Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P70460

- VASP_MOUSE

UniProt

P70460 - VASP_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Vasodilator-stimulated phosphoprotein

Gene

Vasp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Biological processi

  1. actin cytoskeleton organization Source: MGI
  2. actin polymerization or depolymerization Source: InterPro
  3. axon guidance Source: MGI
  4. neural tube closure Source: MGI
  5. positive regulation of actin filament polymerization Source: Ensembl
  6. protein homotetramerization Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_221567. Signaling by Robo receptor.
REACT_225768. Generation of second messenger molecules.
REACT_243772. Cell-extracellular matrix interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Vasodilator-stimulated phosphoprotein
Short name:
VASP
Gene namesi
Name:Vasp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:109268. Vasp.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication. Cell junctionfocal adhesion 1 Publication. Cell junctiontight junction By similarity. Cell projectionlamellipodium membrane 1 Publication. Cell projectionfilopodium membrane 1 Publication
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 (By similarity). In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes) (By similarity).By similarity

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. filopodium Source: MGI
  5. focal adhesion Source: MGI
  6. lamellipodium Source: MGI
  7. plasma membrane Source: UniProtKB-KW
  8. tight junction Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi153 – 1531S → D: Reduces actin polymerization to a lesser extent than wild-type. Greater effect on actin polymerization; when associated with D-235 and E-274. 1 Publication
Mutagenesisi232 – 2332RK → GE or EE: Reduced binding to monomeric actin. No VASP-induced actin polymerization. 1 Publication
Mutagenesisi235 – 2351S → D: Reduces actin polymerization to a lesser extent than wild-type. 1 Publication
Mutagenesisi274 – 2741T → E: Reduces actin polymerization to a lesser extent than wild-type. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 375374Vasodilator-stimulated phosphoproteinPRO_0000065768Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei39 – 391PhosphotyrosineBy similarity
Modified residuei153 – 1531Phosphoserine; by PKA, PKC, PKG/PRKG1 and ROCK11 Publication
Modified residuei235 – 2351Phosphoserine; by PKA and PKG1 Publication
Modified residuei274 – 2741Phosphothreonine; by PKA, PKG/PRKG1 and AMPKBy similarity
Modified residuei279 – 2791N6-acetyllysineBy similarity
Modified residuei311 – 3111PhosphothreonineBy similarity
Modified residuei317 – 3171PhosphoserineBy similarity
Modified residuei318 – 3181Phosphoserine; by AMPK1 Publication

Post-translational modificationi

Major substrate for cAMP-dependent (PKA) and cGMP-dependent protein kinase (PKG) in platelets. The preferred site for PKA is Ser-153, the preferred site for PKG, Ser-235. In ADP-activated platelets, phosphorylation by PKA or PKG/PRKG1 on Ser-153 leads to fibrinogen receptor inhibition. Phosphorylation on Thr-274 requires prior phosphorylation on Ser-153 and Ser-235. In response to phorbol ester (PMA) stimulation, phosphorylated by PKC/PRKCA. In response to thrombin, phosphorylated by both PKC and ROCK1. Phosphorylation at Thr-274 by AMPK does not require prior phosphorylation at Ser-153 or Ser-235. Phosphorylation at Ser-153 by PKA is required for localization to the tight junctions in epithelial cells. Phosphorylation modulates F-actin binding, actin filament elongation and platelet activation. Phosphorylation at Ser-318 by AMPK also alters actin filament binding. Carbon monoxide (CO) promotes phosphorylation at Ser-153, while nitric oxide (NO) promotes phosphorylation at Ser-153, but also at Ser-235.4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP70460.
PaxDbiP70460.
PRIDEiP70460.

PTM databases

PhosphoSiteiP70460.

Expressioni

Tissue specificityi

Highly expressed in thymus and spleen. Lower levels in lung, ovary, placenta and fat.1 Publication

Developmental stagei

Expressed constantly throughout brain development, with lower levels in adulthood.1 Publication

Gene expression databases

BgeeiP70460.
CleanExiMM_VASP.
GenevestigatoriP70460.

Interactioni

Subunit structurei

Homotetramer (By similarity). 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. Interacts weakly with MEFV (By similarity).By similarity

Protein-protein interaction databases

BioGridi204499. 2 interactions.
IntActiP70460. 3 interactions.
MINTiMINT-1215713.

