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P60710

- ACTB_MOUSE

UniProt

P60710 - ACTB_MOUSE

Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Mus musculus (Mouse)
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 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: IntAct

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_209040. Gap junction degradation.
    REACT_220352. Formation of annular gap junctions.
    REACT_226917. HATs acetylate histones.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, cytoplasmic 1
    Alternative name(s):
    Beta-actin
    Cleaved into the following chain:
    Gene namesi
    Name:Actb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 5

    Organism-specific databases

    MGIiMGI:87904. Actb.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cortical cytoskeleton Source: MGI
    2. cytosol Source: MGI
    3. extracellular vesicular exosome Source: Ensembl
    4. MLL5-L complex Source: Ensembl
    5. NuA4 histone acetyltransferase complex Source: Ensembl
    6. ribonucleoprotein complex Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367076Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate1 Publication
    Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000775Add
    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 processed2 Publications
    Modified residuei44 – 441Methionine (R)-sulfoxide1 Publication
    Modified residuei47 – 471Methionine (R)-sulfoxide1 Publication
    Modified residuei73 – 731Tele-methylhistidine1 Publication
    Modified residuei84 – 841N6-methyllysineBy similarity

    Post-translational modificationi

    ISGylated.1 Publication
    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.1 Publication
    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

    MaxQBiP60710.
    PRIDEiP60710.

    2D gel databases

    COMPLUYEAST-2DPAGEP60710.
    REPRODUCTION-2DPAGEP60710.
    SWISS-2DPAGEP99041.
    UCD-2DPAGEP60710.

    PTM databases

    PhosphoSiteiP60710.

    Expressioni

    Gene expression databases

    ArrayExpressiP60710.
    BgeeiP60710.
    CleanExiMM_ACTB.
    GenevestigatoriP60710.

    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, MARCB1/BAF47, 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 a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. 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
    CxadrP977926EBI-353957,EBI-7429264

    Protein-protein interaction databases

    BioGridi197944. 26 interactions.
    DIPiDIP-31574N.
    IntActiP60710. 41 interactions.
    MINTiMINT-1202772.

    Structurei

    3D structure databases

    ProteinModelPortaliP60710.
    SMRiP60710. Positions 6-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    GeneTreeiENSGT00710000106384.
    HOVERGENiHBG003771.
    InParanoidiP60710.
    KOiK05692.
    OMAiSIVHLKC.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP60710.
    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.

    P60710-1 [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti38 – 381P → S in CAA27396. (PubMed:3084797)Curated
    Sequence conflicti38 – 381P → S in AAA37144. (PubMed:3084797)Curated
    Sequence conflicti52 – 521S → F in BAE39957. (PubMed:16141072)Curated
    Sequence conflicti80 – 801D → E in BAE35572. (PubMed:16141072)Curated
    Sequence conflicti109 – 1091P → T in BAE39957. (PubMed:16141072)Curated
    Sequence conflicti156 – 1561G → R in BAE39957. (PubMed:16141072)Curated
    Sequence conflicti178 – 1781L → V in BAE39957. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03672 mRNA. Translation: CAA27307.1.
    AK088691 mRNA. Translation: BAC40507.1.
    AK145191 mRNA. Translation: BAE26283.1.
    AK145196 mRNA. Translation: BAE26288.1.
    AK145308 mRNA. Translation: BAE26359.1.
    AK150711 mRNA. Translation: BAE29789.1.
    AK150879 mRNA. Translation: BAE29928.1.
    AK151010 mRNA. Translation: BAE30031.1.
    AK151136 mRNA. Translation: BAE30144.1.
    AK151145 mRNA. Translation: BAE30152.1.
    AK151159 mRNA. Translation: BAE30164.1.
    AK151166 mRNA. Translation: BAE30169.1.
    AK151190 mRNA. Translation: BAE30187.1.
    AK151202 mRNA. Translation: BAE30199.1.
    AK151226 mRNA. Translation: BAE30218.1.
    AK151277 mRNA. Translation: BAE30264.1.
    AK151350 mRNA. Translation: BAE30326.1.
    AK151398 mRNA. Translation: BAE30366.1.
    AK151995 mRNA. Translation: BAE30859.1.
    AK151999 mRNA. Translation: BAE30863.1.
    AK152615 mRNA. Translation: BAE31359.1.
    AK152651 mRNA. Translation: BAE31388.1.
    AK152844 mRNA. Translation: BAE31537.1.
    AK159759 mRNA. Translation: BAE35350.1.
    AK159834 mRNA. Translation: BAE35412.1.
    AK160029 mRNA. Translation: BAE35572.1.
    AK166349 mRNA. Translation: BAE38723.1.
    AK166498 mRNA. Translation: BAE38810.1.
    AK167117 mRNA. Translation: BAE39265.1.
    AK167960 mRNA. Translation: BAE39957.1.
    X03765 mRNA. Translation: CAA27396.1.
    M12481 mRNA. Translation: AAA37144.1.
    CCDSiCCDS19833.1.
    PIRiA39104. ATMSB.
    RefSeqiNP_031419.1. NM_007393.3.
    UniGeneiMm.328431.
    Mm.391967.
    Mm.469717.

