Reviewed,
UniProtKB/Swiss-Prot P60709 (ACTB_HUMAN)
Last modified
January 19, 2010.
Version 82.
History...
Clusters with 100%,
90%,
50% identity |
Documents (6) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Actin, cytoplasmic 1 Alternative name(s): Beta-actin Cleaved into the following chain: 1- Recommended name: Actin, cytoplasmic 1, N-terminally processed | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) [Complete proteome] | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 375 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. |
| Subunit structure | 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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 MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Ref.11 Ref.12 |
| Subcellular location | Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.15 |
| Involvement in disease | Defects in ACTB are a cause of dystonia juvenile-onset (DYTJ) [MIM:607371]. DYTJ is a form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. DYTJ patients manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss. Ref.20 |
| 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. |
| Sequence similarities | Belongs to the actin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton |
| Coding sequence diversity | Polymorphism |
| Disease | Deafness Disease mutation Dystonia |
| Ligand | ATP-binding Nucleotide-binding |
| PTM | Acetylation Methylation Phosphoprotein |
| Technical term | 3D-structure Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cellular component movement Traceable author statement. Source: UniProtKB |
| Cellular component | MLL5-L complex Ref.21 Inferred from direct assay. Source: UniProtKB NuA4 histone acetyltransferase complexInferred from direct assay. Source: UniProtKB ribonucleoprotein complex Ref.15Inferred from direct assay. Source: UniProtKB |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW kinesin bindingInferred from physical interaction. Source: UniProtKB nitric-oxide synthase bindingInferred from physical interaction. Source: UniProtKB structural constituent of cytoskeletonTraceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| CFL2 | Q9Y281 | 1 | EBI-353944,EBI-351218 | |
| MDM2 | Q00987 | 1 | EBI-353944,EBI-389668 | |
| SMAD3 | P84022 | 1 | EBI-353944,EBI-347161 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 375 | 375 | Actin, cytoplasmic 1 | PRO_0000367073 | |||||
| Initiator methionine | 1 | 1 | Removed; alternate Ref.7 Ref.8 | ||||||
| Chain | 2 – 375 | 374 | Actin, cytoplasmic 1, N-terminally processed | PRO_0000000771 | |||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine; in Actin, cytoplasmic 1; alternate By similarity | ||||||
| Modified residue | 2 | 1 | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed Ref.8 | ||||||
| Modified residue | 53 | 1 | Phosphotyrosine Ref.14 Ref.18 | ||||||
| Modified residue | 73 | 1 | Tele-methylhistidine By similarity | ||||||
| Modified residue | 91 | 1 | Phosphotyrosine Ref.14 Ref.18 | ||||||
| Modified residue | 166 | 1 | Phosphotyrosine Ref.13 | ||||||
| Modified residue | 169 | 1 | Phosphotyrosine Ref.18 Ref.19 | ||||||
| Modified residue | 198 | 1 | Phosphotyrosine Ref.14 Ref.18 Ref.19 | ||||||
| Modified residue | 218 | 1 | Phosphotyrosine Ref.13 Ref.19 | ||||||
| Modified residue | 294 | 1 | Phosphotyrosine Ref.14 Ref.13 Ref.19 | ||||||
| Modified residue | 318 | 1 | Phosphothreonine Ref.17 | ||||||
Natural variations | |||||||||
| Natural variant | 183 | 1 | R → W in DYTJ; modifies cell response to latrunculin A. Ref.20 | VAR_030026 | |||||
| Natural variant | 243 | 1 | P → L: dbSNP rs11546899. | VAR_048185 | |||||
Experimental info | |||||||||
| Sequence conflict | 97 | 1 | A → P in AAH16045. Ref.6 | ||||||
| Sequence conflict | 116 | 1 | R → L in AAH12854. Ref.6 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 6322116] [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: 2994062] [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: 1734024] [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. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [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: 15489334] [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: 12665801] [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, 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, 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: 6842590] [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: 14592989] [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: 15328537] [Abstract] Cited for: INTERACTION WITH EMD. |
