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P61160

- ARP2_HUMAN

UniProt

P61160 - ARP2_HUMAN

Protein

Actin-related protein 2

Gene

ACTR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (10 May 2004)
      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.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi160 – 1623ATPBy similarity
    Nucleotide bindingi214 – 2185ATPBy similarity
    Nucleotide bindingi305 – 3106ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW

    GO - Biological processi

    1. actin cytoskeleton organization Source: Ensembl
    2. asymmetric cell division Source: Ensembl
    3. cellular component movement Source: UniProtKB
    4. cytoplasmic transport Source: Ensembl
    5. establishment or maintenance of cell polarity Source: Ensembl
    6. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    7. innate immune response Source: Reactome
    8. meiotic cytokinesis Source: Ensembl
    9. spindle localization Source: Ensembl

    Keywords - Ligandi

    Actin-binding, ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinkiP61160.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin-related protein 2
    Alternative name(s):
    Actin-like protein 2
    Gene namesi
    Name:ACTR2
    Synonyms:ARP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:169. ACTR2.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cell projection 1 Publication

    GO - Cellular componenti

    1. actin cap Source: Ensembl
    2. actin cytoskeleton Source: UniProtKB
    3. Arp2/3 protein complex Source: UniProtKB
    4. cell projection Source: UniProtKB-SubCell
    5. cytosol Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24488.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 394394Actin-related protein 2PRO_0000089067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei299 – 2991N6-acetyllysine1 Publication
    Modified residuei322 – 3221N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP61160.
    PaxDbiP61160.
    PRIDEiP61160.

    2D gel databases

    SWISS-2DPAGEP61160.

    PTM databases

    PhosphoSiteiP61160.

    Expressioni

    Gene expression databases

    ArrayExpressiP61160.
    BgeeiP61160.
    CleanExiHS_ACTR2.
    GenevestigatoriP61160.

    Organism-specific databases

    HPAiCAB005083.
    HPA015050.

    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

    BioGridi115404. 66 interactions.
    DIPiDIP-33165N.
    IntActiP61160. 8 interactions.
    MINTiMINT-5000145.
    STRINGi9606.ENSP00000367220.

    Structurei

    3D structure databases

    ProteinModelPortaliP61160.
    SMRiP61160. Positions 4-388.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family. ARP2 subfamily.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    HOGENOMiHOG000233340.
    HOVERGENiHBG003771.
    KOiK17260.
    OMAiDYTFNEK.
    OrthoDBiEOG78D7K6.
    PhylomeDBiP61160.
    TreeFamiTF300467.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    PRINTSiPR00190. ACTIN.
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]
    PROSITEiPS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P61160-1) [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

    MDSQGRKVVV CDNGTGFVKC GYAGSNFPEH IFPALVGRPI IRSTTKVGNI    50
    EIKDLMVGDE ASELRSMLEV NYPMENGIVR NWDDMKHLWD YTFGPEKLNI 100
    DTRNCKILLT EPPMNPTKNR EKIVEVMFET YQFSGVYVAI QAVLTLYAQG 150
    LLTGVVVDSG DGVTHICPVY EGFSLPHLTR RLDIAGRDIT RYLIKLLLLR 200
    GYAFNHSADF ETVRMIKEKL CYVGYNIEQE QKLALETTVL VESYTLPDGR 250
    IIKVGGERFE APEALFQPHL INVEGVGVAE LLFNTIQAAD IDTRSEFYKH 300
    IVLSGGSTMY PGLPSRLERE LKQLYLERVL KGDVEKLSKF KIRIEDPPRR 350
    KHMVFLGGAV LADIMKDKDN FWMTRQEYQE KGVRVLEKLG VTVR 394
    Length:394
    Mass (Da):44,761
    Last modified:May 10, 2004 - v1
    Checksum:i1BFA6B442ED1A797
    GO
    Isoform 2 (identifier: P61160-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         53-53: K → KNNKKM

    Note: No experimental confirmation available.

    Show »
    Length:399
    Mass (Da):45,377
    Checksum:iCF06512483DAD60A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti67 – 671M → T in AAH14546. (PubMed:15489334)Curated
    Sequence conflicti172 – 1721G → S in AAH14546. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei53 – 531K → KNNKKM in isoform 2. 1 PublicationVSP_046178

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006082 mRNA. Translation: AAB64187.1.
    AK315205 mRNA. Translation: BAG37642.1.
    BX649080 mRNA. No translation available.
    AC007318 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99908.1.
    CH471053 Genomic DNA. Translation: EAW99910.1.
    CH471053 Genomic DNA. Translation: EAW99912.1.
    CH471053 Genomic DNA. Translation: EAW99913.1.
    BC014546 mRNA. Translation: AAH14546.1.
    CCDSiCCDS1881.1. [P61160-1]
    CCDS46307.1. [P61160-2]
    RefSeqiNP_001005386.1. NM_001005386.2. [P61160-2]
    NP_005713.1. NM_005722.3. [P61160-1]
    UniGeneiHs.643727.
    Hs.744913.

