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

Overview
Villin Epithelial cell-specific Ca(2+)-regulated actin- modifying protein that modulates the reorganization of microvillar actin filaments. Plays a role in the actin nucleation, actin filament bundle assembly, actin filament capping and severing. Binds phosphatidylinositol 4,5-bisphosphate (PIP2) and lysophosphatidic acid (LPA); binds LPA with higher affinity than PIP2. Binding to LPA increases its phosphorylation by SRC and inhibits all actin-modifying activities. Binding to PIP2 inhibits actin-capping and -severing activities but enhances actin-bundling activity. Regulates the intestinal epithelial cell morphology, cell invasion, cell migration and apoptosis. Protects against apoptosis induced by dextran sodium sulfate (DSS) in the gastrointestinal epithelium. Appears to regulate cell death by maintaining mitochondrial integrity. Enhances hepatocyte growth factor (HGF)-induced epithelial cell motility, chemotaxis and wound repair. Upon S.flexneri cell infection, its actin-severing activity enhances actin-based motility of the bacteria and plays a role during the dissemination. Monomer. Homodimer; homodimerization is necessary for actin-bundling. Associates with F-actin; phosphorylation at tyrosines residues decreases the association with F-actin. Interacts (phosphorylated at C-terminus tyrosine phosphorylation sites) with PLCG1 (via the SH2 domains). Interacts (phosphorylated form) with PLCG1; the interaction is enhanced by hepatocyte growth factor (HGF). Specifically expressed in epithelial cells. Major component of microvilli of intestinal epithelial cells and kidney proximal tubule cells. Expressed in canalicular microvilli of hepatocytes. Belongs to the villin/gelsolin family. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Actin binding protein
Cellular Component: ruffle; filopodium tip; microvillus; lamellipodium; cytoplasm; actin filament bundle; filopodium
Molecular Function: actin filament binding; identical protein binding; protein binding; phosphatidylinositol-4,5-bisphosphate binding; protein homodimerization activity; caspase inhibitor activity; calcium ion binding
Biological Process: epidermal growth factor receptor signaling pathway; actin filament depolymerization; actin filament severing; actin filament capping; negative regulation of caspase activity; regulation of cell shape; response to bacterium; epithelial cell differentiation; actin filament polymerization; protein complex assembly; regulation of actin nucleation; positive regulation of actin filament bundle formation; positive regulation of cell migration
Reference #:  P09327 (UniProtKB)
Alt. Names/Synonyms: D2S1471; VIL; VIL1; VILI; villin 1; Villin-1
Gene Symbols: VIL1
Molecular weight: 92,695 Da
Basal Isoelectric point: 5.99  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Villin

Protein Structure Not Found.


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Sites Implicated In
cell motility, altered: Y286‑p
cytoskeletal reorganization: Y46‑p, Y60‑p, Y64‑p, Y81‑p, Y256‑p, Y286‑p
intracellular localization: Y60‑p, Y81‑p, Y256‑p
molecular association, regulation: Y60‑p, Y81‑p, Y256‑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 1 T2-p ______MtKLsAQVK
0 1 S5-p ___MtKLsAQVKGSL
0 1 T15-p VKGSLNItTPGLQIW
0 1 S39 VPSSTFGSFFDGDCy
2 1 Y46-p SFFDGDCyIILAIHK
3 0 Y60-p KTASSLSyDIHyWIG
1 0 Y64-p SLSyDIHyWIGQDSS
3 0 Y81-p EQGAAAIyTTQMDDF
0 1 K119-ac KQGLVIRkGGVAsGM
0 1 S124-p IRkGGVAsGMKHVET
0 3 Y134-p KHVETNSyDVQRLLH
0 1 T206-p DQERGGRtyVGVVDG
0 2 Y207-p QERGGRtyVGVVDGE
0 2 K237-ub LGKRRELkAAVPDTV
0 1 K250 TVVEPALKAALKLyH
2 0 Y256-p LKAALKLyHVSDSEG
0 1 N264 HVSDSEGNLVVREVA
0 1 S281 PLTQDLLSHEDCyIL
1 0 Y286-p LLSHEDCyILDQGGL
0 1 K320 SHALNFIKAKQyPPS
1 0 Y324-p NFIKAKQyPPSTQVE
0 1 T350 QQLFQKWTASNRTsG
0 1 S356-p WTASNRTsGLGKTHT
0 1 S366-p GKTHTVGsVAKVEQV
1 0 Y461-p DEITASAyQAVILDQ
0 1 T506 YQGGTSRTNNLETGP
0 3 K529-ub GTGANNTkAFEVPAR
1 0 Y555-p LKTQSCCyLWCGKGC
1 0 Y604-p ALGGKAPyANTKRLQ
0 1 K672 HANEEEKKAAATTAQ
0 2 Y681-p AATTAQEyLKTHPSG
0 1 K683 TTAQEyLKTHPSGRD
0 1 T693-p PSGRDPEtPIIVVKQ
0 1 S724-p FKWSNTKsyEDLkAE
1 0 Y725-p KWSNTKsyEDLkAEL
0 1 K729-ac TKsyEDLkAELGNSR
0 1 S735 LkAELGNSRDWSQIT
0 1 P776 LEQLVNKPVEELPEG
  mouse