| [13] | "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166; TYR-218 AND TYR-294, MASS SPECTROMETRY. |
| [14] | "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J.Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-198 AND TYR-294, MASS SPECTROMETRY. Tissue: Lung. |
| [15] | "Molecular composition of IMP1 ribonucleoprotein granules." Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C. Mol. Cell. Proteomics 6:798-811(2007) [PubMed: 17289661] [Abstract] 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: 18765789] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY. |
| [17] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Platelet. |
| [18] | "An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-169 AND TYR-198, MASS SPECTROMETRY. Tissue: Mammary epithelium. |
| [19] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-169; TYR-198; TYR-218 AND TYR-294, MASS SPECTROMETRY. Tissue: T-cell. |
| [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: 16685646] [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: 19377461] [Abstract] Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||
| IPI | IPI00021439. | ||||||||||||||||||
| PIR | ATHUB. A25168. | ||||||||||||||||||
| RefSeq | NP_001092.1. | ||||||||||||||||||
| UniGene | Hs.520640 Hs.708120 | ||||||||||||||||||
3D structure databases | |||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||
| SMR | P60709. Positions 2-375. | ||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||
| DIP | DIP-29686N. | ||||||||||||||||||
| IntAct | P60709. 98 interactions. | ||||||||||||||||||
| STRING | P60709. | ||||||||||||||||||
PTM databases | |||||||||||||||||||
| PhosphoSite | P60709. | ||||||||||||||||||
2-D gel databases | |||||||||||||||||||
| SWISS-2DPAGE | P60709. | ||||||||||||||||||
| Aarhus/Ghent-2DPAGE | 7316. IEF. | ||||||||||||||||||
| DOSAC-COBS-2DPAGE | P60709. | ||||||||||||||||||
| REPRODUCTION-2DPAGE | P60709. | ||||||||||||||||||
| Siena-2DPAGE | P60709. | ||||||||||||||||||
Proteomic databases | |||||||||||||||||||
| PeptideAtlas | P60709. | ||||||||||||||||||
| PRIDE | P60709. | ||||||||||||||||||
Genome annotation databases | |||||||||||||||||||
| Ensembl | ENST00000331789; ENSP00000349960; ENSG00000075624; Homo sapiens. [Genome view] | ||||||||||||||||||
| GeneID | 60. | ||||||||||||||||||
| KEGG | hsa:60. | ||||||||||||||||||
| UCSC | uc003sos.2. human. | ||||||||||||||||||
Organism-specific databases | |||||||||||||||||||
| CTD | 60. | ||||||||||||||||||
| GeneCards | GC07M005533. | ||||||||||||||||||
| HGNC | HGNC:132. ACTB. | ||||||||||||||||||
| HPA | CAB002621. | ||||||||||||||||||
| MIM | 102630. gene. 607371. phenotype. | ||||||||||||||||||
| Orphanet | 79107. Developmental malformations - deafness - dystonia. | ||||||||||||||||||
| PharmGKB | PA24457. | ||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||
| eggNOG | prNOG18221. | ||||||||||||||||||
| HOVERGEN | P60709. | ||||||||||||||||||
| InParanoid | P60709. | ||||||||||||||||||
| OMA | LETANTS. | ||||||||||||||||||
| PhylomeDB | P60709. | ||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||
| Reactome | REACT_17015. Metabolism of proteins. | ||||||||||||||||||
Gene expression databases | |||||||||||||||||||
| ArrayExpress | P60709. | ||||||||||||||||||
| Bgee | P60709. | ||||||||||||||||||
| CleanEx | HS_ACTB. | ||||||||||||||||||
| Genevestigator | P60709. | ||||||||||||||||||
| GermOnline | ENSG00000075624. Homo sapiens. | ||||||||||||||||||
Family and domain databases | |||||||||||||||||||
| InterPro | IPR004000. Actin-like. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view] | ||||||||||||||||||
| PANTHER | PTHR11937. Actin_like. 1 hit. | ||||||||||||||||||
| Pfam | PF00022. Actin. 1 hit. [Graphical view] | ||||||||||||||||||
| PRINTS | PR00190. ACTIN. | ||||||||||||||||||
| SMART | SM00268. ACTIN. 1 hit. [Graphical view] | ||||||||||||||||||
| PROSITE | PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view] | ||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||
Other Resources | |||||||||||||||||||
| NextBio | 253. | ||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||
Entry information
| Entry name | ACTB_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P60709 Secondary accession number(s): P02570 Q96HG5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
| Disclaimer | Any 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. | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


