TRPV1_MOUSE - dbPTM
TRPV1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TRPV1_MOUSE
UniProt AC Q704Y3
Protein Name Transient receptor potential cation channel subfamily V member 1
Gene Name Trpv1
Organism Mus musculus (Mouse).
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. [PubMed: 15194687]
Protein Sequence MEKWASLDSDESEPPAQENSCPDPPDRDPNSKPPPAKPHIFATRSRTRLFGKGDSEEASPMDCPYEEGGLASCPIITVSSVVTLQRSVDGPTCLRQTSQDSVSTGVETPPRLYDRRSIFDAVAQSNCQELESLLSFLQKSKKRLTDSEFKDPETGKTCLLKAMLNLHNGQNDTIALLLDIARKTDSLKQFVNASYTDSYYKGQTALHIAIERRNMALVTLLVENGADVQAAANGDFFKKTKGRPGFYFGELPLSLAACTNQLAIVKFLLQNSWQPADISARDSVGNTVLHALVEVADNTADNTKFVTNMYNEILILGAKLHPTLKLEELTNKKGLTPLALAASSGKIGVLAYILQREIHEPECRHLSRKFTEWAYGPVHSSLYDLSCIDTCEKNSVLEVIAYSSSETPNRHDMLLVEPLNRLLQDKWDRFVKRIFYFNFFVYCLYMIIFTTAAYYRPVEGLPPYKLNNTVGDYFRVTGEILSVSGGVYFFFRGIQYFLQRRPSLKSLFVDSYSEILFFVQSLFMLVSVVLYFSHRKEYVASMVFSLAMGWTNMLYYTRGFQQMGIYAVMIEKMILRDLCRFMFVYLVFLFGFSTAVVTLIEDGKNNSLPVESPPHKCRGSACRPGNSYNSLYSTCLELFKFTIGMGDLEFTENYDFKAVFIILLLAYVILTYILLLNMLIALMGETVNKIAQESKNIWKLQRAITILDTEKSFLKCMRKAFRSGKLLQVGFTPDGKDDFRWCFRVDEVNWTTWNTNVGIINEDPGNCEGVKRTLSFSLRSGRVSGRNWKNFALVPLLRDASTRDRHSTQPEEVQLKHYTGSLKPEDAEVFKDSMAPGEK
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
117PhosphorylationPRLYDRRSIFDAVAQ
CCCCCHHHHHHHHHH
28.62-
145PhosphorylationQKSKKRLTDSEFKDP
HHHHHCCCCCCCCCC
41.3216954222
266AcetylationTNQLAIVKFLLQNSW
HCHHHHHHHHHHCCC
24.967610815
330PhosphorylationTLKLEELTNKKGLTP
CCCHHHHCCCCCCCH
48.55-
371PhosphorylationRHLSRKFTEWAYGPV
HHHHHHHHHHHHCCC
33.3816954222
407PhosphorylationIAYSSSETPNRHDML
EEEECCCCCCCCHHE
28.01-
503PhosphorylationYFLQRRPSLKSLFVD
HHHHHCCCCHHHCCC
46.77-
605N-linked_GlycosylationTLIEDGKNNSLPVES
HHHHCCCCCCCCCCC
49.18-
628PhosphorylationACRPGNSYNSLYSTC
CCCCCCCHHHHHHHH
16.8725521595
630PhosphorylationRPGNSYNSLYSTCLE
CCCCCHHHHHHHHHH
22.0525521595
634PhosphorylationSYNSLYSTCLELFKF
CHHHHHHHHHHHHHH
13.9325521595
705PhosphorylationWKLQRAITILDTEKS
HHHHHHHHHHHCHHH
17.95-
775PhosphorylationEGVKRTLSFSLRSGR
CCCCEEEEEEECCCC
16.5122942356
777PhosphorylationVKRTLSFSLRSGRVS
CCEEEEEEECCCCCC
21.3522942356
801PhosphorylationVPLLRDASTRDRHST
HHHHCCCCCCCCCCC
28.4118495351
821PhosphorylationQLKHYTGSLKPEDAE
HHHHCCCCCCHHHCH
25.97-

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
371TPhosphorylationKinasePKA-Uniprot
407TPhosphorylationKinaseCDK5Q00535
PSP
503SPhosphorylationKinasePRKCEP16054
Uniprot
801SPhosphorylationKinasePRKCEP16054
Uniprot
801SPhosphorylationKinasePRKCZQ02956
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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RFIP3_HUMANRAB11FIP3physical
15883036
AKAP5_MOUSEAkap5physical
18463244
KAPCA_MOUSEPrkacaphysical
18463244

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TRPV1_MOUSE

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Related Literatures of Post-Translational Modification

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