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P60709

- ACTB_HUMAN

UniProt

P60709 - ACTB_HUMAN

Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 133 (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. kinesin binding Source: UniProtKB
    3. nitric-oxide synthase binding Source: BHF-UCL
    4. protein binding Source: UniProtKB
    5. structural constituent of cytoskeleton Source: UniProtKB
    6. Tat protein binding Source: BHF-UCL

    GO - Biological processi

    1. 'de novo' posttranslational protein folding Source: Reactome
    2. adherens junction organization Source: Reactome
    3. ATP-dependent chromatin remodeling Source: UniProt
    4. axon guidance Source: Reactome
    5. blood coagulation Source: Reactome
    6. cell-cell junction organization Source: Reactome
    7. cell junction assembly Source: Reactome
    8. cellular component movement Source: UniProtKB
    9. cellular protein metabolic process Source: Reactome
    10. chromatin organization Source: Reactome
    11. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
    12. innate immune response Source: Reactome
    13. membrane organization Source: Reactome
    14. protein folding Source: Reactome
    15. retina homeostasis Source: UniProt
    16. substantia nigra development Source: UniProt

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_17050. Folding of actin by CCT/TriC.
    REACT_172610. HATs acetylate histones.
    REACT_19195. Adherens junctions interactions.
    REACT_197820. HATs acetylate histones.
    REACT_20649. Cell-extracellular matrix interactions.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_22365. Recycling pathway of L1.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinkiP60709.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Actin, cytoplasmic 1
    Alternative name(s):
    Beta-actin
    Cleaved into the following chain:
    Gene namesi
    Name:ACTB
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:132. ACTB.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication
    Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.

    GO - Cellular componenti

    1. axon Source: Ensembl
    2. blood microparticle Source: UniProt
    3. cortical cytoskeleton Source: Ensembl
    4. cytoplasm Source: UniProtKB
    5. cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
    6. cytoskeleton Source: UniProtKB
    7. cytosol Source: Reactome
    8. extracellular space Source: UniProt
    9. extracellular vesicular exosome Source: UniProtKB
    10. membrane Source: UniProtKB
    11. MLL5-L complex Source: UniProtKB
    12. NuA4 histone acetyltransferase complex Source: UniProtKB
    13. nuclear chromatin Source: UniProt
    14. nucleoplasm Source: Reactome
    15. postsynaptic density Source: Ensembl
    16. protein complex Source: UniProt
    17. ribonucleoprotein complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Involvement in diseasei

    Dystonia, juvenile-onset (DYTJ) [MIM:607371]: A form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti183 – 1831R → W in DYTJ; modifies cell response to latrunculin A. 1 Publication
    VAR_030026
    Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121N → D in BRWS1. 1 Publication
    Corresponds to variant rs281875331 [ dbSNP | Ensembl ].
    VAR_067810
    Natural varianti65 – 651L → V in BRWS1. 1 Publication
    Corresponds to variant rs281875332 [ dbSNP | Ensembl ].
    VAR_067811
    Natural varianti196 – 1961R → C in BRWS1. 1 Publication
    Corresponds to variant rs281875333 [ dbSNP | Ensembl ].
    VAR_067812
    Natural varianti196 – 1961R → H in BRWS1. 1 Publication
    Corresponds to variant rs281875334 [ dbSNP | Ensembl ].
    VAR_067813

    Keywords - Diseasei

    Deafness, Disease mutation, Dystonia, Mental retardation

    Organism-specific databases

    MIMi243310. phenotype.
    607371. phenotype.
    Orphaneti2995. Baraitser-Winter syndrome.
    79107. Developmental malformations - deafness - dystonia.
    PharmGKBiPA24457.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367073Add
    BLAST
    Initiator methioninei1 – 11Removed; alternate3 Publications
    Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000771Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed3 Publications
    Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
    Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
    Modified residuei73 – 731Tele-methylhistidineBy similarity
    Modified residuei84 – 841N6-methyllysine1 Publication

    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 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.

    Keywords - PTMi

    Acetylation, Methylation, Oxidation, Ubl conjugation

    Proteomic databases

    MaxQBiP60709.
    PaxDbiP60709.
    PeptideAtlasiP60709.
    PRIDEiP60709.

    2D gel databases

    DOSAC-COBS-2DPAGEP60709.
    P60709_OR_P63261.
    REPRODUCTION-2DPAGEP60709.
    SWISS-2DPAGEP60709.
    UCD-2DPAGEP60709.

    PTM databases

    PhosphoSiteiP60709.

    Expressioni

    Gene expression databases

    ArrayExpressiP60709.
    BgeeiP60709.
    CleanExiHS_ACTB.
    GenevestigatoriP60709.

    Organism-specific databases

    HPAiCAB002621.
    HPA041264.
    HPA041271.

