dbPTM

TRPV3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TRPV3_HUMAN
UniProt AC	Q8NET8
Protein Name	Transient receptor potential cation channel subfamily V member 3
Gene Name	TRPV3
Organism	Homo sapiens (Human).
Sequence Length	790
Subcellular Localization	Membrane Multi-pass membrane protein.
Protein Description	Putative receptor-activated non-selective calcium permeant cation channel. It is activated by innocuous (warm) temperatures and shows an increased response at noxious temperatures greater than 39 degrees Celsius. Activation exhibits an outward rectification. May associate with TRPV1 and may modulate its activity. Is a negative regulator of hair growth and cycling: TRPV3-coupled signaling suppresses keratinocyte proliferation in hair follicles and induces apoptosis and premature hair follicle regression (catagen)..
Protein Sequence	MKAHPKEMVPLMGKRVAAPSGNPAILPEKRPAEITPTKKSAHFFLEIEGFEPNPTVAKTSPPVFSKPMDSNIRQCISGNCDDMDSPQSPQDDVTETPSNPNSPSAQLAKEEQRRKKRRLKKRIFAAVSEGCVEELVELLVELQELCRRRHDEDVPDFLMHKLTASDTGKTCLMKALLNINPNTKEIVRILLAFAEENDILGRFINAEYTEEAYEGQTALNIAIERRQGDIAALLIAAGADVNAHAKGAFFNPKYQHEGFYFGETPLALAACTNQPEIVQLLMEHEQTDITSRDSRGNNILHALVTVAEDFKTQNDFVKRMYDMILLRSGNWELETTRNNDGLTPLQLAAKMGKAEILKYILSREIKEKRLRSLSRKFTDWAYGPVSSSLYDLTNVDTTTDNSVLEITVYNTNIDNRHEMLTLEPLHTLLHMKWKKFAKHMFFLSFCFYFFYNITLTLVSYYRPREEEAIPHPLALTHKMGWLQLLGRMFVLIWAMCISVKEGIAIFLLRPSDLQSILSDAWFHFVFFIQAVLVILSVFLYLFAYKEYLACLVLAMALGWANMLYYTRGFQSMGMYSVMIQKVILHDVLKFLFVYIVFLLGFGVALASLIEKCPKDNKDCSSYGSFSDAVLELFKLTIGLGDLNIQQNSKYPILFLFLLITYVILTFVLLLNMLIALMGETVENVSKESERIWRLQRARTILEFEKMLPEWLRSRFRMGELCKVAEDDFRLCLRINEVKWTEWKTHVSFLNEDPGPVRRTDFNKIQDSSRNNSKTTLNAFEEVEEFPETSV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
29	Acetylation	NPAILPEKRPAEITP CCCCCCCCCCCCCCC	62.84	19811893
35	Phosphorylation	EKRPAEITPTKKSAH CCCCCCCCCCCCCEE	19.19	23312004
37	Phosphorylation	RPAEITPTKKSAHFF CCCCCCCCCCCEEEE	42.32	23312004
264	Phosphorylation	EGFYFGETPLALAAC CCEECCCCHHHHHHH	24.79	-
321	Phosphorylation	NDFVKRMYDMILLRS CHHHHHHHHHHEECC	13.34	24719451
336	Phosphorylation	GNWELETTRNNDGLT CCEEEEECCCCCCCC	23.25	24719451
358	Ubiquitination	MGKAEILKYILSREI HCHHHHHHHHHCHHH	35.59	-
372	Phosphorylation	IKEKRLRSLSRKFTD HHHHHHHHHHHHCCH	34.98	24702127
374	Phosphorylation	EKRLRSLSRKFTDWA HHHHHHHHHHCCHHH	34.37	23927012
378	Phosphorylation	RSLSRKFTDWAYGPV HHHHHHCCHHHHCCC	33.40	-
382	Phosphorylation	RKFTDWAYGPVSSSL HHCCHHHHCCCCCHH	20.08	-
387	Phosphorylation	WAYGPVSSSLYDLTN HHHCCCCCHHHCCCC	25.29	-
388	Phosphorylation	AYGPVSSSLYDLTNV HHCCCCCHHHCCCCC	24.36	30576142
390	Phosphorylation	GPVSSSLYDLTNVDT CCCCCHHHCCCCCCC	15.74	30576142
397	Phosphorylation	YDLTNVDTTTDNSVL HCCCCCCCCCCCCEE	27.58	30576142
607	Phosphorylation	GFGVALASLIEKCPK HHHHHHHHHHHHCCC	30.63	24719451

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
264	T	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TRPV3_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 TRPV3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of TRPV3_HUMAN !!

Drug and Disease Associations

Kegg Disease
OMIM Disease
614594	Olmsted syndrome (OLMS)
616400	Palmoplantar keratoderma, non-epidermolytic, focal 2 (FNEPPK2)
Kegg Drug
DrugBank
DB00825	Menthol

Regulatory Network of TRPV3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-374, AND MASSSPECTROMETRY.	18187866 [Abstract]