Search Results

Overview

Uniprot IDP50552
Protein NameVasodilator-stimulated phosphoprotein
Gene NameVASP
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
240 AKLRKVSKQEEASGG
252 SGGPTAPKAESGRSG
276 AMLARRRKATQVGEK
283 KATQVGEKTPKDESA
286 QVGEKTPKDESANQE
312 SVRRPWEKNSTTLPR
321 STTLPRMKSSSSVTT
348 YSDLQRVKQELLEEV

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

Protein Sequence

10 MSETVICSSR 20 ATVMLYDDGN 30 KRWLPAGTGP 40 QAFSRVQIYH 50 NPTANSFRVV 60 GRKMQPDQQV 70 VINCAIVRGV 80 KYNQATPNFH 90 QWRDARQVWG 100 LNFGSKEDAA 110 QFAAGMASAL 120 EALEGGGPPP 130 PPALPTWSVP 140 NGPSPEEVEQ 150 QKRQQPGPSE 160 HIERRVSNAG 170 GPPAPPAGGP 180 PPPPGPPPPP 190 GPPPPPGLPP 200 SGVPAAAHGA 210 GGGPPPAPPL 220 PAAQGPGGGG 230 AGAPGLAAAI 240 AGAKLRKVSK 250 QEEASGGPTA 260 PKAESGRSGG 270 GGLMEEMNAM 280 LARRRKATQV 290 GEKTPKDESA 300 NQEEPEARVP 310 AQSESVRRPW 320 EKNSTTLPRM 330 KSSSSVTTSE 340 TQPCTPSSSD 350 YSDLQRVKQE 360 LLEEVKKELQ 370 KVKEEIIEAF 380 VQELRKRGSP

Gene Ontology

Classification GO ID Description
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005923 bicellular tight junction
Cellular Component GO:0030054 cell junction
Cellular Component GO:0005829 cytosol
Cellular Component GO:0031527 filopodium membrane
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0031258 lamellipodium membrane
Cellular Component GO:0005886 plasma membrane
Cellular Component GO:0098794 postsynapse
Molecular Function GO:0003779 actin binding
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0042802 identical protein binding
Molecular Function GO:0005522 profilin binding
Molecular Function GO:0017124 SH3 domain binding
Biological Process GO:0008154 actin polymerization or depolymerization
Biological Process GO:0007411 axon guidance
Biological Process GO:0001843 neural tube closure
Biological Process GO:0030838 positive regulation of actin filament polymerization
Biological Process GO:0051289 protein homotetramerization

Reference

[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.

[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.

[3] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.

[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[5] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.

[6] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.

[7] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.