    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.7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ACTG1P632613EBI-353944,EBI-351292
    CFL2Q9Y2813EBI-353944,EBI-351218
    ERBB2P0462610EBI-353944,EBI-641062
    FBXO25Q8TCJ0-23EBI-353944,EBI-6264551
    HSPA8P111422EBI-353944,EBI-351896
    Mkl1Q8K4J63EBI-353944,EBI-8291665From a different organism.
    MYL12BO149503EBI-353944,EBI-1642165
    NCF1P145983EBI-353944,EBI-395044
    NSMAFQ926362EBI-353944,EBI-2947053
    TAGLN2P378023EBI-353944,EBI-1056740
    YWHAZP631043EBI-353944,EBI-347088

    Protein-protein interaction databases

    BioGridi106575. 193 interactions.
    DIPiDIP-29686N.
    IntActiP60709. 165 interactions.
    MINTiMINT-220312.

    Structurei

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3BYHelectron microscopy12.00A2-375[»]
    3D2UX-ray2.21C/G170-178[»]
    3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
    ProteinModelPortaliP60709.
    SMRiP60709. Positions 6-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60709.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    Phylogenomic databases

    eggNOGiCOG5277.
    HOVERGENiHBG003771.
    InParanoidiP60709.
    KOiK05692.
    OMAiSIVHLKC.
    OrthoDBiEOG72RMZ1.
    PhylomeDBiP60709.
    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.

    P60709-1 [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 conflicti97 – 971A → P in AAH16045. (PubMed:15489334)Curated
    Sequence conflicti116 – 1161R → L in AAH12854. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti12 – 121N → D in BRWS1. 1 Publication
    Corresponds to variant rs281875331 [ dbSNP | Ensembl ].
    VAR_067810
    Natural varianti65 – 651L → V in BRWS1. 1 Publication
    Corresponds to variant rs281875332 [ dbSNP | Ensembl ].
    VAR_067811
    Natural varianti183 – 1831R → W in DYTJ; modifies cell response to latrunculin A. 1 Publication
    VAR_030026
    Natural varianti196 – 1961R → C in BRWS1. 1 Publication
    Corresponds to variant rs281875333 [ dbSNP | Ensembl ].
    VAR_067812
    Natural varianti196 – 1961R → H in BRWS1. 1 Publication
    Corresponds to variant rs281875334 [ dbSNP | Ensembl ].
    VAR_067813
    Natural varianti243 – 2431P → L.
    Corresponds to variant rs11546899 [ dbSNP | Ensembl ].
    VAR_048185

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00351 mRNA. Translation: CAA25099.1.
    M10277 Genomic DNA. Translation: AAA51567.1.
    X63432 mRNA. Translation: CAA45026.1.
    AY582799 Genomic DNA. Translation: AAS79319.1.
    AC006483 Genomic DNA. Translation: AAP22343.1.
    BC001301 mRNA. Translation: AAH01301.1.
    BC002409 mRNA. Translation: AAH02409.1.
    BC004251 mRNA. Translation: AAH04251.1.
    BC008633 mRNA. Translation: AAH08633.1.
    BC012854 mRNA. Translation: AAH12854.1.
    BC013380 mRNA. Translation: AAH13380.1.
    BC014861 mRNA. Translation: AAH14861.1.
    BC016045 mRNA. Translation: AAH16045.1.
    V00478 mRNA. Translation: CAA23745.1.
    CCDSiCCDS5341.1.
    PIRiA25168. ATHUB.
    RefSeqiNP_001092.1. NM_001101.3.
    UniGeneiHs.520640.

    Genome annotation databases

    EnsembliENST00000331789; ENSP00000349960; ENSG00000075624.
    GeneIDi60.
    KEGGihsa:60.
    UCSCiuc003soq.4. human.

    Polymorphism databases

    DMDMi46397333.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    NIEHS-SNPs
    Mendelian genes actin, beta (ACTB)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X00351 mRNA. Translation: CAA25099.1 .
    M10277 Genomic DNA. Translation: AAA51567.1 .
    X63432 mRNA. Translation: CAA45026.1 .
    AY582799 Genomic DNA. Translation: AAS79319.1 .
    AC006483 Genomic DNA. Translation: AAP22343.1 .
    BC001301 mRNA. Translation: AAH01301.1 .
    BC002409 mRNA. Translation: AAH02409.1 .
    BC004251 mRNA. Translation: AAH04251.1 .
    BC008633 mRNA. Translation: AAH08633.1 .
    BC012854 mRNA. Translation: AAH12854.1 .
    BC013380 mRNA. Translation: AAH13380.1 .
    BC014861 mRNA. Translation: AAH14861.1 .
    BC016045 mRNA. Translation: AAH16045.1 .
    V00478 mRNA. Translation: CAA23745.1 .
    CCDSi CCDS5341.1.
    PIRi A25168. ATHUB.
    RefSeqi NP_001092.1. NM_001101.3.
    UniGenei Hs.520640.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3BYH electron microscopy 12.00 A 2-375 [» ]
    3D2U X-ray 2.21 C/G 170-178 [» ]
    3LUE electron microscopy - A/B/C/D/E/F/G/H/I/J 2-375 [» ]
    ProteinModelPortali P60709.
    SMRi P60709. Positions 6-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106575. 193 interactions.
    DIPi DIP-29686N.
    IntActi P60709. 165 interactions.
    MINTi MINT-220312.

    Chemistry

    ChEMBLi CHEMBL2062353.

