P50552 (VASP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vasodilator-stimulated phosphoprotein
Short name=VASP

Gene names

Name:

VASP

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.1 Ref.2 Ref.11 Ref.16 Ref.20 Ref.21
Subunit structure	Homotetramer. Interacts with PFN1, PFN2, LPP, ACTN1 and ACTG1. Interacts, via the EVH1 domain, with the Pro-rich regions of ZYX. This interaction is important for targeting to focal adhesions and the formation of actin-rich structures at the apical surface of cells. Interacts, via the EVH1 domain, with the Pro-rich domain of Listeria monocytogenes actA. Interacts with APBB1IP. Interacts, via the Pro-rich domain, with the C-terminal SH3 domain of DNMBP By similarity. Ref.2 Ref.10 Ref.12 Ref.13 Ref.14 Ref.19 Ref.30 Ref.31
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cell junction › focal adhesion. Cell projection › lamellipodium membrane. Cell projection › filopodium membrane. Note: Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. Ref.1 Ref.18 Ref.21
Tissue specificity	Highly expressed in platelets. Ref.1
Domain	The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization. Ref.11 The WH1 domain mediates interaction with XIRP1. Ref.11
Post-translational modification	Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-157, the preferred site for PKG/PRKG1, Ser-239. In ADP-activated platelets, phosphorylation by PKA or PKG on Ser-157 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-278 requires prior phosphorylation on Ser-157 and Ser-239. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-278 by AMPK does not require prior phosphorylation at Ser-157 or Ser-239. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-322 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-157, while nitric oxide (NO) promotes phosphorylation at Ser-157, but also at Ser-239. Response to NO and CO is blunted in platelets from diabetic patients, and VASP is not phosphorylated efficiently at Ser-157 and Ser-239. Ref.8 Ref.9 Ref.15 Ref.18 Ref.20 Ref.21
Miscellaneous	VASP phosphorylation is used to monitor the effect of so-called antiplatelet drugs that reduce platelet reactivity and are used to prevent stent thrombosis, strokes and heart attacks in patients at risk for these problems.
Sequence similarities	Belongs to the Ena/VASP family. Contains 1 WH1 domain.

Ontologies

Keywords
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Polymorphism
Domain	Coiled coil Repeat SH3-binding
Ligand	Actin-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Traceable author statement. Source: Reactome actin polymerization or depolymerization Inferred from electronic annotation. Source: InterPro axon guidance Traceable author statement. Source: Reactome cell junction assembly Traceable author statement. Source: Reactome neural tube closure Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: InterPro
Cellular_component	actin cytoskeleton Traceable author statement Ref.1. Source: ProtInc cytosol Traceable author statement. Source: Reactome filopodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: HPA lamellipodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NR4A1	P22736	2	EBI-748201,EBI-721550
RPS6KA1	Q15418	4	EBI-748201,EBI-963034
VCL	P12003	2	EBI-748201,EBI-1039563	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.6

Chain

2 – 380

379

Vasodilator-stimulated phosphoprotein

PRO_0000065767

Regions

Domain

2 – 113

112

WH1

Repeat

344 – 358

15

1

Repeat

359 – 373

15

2

Region

225 – 377

153

EVH2

Region

225 – 245

21

EVH2 block A

Region

259 – 278

20

EVH2 block B

Region

343 – 377

35

EVH2 block C

Region

344 – 373

30

2 X 15 AA tandem repeats of L-[EQ]-[KR]-[MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-E

Coiled coil

337 – 373

37

Potential

Motif

234 – 237

4

KLKR

Compositional bias

118 – 216

99

Pro-rich

Compositional bias

215 – 222

8

Poly-Gly

Compositional bias

259 – 262

4

Poly-Gly

Compositional bias

322 – 325

4

Poly-Ser

Amino acid modifications

Modified residue

2

1

N-acetylserine Ref.6

Modified residue

39

1

Phosphotyrosine Ref.17

Modified residue

157

1

Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK1 Ref.8 Ref.9 Ref.18 Ref.21

Modified residue

239

1

Phosphoserine; by PKA and PKG/PRKG1 Ref.8 Ref.21

Modified residue

278

1

Phosphothreonine; by PKA, PKG/PRKG1 and AMPK Ref.8 Ref.20

Modified residue

283

1

N6-acetyllysine Ref.25

Modified residue

316

1

Phosphothreonine Ref.23 Ref.26

Modified residue

322

1

Phosphoserine; by AMPK Ref.23

Modified residue

323

1

Phosphoserine By similarity

Natural variations

Natural variant

104

1

A → T.
Corresponds to variant rs10415373 [ dbSNP | Ensembl ].

