UniProt Accession

 VASP_HUMAN; P50552; B2RBT9; Q6PIZ1; Q93035 

Genbank Protein ID

 Z46389; CH471126; AK314812; BC026019; BC038224; X98534; X98533 

Genbank Nucleotide ID

 CAA86523.1; EAW57362.1; BAG37336.1; AAH26019.1; AAH38224.1; CAA67147.2; CAA67147.2 

Protein Name

 Vasodilator-stimulated phosphoprotein 

Protein Synonyms/Alias

 VASP 

Gene Name

 VASP 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
71	CAIVRGVKYNQATPN	ubiquitination	[1, 2, 3]
283	KATQVGEKTPKDESA	acetylation	[4]
286	QVGEKTPKDESANQE	sumoylation	[5]
363	KKELQKVKEEIIEAF	ubiquitination	[6]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 

Functional Description

 Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin- bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation. 

Sequence Annotation

 DOMAIN 2 113 WH1.
 REPEAT 344 358 1.
 REPEAT 359 373 2.
 REGION 225 377 EVH2.
 REGION 225 245 EVH2 block A.
 REGION 259 278 EVH2 block B.
 REGION 343 377 EVH2 block C.
 REGION 344 373 2 X 15 AA tandem repeats of L-[EQ]-[KR]-
 MOTIF 234 237 KLKR.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 39 39 Phosphotyrosine.
 MOD_RES 157 157 Phosphoserine; by PKA, PKC, PKG/PRKG1 and
 MOD_RES 239 239 Phosphoserine; by PKA and PKG/PRKG1.
 MOD_RES 278 278 Phosphothreonine; by PKA, PKG/PRKG1 and
 MOD_RES 283 283 N6-acetyllysine.
 MOD_RES 316 316 Phosphothreonine.
 MOD_RES 322 322 Phosphoserine; by AMPK.
 MOD_RES 323 323 Phosphoserine (By similarity).  

Keyword

 3D-structure; Acetylation; Actin-binding; Cell junction; Cell membrane; Cell projection; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; SH3-binding. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 380 AA 

Protein Sequence

Gene Ontology

 GO:0015629; C:actin cytoskeleton; TAS:ProtInc.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031527; C:filopodium membrane; IEA:UniProtKB-SubCell.
 GO:0005925; C:focal adhesion; IDA:HPA.
 GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0008154; P:actin polymerization or depolymerization; IEA:InterPro.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0034329; P:cell junction assembly; TAS:Reactome.
 GO:0001843; P:neural tube closure; IEA:Compara.
 GO:0051289; P:protein homotetramerization; IEA:InterPro.
 GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome. 

Interpro

 IPR000697; EVH1.
 IPR011993; PH_like_dom.
 IPR017354; Vasodilator_phosphoprotein.
 IPR014885; VASP_tetra. 

Pfam

 PF08776; VASP_tetra
 PF00568; WH1 

SMART

 SM00461; WH1 

PROSITE

 PS50229; WH1 

PRINTS