Search Results

Overview

Uniprot IDO15144
Protein NameActin-related protein 2/3 complex subunit 2
Gene NameARPC2
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
117 VHQAGMLKRNCFASV
259 HYHIKCSKAYIHTRM
269 IHTRMRAKTSDFLKV
275 AKTSDFLKVLNRARP
286 RARPDAEKKEMKTIT
295 EMKTITGKTFSSR**
65 SISLKFYKELQAHGA

Function

Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:9230079). Seems to contact the mother actin filament (PubMed:9230079). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA (PubMed:29925947). The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (PubMed:29925947)

Protein Sequence

10 MILLEVNNRI 20 IEETLALKFE 30 NAAAGNKPEA 40 VEVTFADFDG 50 VLYHISNPNG 60 DKTKVMVSIS 70 LKFYKELQAH 80 GADELLKRVY 90 GSFLVNPESG 100 YNVSLLYDLE 110 NLPASKDSIV 120 HQAGMLKRNC 130 FASVFEKYFQ 140 FQEEGKEGEN 150 RAVIHYRDDE 160 TMYVESKKDR 170 VTVVFSTVFK 180 DDDDVVIGKV 190 FMQEFKEGRR 200 ASHTAPQVLF 210 SHREPPLELK 220 DTDAAVGDNI 230 GYITFVLFPR 240 HTNASARDNT 250 INLIHTFRDY 260 LHYHIKCSKA 270 YIHTRMRAKT 280 SDFLKVLNRA 290 RPDAEKKEMK 300 TITGKTFSSR

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005885 Arp2/3 protein complex
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005768 endosome
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0098978 glutamatergic synapse
Cellular Component GO:0030027 lamellipodium
Cellular Component GO:0036195 muscle cell projection membrane
Cellular Component GO:0043005 neuron projection
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0098794 postsynapse
Cellular Component GO:0035861 site of double-strand break
Cellular Component GO:0030672 synaptic vesicle membrane
Molecular Function GO:0003779 actin binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0030041 actin filament polymerization
Biological Process GO:0070358 actin polymerization-dependent cell motility
Biological Process GO:0034314 Arp2/3 complex-mediated actin nucleation
Biological Process GO:0010592 positive regulation of lamellipodium assembly

Reference

[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.

[2] 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.

[3] 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.

[4] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[5] 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.

[6] 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.