Structurei

3D structure databases

ProteinModelPortaliP70460.
SMRiP70460. Positions 1-115, 333-372.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 113112WH1PROSITE-ProRule annotationAdd
BLAST
Repeati340 – 354151Add
BLAST
Repeati355 – 369152Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni221 – 373153EVH2Add
BLAST
Regioni221 – 24121EVH2 block AAdd
BLAST
Regioni257 – 27418EVH2 block BAdd
BLAST
Regioni338 – 37235EVH2 block CAdd
BLAST
Regioni339 – 368302 X 15 AA tandem repeats of L-[EQ]-[KR] [MV]-K-[EQ]-E-[IL]-[IL]-E-[AEV]-[FV]-[KRV]-[KQ]-EAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili337 – 36731Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi230 – 2334KLKR

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi166 – 18217Poly-ProAdd
BLAST
Compositional biasi317 – 3204Poly-Ser

Domaini

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.
The WH1 domain mediates interaction with XIRP1.By similarity

Sequence similaritiesi

Belongs to the Ena/VASP family.Curated
Contains 1 WH1 domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, SH3-binding

Phylogenomic databases

eggNOGiNOG265043.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiP70460.
KOiK06274.
OMAiQPEHMER.
OrthoDBiEOG72JWGQ.
PhylomeDBiP70460.
TreeFamiTF321411.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFiPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P70460-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSETVICSSR ATVMLYDDSN KRWLPAGTGP QAFSRVQIYH NPTANSFRVV
60 70 80 90 100
GRKMQPDQQV VINCAIIRGV KYNQATPIFH QWRDARQVWG LNFGSKEDAI
110 120 130 140 150
QFATGMANAL EALEGGGPPP APAPPAWSAQ NGPSPEELEQ QKRQPEHMER
160 170 180 190 200
RVSNAGGPPA PPAGGPPPPP GPPPPPGPPP PPGLPSSGVS GAGHGAGAAP
210 220 230 240 250
PPAPPLPTAQ GPNSGGSGAP GLAAAIAGAK LRKVSKQEEA SGGPLAPKAE
260 270 280 290 300
NSRSTGGGLM EEMNAMLARR RKATQVGEKP PKDESASEES EARLPAQSEP
310 320 330 340 350
VRRPWEKNST TLPRMKSSSS VTTSEAHPST PCSSDDSDLE RVKQELLEEV
360 370
RKELQKMKEE IIEVFVQELR KRGSP
Length:375
Mass (Da):39,667
Last modified:January 23, 2007 - v4
Checksum:i19369286CF4276C7
GO

Sequence cautioni

The sequence CAA67108.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti106 – 11510Missing in BAE42025. (PubMed:16141072)Curated
Sequence conflicti237 – 2371Missing in BAE33933. (PubMed:16141072)Curated
Sequence conflicti337 – 3371S → Y in BAE29310. (PubMed:16141072)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti209 – 2091A → T.2 Publications

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98475 Genomic DNA. Translation: CAA67108.1. Sequence problems.
AF084548 mRNA. Translation: AAD16045.1.
AK140329 mRNA. Translation: BAE24338.1.
AK150103 mRNA. Translation: BAE29310.1.
AK157021 mRNA. Translation: BAE33933.1.
AK170780 mRNA. Translation: BAE42025.1.
AK171715 mRNA. Translation: BAE42628.1.
BC010223 mRNA. Translation: AAH10223.1.
BC015289 mRNA. Translation: AAH15289.1.
CCDSiCCDS52056.1.
RefSeqiNP_001268950.1. NM_001282021.1.
NP_001268951.1. NM_001282022.1.
NP_033525.2. NM_009499.3.
UniGeneiMm.9684.

Genome annotation databases

EnsembliENSMUST00000032561; ENSMUSP00000032561; ENSMUSG00000030403.
GeneIDi22323.
KEGGimmu:22323.
UCSCiuc009fle.2. mouse.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X98475 Genomic DNA. Translation: CAA67108.1 . Sequence problems.
AF084548 mRNA. Translation: AAD16045.1 .
AK140329 mRNA. Translation: BAE24338.1 .
AK150103 mRNA. Translation: BAE29310.1 .
AK157021 mRNA. Translation: BAE33933.1 .
AK170780 mRNA. Translation: BAE42025.1 .
AK171715 mRNA. Translation: BAE42628.1 .
BC010223 mRNA. Translation: AAH10223.1 .
BC015289 mRNA. Translation: AAH15289.1 .
CCDSi CCDS52056.1.
RefSeqi NP_001268950.1. NM_001282021.1.
NP_001268951.1. NM_001282022.1.
NP_033525.2. NM_009499.3.
UniGenei Mm.9684.