    Genome annotation databases

    EnsembliENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580.
    GeneIDi11461.
    KEGGimmu:11461.
    UCSCiuc009ajk.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03672 mRNA. Translation: CAA27307.1 .
    AK088691 mRNA. Translation: BAC40507.1 .
    AK145191 mRNA. Translation: BAE26283.1 .
    AK145196 mRNA. Translation: BAE26288.1 .
    AK145308 mRNA. Translation: BAE26359.1 .
    AK150711 mRNA. Translation: BAE29789.1 .
    AK150879 mRNA. Translation: BAE29928.1 .
    AK151010 mRNA. Translation: BAE30031.1 .
    AK151136 mRNA. Translation: BAE30144.1 .
    AK151145 mRNA. Translation: BAE30152.1 .
    AK151159 mRNA. Translation: BAE30164.1 .
    AK151166 mRNA. Translation: BAE30169.1 .
    AK151190 mRNA. Translation: BAE30187.1 .
    AK151202 mRNA. Translation: BAE30199.1 .
    AK151226 mRNA. Translation: BAE30218.1 .
    AK151277 mRNA. Translation: BAE30264.1 .
    AK151350 mRNA. Translation: BAE30326.1 .
    AK151398 mRNA. Translation: BAE30366.1 .
    AK151995 mRNA. Translation: BAE30859.1 .
    AK151999 mRNA. Translation: BAE30863.1 .
    AK152615 mRNA. Translation: BAE31359.1 .
    AK152651 mRNA. Translation: BAE31388.1 .
    AK152844 mRNA. Translation: BAE31537.1 .
    AK159759 mRNA. Translation: BAE35350.1 .
    AK159834 mRNA. Translation: BAE35412.1 .
    AK160029 mRNA. Translation: BAE35572.1 .
    AK166349 mRNA. Translation: BAE38723.1 .
    AK166498 mRNA. Translation: BAE38810.1 .
    AK167117 mRNA. Translation: BAE39265.1 .
    AK167960 mRNA. Translation: BAE39957.1 .
    X03765 mRNA. Translation: CAA27396.1 .
    M12481 mRNA. Translation: AAA37144.1 .
    CCDSi CCDS19833.1.
    PIRi A39104. ATMSB.
    RefSeqi NP_031419.1. NM_007393.3.
    UniGenei Mm.328431.
    Mm.391967.
    Mm.469717.

    3D structure databases

    ProteinModelPortali P60710.
    SMRi P60710. Positions 6-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 197944. 26 interactions.
    DIPi DIP-31574N.
    IntActi P60710. 41 interactions.
    MINTi MINT-1202772.

    PTM databases

    PhosphoSitei P60710.

    2D gel databases

    COMPLUYEAST-2DPAGE P60710.
    REPRODUCTION-2DPAGE P60710.
    SWISS-2DPAGE P99041.
    UCD-2DPAGE P60710.

    Proteomic databases

    MaxQBi P60710.
    PRIDEi P60710.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000100497 ; ENSMUSP00000098066 ; ENSMUSG00000029580 .
    GeneIDi 11461.
    KEGGi mmu:11461.
    UCSCi uc009ajk.1. mouse.

    Organism-specific databases

    CTDi 60.
    MGIi MGI:87904. Actb.

    Phylogenomic databases

    GeneTreei ENSGT00710000106384.
    HOVERGENi HBG003771.
    InParanoidi P60710.
    KOi K05692.
    OMAi SIVHLKC.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P60710.
    TreeFami TF354237.

    Enzyme and pathway databases

    Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
    REACT_198649. Factors involved in megakaryocyte development and platelet production.
    REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_209040. Gap junction degradation.
    REACT_220352. Formation of annular gap junctions.
    REACT_226917. HATs acetylate histones.

    Miscellaneous databases

    ChiTaRSi ACTB. mouse.
    NextBioi 278784.
    PROi P60710.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60710.
    Bgeei P60710.
    CleanExi MM_ACTB.
    Genevestigatori P60710.

    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. "Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA."
      Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S.
      Nucleic Acids Res. 14:2829-2829(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: BALB/c, C57BL/6J and NOD.
      Tissue: Bone marrow, Mammary gland and Thymus.
    3. "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin."
      Vandekerckhove J., Weber K.
      Eur. J. Biochem. 90:451-462(1978) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, METHYLATION AT HIS-73.
      Tissue: Thymus.
    4. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
      Submitted (JAN-2009) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-39; 51-61; 85-113; 148-177; 184-191; 197-206; 216-254; 257-284; 291-326 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6 and OF1.
      Tissue: Brain and Hippocampus.
    5. "Comparison of three actin-coding sequences in the mouse; evolutionary relationships between the actin genes of warm-blooded vertebrates."
      Alonso S., Minty A., Bourlet Y., Buckingham M.
      J. Mol. Evol. 23:11-22(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-375.
    6. Vilbois F.
      Submitted (OCT-1998) to UniProtKB
      Cited for: ACETYLATION.
      Tissue: Muscle.
    7. Cited for: ISGYLATION.
    8. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
      Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
      Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: OXIDATION AT MET-44 AND MET-47, DEOXIDATION AT MET-44 AND MET-47.

    Entry informationi

    Entry nameiACTB_MOUSE
    AccessioniPrimary (citable) accession number: P60710
    Secondary accession number(s): P02570
    , P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 114 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3