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Beta-actin

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(Redirected from ACTB) Protein-coding gene in the species Homo sapiens
ACTB
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3BYH, 3D2U, 3J82, 3LUE

Identifiers
AliasesACTB, BRWS1, PS1TP5BP1, Beta-actin, actin, beta, actin beta
External IDsOMIM: 102630; MGI: 87904; HomoloGene: 110648; GeneCards: ACTB; OMA:ACTB - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)
Chromosome 7 (human)Genomic location for ACTBGenomic location for ACTB
Band7p22.1Start5,526,409 bp
End5,563,902 bp
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)
Chromosome 5 (mouse)Genomic location for ACTBGenomic location for ACTB
Band5 G2|5 81.8 cMStart142,888,870 bp
End142,892,509 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • saphenous vein

  • urethra

  • postcentral gyrus

  • synovial joint

  • orbitofrontal cortex

  • mucosa of ileum

  • Brodmann area 46

  • nipple

  • vena cava

  • olfactory bulb
Top expressed in
  • human fetus

  • vas deferens

  • lateral septal nucleus

  • Gonadal ridge

  • mandibular prominence

  • migratory enteric neural crest cell

  • maxillary prominence

  • ventromedial nucleus

  • abdominal wall

  • medial ganglionic eminence
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

60

11461

Ensembl

ENSG00000075624

ENSMUSG00000029580

UniProt

P60709

P60710

RefSeq (mRNA)

NM_001101

NM_007393

RefSeq (protein)

NP_001092

NP_031419

Location (UCSC)Chr 7: 5.53 – 5.56 MbChr 5: 142.89 – 142.89 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

Actin beta (HUGO Gene Nomenclature Committee abbreviation ACTB/ACTB) is one of six different actin isoforms which have been identified in humans. This is one of the two nonmuscle cytoskeletal actins. Actins are highly conserved proteins that are involved in cell motility, structure and integrity. Alpha actins are a major constituent of the contractile apparatus.

Interactions

Actin beta has been shown to interact with SPTBN2. In addition, RNA-binding protein Sam68 was found to interact with the mRNA encoding actin beta, which regulates the synaptic formation of the dendritic spines with its cytoskeletal components.

Actin beta has been shown to activate eNOS, thereby increasing NO production. An eight-amino acid motif (326-333) in eNOS has been shown to mediate the interaction between actin and eNOS.

Clinical relevance

Recurrent mutations in this gene have been associated to cases of diffuse large B-cell lymphoma.

Applications

Actin beta is often used in Western blotting as a loading control, to normalize total protein amounts and check for eventual protein degradation in the samples. Its transcript is also commonly used as a housekeeping gene standard in qPCR. Its molecular weight is approximately 42 kDa.

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000075624 – Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000029580 – Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Gunning PW, Ghoshdastider U, Whitaker S, Popp D, Robinson RC (Jun 2015). "The evolution of compositionally and functionally distinct actin filaments". Journal of Cell Science. 128 (11): 2009–2019. doi:10.1242/jcs.165563. PMID 25788699.
  6. Hanukoglu I, Tanese N, Fuchs E (Feb 1983). "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions". Journal of Molecular Biology. 163 (4): 673–8. doi:10.1016/0022-2836(83)90117-1. PMID 6842590.
  7. "Entrez Gene: ACTB actin, beta".
  8. Mao B, Wu W, Li Y, Hoppe D, Stannek P, Glinka A, Niehrs C (May 2001). "LDL-receptor-related protein 6 is a receptor for Dickkopf proteins". Nature. 411 (6835): 321–5. Bibcode:2001Natur.411..321M. doi:10.1038/35077108. PMID 11357136. S2CID 4323027.
  9. Holleran EA, Ligon LA, Tokito M, Stankewich MC, Morrow JS, Holzbaur EL (Sep 2001). "beta III spectrin binds to the Arp1 subunit of dynactin". The Journal of Biological Chemistry. 276 (39): 36598–605. doi:10.1074/jbc.M104838200. PMID 11461920.
  10. Kondrikov D, Fonseca FV, Elms S, Fulton D, Black SM, Block ER, Su Y (Feb 2010). "Beta-actin association with endothelial nitric-oxide synthase modulates nitric oxide and superoxide generation from the enzyme". The Journal of Biological Chemistry. 285 (7): 4319–27. doi:10.1074/jbc.M109.063172. PMC 2836036. PMID 19946124.
  11. Lohr JG, Stojanov P, Lawrence MS, Auclair D, Chapuy B, Sougnez C, Cruz-Gordillo P, Knoechel B, Asmann YW, Slager SL, Novak AJ, Dogan A, Ansell SM, Link BK, Zou L, Gould J, Saksena G, Stransky N, Rangel-Escareño C, Fernandez-Lopez JC, Hidalgo-Miranda A, Melendez-Zajgla J, Hernández-Lemus E, Schwarz-Cruz y Celis A, Imaz-Rosshandler I, Ojesina AI, Jung J, Pedamallu CS, Lander ES, Habermann TM, Cerhan JR, Shipp MA, Getz G, Golub TR (Mar 2012). "Discovery and prioritization of somatic mutations in diffuse large B-cell lymphoma (DLBCL) by whole-exome sequencing". Proceedings of the National Academy of Sciences of the United States of America. 109 (10): 3879–84. Bibcode:2012PNAS..109.3879L. doi:10.1073/pnas.1121343109. PMC 3309757. PMID 22343534.

