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P60711

- ACTB_RAT

UniProt

P60711 - ACTB_RAT

Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 107 (01 Oct 2014)
      Sequence version 1 (01 Apr 1988)
      Previous versions | rss
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    Functioni

    Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase binding Source: RGD

    GO - Biological processi

    1. axonogenesis Source: RGD

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_196232. Factors involved in megakaryocyte development and platelet production.
    REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198384. HATs acetylate histones.
    REACT_199176. Translocation of GLUT4 to the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, cytoplasmic 1
    Alternative name(s):
    Beta-actin
    Cleaved into the following chain:
    Gene namesi
    Name:Actb
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 12

    Organism-specific databases

    RGDi628837. Actb.

    Subcellular locationi

    Cytoplasmcytoskeleton
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

    GO - Cellular componenti

    1. axon Source: RGD
    2. cytosol Source: Reactome
    3. extracellular vesicular exosome Source: Ensembl
    4. MLL5-L complex Source: Ensembl
    5. NuA4 histone acetyltransferase complex Source: Ensembl
    6. postsynaptic density Source: RGD
    7. protein complex Source: RGD
    8. ribonucleoprotein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367081Add
    BLAST
    Initiator methioninei1 – 11Removed; alternateBy similarity
    Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000781Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity
    Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
    Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
    Modified residuei73 – 731Tele-methylhistidineBy similarity
    Modified residuei84 – 841N6-methyllysineBy similarity

    Post-translational modificationi

    ISGylated.By similarity
    Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization By similarity.By similarity
    Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration By similarity.By similarity

    Keywords - PTMi

    Acetylation, Methylation, Oxidation, Ubl conjugation

    Proteomic databases

    PaxDbiP60711.
    PRIDEiP60711.

    2D gel databases

    World-2DPAGE0004:P60711.

    PTM databases

    PhosphoSiteiP60711.

    Expressioni

    Gene expression databases

    ArrayExpressiP60711.
    GenevestigatoriP60711.

    Interactioni

    Subunit structurei

    Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Wasf1Q5BJU72EBI-349272,EBI-7269229

    Protein-protein interaction databases

    BioGridi249680. 12 interactions.
    IntActiP60711. 18 interactions.
    MINTiMINT-132123.

    Structurei

    3D structure databases

    ProteinModelPortaliP60711.
    SMRiP60711. Positions 6-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    GeneTreeiENSGT00710000106384.
    HOGENOMiHOG000233340.
    HOVERGENiHBG003771.
    InParanoidiP60711.
    KOiK05692.
    OMAiDARAPIM.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP60711.
    TreeFamiTF354237.

    Family and domain databases

    InterProiIPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_CS.
    [Graphical view]
    PANTHERiPTHR11937. PTHR11937. 1 hit.
    PfamiPF00022. Actin. 1 hit.
    [Graphical view]
    PRINTSiPR00190. ACTIN.
    SMARTiSM00268. ACTIN. 1 hit.
    [Graphical view]
    PROSITEiPS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P60711-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK    50
    DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE 100
    HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG 150
    IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF 200
    TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI 250
    GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 300
    GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS 350
    TFQQMWISKQ EYDESGPSIV HRKCF 375
    Length:375
    Mass (Da):41,737
    Last modified:April 1, 1988 - v1
    Checksum:i6AFD05CA94E360E2
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01217 Genomic DNA. Translation: CAA24528.1.
    BC063166 mRNA. Translation: AAH63166.1.
    RefSeqiNP_112406.1. NM_031144.3.
    UniGeneiRn.94978.

    Genome annotation databases

    EnsembliENSRNOT00000042459; ENSRNOP00000044296; ENSRNOG00000034254.
    GeneIDi81822.
    KEGGirno:81822.
    UCSCiRGD:628837. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    V01217 Genomic DNA. Translation: CAA24528.1 .
    BC063166 mRNA. Translation: AAH63166.1 .
    RefSeqi NP_112406.1. NM_031144.3.
    UniGenei Rn.94978.

    3D structure databases

    ProteinModelPortali P60711.
    SMRi P60711. Positions 6-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 249680. 12 interactions.
    IntActi P60711. 18 interactions.
    MINTi MINT-132123.

    PTM databases

    PhosphoSitei P60711.

    2D gel databases

    World-2DPAGE 0004:P60711.

    Proteomic databases

    PaxDbi P60711.
    PRIDEi P60711.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000042459 ; ENSRNOP00000044296 ; ENSRNOG00000034254 .
    GeneIDi 81822.
    KEGGi rno:81822.
    UCSCi RGD:628837. rat.

    Organism-specific databases

    CTDi 60.
    RGDi 628837. Actb.

    Phylogenomic databases

    eggNOGi COG5277.
    GeneTreei ENSGT00710000106384.
    HOGENOMi HOG000233340.
    HOVERGENi HBG003771.
    InParanoidi P60711.
    KOi K05692.
    OMAi DARAPIM.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P60711.
    TreeFami TF354237.

    Enzyme and pathway databases

    Reactomei REACT_196232. Factors involved in megakaryocyte development and platelet production.
    REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198384. HATs acetylate histones.
    REACT_199176. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    NextBioi 615747.

    Gene expression databases

    ArrayExpressi P60711.
    Genevestigatori P60711.

    Family and domain databases

    InterProi IPR004000. Actin-related.
    IPR020902. Actin/actin-like_CS.
    IPR004001. Actin_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 PS00406. ACTINS_1. 1 hit.
    PS00432. ACTINS_2. 1 hit.
    PS01132. ACTINS_ACT_LIKE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The nucleotide sequence of the rat cytoplasmic beta-actin gene."
      Nudel U., Zakut R., Shani M., Neuman S., Levy Z., Yaffe D.
      Nucleic Acids Res. 11:1759-1771(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE.
    2. "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: Pituitary.
    3. Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-39; 51-62; 85-113; 184-191; 197-206; 239-254; 292-312; 316-326; 329-335 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain, Hippocampus and Spinal cord.

    Entry informationi

    Entry nameiACTB_RAT
    AccessioniPrimary (citable) accession number: P60711
    Secondary accession number(s): P02570
    , P70514, P99021, Q11211, Q64316
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 107 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3