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P61158

- ARP3_HUMAN

UniProt

P61158 - ARP3_HUMAN

Protein

Actin-related protein 3

Gene

ACTR3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Functions as ATP-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 pointed end of the daughter actin filament. Plays a role in ciliogenesis.2 Publications

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: IntAct

    GO - Biological processi

    1. asymmetric cell division Source: Ensembl
    2. cellular component movement Source: UniProtKB
    3. cilium morphogenesis Source: UniProtKB
    4. establishment or maintenance of cell polarity Source: Ensembl
    5. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    6. innate immune response Source: Reactome
    7. meiotic cytokinesis Source: Ensembl
    8. positive regulation of actin filament polymerization Source: Ensembl
    9. positive regulation of dendrite morphogenesis Source: Ensembl
    10. positive regulation of filopodium assembly Source: Ensembl
    11. positive regulation of lamellipodium assembly Source: Ensembl
    12. positive regulation of neuron differentiation Source: Ensembl
    13. regulation of myosin II filament organization Source: Ensembl
    14. response to antibiotic Source: Ensembl
    15. response to carbohydrate Source: Ensembl
    16. spindle localization Source: Ensembl

    Keywords - Biological processi

    Cilium biogenesis/degradation

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinkiP61158.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-related protein 3
    Alternative name(s):
    Actin-like protein 3
    Gene namesi
    Name:ACTR3
    Synonyms:ARP3
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:170. ACTR3.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cell projection
    Note: In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).

    GO - Cellular componenti

    1. actin cytoskeleton Source: UniProtKB
    2. Arp2/3 protein complex Source: UniProtKB
    3. cytosol Source: Reactome
    4. excitatory synapse Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi membrane Source: Ensembl
    7. hemidesmosome Source: Ensembl
    8. lamellipodium Source: Ensembl
    9. membrane Source: UniProtKB
    10. podosome Source: Ensembl

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24489.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 418417Actin-related protein 3PRO_0000089079Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine2 Publications
    Modified residuei240 – 2401N6-acetyllysine1 Publication
    Modified residuei244 – 2441N6-acetyllysine1 Publication
    Modified residuei251 – 2511N6-acetyllysine1 Publication
    Modified residuei254 – 2541N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP61158.
    PeptideAtlasiP61158.
    PRIDEiP61158.

    2D gel databases

    OGPiP32391.

    PTM databases

    PhosphoSiteiP61158.

    Miscellaneous databases

    PMAP-CutDBP61158.

    Expressioni

    Gene expression databases

    ArrayExpressiP61158.
    BgeeiP61158.
    CleanExiHS_ACTR3.
    GenevestigatoriP61158.

    Organism-specific databases

    HPAiCAB005085.
    HPA047016.
    HPA051683.

    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. Interacts with WHDC1. Interacts weakly with MEFV.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    JUNDP175352EBI-351428,EBI-2682803

    Protein-protein interaction databases

    BioGridi115403. 51 interactions.
    DIPiDIP-33140N.
    IntActiP61158. 14 interactions.
    MINTiMINT-3022340.
    STRINGi9606.ENSP00000263238.

    Structurei

    3D structure databases

    ProteinModelPortaliP61158.
    SMRiP61158. Positions 3-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family. ARP3 subfamily.Curated

    Phylogenomic databases

    HOGENOMiHOG000233339.
    HOVERGENiHBG003771.
    InParanoidiP61158.
    OMAiASWSSNR.
    OrthoDBiEOG7TMZRM.
    PhylomeDBiP61158.
    TreeFamiTF300644.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]
    PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P61158-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGRLPACVV DCGTGYTKLG YAGNTEPQFI IPSCIAIKES AKVGDQAQRR    50
    VMKGVDDLDF FIGDEAIEKP TYATKWPIRH GIVEDWDLME RFMEQVIFKY 100
    LRAEPEDHYF LLTEPPLNTP ENREYTAEIM FESFNVPGLY IAVQAVLALA 150
    ASWTSRQVGE RTLTGTVIDS GDGVTHVIPV AEGYVIGSCI KHIPIAGRDI 200
    TYFIQQLLRD REVGIPPEQS LETAKAVKER YSYVCPDLVK EFNKYDTDGS 250
    KWIKQYTGIN AISKKEFSID VGYERFLGPE IFFHPEFANP DFTQPISEVV 300
    DEVIQNCPID VRRPLYKNIV LSGGSTMFRD FGRRLQRDLK RTVDARLKLS 350
    EELSGGRLKP KPIDVQVITH HMQRYAVWFG GSMLASTPEF YQVCHTKKDY 400
    EEIGPSICRH NPVFGVMS 418
    Length:418
    Mass (Da):47,371
    Last modified:January 23, 2007 - v3
    Checksum:i23E5564198B81C63
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006083 mRNA. Translation: AAB64188.1.
    AF127773 mRNA. Translation: AAD51904.1.
    AK312659 mRNA. Translation: BAG35542.1.
    AC110769 Genomic DNA. Translation: AAX93226.1.
    CH471103 Genomic DNA. Translation: EAW95179.1.
    BC044590 mRNA. Translation: AAH44590.1.
    CCDSiCCDS33277.1.
    RefSeqiNP_005712.1. NM_005721.4.
    UniGeneiHs.433512.
    Hs.595349.

