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O15145 (ARPC3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin-related protein 2/3 complex subunit 3
Alternative name(s):
Arp2/3 complex 21 kDa subunit
Short name=p21-ARC
Gene names
Name:ARPC3
Synonyms:ARC21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length178 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions as 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.

Subunit structure

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. Ref.2

Subcellular location

Cytoplasmcytoskeleton. Cell projection Ref.1 Ref.2.

Sequence similarities

Belongs to the ARPC3 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 178177Actin-related protein 2/3 complex subunit 3
PRO_0000124042

Amino acid modifications

Modified residue471Phosphotyrosine Ref.7
Modified residue561N6-acetyllysine Ref.8
Modified residue611N6-acetyllysine Ref.8

Experimental info

Sequence conflict1341Q → P in AAB61466. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O15145 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7149F598B48F0EAC

FASTA17820,547
        10         20         30         40         50         60 
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK ANVFFKNYEI 

        70         80         90        100        110        120 
KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI TNFPIPGEPG FPLNAIYAKP 

       130        140        150        160        170 
ANKQEDEVMR AYLQQLRQET GLRLCEKVFD PQNDKPSKWW TCFVKRQFMN KSLSGPGQ 

« Hide

References

« Hide 'large scale' references
[1]"Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins."
Machesky L.M., Reeves E., Wientjes F., Mattheyse F.J., Grogan A., Totty N.F., Burlingame A.L., Hsuan J.J., Segal A.W.
Biochem. J. 328:105-112(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
[2]"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.
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (MAY-2004) 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: Brain and 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 2-25.
Tissue: Platelet.
[6]"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: RECONSTITUTION OF THE ARP2/3 COMPLEX.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-47, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"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-56 AND LYS-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF004561 mRNA. Translation: AAB61466.1.
AF006086 mRNA. Translation: AAB64191.1.
CR407667 mRNA. Translation: CAG28595.1.
BC067747 mRNA. Translation: AAH67747.1.
BC078162 mRNA. Translation: AAH78162.1.
CCDSCCDS9146.1.
RefSeqNP_001265485.1. NM_001278556.1.
NP_001274151.1. NM_001287222.1.
UniGeneHs.524741.

3D structure databases

ProteinModelPortalO15145.
SMRO15145. Positions 2-175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115401. 30 interactions.
DIPDIP-33187N.
IntActO15145. 16 interactions.
MINTMINT-156243.
STRING9606.ENSP00000228825.

PTM databases

PhosphoSiteO15145.

2D gel databases

OGPO15145.

Proteomic databases

MaxQBO15145.
PaxDbO15145.
PRIDEO15145.

Protocols and materials databases

DNASU10094.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228825; ENSP00000228825; ENSG00000111229.
GeneID10094.
KEGGhsa:10094.
UCSCuc001tqq.3. human.

Organism-specific databases

CTD10094.
GeneCardsGC12M110872.
HGNCHGNC:706. ARPC3.
HPAHPA006550.
MIM604225. gene.
neXtProtNX_O15145.
PharmGKBPA25000.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG324671.
HOGENOMHOG000161465.
HOVERGENHBG050581.
KOK05756.
OMATGKPSKW.
OrthoDBEOG7BS4BV.
PhylomeDBO15145.
TreeFamTF314598.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressO15145.
BgeeO15145.
GenevestigatorO15145.

Family and domain databases

Gene3D1.10.1760.10. 1 hit.
InterProIPR007204. ARP2/3_p21-Arc.
[Graphical view]
PANTHERPTHR12391. PTHR12391. 1 hit.
PfamPF04062. P21-Arc. 1 hit.
[Graphical view]
PIRSFPIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMSSF69060. SSF69060. 1 hit.
ProtoNetSearch...

Other

ChiTaRSARPC3. human.
GeneWikiARPC3.
GenomeRNAi10094.
NextBio38177.
PROO15145.
SOURCESearch...

Entry information

Entry nameARPC3_HUMAN
AccessionPrimary (citable) accession number: O15145
Secondary accession number(s): O00554
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 120 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM