| Type | Description |
|---|---|
| Definition | actin-like protein Arp3 |
| Date | Results | Publications |
|---|---|---|
| 2021-02-02 13:27:00 | Cryo-EM reveals the transition of Arp2/3 complex from inactive to nucleation-competent state. | 32839613 |
| 2020-09-12 16:05:00 | Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. | 32461373 |
| 2018-10-20 10:44:00 | WASp-VCA binding to Arp2/3 protein complex causes a conformational change that favors binding to the side of an actin filament, which allows further changes required to nucleate a daughter filament. | 30150414 |
| 2018-09-15 12:03:00 | role in the actin filament nucleation.ATP binding destabilizes this interaction via an allosteric link between the Arp3 nucleotide cleft and the hydrophobic groove, thereby promoting the short-pitch conformation. | 27417392 |
| 2016-04-09 11:21:00 | Arp2/3 complex participates in regulating formin F-actin networks. | 24560576 |
| Type | IDs |
|---|---|
| Synonymous | act2 |
| Gene |
UniProtKB-ID:
ARP3_SCHPO
UniprotKB:
P32390
UniParc:
UPI000012605D
EMBL:
CU329670,
M81068
EnsemblGenome:
SPAC630.03
KO:
spo:SPAC630.03
|
| Nucleutide sequences |
EMBL-CDS:
CAB52725.1
Gene_ORFName:
SPAC630.03
EnsemblGenome_TRS:
SPAC630.03.1
|
| Protein sequencees |
EnsemblGenome_PRO:
SPAC630.03.1:pep
RefSeq:
NP_592898.1
|
| Others |
UniRef100:
UniRef100_P32390
UniRef90:
UniRef90_P32390
UniRef50:
UniRef50_P32390
|
| {{proteinIndex+1}} | mRNA | Protein | UniprotKB | Description | ||||
|---|---|---|---|---|---|---|---|---|
| Refseq |
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| Location | {{protein.contigId}} ( {{protein.positionStart}}..{{protein.positionEnd}} , {{protein.orientation}} ) | |||||||
| Conserved domain | Region: {{conservedDomain.region == '' || conservedDomain.region == null ? "-": conservedDomain.region}} GFID: {{conservedDomain.gfid == '' || conservedDomain.gfid == null ? "-": conservedDomain.gfid}} Family: {{conservedDomain.family == '' || conservedDomain.family == null ? "-": conservedDomain.family}} CDD: {{conservedDomain.cdd}} - |
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