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Protein

Actin-related protein 2/3 complex subunit 3

Gene

ARPC3

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

Functioni

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.

GO - Molecular functioni

  • structural constituent of cytoskeleton Source: FlyBase

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-related protein 2/3 complex subunit 3
Alternative name(s):
Arp2/3 complex 21 kDa subunit
Short name:
p21-ARC
Gene namesi
Name:ARPC3
Synonyms:ARC21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:706. ARPC3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: ProtInc
  • Arp2/3 protein complex Source: FlyBase
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: Ensembl
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell projection, Cytoplasm, Cytoskeleton

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25000.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 178177Actin-related protein 2/3 complex subunit 3PRO_0000124042Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei47 – 471Phosphotyrosine1 Publication
Modified residuei56 – 561N6-acetyllysine1 Publication
Modified residuei61 – 611N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO15145.
PaxDbiO15145.
PRIDEiO15145.

2D gel databases

OGPiO15145.

PTM databases

PhosphoSiteiO15145.

Expressioni

Gene expression databases

BgeeiO15145.
ExpressionAtlasiO15145. baseline and differential.
GenevisibleiO15145. HS.

Organism-specific databases

HPAiHPA006550.

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GOLGA2Q083793EBI-351829,EBI-618309
HOXA3O433653EBI-351829,EBI-8643838
NRIP1P485523EBI-351829,EBI-746484
WASLO004013EBI-351829,EBI-957615

Protein-protein interaction databases

BioGridi115401. 40 interactions.
DIPiDIP-33187N.
IntActiO15145. 20 interactions.
MINTiMINT-156243.
STRINGi9606.ENSP00000228825.

Structurei

3D structure databases

ProteinModelPortaliO15145.
SMRiO15145. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC3 family.Curated

Phylogenomic databases

eggNOGiNOG324671.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiO15145.
KOiK05756.
OMAiTGKPSKW.
OrthoDBiEOG7BS4BV.
PhylomeDBiO15145.
TreeFamiTF314598.

Family and domain databases

Gene3Di1.10.1760.10. 1 hit.
InterProiIPR007204. ARPC3.
[Graphical view]
PANTHERiPTHR12391. PTHR12391. 1 hit.
PfamiPF04062. P21-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMiSSF69060. SSF69060. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O15145-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK
60 70 80 90 100
ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI
110 120 130 140 150
TNFPIPGEPG FPLNAIYAKP ANKQEDEVMR AYLQQLRQET GLRLCEKVFD
160 170
PQNDKPSKWW TCFVKRQFMN KSLSGPGQ
Length:178
Mass (Da):20,547
Last modified:January 23, 2007 - v3
Checksum:i7149F598B48F0EAC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341Q → P in AAB61466 (PubMed:9359840).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9146.1.
RefSeqiNP_001265485.1. NM_001278556.1.
NP_001274151.1. NM_001287222.1.
UniGeneiHs.524741.

Genome annotation databases

EnsembliENST00000228825; ENSP00000228825; ENSG00000111229.
GeneIDi10094.
KEGGihsa:10094.
UCSCiuc001tqq.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9146.1.
RefSeqiNP_001265485.1. NM_001278556.1.
NP_001274151.1. NM_001287222.1.
UniGeneiHs.524741.

3D structure databases

ProteinModelPortaliO15145.
SMRiO15145. Positions 2-175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115401. 40 interactions.
DIPiDIP-33187N.
IntActiO15145. 20 interactions.
MINTiMINT-156243.
STRINGi9606.ENSP00000228825.

PTM databases

PhosphoSiteiO15145.

2D gel databases

OGPiO15145.

Proteomic databases

MaxQBiO15145.
PaxDbiO15145.
PRIDEiO15145.

Protocols and materials databases

DNASUi10094.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000228825; ENSP00000228825; ENSG00000111229.
GeneIDi10094.
KEGGihsa:10094.
UCSCiuc001tqq.3. human.

Organism-specific databases

CTDi10094.
GeneCardsiGC12M110872.
HGNCiHGNC:706. ARPC3.
HPAiHPA006550.
MIMi604225. gene.
neXtProtiNX_O15145.
PharmGKBiPA25000.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG324671.
GeneTreeiENSGT00390000018018.
HOGENOMiHOG000161465.
HOVERGENiHBG050581.
InParanoidiO15145.
KOiK05756.
OMAiTGKPSKW.
OrthoDBiEOG7BS4BV.
PhylomeDBiO15145.
TreeFamiTF314598.

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_263952. EPHB-mediated forward signaling.
REACT_355372. RHO GTPases Activate WASPs and WAVEs.

Miscellaneous databases

ChiTaRSiARPC3. human.
GeneWikiiARPC3.
GenomeRNAii10094.
NextBioi38177.
PROiO15145.
SOURCEiSearch...

Gene expression databases

BgeeiO15145.
ExpressionAtlasiO15145. baseline and differential.
GenevisibleiO15145. HS.

Family and domain databases

Gene3Di1.10.1760.10. 1 hit.
InterProiIPR007204. ARPC3.
[Graphical view]
PANTHERiPTHR12391. PTHR12391. 1 hit.
PfamiPF04062. P21-Arc. 1 hit.
[Graphical view]
PIRSFiPIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMiSSF69060. SSF69060. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.

Entry informationi

Entry nameiARPC3_HUMAN
AccessioniPrimary (citable) accession number: O15145
Secondary accession number(s): O00554
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 132 of the entry and version 3 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 12
    Human chromosome 12: 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

External Data

Dasty 3

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 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.