External links

Further reading

See also

PDB gallery
  • 1atn: Atomic structure of the actin:DNASE I complex 1atn: Atomic structure of the actin:DNASE I complex
  • 1c0f: CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 1 1c0f: CRYSTAL STRUCTURE OF DICTYOSTELIUM CAATP-ACTIN IN COMPLEX WITH GELSOLIN SEGMENT 1
  • 1c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H) 1c0g: CRYSTAL STRUCTURE OF 1:1 COMPLEX BETWEEN GELSOLIN SEGMENT 1 AND A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 228: Q228K/T229A/A230Y/E360H)
  • 1d4x: Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution. 1d4x: Crystal Structure of Caenorhabditis Elegans Mg-ATP Actin Complexed with Human Gelsolin Segment 1 at 1.75 A resolution.
  • 1dej: CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1 1dej: CRYSTAL STRUCTURE OF A DICTYOSTELIUM/TETRAHYMENA CHIMERA ACTIN (MUTANT 646: Q228K/T229A/A230Y/A231K/S232E/E360H) IN COMPLEX WITH HUMAN GELSOLIN SEGMENT 1
  • 1eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1 1eqy: COMPLEX BETWEEN RABBIT MUSCLE ALPHA-ACTIN: HUMAN GELSOLIN DOMAIN 1
  • 1esv: COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1 1esv: COMPLEX BETWEEN LATRUNCULIN A:RABBIT MUSCLE ALPHA ACTIN:HUMAN GELSOLIN DOMAIN 1
  • 1h1v: GELSOLIN G4-G6/ACTIN COMPLEX 1h1v: GELSOLIN G4-G6/ACTIN COMPLEX
  • 1hlu: STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE 1hlu: STRUCTURE OF BOVINE BETA-ACTIN-PROFILIN COMPLEX WITH ACTIN BOUND ATP PHOSPHATES SOLVENT ACCESSIBLE
  • 1ijj: THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION 1ijj: THE X-RAY CRYSTAL STRUCTURE OF THE COMPLEX BETWEEN RABBIT SKELETAL MUSCLE ACTIN AND LATRUNCULIN A AT 2.85 A RESOLUTION
  • 1j6z: UNCOMPLEXED ACTIN 1j6z: UNCOMPLEXED ACTIN
  • 1kxp: CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN 1kxp: CRYSTAL STRUCTURE OF HUMAN VITAMIN D-BINDING PROTEIN IN COMPLEX WITH SKELETAL ACTIN
  • 1lcu: Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution 1lcu: Polylysine Induces an Antiparallel Actin Dimer that Nucleates Filament Assembly: Crystal Structure at 3.5 A Resolution
  • 1lot: CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN 1lot: CRYSTAL STRUCTURE OF THE COMPLEX OF ACTIN WITH VITAMIN D-BINDING PROTEIN
  • 1m8q: Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle 1m8q: Molecular Models of Averaged Rigor Crossbridges from Tomograms of Insect Flight Muscle
  • 1ma9: Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin 1ma9: Crystal structure of the complex of human vitamin D binding protein and rabbit muscle actin
  • 1mdu: Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1) 1mdu: Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)
  • 1mvw: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1mvw: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1nlv: Crystal Structure Of Dictyostelium Discoideum Actin Complexed With Ca ATP And Human Gelsolin Segment 1 1nlv: Crystal Structure Of Dictyostelium Discoideum Actin Complexed With Ca ATP And Human Gelsolin Segment 1
  • 1nm1: Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution 1nm1: Crystal Structure of D. Dicsoideum Actin Complexed With Gelsolin Segment 1 and Mg ATP at 1.8 A Resolution
  • 1nmd: Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP 1nmd: Crystal Structure of D. Discoideum Actin-Gelsolin Segment 1 Complex Crystallized In Presence Of Lithium ATP
  • 1nwk: CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE 1nwk: CRYSTAL STRUCTURE OF MONOMERIC ACTIN IN THE ATP STATE
  • 1o18: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o18: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o19: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o19: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1a: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1a: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1b: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1b: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1c: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1c: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1d: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1d: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1e: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1e: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1f: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1f: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1o1g: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE 1o1g: MOLECULAR MODELS OF AVERAGED RIGOR CROSSBRIDGES FROM TOMOGRAMS OF INSECT FLIGHT MUSCLE
  • 1p8z: Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156 1p8z: Complex Between Rabbit Muscle alpha-Actin: Human Gelsolin Residues Val26-Glu156
  • 1qz5: Structure of rabbit actin in complex with kabiramide C 1qz5: Structure of rabbit actin in complex with kabiramide C
