Overview
| Uniprot ID | D3YXG6 |
|---|
| Protein Name | Arp2/3 complex 34 kDa subunit |
|---|
| Gene Name | Arpc2 |
|---|
| Organism | Mus musculus |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 279 |
EMKTITGKTFSSR** |
Function
Actin-binding component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility. Seems to contact the mother actin filament. 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. 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)
Protein Sequence
10
MDVGSHGARN
20
KPEAVEVTFA
30
DFDGVLYHIS
40
NPNGDKTKVM
50
VSISLKFYKE
60
LQAHGADELL
70
KRVYGSFLVN
80
PEPGYNVSLL
90
YDLENLPASK
100
DSIVHQAGML
110
KRNCFASVFE
120
KYFQFQEEGK
130
EGENRAVIHY
140
RDDETMYVES
150
KKDRVTVVFS
160
TVFKDDDDVV
170
IGKVFMQEFK
180
EGRRASHTAP
190
QVLFSHREPP
200
LELKDTDAAV
210
GDNIGYITFV
220
LFPRHTNATA
230
RDNTINLIHT
240
FRDYLHYHIK
250
CSKAYIHTRM
260
RAKTSDFLKV
270
LNRARPDAEK
280
KEMKTITGKT
FSSR
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005885 |
Arp2/3 protein complex |
| Cellular Component |
GO:0043005 |
neuron projection |
| Cellular Component |
GO:0045202 |
synapse |
| Molecular Function |
GO:0003779 |
actin binding |
| Biological Process |
GO:0030041 |
actin filament polymerization |
| Biological Process |
GO:0034314 |
Arp2/3 complex-mediated actin nucleation |
| Biological Process |
GO:0031334 |
positive regulation of protein-containing complex assembly |
| Biological Process |
GO:0030833 |
regulation of actin filament polymerization |
Reference
[1] Sung E, Sim H, Cho YC, Lee W, Bae JS et al.. Global Profiling of Lysine Acetylation and Lactylation in Kupffer Cells.. J Proteome Res 22(12):3683-3691. 2023 Dec 1. PMID: 37897433.