	QRSKKRLTDSEFKDP HHHHCCCCCCCCCCC	41.32	12194871
199	Phosphorylation	ASYTDSYYKGQTALH HHHCCCCCCCCCHHH	16.76	17582331
370	Phosphorylation	RHLSRKFTEWAYGPV HHHHHHHHHHHHCCC	33.38	12194871
406	Phosphorylation	IAYSSSETPNRHDML EEEECCCCCCCCHHE	28.01	17194758
502	Phosphorylation	YFLQRRPSLKSLFVD HHHHHCCCCHHHCCC	46.77	15375192
604	N-linked_Glycosylation	TLIEDGKNNSLPMES HHHHCCCCCCCCCCC	49.18	11683872
616	S-nitrosocysteine	MESTPHKCRGSACKP CCCCCCCCCCCCCCC	5.61	-
616	S-nitrosylation	MESTPHKCRGSACKP CCCCCCCCCCCCCCC	5.61	22178444
621	S-nitrosocysteine	HKCRGSACKPGNSYN CCCCCCCCCCCCCHH	6.14	-
621	S-nitrosylation	HKCRGSACKPGNSYN CCCCCCCCCCCCCHH	6.14	22178444
704	Phosphorylation	WKLQRAITILDTEKS HHHHHHHHHHHCHHH	17.95	14630912
772	Phosphorylation	NCEGVKRTLSFSLRS CCCCCCEEEEEEECC	22.49	28432305
774	Phosphorylation	EGVKRTLSFSLRSGR CCCCEEEEEEECCCC	16.51	12194871
800	Phosphorylation	VPLLRDASTRDRHAT HHHHCCCCCCCCCCC	28.41	18001466
820	Phosphorylation	QLKHYTGSLKPEDAE HHHHHCCCCCHHHCH	25.97	14630912

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
6	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
6	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
116	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
116	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
116	S	Phosphorylation	Kinase	PKD-FAMILY	-	GPS
116	S	Phosphorylation	Kinase	PRKD1	Q9WTQ1	PSP
116	S	Phosphorylation	Kinase	PKD	-	Uniprot
116	S	Phosphorylation	Kinase	PKA	-	Uniprot
144	T	Phosphorylation	Kinase	PRKACA	P00517	GPS
144	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
144	T	Phosphorylation	Kinase	PKA	-	Uniprot
144	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
370	T	Phosphorylation	Kinase	PRKACA	P00517	GPS
370	T	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
370	T	Phosphorylation	Kinase	PKA	-	Uniprot
406	T	Phosphorylation	Kinase	CDK5	Q03114	PSP
502	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
502	S	Phosphorylation	Kinase	PKCA	P05696	PSP
502	S	Phosphorylation	Kinase	PKCE	P09216	PSP
502	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
502	S	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
502	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
502	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
502	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
704	T	Phosphorylation	Kinase	PRKCA	P17252	GPS
704	T	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
704	T	Phosphorylation	Kinase	CAMK2-FAMILY	-	GPS
774	S	Phosphorylation	Kinase	PKA	-	Uniprot
774	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
774	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
774	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
800	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
800	S	Phosphorylation	Kinase	PRKCZ	P09217	Uniprot
800	S	Phosphorylation	Kinase	PKCE	P09216	PSP
800	S	Phosphorylation	Kinase	PKCA	P05696	PSP
800	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
820	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
820	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
820	S	Phosphorylation	Kinase	PRKACA	P00517	GPS
820	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
116	S	Phosphorylation		12194871
Phosphorylation by PKA reverses capsaicin-induced dephosphorylation at multiple sites, probably including Ser-116 as a major phosphorylation site.

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
FAF1_RAT	Faf1	physical	16510717

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of TRPV1_RAT

Related Literatures of Post-Translational Modification

N-linked Glycosylation
Reference	PubMed
"Biochemical characterization of the vanilloid receptor 1 expressed ina dorsal root ganglia derived cell line."; Jahnel R., Dreger M., Gillen C., Bender O., Kurreck J., Hucho F.; Eur. J. Biochem. 268:5489-5496(2001). Cited for: SUBCELLULAR LOCATION, AND GLYCOSYLATION AT ASN-604.	11683872 [Abstract]
Phosphorylation
Reference	PubMed
"Interaction between protein kinase Cmu and the vanilloid receptortype 1."; Wang Y., Kedei N., Wang M., Wang Q.J., Huppler A.R., Toth A., Tran R.,Blumberg P.M.; J. Biol. Chem. 279:53674-53682(2004). Cited for: INTERACTION WITH PRKCM, PHOSPHORYLATION AT SER-116, AND MUTAGENESIS OFSER-116.	15471852 [Abstract]
"Phosphorylation of vanilloid receptor 1 by Ca2+/calmodulin-dependentkinase II regulates its vanilloid binding."; Jung J., Shin J.S., Lee S.-Y., Hwang S.W., Koo J., Cho H., Oh U.; J. Biol. Chem. 279:7048-7054(2004). Cited for: FUNCTION, PHOSPHORYLATION AT SER-502 AND THR-704, AND MUTAGENESIS OFSER-502 AND THR-704.	14630912 [Abstract]
"cAMP-dependent protein kinase regulates desensitization of thecapsaicin receptor (VR1) by direct phosphorylation."; Bhave G., Zhu W., Wang H., Brasier D.J., Oxford G.S., Gereau R.W. IV; Neuron 35:721-731(2002). Cited for: FUNCTION, AND PHOSPHORYLATION AT SER-116; THR-144; THR-370; SER-502;SER-774 AND SER-820.	12194871 [Abstract]
"Direct phosphorylation of capsaicin receptor VR1 by protein kinaseCepsilon and identification of two target serine residues."; Numazaki M., Tominaga T., Toyooka H., Tominaga M.; J. Biol. Chem. 277:13375-13378(2002). Cited for: PHOSPHORYLATION AT SER-502 AND SER-800, AND MUTAGENESIS OF SER-502 ANDSER-800.	11884385 [Abstract]

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