VAR_048929

Natural variant

140

1

Q → H.
Corresponds to variant rs34345197 [ dbSNP | Ensembl ].

VAR_048930

Experimental info

Mutagenesis

157

1

S → A: Promotes F-actin assembly; when associated with A-239 and A-278. Interferes with F-actin assembly; when associated with A-239 and E-278. Ref.20

Mutagenesis

239

1

S → A: Promotes F-actin assembly; when associated with A-157 and A-278. Interferes with F-actin assembly; when associated with A-157 and E-278. Ref.20

Mutagenesis

278

1

T → A: Promotes F-actin assembly; when associated with A-157 and A-239. Ref.20

Mutagenesis

278

1

T → E: Interferes with F-actin assembly; when associated with A-157 and A-239. Ref.20

Mutagenesis

370

1

F → A: Lower stability of tetramerization domain. Ref.30

Mutagenesis

370

1

F → I or K: No change in stability of tetramerization domain. Ref.30

Sequence conflict

2

1

S → SS in AAH26019. Ref.5

Sequence conflict

241

1

Missing in AAH26019. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

380

Helix Strand Turn

Details...

Beta strand

5 – 12

8

Beta strand

14 – 16

3

Turn

18 – 20

3

Beta strand

25 – 27

3

Beta strand

34 – 41

8

Turn

42 – 45

4

Beta strand

46 – 55

10

Beta strand

60 – 66

7

Beta strand

79 – 86

8

Beta strand

88 – 95

8

Helix

96 – 114

19

Helix

226 – 231

6

Helix

341 – 376

36

Sequences

	Sequence		Length	Mass (Da)
	P50552 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 17634B8134DEBF59	FASTA	380	39,830
	10 20 30 40 50 60 MSETVICSSR ATVMLYDDGN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV GRKMQPDQQV 70 80 90 100 110 120 VINCAIVRGV KYNQATPNFH QWRDARQVWG LNFGSKEDAA QFAAGMASAL EALEGGGPPP 130 140 150 160 170 180 PPALPTWSVP NGPSPEEVEQ QKRQQPGPSE HIERRVSNAG GPPAPPAGGP PPPPGPPPPP 190 200 210 220 230 240 GPPPPPGLPP SGVPAAAHGA GGGPPPAPPL PAAQGPGGGG AGAPGLAAAI AGAKLRKVSK 250 260 270 280 290 300 QEEASGGPTA PKAESGRSGG GGLMEEMNAM LARRRKATQV GEKTPKDESA NQEEPEARVP 310 320 330 340 350 360 AQSESVRRPW EKNSTTLPRM KSSSSVTTSE TQPCTPSSSD YSDLQRVKQE LLEEVKKELQ 370 380 KVKEEIIEAF VQELRKRGSP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, structural analysis and functional expression of the proline-rich focal adhesion and microfilament-associated protein VASP." Haffner C., Jarchau T., Reinhard M., Hoppe J., Lohmann S.M., Walter U. EMBO J. 14:19-27(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 11-32; 87-96; 140-154; 255-282 AND 297-322, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, POSSIBLE FUNCTION. Tissue: Promyelocyte.
[2]	"Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes." Laurent V., Loisel T.P., Harbeck B., Wehman A., Groebe L., Jockusch B.M., Wehland J., Gertler F.B., Carlier M.-F. J. Cell Biol. 144:1245-1258(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH L.MONOCYTOGENES ACTA.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Substantia nigra.
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Fetal lung, Fetal spleen and Skin.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-10, ACETYLATION AT SER-2. Tissue: Platelet.
[7]	"Cloning of the VASP (vasodilator-stimulated phosphoprotein) genes in human and mouse: structure, sequence, and chromosomal localization." Zimmer M., Fink T., Fischer L., Hauser W., Scherer K., Lichter P., Walter U. Genomics 36:227-233(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 3-380.
[8]	"cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets." Butt E., Abel K., Krieger M., Palm D., Hoppe V., Hoppe J., Walter U. J. Biol. Chem. 269:14509-14517(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 143-164; 235-244 AND 267-285, PHOSPHORYLATION AT SER-157; SER-239 AND THR-278 BY PRKG1.
[9]	"Phosphorylation of focal adhesion vasodilator-stimulated phosphoprotein at Ser157 in intact human platelets correlates with fibrinogen receptor inhibition." Horstrup K., Jablonka B., Honig-Liedl P., Just M., Kochsiek K., Walter U. Eur. J. Biochem. 225:21-27(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-157, FIBRINOGEN RECEPTOR INHIBITION.
[10]	"The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins." Reinhard M., Giehl K., Abel K., Haffner C., Jarchau T., Hoppe V., Jockusch B.M., Walter U. EMBO J. 14:1583-1589(1995) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ACTG1 AND PFN1.
[11]	"The EVH2 domain of the vasodilator-stimulated phosphoprotein mediates tetramerization, F-actin binding, and actin bundle formation." Bachmann C., Fischer L., Walter U., Reinhard M. J. Biol. Chem. 274:23549-23557(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF EVH2 DOMAIN.
