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Protein Page:
TRPV4 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
TRPV4 a non-selective calcium permeant cation channel probably involved in osmotic sensitivity and mechanosensitivity. Activation by exposure to hypotonicity within the physiological range exhibits an outward rectification. Also activated by low pH, citrate and phorbol esters. Increase of intracellular Ca(2+) potentiates currents. Channel activity seems to be regulated by a calmodulin-dependent mechanism with a negative feedback mechanism. Promotes cell-cell junction formation in skin keratinocytes and plays an important role in the formation and/or maintenance of functional intercellular barriers. Acts as a regulator of intracellular Ca(2+) in synoviocytes. Plays an obligatory role as a molecular component in the nonselective cation channel activation induced by 4-alpha-phorbol 12,13-didecanoate and hypotonic stimulation in synoviocytes and also regulates production of IL-8. Belongs to the transient receptor (TC 1.A.4) family. TrpV subfamily. TRPV4 sub-subfamily. 6 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Channel, cation; Membrane protein, multi-pass
Cellular Component: cortical actin cytoskeleton; focal adhesion; adherens junction; growth cone; cell surface; cytoplasmic microtubule; lamellipodium; plasma membrane; integral to membrane; cytoplasmic vesicle; filopodium; cilium
Molecular Function: calcium channel activity; microtubule binding; beta-tubulin binding; actin binding; protein kinase binding; calmodulin binding; actin filament binding; protein kinase C binding; osmosensor activity; cation channel activity; SH2 domain binding; alpha-tubulin binding; ATP binding
Biological Process: cell death; intercellular junction assembly; actin filament organization; regulation of response to osmotic stress; osmosensory signaling pathway; cellular calcium ion homeostasis; vasopressin secretion; elevation of cytosolic calcium ion concentration; positive regulation of microtubule depolymerization; hyperosmotic salinity response; response to mechanical stimulus; calcium ion transport; actin cytoskeleton reorganization; cell volume homeostasis; cortical microtubule organization and biogenesis; transmembrane transport; microtubule polymerization
Reference #:  Q9HBA0 (UniProtKB)
Alt. Names/Synonyms: CMT2C; HMSN2C; Osm-9-like TRP channel 4; OSM9-like transient receptor potential channel 4; osmosensitive transient receptor potential channel 4; OTRPC4; SPSMA; Transient receptor potential cation channel subfamily V member 4; transient receptor potential cation channel, subfamily V, member 4; Transient receptor potential protein 12; TRP12; TRPV4; Vanilloid receptor-like channel 2; Vanilloid receptor-like protein 2; vanilloid receptor-related osmotically activated channel; Vanilloid receptor-related osmotically-activated channel; VR-OAC; VRL-2; VRL2; VROAC
Gene Symbols: TRPV4
Molecular weight: 98,281 Da
Basal Isoelectric point: 7.83  Predict pI for various phosphorylation states
Select Structure to View Below

TRPV4

Protein Structure Not Found.


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Sites Implicated In
activity, induced: S162‑p, T175‑p, S189‑p, S824‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 2 Y91-p DLLESTLyESSVVPG
2 2 Y110-p PMDSLFDyGTyRHHS
0 3 Y113-p SLFDyGTyRHHSSDN
1 0 S162-p FDIVSRGsTADLDGL
1 0 T175-p GLLPFLLtHKKRLTD
0 1 K177 LPFLLtHKKRLTDEE
0 1 T181 LtHKKRLTDEEFREP
1 0 S189-p DEEFREPsTGKTCLP
0 1 K192 FREPsTGKTCLPKAL
0 1 K197 TGKTCLPKALLNLSN
1 0 Y253 IERRCKHYVELLVAQ
0 2 T335-p LVAIADNtRENTKFV
0 1 K344 ENTKFVTKMYDLLLL
0 1 K352 MYDLLLLKCARLFPD
0 1 T505-p PPYPYRTtVDyLRLA
0 1 Y508-p PYRTtVDyLRLAGEV
0 1 K766 GEMVTVGKSSDGTPD
2 1 Y805-p DPGKNETyQYYGFSH
0 1 S823 RLRRDRWSsVVPRVV
3 2 S824-p LRRDRWSsVVPRVVE
  mouse

 
Y91 DLLESTLYESSVVPG
Y110-p PMDSLFDyGTYRHHP
Y113 SLFDyGTYRHHPSDN
S162 FDIVSRGSTADLDGL
T175 GLLSFLLTHkKRLtD
K177-u LSFLLTHkKRLtDEE
T181-p LTHkKRLtDEEFREP
S189 DEEFREPSTGkTCLP
K192-u FREPSTGkTCLPkAL
K197-u TGkTCLPkALLNLSN
Y253-p IERRCKHyVELLVAQ
T335 LVAIADNTRENTKFV
K344-u ENTKFVTkMYDLLLL
K352-u MYDLLLLkCSRLFPD
T505 PPYPYRTTVDYLRLA
Y508 PYRTTVDYLRLAGEV
K766-u GEMVTVGkSSDGTPD
Y805-p DPGKSEIyQYYGFSH
S823-p RLRRDRWssVVPRVV
S824-p LRRDRWssVVPRVVE
  rat

 
Y91 DLLESTLYESSVVPG
Y110 PMDSLFDYGTYRHHP
Y113 SLFDYGTYRHHPSDN
S162 FDIVSRGSTADLDGL
T175 GLLSYLLTHKKRLTD
K177 LSYLLTHKKRLTDEE
T181 LTHKKRLTDEEFREP
S189 DEEFREPSTGKTCLP
K192 FREPSTGKTCLPKAL
K197 TGKTCLPKALLNLSN
Y253 IERRCKHYVELLVAQ
T335 LVAIADNTRENTKFV
K344 ENTKFVTKMYDLLLL
K352 MYDLLLLKCSRLFPD
T505 PPYPYRTTVDYLRLA
Y508 PYRTTVDYLRLAGEV
K766 GEMVTVGKSSDGTPD
Y805 DPGKSEIYQYYGFSH
S823 RLRRDRWSSVVPRVV
S824 LRRDRWSSVVPRVVE
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