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O15145

- ARPC3_HUMAN

UniProt

O15145 - ARPC3_HUMAN

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Protein
Actin-related protein 2/3 complex subunit 3
Gene
ARPC3, ARC21
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. protein binding Source: UniProtKB
  2. structural constituent of cytoskeleton Source: ProtInc

GO - Biological processi

  1. Arp2/3 complex-mediated actin nucleation Source: InterPro
  2. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  3. cellular component movement Source: ProtInc
  4. innate immune response Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.

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: Chromosome 12

Organism-specific databases

HGNCiHGNC:706. ARPC3.

Subcellular locationi

Cytoplasmcytoskeleton. Cell projection 2 Publications

GO - Cellular componenti

  1. Arp2/3 protein complex Source: ProtInc
  2. actin cytoskeleton Source: ProtInc
  3. cytosol Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. lamellipodium Source: Ensembl
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 3
PRO_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

ArrayExpressiO15145.
BgeeiO15145.
GenevestigatoriO15145.

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

Protein-protein interaction databases

BioGridi115401. 30 interactions.
DIPiDIP-33187N.
IntActiO15145. 16 interactions.
MINTiMINT-156243.
STRINGi9606.ENSP00000228825.

Structurei

3D structure databases

ProteinModelPortaliO15145.
SMRiO15145. Positions 2-175.

Family & Domainsi

Sequence similaritiesi

Belongs to the ARPC3 family.

Phylogenomic databases

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

Family and domain databases

Gene3Di1.10.1760.10. 1 hit.
InterProiIPR007204. ARP2/3_p21-Arc.
[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

MPAYHSSLMD PDTKLIGNMA LLPIRSQFKG PAPRETKDTD IVDEAIYYFK    50
ANVFFKNYEI KNEADRTLIY ITLYISECLK KLQKCNSKSQ GEKEMYTLGI 100
TNFPIPGEPG FPLNAIYAKP ANKQEDEVMR AYLQQLRQET GLRLCEKVFD 150
PQNDKPSKWW TCFVKRQFMN KSLSGPGQ 178
Length:178
Mass (Da):20,547
Last modified:January 23, 2007 - v3
Checksum:i7149F598B48F0EAC
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti134 – 1341Q → P in AAB61466. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS9146.1.
RefSeqi NP_001265485.1. NM_001278556.1.
NP_001274151.1. NM_001287222.1.
UniGenei Hs.524741.

3D structure databases

ProteinModelPortali O15145.
SMRi O15145. Positions 2-175.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115401. 30 interactions.
DIPi DIP-33187N.
IntActi O15145. 16 interactions.
MINTi MINT-156243.
STRINGi 9606.ENSP00000228825.

PTM databases

PhosphoSitei O15145.

2D gel databases

OGPi O15145.

Proteomic databases

MaxQBi O15145.
PaxDbi O15145.
PRIDEi O15145.

Protocols and materials databases

DNASUi 10094.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000228825 ; ENSP00000228825 ; ENSG00000111229 .
GeneIDi 10094.
KEGGi hsa:10094.
UCSCi uc001tqq.3. human.

Organism-specific databases

CTDi 10094.
GeneCardsi GC12M110872.
HGNCi HGNC:706. ARPC3.
HPAi HPA006550.
MIMi 604225. gene.
neXtProti NX_O15145.
PharmGKBi PA25000.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG324671.
HOGENOMi HOG000161465.
HOVERGENi HBG050581.
KOi K05756.
OMAi TGKPSKW.
OrthoDBi EOG7BS4BV.
PhylomeDBi O15145.
TreeFami TF314598.

Enzyme and pathway databases

Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.

Miscellaneous databases

ChiTaRSi ARPC3. human.
GeneWikii ARPC3.
GenomeRNAii 10094.
NextBioi 38177.
PROi O15145.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15145.
Bgeei O15145.
Genevestigatori O15145.

Family and domain databases

Gene3Di 1.10.1760.10. 1 hit.
InterProi IPR007204. ARP2/3_p21-Arc.
[Graphical view ]
PANTHERi PTHR12391. PTHR12391. 1 hit.
Pfami PF04062. P21-Arc. 1 hit.
[Graphical view ]
PIRSFi PIRSF016315. ARP2/3_P21-Arc. 1 hit.
SUPFAMi SSF69060. SSF69060. 1 hit.
ProtoNeti Search...

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].

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: September 3, 2014
This is version 121 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

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