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P59998

- ARPC4_HUMAN

UniProt

P59998 - ARPC4_HUMAN

Protein

Actin-related protein 2/3 complex subunit 4

Gene

ARPC4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    1. enzyme binding Source: BHF-UCL
    2. protein binding Source: UniProtKB

    GO - Biological processi

    1. actin filament polymerization Source: InterPro
    2. actin nucleation Source: UniProtKB
    3. Arp2/3 complex-mediated actin nucleation Source: InterPro
    4. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    5. 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 4
    Alternative name(s):
    Arp2/3 complex 20 kDa subunit
    Short name:
    p20-ARC
    Gene namesi
    Name:ARPC4
    Synonyms:ARC20
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:707. ARPC4.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell projection 1 Publication

    GO - Cellular componenti

    1. Arp2/3 protein complex Source: UniProtKB
    2. cell projection Source: UniProtKB-SubCell
    3. cytosol Source: Reactome
    4. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA25002.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 168167Actin-related protein 2/3 complex subunit 4PRO_0000124049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP59998.
    PaxDbiP59998.
    PRIDEiP59998.

    PTM databases

    PhosphoSiteiP59998.

    Expressioni

    Gene expression databases

    ArrayExpressiP59998.
    BgeeiP59998.
    CleanExiHS_ARPC4.
    GenevestigatoriP59998.

    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.

    Protein-protein interaction databases

    BioGridi115400. 41 interactions.
    DIPiDIP-33188N.
    IntActiP59998. 9 interactions.
    MINTiMINT-5000208.
    STRINGi9606.ENSP00000380431.

    Structurei

    3D structure databases

    ProteinModelPortaliP59998.
    SMRiP59998. Positions 2-168.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the ARPC4 family.Curated

    Phylogenomic databases

    eggNOGiNOG261545.
    HOGENOMiHOG000202303.
    HOVERGENiHBG050582.
    KOiK05755.
    OMAiMLKHKIV.
    OrthoDBiEOG7VTDPM.
    PhylomeDBiP59998.
    TreeFamiTF105621.
    TF313087.

    Family and domain databases

    InterProiIPR008384. ARPC4.
    [Graphical view]
    PANTHERiPTHR22629. PTHR22629. 1 hit.
    PfamiPF05856. ARPC4. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

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

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P59998-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTATLRPYLS AVRATLQAAL CLENFSSQVV ERHNKPEVEV RSSKELLLQP    50
    VTISRNEKEK VLIEGSINSV RVSIAVKQAD EIEKILCHKF MRFMMMRAEN 100
    FFILRRKPVE GYDISFLITN FHTEQMYKHK LVDFVIHFME EIDKEISEMK 150
    LSVNARARIV AEEFLKNF 168
    Length:168
    Mass (Da):19,667
    Last modified:January 23, 2007 - v3
    Checksum:i273CCB230AC703DF
    GO
    Isoform 2 (identifier: P59998-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         110-168: EGYDISFLIT...IVAEEFLKNF → EQKKIFTIQG...LRPCRPQARP

    Note: No experimental confirmation available.

    Show »
    Length:625
    Mass (Da):71,719
    Checksum:iE05F7DC236DF9674
    GO
    Isoform 3 (identifier: P59998-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MVREPGPRPGTPGCSASGQW

    Note: No experimental confirmation available.

    Show »
    Length:187
    Mass (Da):21,588
    Checksum:iF61DD748D01B8880
    GO
    Isoform 4 (identifier: P59998-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-90: Missing.

    Note: No experimental confirmation available. Gene prediction based on EST data.

    Show »
    Length:78
    Mass (Da):9,552
    Checksum:i32DD605A770B6706
    GO

    Sequence cautioni

    The sequence AAH12596.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti94 – 941M → T in AAH12596. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 9090Missing in isoform 4. CuratedVSP_046753Add
    BLAST
    Alternative sequencei1 – 11M → MVREPGPRPGTPGCSASGQW in isoform 3. 1 PublicationVSP_046150
    Alternative sequencei110 – 16859EGYDI…FLKNF → EQKKIFTIQGCYPVIRCLLR RRGWVEKKMVHRSGPTLLPP QKDLDSSAMGDSDTTEDEDE DEDEEFQPSQLFDFDDLLKF DDLDGTHALMVGLCLNLRNL PWFDEVDANSFFPRCYCLGA EDDKKAFIGDKQPKKQEKNP VLVSPEFVDEALCACEEYLS NLAHMDIDKDLEAPLYLTPE GWSLFLQRYYQVVHEGAELR HLDTQVQRCEDILQQLQAVV PQIDMEGDRNIWIVKPGAKS RGRGIMCMDHLEEMLKLVNG NPVVMKDGKWVVQKYIERPL LIFGTKFDLRQWFLVTDWNP LTVWFYRDSYIRFSTQPFSL KNLDNSVHLCNNSIQKHLEN SCHRHPLLPPDNMWSSQRFQ AHLQEMGAPNAWSTIIVPGM KDAVIHALQTSQDTVQCRKA SFELYGADFVFGEDFQPWLI EINASPTMAPSTAVTARLCA GVQADTLRVVIDRMLDRNCD TGAFELIYKQPVTTSPASTP RPSCLLPMYSDTRARSSDDS TASWWALRPCRPQARP in isoform 2. 1 PublicationVSP_046151Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019888 mRNA. Translation: AAB71548.1.
    AF006087 mRNA. Translation: AAB64192.1.
    BX419672 mRNA. No translation available.
    AC022382 Genomic DNA. No translation available.
    BC012596 mRNA. Translation: AAH12596.3. Different initiation.
    BC025289 mRNA. No translation available.
    CCDSiCCDS43047.1. [P59998-1]
    CCDS46743.1. [P59998-4]
    CCDS56238.1. [P59998-3]
    RefSeqiNP_001020130.1. NM_001024959.2. [P59998-4]
    NP_001020131.1. NM_001024960.2. [P59998-4]
    NP_001185709.1. NM_001198780.1. [P59998-3]
    NP_001185722.1. NM_001198793.1. [P59998-2]
    NP_005709.1. NM_005718.4. [P59998-1]
    UniGeneiHs.323342.