[12]	"Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins." Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., Golsteyn R.M. J. Biol. Chem. 275:22503-22511(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ZYX.
[13]	"LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity." Petit M.M., Fradelizi J., Golsteyn R.M., Ayoubi T.A., Menichi B., Louvard D., Van de Ven W.J.M., Friederich E. Mol. Biol. Cell 11:117-129(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LPP.
[14]	"Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics." Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F., Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M., Yaffe M.B., Boussiotis V.A., Gertler F.B. Dev. Cell 7:571-583(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH RAPH1.
[15]	"Vasodilator-stimulated phosphoprotein is a substrate for protein kinase C." Chitaley K., Chen L., Galler A., Walter U., Daum G., Clowes A.W. FEBS Lett. 556:211-215(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION BY PKC.
[16]	"Ena/VASP proteins enhance actin polymerization in the presence of barbed end capping proteins." Barzik M., Kotova T.I., Higgs H.N., Hazelwood L., Hanein D., Gertler F.B., Schafer D.A. J. Biol. Chem. 280:28653-28662(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, LACK OF ACTIN NUCLEATION ACTIVITY, FUNCTION IN ACTIN FILAMENT ELONGATION.
[17]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39, MASS SPECTROMETRY.
[18]	"Vasodilator-stimulated phosphoprotein (VASP) is phosphorylated on Ser 157 by protein kinase C-dependent and -independent mechanisms in thrombin-stimulated human platelets." Wentworth J.K., Pula G., Poole A.W. Biochem. J. 393:555-564(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-157, SUBCELLULAR LOCATION.
[19]	"Unusual splicing events result in distinct Xin isoforms that associate differentially with filamin c and Mena/VASP." van der Ven P.F.M., Ehler E., Vakeel P., Eulitz S., Schenk J.A., Milting H., Micheel B., Fuerst D.O. Exp. Cell Res. 312:2154-2167(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH XIRP1.
[20]	"AMP-activated protein kinase impairs endothelial actin cytoskeleton assembly by phosphorylating vasodilator-stimulated phosphoprotein." Blume C., Benz P.M., Walter U., Ha J., Kemp B.E., Renne T. J. Biol. Chem. 282:4601-4612(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-278, MUTAGENESIS OF SER-157; SER-239 AND THR-278, FUNCTION.
[21]	"Carbon monoxide and nitric oxide mediate cytoskeletal reorganization in microvascular cells via vasodilator-stimulated phosphoprotein phosphorylation: evidence for blunted responsiveness in diabetes." Li Calzi S., Purich D.L., Chang K.H., Afzal A., Nakagawa T., Busik J.V., Agarwal A., Segal M.S., Grant M.B. Diabetes 57:2488-2494(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-157 AND SER-239.
[22]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Platelet.
[23]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316 AND SER-322, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[24]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[25]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, MASS SPECTROMETRY.
[26]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-316, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[27]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]	"Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity." Ball L.J., Kuehne R., Hoffmann B., Haefner A., Schmieder P., Volkmer-Engert R., Hof M., Wahl M., Schneider-Mergener J., Walter U., Oschkinat H., Jarchau T. EMBO J. 19:4903-4914(2000) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 1-115.
[30]	"The VASP tetramerization domain is a right-handed coiled coil based on a 15-residue repeat." Kuehnel K., Jarchau T., Wolf E., Schlichting I., Walter U., Wittinghofer A., Strelkov S.V. Proc. Natl. Acad. Sci. U.S.A. 101:17027-17032(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-380, TETRAMERIZATION, MUTAGENESIS OF PHE-370.
[31]	"Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP." Ferron F., Rebowski G., Lee S.H., Dominguez R. EMBO J. 26:4597-4606(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 203-245 IN COMPLEXES WITH PFN1 AND ACTIN, INTERACTION WITH PFN1 AND MONOMERIC ACTIN.
[32]	"Modulation of actin structure and function by phosphorylation of Tyr-53 and profilin binding." Baek K., Liu X., Ferron F., Shu S., Korn E.D., Dominguez R. Proc. Natl. Acad. Sci. U.S.A. 105:11748-11753(2008) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 199-214 IN COMPLEX WITH PFN1 AND ACTIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

