Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
VASP (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
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
Chromosomal Location of Human Ortholog: 19q13.32
Cellular Component: actin cytoskeleton; cytoplasm; cytosol; focal adhesion; plasma membrane
Molecular Function: profilin binding; protein binding
Biological Process: axon guidance; positive regulation of actin filament polymerization
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.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  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
cell motility, inhibited: S157‑p, S322‑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
molecular association, regulation: S157‑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 S8‑p MSETVICsSRATVML
0 40 Y16‑p SRATVMLyDDGNKRW
1 1417 Y39‑p AFSRVQIyHNPtANs
0 9 T43‑p VQIyHNPtANsFRVV
0 1 S46‑p yHNPtANsFRVVGRK
0 1 K71‑ub CAIVRGVkYNQATPN
41 3 S157‑p EHIERRVsNAGGPPA
45 21 S239‑p GAKLRKVsKQEEASG
0 1 T249‑p EEASGGPtAPkAESG
0 1 K252‑ac SGGPtAPkAESGRsG
0 1 S258‑p PkAESGRsGGGGLME
9 21 T278‑p LARRRKAtQVGEktP
0 3 K283‑ac KAtQVGEktPkDEsA
0 7 T284‑p AtQVGEktPkDEsAN
0 1 K286‑sm QVGEktPkDEsANQE
0 3 S289‑p EktPkDEsANQEEPE
0 1 S305‑p RVPAQSEsVRRPWEK
0 3 S314‑p RRPWEKNsTtLPRMK
0 31 T316‑p PWEKNsTtLPRMKss
3 56 S322‑p TtLPRMKssssVttS
0 19 S323‑p tLPRMKssssVttSE
0 20 S324‑p LPRMKssssVttSEt
0 25 S325‑p PRMKssssVttSEtQ
0 9 T327‑p MKssssVttSEtQPC
0 1 T328‑p KssssVttSEtQPCt
0 1 T331‑p ssVttSEtQPCtPsS
0 1 C334 ttSEtQPCtPsSSDy
0 49 T335‑p tSEtQPCtPsSSDyS
0 3 S337‑p EtQPCtPsSSDySDL
0 2 Y341‑p CtPsSSDySDLQRVK
0 1 K363‑ub KKELQKVkEEIIEAF
3111 : Phospho-VASP (Ser157) Antibody
84519 : Phospho-VASP (Ser157) (D1C8O) Rabbit mAb
3114 : Phospho-VASP (Ser239) Antibody
  mouse

 
S8 MSETVICSSRATVML
Y16 SRATVMLYDDSNKRW
Y39‑p AFSRVQIyHNPtANS
T43‑p VQIyHNPtANSFRVV
S46 yHNPtANSFRVVGRK
K71 CAIIRGVKYNQATPI
S153‑p EHMERRVsNAGGPPA
S235‑p GAKLRKVsKQEEASG
L245 EEASGGPLAPKAENS
K248 SGGPLAPKAENSRST
S254 PKAENSRSTGGGLME
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
T323 KssssVtTSEAHPst
A326 ssVtTSEAHPstPCS
S329‑p tTSEAHPstPCSSDD
T330‑p TSEAHPstPCSSDDS
C332 EAHPstPCSSDDSDL
D336 stPCSSDDSDLERVK
K358 RKELQKMKEEIIEVF
3111 : Phospho-VASP (Ser157) Antibody
84519 : Phospho-VASP (Ser157) (D1C8O) Rabbit mAb
3114 : Phospho-VASP (Ser239) Antibody
  rat

 
S9 SNETVICSSRATVML
Y17 SRATVMLYDDSNKRW
Y40‑p AFSRVQIyHNPTANS
T44 VQIyHNPTANSFRVV
S47 yHNPTANSFRVVGRK
K72 CAIIRGVKYNQATPI
S154‑p EHLERRVsNAGGPPA
S236‑p GAKLRKVsKEEASGG
L245 EEASGGPLAPKAENS
K248 SGGPLAPKAENSRGT
G254 PKAENSRGTGGGLME
T274‑p LARRRKAtQVGEKPP
K279 KAtQVGEKPPKDESA
P280 AtQVGEKPPKDESAS
K282 QVGEKPPKDESASQE
S285 EKPPKDESASQEESE
P301 RIPAQSEPVRRPWEK
S310 RRPWEKNSTTLPRMK
T312 PWEKNSTTLPRMKsS
S318‑p TTLPRMKsSSsVTTS
S319 TLPRMKsSSsVTTSE
S320 LPRMKsSSsVTTSEA
S321‑p PRMKsSSsVTTSEAH
T323 MKsSSsVTTSEAHPS
T324 KsSSsVTTSEAHPSV
A327 SsVTTSEAHPSVPSS
S330 TTSEAHPSVPSSSDD
V331 TSEAHPSVPSSSDDS
S333 EAHPSVPSSSDDSDL
D337 SVPSSSDDSDLERVK
K359 RKELQKMKEEIIEVF
3111 : Phospho-VASP (Ser157) Antibody
84519 : Phospho-VASP (Ser157) (D1C8O) Rabbit mAb
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.