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Protein Page:
VASP (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
VASP vasodilator-stimulated phosphoprotein. Actin- and profilin-binding microfilament-associated protein. The phosphorylation of VASP is dynamically regulated by cellular adhesion to extracellular matrix. Note: This description may include information from UniProtKB.
Protein type: Motility/polarity/chemotaxis; Cytoskeletal protein
Cellular Component: filopodium membrane; tight junction; focal adhesion; cytoplasm; plasma membrane; cytosol; actin cytoskeleton
Molecular Function: protein binding; actin binding; SH3 domain binding; profilin binding
Biological Process: axon guidance; positive regulation of actin filament polymerization; actin polymerization and/or depolymerization; neural tube closure; T cell receptor signaling pathway; protein homotetramerization
Reference #:  P50552 (UniProtKB)
Alt. Names/Synonyms: Vasodilator-stimulated phosphoprotein; VASP
Gene Symbols: VASP
Molecular weight: 39,830 Da
Basal Isoelectric point: 9.05  Predict pI for various phosphorylation states
CST Pathways:  Actin Dynamics
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

VASP

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  UCSD-Nature  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
carcinogenesis, altered: T278‑p
cell adhesion, altered: S157‑p, S239‑p
cell growth, altered: S157‑p, S239‑p
cell motility, altered: S239‑p, T278‑p
cytoskeletal reorganization: S157‑p, S239‑p, T278‑p
transcription, inhibited: S157‑p, S239‑p, T278‑p
activity, induced: S157‑p
intracellular localization: S157‑p, S239‑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 40 Y16-p SRATVMLyDDGNKRW
0 1395 Y39-p AFSRVQIyHNPtANs
0 9 T43-p VQIyHNPtANsFRVV
0 1 S46-p yHNPtANsFRVVGRK
0 1 K71-u CAIVRGVkYNQATPN
35 3 S157-p EHIERRVsNAGGPPA
41 14 S239-p GAKLRKVsKQEEASG
0 1 T249-p EEASGGPtAPKAESG
9 21 T278-p LARRRKAtQVGEktP
0 3 K283-a KAtQVGEktPkDESA
0 3 T284-p AtQVGEktPkDESAN
0 1 K286-s QVGEktPkDESANQE
0 1 S289 EktPkDESANQEEPE
0 1 S305-p RVPAQSEsVRRPWEK
0 3 S314-p RRPWEKNsTtLPRMK
0 24 T316-p PWEKNsTtLPRMKss
2 53 S322-p TtLPRMKssssVtTS
0 19 S323-p tLPRMKssssVtTSE
0 20 S324-p LPRMKssssVtTSET
0 22 S325-p PRMKssssVtTSETQ
0 8 T327-p MKssssVtTSETQPC
0 48 T335-p TSETQPCtPsSSDYS
0 3 S337-p ETQPCtPsSSDYSDL
0 1 K363-u KKELQKVkEEIIEAF
3111 : Phospho-VASP (Ser157) Antibody
3114 : Phospho-VASP (Ser239) Antibody
  mouse

 
Y16 SRATVMLYDDSNKRW
Y39-p AFSRVQIyHNPtANS
T43-p VQIyHNPtANSFRVV
S46 yHNPtANSFRVVGRK
K71 CAIIRGVKYNQATPI
S153-p EHMERRVsNAGGPPA
S235-p GAKLRKVsKQEEASG
L245 EEASGGPLAPKAENS
T274-p LARRRKAtQVGEKPP
K279 KAtQVGEKPPKDEsA
P280 AtQVGEKPPKDEsAS
K282 QVGEKPPKDEsASEE
S285-p EKPPKDEsASEESEA
P300 RLPAQSEPVRRPWEK
S309 RRPWEKNSTtLPRMK
T311-p PWEKNSTtLPRMKss
S317-p TtLPRMKssssVtTS
S318-p tLPRMKssssVtTSE
S319-p LPRMKssssVtTSEA
S320-p PRMKssssVtTSEAH
T322-p MKssssVtTSEAHPS
T330-p TSEAHPStPCSSDDS
C332 EAHPStPCSSDDSDL
K358 RKELQKMKEEIIEVF
3111 : Phospho-VASP (Ser157) Antibody
3114 : Phospho-VASP (Ser239) Antibody
  rat

 
Y17 SRATVMLYDDSNKRW
Y40-p AFSRVQIyHNPTANS
T44 VQIyHNPTANSFRVV
S47 yHNPTANSFRVVGRK
K72 CAIIRGVKYNQATPI
S154-p EHLERRVsNAGGPPA
S236-p GAKLRKVsKEEASGG
L245 EEASGGPLAPKAENS
T274-p LARRRKAtQVGEKPP
K279 KAtQVGEKPPKDESA
P280 AtQVGEKPPKDESAS
K282 QVGEKPPKDESASQE
S285 EKPPKDESASQEESE
P301 RIPAQSEPVRRPWEK
S310 RRPWEKNSTTLPRMK
T312 PWEKNSTTLPRMKSS
S318 TTLPRMKSSSSVTTS
S319 TLPRMKSSSSVTTSE
S320 LPRMKSSSSVTTSEA
S321 PRMKSSSSVTTSEAH
T323 MKSSSSVTTSEAHPS
V331 TSEAHPSVPSSSDDS
S333 EAHPSVPSSSDDSDL
K359 RKELQKMKEEIIEVF
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