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Protein Page:
TRPV4 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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, multi-pass; Channel, cation; Membrane protein, integral
Chromosomal Location of Human Ortholog: 12q24.1
Cellular Component: adherens junction; apical plasma membrane; cell surface; cilium; cortical actin cytoskeleton; cytoplasmic microtubule; cytoplasmic vesicle; filopodium; focal adhesion; growth cone; integral to membrane; lamellipodium; plasma membrane
Molecular Function: actin binding; actin filament binding; alpha-tubulin binding; ATP binding; beta-tubulin binding; calcium channel activity; calmodulin binding; cation channel activity; microtubule binding; osmosensor activity; protein binding; protein kinase binding; protein kinase C binding; SH2 domain binding; stretch-activated, cation-selective, calcium channel activity
Biological Process: actin cytoskeleton reorganization; actin filament organization; calcium ion transport; cell volume homeostasis; cellular calcium ion homeostasis; cortical microtubule organization and biogenesis; diet induced thermogenesis; elevation of cytosolic calcium ion concentration; glucose homeostasis; hyperosmotic salinity response; intercellular junction assembly; microtubule polymerization; multicellular organismal water homeostasis; negative regulation of transcription from RNA polymerase II promoter; osmosensory signaling pathway; positive regulation of inflammatory response; positive regulation of JNK cascade; positive regulation of microtubule depolymerization; positive regulation of vascular permeability; regulation of response to osmotic stress; response to insulin stimulus; response to mechanical stimulus; vasopressin secretion
Disease: Brachyolmia Type 3; Digital Arthropathy-brachydactyly, Familial; Hereditary Motor And Sensory Neuropathy, Type Iic; Metatropic Dysplasia; Parastremmatic Dwarfism; Scapuloperoneal Spinal Muscular Atrophy; Sodium Serum Level Quantitative Trait Locus 1; Spinal Muscular Atrophy, Distal, Congenital Nonprogressive; Spondyloepiphyseal Dysplasia, Maroteaux Type; Spondylometaphyseal Dysplasia, Kozlowski Type
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.
Download PyMol Script
Download ChimeraX Script


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Sites Implicated In
activity, induced: S162‑p, T175‑p, S189‑p, S824‑p
intracellular localization: S824‑p
molecular association, regulation: 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


 LTP 

LTP: 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.


 HTP 

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


       human

 
0 1 Y91‑p DLLESTLyESSVVPG
3 4 Y110‑p PMDSLFDyGtyRHHS
0 1 T112‑p DSLFDyGtyRHHSSD
0 3 Y113‑p SLFDyGtyRHHSSDN
0 1 S134‑p IIEKQPQsPKAPAPQ
1 1 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 1 S319‑p ADMRRQDsRGNTVLH
0 3 T335‑p LVAIADNtRENTKFV
0 1 K344 ENTKFVTKMYDLLLL
0 1 K352 MYDLLLLKCARLFPD
0 1 S470‑p WRKFGAVsFYINVVS
0 1 T505‑p PPYPYRTtVDyLRLA
0 1 Y508‑p PYRTtVDyLRLAGEV
0 1 K766 GEMVTVGKSSDGTPD
2 2 Y805‑p DPGKNETyQYYGFSH
0 1 S823 RLRRDRWSsVVPRVV
4 3 S824‑p LRRDRWSsVVPRVVE
  mouse

 
Y91 DLLESTLYESSVVPG
Y110‑p PMDSLFDyGTYRHHP
T112 DSLFDyGTYRHHPSD
Y113 SLFDyGTYRHHPSDN
S134 VVEKQPQSPKAPAPQ
S162 FDIVSRGSTADLDGL
T175 GLLSFLLTHkKRLtD
K177‑ub LSFLLTHkKRLtDEE
T181‑p LTHkKRLtDEEFREP
S189 DEEFREPSTGkTCLP
K192‑ub FREPSTGkTCLPkAL
K197‑ub TGkTCLPkALLNLSN
Y253‑p IERRCKHyVELLVAQ
S319 ADMRRQDSRGNTVLH
T335 LVAIADNTRENTKFV
K344‑ub ENTKFVTkMYDLLLL
K352‑ub MYDLLLLkCSRLFPD
S470 WRKFGAVSFYINVVS
T505 PPYPYRTTVDYLRLA
Y508 PYRTTVDYLRLAGEV
K766‑ub GEMVTVGkSSDGTPD
Y805‑p DPGKSEIyQYYGFSH
S823‑p RLRRDRWssVVPRVV
S824‑p LRRDRWssVVPRVVE
  rat

 
Y91 DLLESTLYESSVVPG
Y110 PMDSLFDYGTYRHHP
T112 DSLFDYGTYRHHPSD
Y113 SLFDYGTYRHHPSDN
S134 VVEKQPQSPKAPAPQ
S162 FDIVSRGSTADLDGL
T175 GLLSYLLTHKKRLTD
K177 LSYLLTHKKRLTDEE
T181 LTHKKRLTDEEFREP
S189 DEEFREPSTGKTCLP
K192 FREPSTGKTCLPKAL
K197 TGKTCLPKALLNLSN
Y253 IERRCKHYVELLVAQ
S319 ADMRRQDSRGNTVLH
T335 LVAIADNTRENTKFV
K344 ENTKFVTKMYDLLLL
K352 MYDLLLLKCSRLFPD
S470 WRKFGAVSFYINVVS
T505 PPYPYRTTVDYLRLA
Y508 PYRTTVDYLRLAGEV
K766 GEMVTVGKSSDGTPD
Y805 DPGKSEIYQYYGFSH
S823 RLRRDRWSSVVPRVV
S824 LRRDRWSSVVPRVVE
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