  • 1qz6: Structure of rabbit actin in complex with jaspisamide A 1qz6: Structure of rabbit actin in complex with jaspisamide A
  • 1rdw: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer 1rdw: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
  • 1rfq: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer 1rfq: Actin Crystal Dynamics: Structural Implications for F-actin Nucleation, Polymerization and Branching Mediated by the Anti-parallel Dimer
  • 1rgi: Crystal structure of gelsolin domains G1-G3 bound to actin 1rgi: Crystal structure of gelsolin domains G1-G3 bound to actin
  • 1s22: Absolute Stereochemistry of Ulapualide A 1s22: Absolute Stereochemistry of Ulapualide A
  • 1sqk: CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN 1sqk: CRYSTAL STRUCTURE OF CIBOULOT IN COMPLEX WITH SKELETAL ACTIN
  • 1t44: Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation 1t44: Structural basis of actin sequestration by thymosin-B4: Implications for arp2/3 activation
  • 1wua: The structure of Aplyronine A-actin complex 1wua: The structure of Aplyronine A-actin complex
  • 1y64: Bni1p Formin Homology 2 Domain complexed with ATP-actin 1y64: Bni1p Formin Homology 2 Domain complexed with ATP-actin
  • 1yxq: Crystal structure of actin in complex with swinholide A 1yxq: Crystal structure of actin in complex with swinholide A
  • 2a3z: Ternary complex of the WH2 domain of WASP with Actin-DNAse I 2a3z: Ternary complex of the WH2 domain of WASP with Actin-DNAse I
  • 2a40: Ternary complex of the WH2 domain of WAVE with Actin-DNAse I 2a40: Ternary complex of the WH2 domain of WAVE with Actin-DNAse I
  • 2a41: Ternary complex of the WH2 Domain of WIP with Actin-DNAse I 2a41: Ternary complex of the WH2 Domain of WIP with Actin-DNAse I
  • 2a42: Actin-DNAse I Complex 2a42: Actin-DNAse I Complex
  • 2a5x: Crystal Structure of a Cross-linked Actin Dimer 2a5x: Crystal Structure of a Cross-linked Actin Dimer
  • 2asm: Structure of Rabbit Actin In Complex With Reidispongiolide A 2asm: Structure of Rabbit Actin In Complex With Reidispongiolide A
  • 2aso: Structure of Rabbit Actin In Complex With Sphinxolide B 2aso: Structure of Rabbit Actin In Complex With Sphinxolide B
  • 2asp: Structure of Rabbit Actin In Complex With Reidispongiolide C 2asp: Structure of Rabbit Actin In Complex With Reidispongiolide C
  • 2btf: THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN 2btf: THE STRUCTURE OF CRYSTALLINE PROFILIN-BETA-ACTIN
  • 2d1k: Ternary complex of the WH2 domain of mim with actin-dnase I 2d1k: Ternary complex of the WH2 domain of mim with actin-dnase I
  • 2ff3: Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin 2ff3: Crystal structure of Gelsolin domain 1:N-wasp V2 motif hybrid in complex with actin
  • 2ff6: Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin 2ff6: Crystal structure of Gelsolin domain 1:ciboulot domain 2 hybrid in complex with actin
  • 2fxu: X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution. 2fxu: X-ray Structure of Bistramide A- Actin Complex at 1.35 A resolution.
  • 2gwj: SpvB ADP-ribosylated actin: hexagonal crystal form 2gwj: SpvB ADP-ribosylated actin: hexagonal crystal form
  • 2gwk: SpvB ADP-ribosylated actin: orthorhombic crystal form 2gwk: SpvB ADP-ribosylated actin: orthorhombic crystal form
  • 2hf3: Crystal structure of monomeric Actin in the ADP bound state 2hf3: Crystal structure of monomeric Actin in the ADP bound state
  • 2hf4: Crystal structure of Monomeric Actin in its ATP-bound state 2hf4: Crystal structure of Monomeric Actin in its ATP-bound state
  • 2hmp: Uncomplexed actin cleaved with protease ECP32 2hmp: Uncomplexed actin cleaved with protease ECP32
  • 2oan: Structure of oxidized beta-actin 2oan: Structure of oxidized beta-actin
  • 2q1n: Actin Dimer Cross-linked Between Residues 41 and 374 2q1n: Actin Dimer Cross-linked Between Residues 41 and 374
  • 2q31: Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48. 2q31: Actin Dimer Cross-linked Between Residues 41 and 374 and proteolytically cleaved by subtilisin between residues 47 and 48.
  • 2q36: Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C 2q36: Actin Dimer Cross-linked between Residues 191 and 374 and complexed with Kabiramide C
Proteins of the cytoskeleton
Human
Microfilaments
and ABPs
Myofilament
Actins
Myosins
Other
Other
Intermediate
filaments
Type 1/2
(Keratin,
Cytokeratin)
Epithelial keratins
(soft alpha-keratins)
Hair keratins
(hard alpha-keratins)
Ungrouped alpha
Not alpha
Type 3
Type 4
Type 5
Microtubules
and MAPs
Tubulins
MAPs
Kinesins
Dyneins
Microtubule organising proteins
Microtubule severing proteins
Other
Catenins
Membrane
Other
Nonhuman
See also: cytoskeletal defects


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