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O15145

- ARPC3_HUMAN

UniProt

O15145 - ARPC3_HUMAN

Protein

Actin-related protein 2/3 complex subunit 3

Gene

ARPC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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. cellular component movement Source: ProtInc
    3. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    4. innate immune response Source: Reactome

    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

    GO - Cellular componenti

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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ARPC3 family.Curated

    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 122 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