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Protein

Actin-related protein 2/3 complex subunit 2

Gene

ARPC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Functions as actin-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the mother actin filament.

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 2
Alternative name(s):
Arp2/3 complex 34 kDa subunit
Short name:
p34-ARC
Gene namesi
Name:ARPC2
Synonyms:ARC34
ORF Names:PRO2446
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:705. ARPC2.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • Arp2/3 protein complex Source: FlyBase
  • cell leading edge Source: Ensembl
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endosome Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • Golgi apparatus Source: HPA
  • muscle cell projection membrane Source: Ensembl
  • neuron projection Source: UniProtKB-SubCell
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24999.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 300300Actin-related protein 2/3 complex subunit 2PRO_0000124033Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei275 – 2751N6-acetyllysineCombined sources
Modified residuei295 – 2951N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiO15144.
MaxQBiO15144.
PaxDbiO15144.
PeptideAtlasiO15144.
PRIDEiO15144.
TopDownProteomicsiO15144.

2D gel databases

OGPiO15144.

PTM databases

iPTMnetiO15144.
PhosphoSiteiO15144.
SwissPalmiO15144.

Expressioni

Gene expression databases

BgeeiO15144.
CleanExiHS_ARPC2.
ExpressionAtlasiO15144. baseline and differential.
GenevisibleiO15144. HS.

Organism-specific databases

HPAiCAB001994.
HPA008352.

Interactioni

Subunit structurei

Component of the Arp2/3 complex composed of ARP2, ARP3, ARPC1B/p41-ARC, ARPC2/p34-ARC, ARPC3/p21-ARC, ARPC4/p20-ARC and ARPC5/p16-ARC. Interacts with SHANK3; the interaction probably mediates the association of SHANK3 with the Arp2/3 complex.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
CORO1BQ9BR762EBI-352356,EBI-351152
VCLP182062EBI-352356,EBI-716775

Protein-protein interaction databases

BioGridi115415. 80 interactions.
DIPiDIP-33197N.
IntActiO15144. 33 interactions.
MINTiMINT-5000439.
STRINGi9606.ENSP00000295685.

Structurei

3D structure databases

ProteinModelPortaliO15144.
SMRiO15144. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC2 family.Curated

Phylogenomic databases

eggNOGiKOG2826. Eukaryota.
ENOG410YKF6. LUCA.
HOGENOMiHOG000212535.
HOVERGENiHBG050580.
InParanoidiO15144.
KOiK05758.
OMAiVFIQEFV.
OrthoDBiEOG73JKVS.
PhylomeDBiO15144.
TreeFamiTF315006.

Family and domain databases

InterProiIPR007188. ARPC2.
[Graphical view]
PANTHERiPTHR12058. PTHR12058. 1 hit.
PfamiPF04045. P34-Arc. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILLEVNNRI IEETLALKFE NAAAGNKPEA VEVTFADFDG VLYHISNPNG
60 70 80 90 100
DKTKVMVSIS LKFYKELQAH GADELLKRVY GSFLVNPESG YNVSLLYDLE
110 120 130 140 150
NLPASKDSIV HQAGMLKRNC FASVFEKYFQ FQEEGKEGEN RAVIHYRDDE
160 170 180 190 200
TMYVESKKDR VTVVFSTVFK DDDDVVIGKV FMQEFKEGRR ASHTAPQVLF
210 220 230 240 250
SHREPPLELK DTDAAVGDNI GYITFVLFPR HTNASARDNT INLIHTFRDY
260 270 280 290 300
LHYHIKCSKA YIHTRMRAKT SDFLKVLNRA RPDAEKKEMK TITGKTFSSR
Length:300
Mass (Da):34,333
Last modified:January 1, 1998 - v1
Checksum:i3BA57121BE9A05F2
GO

Sequence cautioni

The sequence AAC50874.1 differs from that shown. Reason: Frameshift at position 14. Curated
The sequence AAF71122.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti72 – 721A → C in AAC50874 (PubMed:8812419).Curated
Sequence conflicti289 – 30012MKTIT…TFSSR → KI in AAF71122 (Ref. 6) CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006085 mRNA. Translation: AAB64190.1.
U50523 mRNA. Translation: AAC50874.1. Frameshift.
BT006898 mRNA. Translation: AAP35544.1.
BC000590 mRNA. Translation: AAH00590.1.
AF116702 mRNA. Translation: AAF71122.1. Different initiation.
CCDSiCCDS2410.1.
RefSeqiNP_005722.1. NM_005731.3.
NP_690601.1. NM_152862.2.
UniGeneiHs.529303.

