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VASP (human)

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; focal adhesion; cytoplasm; plasma membrane; cytosol; actin cytoskeleton Molecular Function: protein binding; actin binding; SH3 domain binding; profilin binding Biological Process: axon guidance; 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:  Regulation of Actin Dynamics Protein-Specific Antibodies or siRNAs from Cell Signaling Technology®

Select Structure to View Below VASP 1EGX - A=1-115 (human) 1JNG - A=1-115 (human) 1USD - A=336-380 (human) 1USE - A=336-380 (human) 2PAV - V=199-214 (human) 2PBD - V=203-245 (human) 3CHW - V=199-214 (human)

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB 1EGX 1JNG 1USD 1USE 2PAV 2PBD 3CHW  |  Phospho3D  |  DISEASE  |  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, altered: S157‑p, S239‑p, T278‑p activation: 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

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	39		Y16-p	SRATVMLyDDGNKRW
0	1392		Y39-p	AFSRVQIyHNPtANS
0	9		T43-p	VQIyHNPtANSFRVV
0	1		K71-u	CAIVRGVkYNQATPN
33	3		S157-p	EHIERRVsNAGGPPA
40	11		S239-p	GAKLRKVsKQEEASG
0	1		T249-p	EEASGGPtAPkAESG
0	1		K252-a	SGGPtAPkAESGRSG
9	21		T278-p	LARRRKAtQVGEktP
0	3		K283-a	KAtQVGEktPkDESA
0	1		T284-p	AtQVGEktPkDESAN
0	1		K286-s	QVGEktPkDESANQE
0	1		S289	EktPkDESANQEEPE
0	2		S314-p	RRPWEKNsTtLPRMK
0	22		T316-p	PWEKNsTtLPRMKss
1	52		S322-p	TtLPRMKssssVttS
0	19		S323-p	tLPRMKssssVttSE
0	20		S324-p	LPRMKssssVttSEt
0	21		S325-p	PRMKssssVttSEtQ
0	8		T327-p	MKssssVttSEtQPC
0	1		T328-p	KssssVttSEtQPCt
0	1		T331-p	ssVttSEtQPCtPsS
0	47		T335-p	tSEtQPCtPsSSDyS
0	3		S337-p	EtQPCtPsSSDySDL
0	1		Y341-p	CtPsSSDySDLQRVK
0	1		K363-u	KKELQKVkEEIIEAF

	mouse
Y16	SRATVMLYDDSNKRW
Y39-p	AFSRVQIyHNPtANS
T43-p	VQIyHNPtANSFRVV
K71	CAIIRGVKYNQATPI
S153-p	EHMERRVsNAGGPPA
S235-p	GAKLRKVsKQEEASG
L245	EEASGGPLAPKAENS
K248	SGGPLAPKAENSRST
T274-p	LARRRKAtQVGEKPP
K279	KAtQVGEKPPKDEsA
P280	AtQVGEKPPKDEsAS
K282	QVGEKPPKDEsASEE
S285-p	EKPPKDEsASEESEA
S309	RRPWEKNSTtLPRMK
T311-p	PWEKNSTtLPRMKss
S317-p	TtLPRMKssssVtTS
S318-p	tLPRMKssssVtTSE
S319-p	LPRMKssssVtTSEA
S320-p	PRMKssssVtTSEAH
T322-p	MKssssVtTSEAHPS
T323	KssssVtTSEAHPSt
A326	ssVtTSEAHPStPCS
T330-p	TSEAHPStPCSSDDS
C332	EAHPStPCSSDDSDL
D336	StPCSSDDSDLERVK
K358	RKELQKMKEEIIEVF

	rat
Y17	SRATVMLYDDSNKRW
Y40-p	AFSRVQIyHNPTANS
T44	VQIyHNPTANSFRVV
K72	CAIIRGVKYNQATPI
S154-p	EHLERRVsNAGGPPA
S236-p	GAKLRKVsKEEASGG
L245	EEASGGPLAPKAENS
K248	SGGPLAPKAENSRGT
T274-p	LARRRKAtQVGEKPP
K279	KAtQVGEKPPKDESA
P280	AtQVGEKPPKDESAS
K282	QVGEKPPKDESASQE
S285	EKPPKDESASQEESE
S310	RRPWEKNSTTLPRMK
T312	PWEKNSTTLPRMKSS
S318	TTLPRMKSSSSVTTS
S319	TLPRMKSSSSVTTSE
S320	LPRMKSSSSVTTSEA
S321	PRMKSSSSVTTSEAH
T323	MKSSSSVTTSEAHPS
T324	KSSSSVTTSEAHPSV
A327	SSVTTSEAHPSVPSS
V331	TSEAHPSVPSSSDDS
S333	EAHPSVPSSSDDSDL
D337	SVPSSSDDSDLERVK
K359	RKELQKMKEEIIEVF

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