 
T2 ______MTKLNAQVK
N5 ___MTKLNAQVKGSL
T15 VKGSLNITTPGIQIW
S39-p VPSSTFGsFFDGDCy
Y46-p sFFDGDCyVVLAIHK
Y60 KTSSTLSYDIHYWIG
Y64 TLSYDIHYWIGQDSS
Y81 EQGAAAIYTTQMDDY
K119 KQGLVIRKGGVASGM
S124 IRKGGVASGMKHVET
C134 KHVETNSCDVQRLLH
T206 DQERGGRTYVGVVDG
Y207 QERGGRTYVGVVDGE
K237-ub LGPRKELkAAISDSV
K250-ub SVVEPAAkAALKLYH
Y256 AkAALKLYHVSDSEG
K264-ub HVSDSEGkLVVREVA
K281-ub PLTQDLLkHEDCYIL
Y286 LLkHEDCYILDQGGL
K320-ub SQALNFIkAKQYPPS
Y324 NFIkAKQYPPSTQVE
T350-p QQLFQKWtVPNRTSG
S356 WtVPNRTSGLGKTHT
S366 GKTHTVGSVAKVEQV
Y461 DEIAASAYQAVLLDQ
K506-ub YQGGTSRkNNLEPVP
K529-ub GTNADNTkAFEVTAR
Y555 LKTPSCCYLWCGKGC
Y604 ALGGKAPYANTKRLQ
K672-ub HANEEEKkAAATTVQ
Y681 AATTVQEYLkTHPGN
K683-ub TTVQEYLkTHPGNRD
T693 PGNRDLETPIIVVKQ
S724 FKWSNTKSYDDLKAE
Y725 KWSNTKSYDDLKAEL
K729 TKSYDDLKAELGNsG
S735-p LKAELGNsGDWSQIA
S776-p LEQLVNKsVEDLPEG
  rat

 
T2 ______MTKLTAQVK
T5 ___MTKLTAQVKGSL
T15 VKGSLNTTTPGIQIW
S39 VPSSTFGSFFDGDCY
Y46 SFFDGDCYVVLAIHK
Y60 KTGSTLSYDIHYWIG
Y64 TLSYDIHYWIGQDSS
Y81 EQGAAAIYTTQMDDY
K119 KQGLVIRKGGVASGM
S124 IRKGGVASGMKHVET
C134 KHVETNSCDVQRLLH
T206 DQERGGRTYVGVVDG
Y207 QERGGRTYVGVVDGE
K237 LGPRKELKAAISDSV
K250 SVVEPAAKAALKLYH
Y256 AKAALKLYHVSDSEG
K264 HVSDSEGKMVVREVA
S281 PLTQDLLSHEDCYIL
Y286 LLSHEDCYILDQGGL
K320 NQALNFIKAKQYPPS
Y324 NFIKAKQYPPSTQVE
T350 QQLFQKWTVPNRTSG
S356 WTVPNRTSGLGKTHT
S366 GKTHTVGSVAKVEQV
Y461 DEIAASAYQAVNLDQ
K506 YQGGTSRKNNVEPVP
K529 GTSADNTKAFEVTAR
Y555 LKTPSCCYLWCGKGC
Y604 ALGGKAPYANTKRLQ
K672 HANEEEKKAAATTAQ
Y681 AATTAQEYLKTHPGN
K683 TTAQEYLKTHPGNRD
T693 PGNRDPETPIIVVKQ
S724 FKWSNTKSYDDLKAE
Y725 KWSNTKSYDDLKAEL
K729 TKSYDDLKAELGNsG
S735-p LKAELGNsGDWSQIA
P776 LEQLVNKPVEELPEG
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