Genome annotation databases

EnsembliENST00000295685; ENSP00000295685; ENSG00000163466.
ENST00000315717; ENSP00000327137; ENSG00000163466.
GeneIDi10109.
KEGGihsa:10109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF006085 mRNA. Translation: AAB64190.1.
U50523 mRNA. Translation: AAC50874.1. Frameshift.
BT006898 mRNA. Translation: AAP35544.1.
BC000590 mRNA. Translation: AAH00590.1.
AF116702 mRNA. Translation: AAF71122.1. Different initiation.
CCDSiCCDS2410.1.
RefSeqiNP_005722.1. NM_005731.3.
NP_690601.1. NM_152862.2.
UniGeneiHs.529303.

3D structure databases

ProteinModelPortaliO15144.
SMRiO15144. Positions 1-283.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115415. 80 interactions.
DIPiDIP-33197N.
IntActiO15144. 33 interactions.
MINTiMINT-5000439.
STRINGi9606.ENSP00000295685.

PTM databases

iPTMnetiO15144.
PhosphoSiteiO15144.
SwissPalmiO15144.

2D gel databases

OGPiO15144.

Proteomic databases

EPDiO15144.
MaxQBiO15144.
PaxDbiO15144.
PeptideAtlasiO15144.
PRIDEiO15144.
TopDownProteomicsiO15144.

Protocols and materials databases

DNASUi10109.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000295685; ENSP00000295685; ENSG00000163466.
ENST00000315717; ENSP00000327137; ENSG00000163466.
GeneIDi10109.
KEGGihsa:10109.

Organism-specific databases

CTDi10109.
GeneCardsiARPC2.
HGNCiHGNC:705. ARPC2.
HPAiCAB001994.
HPA008352.
MIMi604224. gene.
neXtProtiNX_O15144.
PharmGKBiPA24999.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2826. Eukaryota.
ENOG410YKF6. LUCA.
HOGENOMiHOG000212535.
HOVERGENiHBG050580.
InParanoidiO15144.
KOiK05758.
OMAiVFIQEFV.
OrthoDBiEOG73JKVS.
PhylomeDBiO15144.
TreeFamiTF315006.

Enzyme and pathway databases

ReactomeiR-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiARPC2. human.
GeneWikiiARPC2.
GenomeRNAii10109.
NextBioi38237.
PROiO15144.
SOURCEiSearch...

Gene expression databases

BgeeiO15144.
CleanExiHS_ARPC2.
ExpressionAtlasiO15144. baseline and differential.
GenevisibleiO15144. HS.

Family and domain databases

InterProiIPR007188. ARPC2.
[Graphical view]
PANTHERiPTHR12058. PTHR12058. 1 hit.
PfamiPF04045. P34-Arc. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly."
    Welch M.D., Depace A.H., Verma S., Iwamatsu A., Mitchison T.J.
    J. Cell Biol. 138:375-384(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE ARP2/2 COMPLEX, SUBCELLULAR LOCATION.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skin.
  5. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-9.
    Tissue: Platelet.
  6. "Functional prediction of the coding sequences of 121 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhou G., Ouyang S., Luo L., Bi J., Liu M., He F.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 25-290.
    Tissue: Fetal liver.
  7. Lubec G., Afjehi-Sadat L.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 191-203, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  8. "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity."
    Gournier H., Goley E.D., Niederstrasser H., Trinh T., Welch M.D.
    Mol. Cell 8:1041-1052(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACTIN-BINDING, RECONSTITUTION OF THE ARP2/3 COMPLEX.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-275 AND LYS-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiARPC2_HUMAN
AccessioniPrimary (citable) accession number: O15144
Secondary accession number(s): Q92801, Q9P1D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 1, 1998
Last modified: May 11, 2016
This is version 145 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.