    PTM databases

    PhosphoSitei P60709.

    Polymorphism databases

    DMDMi 46397333.

    2D gel databases

    DOSAC-COBS-2DPAGE P60709.
    P60709_OR_P63261.
    REPRODUCTION-2DPAGE P60709.
    SWISS-2DPAGE P60709.
    UCD-2DPAGE P60709.

    Proteomic databases

    MaxQBi P60709.
    PaxDbi P60709.
    PeptideAtlasi P60709.
    PRIDEi P60709.

    Protocols and materials databases

    DNASUi 60.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000331789 ; ENSP00000349960 ; ENSG00000075624 .
    GeneIDi 60.
    KEGGi hsa:60.
    UCSCi uc003soq.4. human.

    Organism-specific databases

    CTDi 60.
    GeneCardsi GC07M005566.
    HGNCi HGNC:132. ACTB.
    HPAi CAB002621.
    HPA041264.
    HPA041271.
    MIMi 102630. gene.
    243310. phenotype.
    607371. phenotype.
    neXtProti NX_P60709.
    Orphaneti 2995. Baraitser-Winter syndrome.
    79107. Developmental malformations - deafness - dystonia.
    PharmGKBi PA24457.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5277.
    HOVERGENi HBG003771.
    InParanoidi P60709.
    KOi K05692.
    OMAi SIVHLKC.
    OrthoDBi EOG72RMZ1.
    PhylomeDBi P60709.
    TreeFami TF354237.

    Enzyme and pathway databases

    Reactomei REACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_147867. Translocation of GLUT4 to the plasma membrane.
    REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
    REACT_16936. Prefoldin mediated transfer of substrate to CCT/TriC.
    REACT_17050. Folding of actin by CCT/TriC.
    REACT_172610. HATs acetylate histones.
    REACT_19195. Adherens junctions interactions.
    REACT_197820. HATs acetylate histones.
    REACT_20649. Cell-extracellular matrix interactions.
    REACT_22266. Interaction between L1 and Ankyrins.
    REACT_22365. Recycling pathway of L1.
    REACT_24970. Factors involved in megakaryocyte development and platelet production.
    SignaLinki P60709.

    Miscellaneous databases

    ChiTaRSi ACTB. human.
    EvolutionaryTracei P60709.
    GeneWikii Beta-actin.
    GenomeRNAii 60.
    NextBioi 253.
    PROi P60709.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P60709.
    Bgeei P60709.
    CleanExi HS_ACTB.
    Genevestigatori P60709.

    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. "Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human beta-actin cDNA."
      Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L.
      Nucleic Acids Res. 12:1687-1696(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Molecular structure of the human cytoplasmic beta-actin gene: interspecies homology of sequences in the introns."
      Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T.
      Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Direct proof that the primary site of action of cytochalasin on cell motility processes is actin."
      Ohmori H., Toyama S., Toyama S.
      J. Cell Biol. 116:933-941(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. NIEHS SNPs program
      Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      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, Eye, Kidney, Muscle, Pancreas, Placenta and Skin.
    7. "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 2-28.
      Tissue: Platelet.
    8. Bienvenut W.V.
      Submitted (JUN-2005) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-95; 148-177; 184-191; 197-206; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma.
    9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
      Submitted (DEC-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 19-62; 85-113; 184-191; 197-206; 216-254; 291-312; 316-326 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
    10. "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions."
      Hanukoglu I., Tanese N., Fuchs E.
      J. Mol. Biol. 163:673-678(1983) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 252-375.
    11. "Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes."
      Stueven T., Hartmann E., Goerlich D.
      EMBO J. 22:5928-5940(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, INTERACTION WITH XPO6.
    12. "Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane."
      Holaska J.M., Kowalski A.K., Wilson K.L.
      PLoS Biol. 2:1354-1362(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EMD.
    13. Cited for: ISGYLATION.
    14. "HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and mediates the effects of IL-6 on cell migration."
      Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M., Lossos I.S.
      Blood 110:4268-4277(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GCSAM.
    15. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    16. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
      Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
      Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "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 ASP-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes."
      Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C.
      Cancer Res. 71:4269-4279(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ERBB2.
    19. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ASP-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. "A mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia."
      Procaccio V., Salazar G., Ono S., Styers M.L., Gearing M., Davila A., Jimenez R., Juncos J., Gutekunst C.-A., Meroni G., Fontanella B., Sontag E., Sontag J.-M., Faundez V., Wainer B.H.
      Am. J. Hum. Genet. 78:947-960(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT DYTJ TRP-183, CHARACTERIZATION OF VARIANT DYTJ TRP-183.
    21. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
      Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
      Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
    22. Cited for: METHYLATION AT LYS-84, DEMETHYLATION BY ALKBH4.
    23. Cited for: VARIANTS BRWS1 ASP-12; VAL-65; CYS-196 AND HIS-196.

    Entry informationi

    Entry nameiACTB_HUMAN
    AccessioniPrimary (citable) accession number: P60709
    Secondary accession number(s): P02570
    , P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: April 1, 1988
    Last modified: October 1, 2014
    This is version 133 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

    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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3