3D structure databases

ProteinModelPortali P70460.
SMRi P70460. Positions 1-115, 333-372.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 204499. 2 interactions.
IntActi P70460. 3 interactions.
MINTi MINT-1215713.

PTM databases

PhosphoSitei P70460.

Proteomic databases

MaxQBi P70460.
PaxDbi P70460.
PRIDEi P70460.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000032561 ; ENSMUSP00000032561 ; ENSMUSG00000030403 .
GeneIDi 22323.
KEGGi mmu:22323.
UCSCi uc009fle.2. mouse.

Organism-specific databases

CTDi 7408.
MGIi MGI:109268. Vasp.

Phylogenomic databases

eggNOGi NOG265043.
GeneTreei ENSGT00730000110272.
HOVERGENi HBG006655.
InParanoidi P70460.
KOi K06274.
OMAi QPEHMER.
OrthoDBi EOG72JWGQ.
PhylomeDBi P70460.
TreeFami TF321411.

Enzyme and pathway databases

Reactomei REACT_221567. Signaling by Robo receptor.
REACT_225768. Generation of second messenger molecules.
REACT_243772. Cell-extracellular matrix interactions.

Miscellaneous databases

NextBioi 302545.
PROi P70460.
SOURCEi Search...

Gene expression databases

Bgeei P70460.
CleanExi MM_VASP.
Genevestigatori P70460.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view ]
Pfami PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view ]
PIRSFi PIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTi SM00461. WH1. 1 hit.
[Graphical view ]
PROSITEi PS50229. WH1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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], VARIANT THR-209.
    Strain: 129.
  2. "Cyclic AMP- and cyclic GMP-dependent protein kinases differ in their regulation of cyclic AMP response element-dependent gene transcription."
    Collins S.P., Uhler M.D.
    J. Biol. Chem. 274:8391-8404(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION.
    Strain: C57BL/6J.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-209.
    Strain: C57BL/6J and NOD.
    Tissue: Adipose tissue, Bone marrow, Dendritic cell and Spleen.
  4. "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].
    Strain: FVB/N.
    Tissue: Kidney and Mammary tumor.
  5. Cited for: DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
  6. "Directed actin polymerization is the driving force for epithelial cell-cell adhesion."
    Vasioukhin V., Bauer C., Yin M., Fuchs E.
    Cell 100:209-219(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  7. "Phosphorylation of the vasodilator-stimulated phosphoprotein regulates its interaction with actin."
    Harbeck B., Huttelmaier S., Schlueter K., Jockusch B.M., Illenberger S.
    J. Biol. Chem. 275:30817-30825(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTN1; PFN1; PFN2; VCL AND ZYX, PHOSPHORYLATION AT SER-153 AND SER-235, MUTAGENESIS OF SER-153; SER-235 AND THR-274.
  8. "The vasodilator-stimulated phosphoprotein promotes actin polymerisation through direct binding to monomeric actin."
    Walders-Harbeck B., Khaitlina S.Y., Hinssen H., Jockusch B.M., Illenberger S.
    FEBS Lett. 529:275-280(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACTG1, PHOSPHORYLATION, MUTAGENESIS OF 232-ARG-LYS-233.
  9. "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton."
    Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
    J. Biol. Chem. 278:49031-49043(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DNMBP.
  10. "PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins."
    Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.
    FEBS Lett. 579:455-463(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH APBB1IP.
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Phosphorylation of VASP by AMPK alters actin binding and occurs at a novel site."
    Thomson D.M., Ascione M.P., Grange J., Nelson C., Hansen M.D.
    Biochem. Biophys. Res. Commun. 414:215-219(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-318.

Entry informationi

Entry nameiVASP_MOUSE
AccessioniPrimary (citable) accession number: P70460
Secondary accession number(s): Q3TAP0
, Q3TCD2, Q3U0C2, Q3UDF1, Q91VD2, Q9R214
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 125 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3