    Genome annotation databases

    EnsembliENST00000397261; ENSP00000380431; ENSG00000241553. [P59998-1]
    ENST00000433034; ENSP00000388169; ENSG00000241553. [P59998-3]
    ENST00000498623; ENSP00000432235; ENSG00000241553. [P59998-4]
    GeneIDi100526693.
    10093.
    KEGGihsa:100526693.
    hsa:10093.
    UCSCiuc003bsz.2. human. [P59998-1]

    Polymorphism databases

    DMDMi38372625.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF019888 mRNA. Translation: AAB71548.1 .
    AF006087 mRNA. Translation: AAB64192.1 .
    BX419672 mRNA. No translation available.
    AC022382 Genomic DNA. No translation available.
    BC012596 mRNA. Translation: AAH12596.3 . Different initiation.
    BC025289 mRNA. No translation available.
    CCDSi CCDS43047.1. [P59998-1 ]
    CCDS46743.1. [P59998-4 ]
    CCDS56238.1. [P59998-3 ]
    RefSeqi NP_001020130.1. NM_001024959.2. [P59998-4 ]
    NP_001020131.1. NM_001024960.2. [P59998-4 ]
    NP_001185709.1. NM_001198780.1. [P59998-3 ]
    NP_001185722.1. NM_001198793.1. [P59998-2 ]
    NP_005709.1. NM_005718.4. [P59998-1 ]
    UniGenei Hs.323342.

    3D structure databases

    ProteinModelPortali P59998.
    SMRi P59998. Positions 2-168.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115400. 41 interactions.
    DIPi DIP-33188N.
    IntActi P59998. 9 interactions.
    MINTi MINT-5000208.
    STRINGi 9606.ENSP00000380431.

    PTM databases

    PhosphoSitei P59998.

    Polymorphism databases

    DMDMi 38372625.

    Proteomic databases

    MaxQBi P59998.
    PaxDbi P59998.
    PRIDEi P59998.

    Protocols and materials databases

    DNASUi 10093.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000397261 ; ENSP00000380431 ; ENSG00000241553 . [P59998-1 ]
    ENST00000433034 ; ENSP00000388169 ; ENSG00000241553 . [P59998-3 ]
    ENST00000498623 ; ENSP00000432235 ; ENSG00000241553 . [P59998-4 ]
    GeneIDi 100526693.
    10093.
    KEGGi hsa:100526693.
    hsa:10093.
    UCSCi uc003bsz.2. human. [P59998-1 ]

    Organism-specific databases

    CTDi 100526693.
    10093.
    GeneCardsi GC03P009834.
    HGNCi HGNC:707. ARPC4.
    MIMi 604226. gene.
    neXtProti NX_P59998.
    PharmGKBi PA25002.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG261545.
    HOGENOMi HOG000202303.
    HOVERGENi HBG050582.
    KOi K05755.
    OMAi MLKHKIV.
    OrthoDBi EOG7VTDPM.
    PhylomeDBi P59998.
    TreeFami TF105621.
    TF313087.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi ARPC4. human.
    GeneWikii ARPC4.
    NextBioi 34054911.
    PROi P59998.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P59998.
    Bgeei P59998.
    CleanExi HS_ARPC4.
    Genevestigatori P59998.

    Family and domain databases

    InterProi IPR008384. ARPC4.
    [Graphical view ]
    PANTHERi PTHR22629. PTHR22629. 1 hit.
    Pfami PF05856. ARPC4. 1 hit.
    [Graphical view ]
    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] (ISOFORM 1), 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] (ISOFORM 1).
    3. "Full-length cDNA libraries and normalization."
      Li W.B., Gruber C., Jessee J., Polayes D.
      Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Fetal brain.
    4. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-168 (ISOFORM 1).
      Tissue: Choriocarcinoma and Prostate.
    6. "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 2-13, ACETYLATION AT THR-2.
      Tissue: Platelet.
    7. "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.

    Entry informationi

    Entry nameiARPC4_HUMAN
    AccessioniPrimary (citable) accession number: P59998
    Secondary accession number(s): C9JWM7
    , E7ETI0, F6TTL5, O15509, Q6P0W5, Q96QJ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 109 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 3
      Human chromosome 3: 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