    Genome annotation databases

    EnsembliENST00000260641; ENSP00000260641; ENSG00000138071. [P61160-1]
    ENST00000377982; ENSP00000367220; ENSG00000138071. [P61160-2]
    GeneIDi10097.
    KEGGihsa:10097.
    UCSCiuc002sdq.3. human. [P61160-1]

    Polymorphism databases

    DMDMi47117648.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006082 mRNA. Translation: AAB64187.1 .
    AK315205 mRNA. Translation: BAG37642.1 .
    BX649080 mRNA. No translation available.
    AC007318 Genomic DNA. No translation available.
    CH471053 Genomic DNA. Translation: EAW99908.1 .
    CH471053 Genomic DNA. Translation: EAW99910.1 .
    CH471053 Genomic DNA. Translation: EAW99912.1 .
    CH471053 Genomic DNA. Translation: EAW99913.1 .
    BC014546 mRNA. Translation: AAH14546.1 .
    CCDSi CCDS1881.1. [P61160-1 ]
    CCDS46307.1. [P61160-2 ]
    RefSeqi NP_001005386.1. NM_001005386.2. [P61160-2 ]
    NP_005713.1. NM_005722.3. [P61160-1 ]
    UniGenei Hs.643727.
    Hs.744913.

    3D structure databases

    ProteinModelPortali P61160.
    SMRi P61160. Positions 4-388.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115404. 66 interactions.
    DIPi DIP-33165N.
    IntActi P61160. 8 interactions.
    MINTi MINT-5000145.
    STRINGi 9606.ENSP00000367220.

    Chemistry

    ChEMBLi CHEMBL6090.

    PTM databases

    PhosphoSitei P61160.

    Polymorphism databases

    DMDMi 47117648.

    2D gel databases

    SWISS-2DPAGE P61160.

    Proteomic databases

    MaxQBi P61160.
    PaxDbi P61160.
    PRIDEi P61160.

    Protocols and materials databases

    DNASUi 10097.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260641 ; ENSP00000260641 ; ENSG00000138071 . [P61160-1 ]
    ENST00000377982 ; ENSP00000367220 ; ENSG00000138071 . [P61160-2 ]
    GeneIDi 10097.
    KEGGi hsa:10097.
    UCSCi uc002sdq.3. human. [P61160-1 ]

    Organism-specific databases

    CTDi 10097.
    GeneCardsi GC02P065454.
    HGNCi HGNC:169. ACTR2.
    HPAi CAB005083.
    HPA015050.
    MIMi 604221. gene.
    neXtProti NX_P61160.
    PharmGKBi PA24488.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5277.
    HOGENOMi HOG000233340.
    HOVERGENi HBG003771.
    KOi K17260.
    OMAi DYTFNEK.
    OrthoDBi EOG78D7K6.
    PhylomeDBi P61160.
    TreeFami TF300467.

    Enzyme and pathway databases

    Reactomei REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    SignaLinki P61160.

    Miscellaneous databases

    ChiTaRSi ACTR2. human.
    GeneWikii ACTR2.
    GenomeRNAii 10097.
    NextBioi 38189.
    PROi P61160.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P61160.
    Bgeei P61160.
    CleanExi HS_ACTR2.
    Genevestigatori P61160.

    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 ]
    PRINTSi PR00190. ACTIN.
    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] (ISOFORM 1).
    2. "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] (ISOFORM 1).
      Tissue: Tongue.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Liver.
    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] (ISOFORM 1).
      Tissue: Skeletal muscle.
    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: PARTIAL PROTEIN SEQUENCE, FUNCTION OF THE ARP2/3 COMPLEX, IDENTIFICATION IN THE ARP2/3 COMPLEX, SUBCELLULAR LOCATION.
    8. "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.
    9. "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-299 AND LYS-322, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiARP2_HUMAN
    AccessioniPrimary (citable) accession number: P61160
    Secondary accession number(s): B2RCP5
    , D6W5F4, E9PF41, O15142, Q96C82
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 1 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