Z46389 mRNA. Translation: CAA86523.1.
CH471126 Genomic DNA. Translation: EAW57362.1.
AK314812 mRNA. Translation: BAG37336.1.
BC026019 mRNA. Translation: AAH26019.1.
BC038224 mRNA. Translation: AAH38224.1.
X98534, X98533 Genomic DNA. Translation: CAA67147.2.

IPI

IPI00301058.

PIR

S51797.

RefSeq

NP_003361.1. NM_003370.3.

UniGene

Hs.515469.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EGX	NMR	-	A	1-115	[»]
1JNG	model	-	A	1-115	[»]
1USD	X-ray	1.70	A	336-380	[»]
1USE	X-ray	1.30	A	336-380	[»]
2PAV	X-ray	1.80	V	199-214	[»]
2PBD	X-ray	1.50	V	203-245	[»]
3CHW	X-ray	2.30	V	199-214	[»]

ProteinModelPortal

P50552.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-44105N.

IntAct

P50552. 17 interactions.

MINT

MINT-1437861.

STRING

9606.ENSP00000245932.

PTM databases

PhosphoSite

P50552.

Polymorphism databases

DMDM

1718079.

2D gel databases

OGP

P50552.

Proteomic databases

PaxDb

P50552.

PeptideAtlas

P50552.

PRIDE

P50552.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000245932; ENSP00000245932; ENSG00000125753.

GeneID

7408.

KEGG

hsa:7408.

UCSC

uc002pcg.3. human.

Organism-specific databases

CTD

7408.

GeneCards

GC19P046010.

HGNC

HGNC:12652. VASP.

HPA

CAB004612.
HPA005724.

MIM

601703. gene.

neXtProt

NX_P50552.

PharmGKB

PA37276.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG265043.

HOGENOM

HOG000013015.

HOVERGEN

HBG006655.

InParanoid

P50552.

KO

K06274.

OMA

PTWSVPN.

OrthoDB

EOG49GKHQ.

PhylomeDB

P50552.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_6900. Immune System.

Gene expression databases

Bgee

P50552.

CleanEx

HS_VASP.

Genevestigator

P50552.

GermOnline

ENSG00000125753. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR000697. EVH1.
IPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
[Graphical view]

Pfam

PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]

PIRSF

PIRSF038010. Vasodilator_Phospo. 1 hit.

SMART

SM00461. WH1. 1 hit.
[Graphical view]

PROSITE

PS50229. WH1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VASP. human.

EvolutionaryTrace

P50552.

GenomeRNAi

7408.

NextBio

29004.

SOURCE

Search...

Entry information

Entry name

VASP_HUMAN

Accession

Primary (citable) accession number: P50552
Secondary accession number(s): B2RBT9, Q6PIZ1, Q93035

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.