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Overview

Uniprot IDP59998
Protein NameActin-related protein 2/3 complex subunit 4
Gene NameARPC4
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
128 FHTEQMYKHKLVDFV
44 EVEVRSSKELLLQPV
89 IEKILCHKFMRFMMM

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). 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 MTATLRPYLS 20 AVRATLQAAL 30 CLENFSSQVV 40 ERHNKPEVEV 50 RSSKELLLQP 60 VTISRNEKEK 70 VLIEGSINSV 80 RVSIAVKQAD 90 EIEKILCHKF 100 MRFMMMRAEN 110 FFILRRKPVE 120 GYDISFLITN 130 FHTEQMYKHK 140 LVDFVIHFME 150 EIDKEISEMK 160 LSVNARARIV AEEFLKNF

Gene Ontology

Classification GO ID Description
Cellular Component GO:0015629 actin cytoskeleton
Cellular Component GO:0005885 Arp2/3 protein complex
Cellular Component GO:0042995 cell projection
Cellular Component GO:0005829 cytosol
Cellular Component GO:0070062 extracellular exosome
Cellular Component GO:0005634 nucleus
Cellular Component GO:0035861 site of double-strand break
Molecular Function GO:0003779 actin binding
Molecular Function GO:0019899 enzyme binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0030041 actin filament polymerization
Biological Process GO:0045010 actin nucleation
Biological Process GO:0034314 Arp2/3 complex-mediated actin nucleation

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] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[3] 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.