Search Results

Overview

Uniprot IDO15143
Protein NameActin-related protein 2/3 complex subunit 1B
Gene NameARPC1B
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
307 ERFQNLDKKASSEGG
308 RFQNLDKKASSEGGT
339 ISVLSGGKAKCSQFC
82 NAYVWTLKGRTWKPT
87 TLKGRTWKPTLVILR

Function

Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF) (PubMed:11741539, PubMed:9230079). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (PubMed:11741539, 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 MAYHSFLVEP 20 ISCHAWNKDR 30 TQIAICPNNH 40 EVHIYEKSGA 50 KWTKVHELKE 60 HNGQVTGIDW 70 APESNRIVTC 80 GTDRNAYVWT 90 LKGRTWKPTL 100 VILRINRAAR 110 CVRWAPNENK 120 FAVGSGSRVI 130 SICYFEQEND 140 WWVCKHIKKP 150 IRSTVLSLDW 160 HPNNVLLAAG 170 SCDFKCRIFS 180 AYIKEVEERP 190 APTPWGSKMP 200 FGELMFESSS 210 SCGWVHGVCF 220 SASGSRVAWV 230 SHDSTVCLAD 240 ADKKMAVATL 250 ASETLPLLAL 260 TFITDNSLVA 270 AGHDCFPVLF 280 TYDAAAGMLS 290 FGGRLDVPKQ 300 SSQRGLTARE 310 RFQNLDKKAS 320 SEGGTAAGAG 330 LDSLHKNSVS 340 QISVLSGGKA 350 KCSQFCTTGM 360 DGGMSIWDVK 370 SLESALKDLK IK

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:0070062 extracellular exosome
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005634 nucleus
Cellular Component GO:0036284 tubulobulbar complex
Molecular Function GO:0003779 actin binding
Molecular Function GO:0044877 protein-containing complex binding
Molecular Function GO:0005200 structural constituent of cytoskeleton
Biological Process GO:0034314 Arp2/3 complex-mediated actin nucleation
Biological Process GO:0032355 response to estradiol
Biological Process GO:0043627 response to estrogen

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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.

[4] 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.

[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] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.

[8] 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.