    Genome annotation databases

    EnsembliENST00000263238; ENSP00000263238; ENSG00000115091.
    GeneIDi10096.
    KEGGihsa:10096.
    UCSCiuc002tkx.2. human.

    Polymorphism databases

    DMDMi47117647.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006083 mRNA. Translation: AAB64188.1 .
    AF127773 mRNA. Translation: AAD51904.1 .
    AK312659 mRNA. Translation: BAG35542.1 .
    AC110769 Genomic DNA. Translation: AAX93226.1 .
    CH471103 Genomic DNA. Translation: EAW95179.1 .
    BC044590 mRNA. Translation: AAH44590.1 .
    CCDSi CCDS33277.1.
    RefSeqi NP_005712.1. NM_005721.4.
    UniGenei Hs.433512.
    Hs.595349.

    3D structure databases

    ProteinModelPortali P61158.
    SMRi P61158. Positions 3-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115403. 51 interactions.
    DIPi DIP-33140N.
    IntActi P61158. 14 interactions.
    MINTi MINT-3022340.
    STRINGi 9606.ENSP00000263238.

    PTM databases

    PhosphoSitei P61158.

    Polymorphism databases

    DMDMi 47117647.

    2D gel databases

    OGPi P32391.

    Proteomic databases

    MaxQBi P61158.
    PeptideAtlasi P61158.
    PRIDEi P61158.

    Protocols and materials databases

    DNASUi 10096.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263238 ; ENSP00000263238 ; ENSG00000115091 .
    GeneIDi 10096.
    KEGGi hsa:10096.
    UCSCi uc002tkx.2. human.

    Organism-specific databases

    CTDi 10096.
    GeneCardsi GC02P114647.
    HGNCi HGNC:170. ACTR3.
    HPAi CAB005085.
    HPA047016.
    HPA051683.
    MIMi 604222. gene.
    neXtProti NX_P61158.
    PharmGKBi PA24489.
    GenAtlasi Search...

    Phylogenomic databases

    HOGENOMi HOG000233339.
    HOVERGENi HBG003771.
    InParanoidi P61158.
    OMAi ASWSSNR.
    OrthoDBi EOG7TMZRM.
    PhylomeDBi P61158.
    TreeFami TF300644.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinki P61158.

    Miscellaneous databases

    ChiTaRSi ACTR3. human.
    GeneWikii ACTR3.
    GenomeRNAii 10096.
    NextBioi 38185.
    PMAP-CutDB P61158.
    PROi P61158.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61158.
    Bgeei P61158.
    CleanExi HS_ACTR3.
    Genevestigatori P61158.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    [Graphical view ]
    PANTHERi PTHR11937. PTHR11937. 1 hit.
    Pfami PF00022. Actin. 1 hit.
    [Graphical view ]
    SMARTi SM00268. ACTIN. 1 hit.
    [Graphical view ]
    PROSITEi PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
    2. "Identification of human estrogen-inducible transcripts from a serum resistant variant of breast cancer MCF7 cells."
      Szelei J., Soto A.M., Geck P., Desronvil M., Prechtl N., Weill B., Sonnenschein C.
      Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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.
    7. "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes."
      Welch M.D., Iwamatsu A., Mitchison T.J.
      Nature 385:265-269(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
    8. Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.
      Submitted (MAY-2006) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-17, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: T-cell.
    9. Lubec G., Afjehi-Sadat L.
      Submitted (MAR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 103-123 AND 199-209, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain and Cajal-Retzius cell.
    10. "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.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport."
      Campellone K.G., Webb N.J., Znameroski E.A., Welch M.D.
      Cell 134:148-161(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WHDC1.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Pyrin and ASC co-localize to cellular sites that are rich in polymerizing actin."
      Waite A.L., Schaner P., Hu C., Richards N., Balci-Peynircioglu B., Hong A., Fox M., Gumucio D.L.
      Exp. Biol. Med. (Maywood) 234:40-52(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH MEFV.
    15. "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-240; LYS-244; LYS-251 AND LYS-254, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Functional genomic screen for modulators of ciliogenesis and cilium length."
      Kim J., Lee J.E., Heynen-Genel S., Suyama E., Ono K., Lee K., Ideker T., Aza-Blanc P., Gleeson J.G.
      Nature 464:1048-1051(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiARP3_HUMAN
    AccessioniPrimary (citable) accession number: P61158
    Secondary accession number(s): P32391, Q53QM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 114 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 2
      Human chromosome 2: 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