O15144 · ARPC2_HUMAN

  • Protein
    Actin-related protein 2/3 complex subunit 2
  • Gene
    ARPC2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentactin cytoskeleton
Cellular ComponentArp2/3 protein complex
Cellular Componentcytosol
Cellular Componentendosome
Cellular Componentextracellular exosome
Cellular Componentfocal adhesion
Cellular Componentglutamatergic synapse
Cellular Componentlamellipodium
Cellular Componentmuscle cell projection membrane
Cellular Componentneuron projection
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentsite of double-strand break
Molecular Functionactin binding
Molecular Functionstructural constituent of cytoskeleton
Biological Processactin filament polymerization
Biological Processactin polymerization-dependent cell motility
Biological ProcessArp2/3 complex-mediated actin nucleation
Biological Processpositive regulation of actin filament polymerization
Biological Processpositive regulation of lamellipodium assembly
Biological Processpositive regulation of substrate adhesion-dependent cell spreading

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Actin-related protein 2/3 complex subunit 2
  • Alternative names
    • Arp2/3 complex 34 kDa subunit (p34-ARC)

Gene names

    • Name
      ARPC2
    • Synonyms
      ARC34
    • ORF names
      PRO2446

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O15144
  • Secondary accessions
    • Q92801
    • Q9P1D4

Proteomes

Organism-specific databases

Disease & Variants

Variants

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The viewer provides 253 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00001240331-300UniProt
Modified residue (large scale data)192PRIDEPhosphoserine
Modified residue275UniProtN6-acetyllysine
Modified residue295UniProtN6-acetyllysine

Keywords

Proteomic databases

2D gel databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Component of the Arp2/3 complex composed of ACTR2/ARP2, ACTR3/ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC (PubMed:11741539, PubMed:9230079).
Interacts with SHANK3; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex (By similarity).
Interacts with DNAI3; this interaction reduces binding of the Arp2/3 complex to the VCA domain of nucleation promoting factors (PubMed:32128961).

Binary interactions

View interactors in UniProtKB
View CPX-2490 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Sequence similarities

Belongs to the ARPC2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    300
  • Mass (Da)
    34,333
  • Last updated
    1998-01-01 v1
  • Checksum
    3BA57121BE9A05F2
MILLEVNNRIIEETLALKFENAAAGNKPEAVEVTFADFDGVLYHISNPNGDKTKVMVSISLKFYKELQAHGADELLKRVYGSFLVNPESGYNVSLLYDLENLPASKDSIVHQAGMLKRNCFASVFEKYFQFQEEGKEGENRAVIHYRDDETMYVESKKDRVTVVFSTVFKDDDDVVIGKVFMQEFKEGRRASHTAPQVLFSHREPPLELKDTDAAVGDNIGYITFVLFPRHTNASARDNTINLIHTFRDYLHYHIKCSKAYIHTRMRAKTSDFLKVLNRARPDAEKKEMKTITGKTFSSR

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9JTV5C9JTV5_HUMANARPC289
H7C3F9H7C3F9_HUMANARPC2165
G5E9J0G5E9J0_HUMANARPC291
G5E9S7G5E9S7_HUMANARPC238

Sequence caution

The sequence AAC50874.1 differs from that shown. Reason: Frameshift
The sequence AAF71122.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict72in Ref. 2; AAC50874
Sequence conflict289-300in Ref. 6; AAF71122

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF006085
EMBL· GenBank· DDBJ
AAB64190.1
EMBL· GenBank· DDBJ
mRNA
U50523
EMBL· GenBank· DDBJ
AAC50874.1
EMBL· GenBank· DDBJ
mRNA Frameshift
BT006898
EMBL· GenBank· DDBJ
AAP35544.1
EMBL· GenBank· DDBJ
mRNA
BC000590
EMBL· GenBank· DDBJ
AAH00590.1
EMBL· GenBank· DDBJ
mRNA
AF116702
EMBL· GenBank· DDBJ
AAF71122.1
EMBL· GenBank· DDBJ
mRNA Different initiation

Genome annotation databases

Similar Proteins

Disclaimer

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