P60709 · ACTB_HUMAN
- ProteinActin, cytoplasmic 1
- GeneACTB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (PubMed:25255767, PubMed:29581253).
Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253).
In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction (PubMed:29581253).
In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA (PubMed:29925947).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).
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.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
GO annotations
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActin, cytoplasmic 1
- EC number
- Alternative names
- Cleaved into 1 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP60709
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Dystonia-deafness syndrome 1 (DDS1)
- Note
- DescriptionAn autosomal dominant form of dystonia with juvenile onset, associated with congenital or childhood-onset sensorineural deafness. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Some DDS1 patients have dysmorphic features, skeletal anomalies, and/or mild developmental delay with impaired intellectual development.
- See alsoMIM:607371
Natural variants in DDS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_030026 | 183 | R>W | in DDS1; likely pathogenic; results in reduced actin polymerization rate and increased depolymerization; results in higher ATP hydrolysis compared to the wild type; does not affect thermal stability; modifies cell response to latrunculin A; dbSNP:rs104894003 |
Baraitser-Winter syndrome 1 (BRWS1)
- Note
- DescriptionA 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.
- See alsoMIM:243310
Natural variants in BRWS1
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067810 | 12 | N>D | in BRWS1; dbSNP:rs281875331 | |
VAR_067811 | 65 | L>V | in BRWS1; dbSNP:rs281875332 | |
VAR_088861 | 70 | P>A | in BRWS1; likely pathogenic | |
VAR_067812 | 196 | R>C | in BRWS1; dbSNP:rs281875333 | |
VAR_067813 | 196 | R>H | in BRWS1; dbSNP:rs281875334 |
Thrombocytopenia 8, with dysmorphic features and developmental delay (THC8)
- Note
- DescriptionA form of thrombocytopenia, a hematologic disorder defined by a decrease in the number of platelets in circulating blood, resulting in the potential for increased bleeding and decreased ability for clotting. THC8 is an autosomal dominant form characterized by early-childhood onset of thrombocytopenia with platelet anisotropy. Affected individuals also have dysmorphic facial features and variable developmental delay with speech delay and mildly impaired intellectual development.
- See alsoMIM:620475
Natural variants in THC8
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088870 | 171 | L>F | in THC8; likely pathogenic | |
VAR_088871 | 313 | M>R | in THC8; uncertain significance | |
VAR_088872 | 338-341 | missing | in THC8; likely pathogenic | |
VAR_088873 | 364 | E>K | in THC8; uncertain significance; results in reduced actin polymerization rate without affecting depolymerization; has no effect on ATP hydrolysis rate; does not affect thermal stability |
Becker nevus syndrome (BNS)
- Note
- DescriptionA syndrome characterized by the association of Becker nevi with musculoskeletal abnormalities, unilateral breast hypoplasia, intellectual disability, developmental delay, and cardiomyopathy. Becker nevus is a cutaneous hamartoma that appears in childhood as a unilateral tan patch and increases in thickness, pigmentation, and hair growth during adolescence. Histologically, epidermal acanthosis is accompanied by irregularly dispersed ectopic smooth muscle bundles and increased terminal hair follicles. Most cases are sporadic.
- See alsoMIM:604919
Natural variants in BNS
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088868 | 147 | R>C | in BNS and CSMH; also found in isolated non-syndromic Becker nevi; somatic variant |
Congenital smooth muscle hamartoma, with or without hemihypertrophy (CSMH)
- Note
- DescriptionA benign skin lesion that usually presents as an indurated, slightly pigmented or flesh-colored plaque with perifollicular papules or coarse hair. Histopathologically, there is excessive proliferation of ectopic smooth muscle within the dermis. Hair follicles are normal in number and hyperkeratosis, acanthosis and hyperpigmentation of the basal cell layer can sometimes be seen. Rarely, CSMH is associated with hemihypertrophy.
- See alsoMIM:620470
Natural variants in CSMH
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_088862 | 111 | N>D | in CSMH; uncertain significance; somatic variant | |
VAR_088863 | 137 | Q>H | in CSMH; uncertain significance; somatic variant | |
VAR_088864 | 146 | G>A | in CSMH; somatic variant | |
VAR_088865 | 146 | G>D | in CSMH; somatic variant | |
VAR_088866 | 146 | G>S | in CSMH; somatic variant | |
VAR_088867 | 146 | G>V | in CSMH; somatic variant | |
VAR_088868 | 147 | R>C | in BNS and CSMH; also found in isolated non-syndromic Becker nevi; somatic variant | |
VAR_088869 | 147 | R>S | in CSMH; also found in isolated non-syndromic Becker nevi; somatic variant |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_067810 | 12 | in BRWS1; dbSNP:rs281875331 | |||
Sequence: N → D | ||||||
Natural variant | VAR_067811 | 65 | in BRWS1; dbSNP:rs281875332 | |||
Sequence: L → V | ||||||
Mutagenesis | 69 | Decreased interaction with SETD3. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_088861 | 70 | in BRWS1; likely pathogenic | |||
Sequence: P → A | ||||||
Mutagenesis | 71 | Decreased interaction with SETD3. | ||||
Sequence: I → A | ||||||
Mutagenesis | 71 | Impaired methylation by SETD3. | ||||
Sequence: I → A | ||||||
Mutagenesis | 73 | Abolished methylation by SETD3. | ||||
Sequence: H → A | ||||||
Mutagenesis | 73 | Weak methylation by a A-256 or V-256 SETD3 mutant. High methylation by a F-256 and A-274 SETD3 mutant. | ||||
Sequence: H → K | ||||||
Mutagenesis | 74 | Impaired methylation by SETD3. | ||||
Sequence: G → A | ||||||
Mutagenesis | 79 | Does not affect methylation by SETD3. | ||||
Sequence: W → E | ||||||
Mutagenesis | 80 | Decreased interaction with SETD3. | ||||
Sequence: D → A | ||||||
Mutagenesis | 81 | Decreased interaction with SETD3. | ||||
Sequence: D → A | ||||||
Mutagenesis | 82 | Decreased interaction with SETD3. | ||||
Sequence: M → A | ||||||
Natural variant | VAR_088862 | 111 | in CSMH; uncertain significance; somatic variant | |||
Sequence: N → D | ||||||
Natural variant | VAR_088863 | 137 | in CSMH; uncertain significance; somatic variant | |||
Sequence: Q → H | ||||||
Natural variant | VAR_088864 | 146 | in CSMH; somatic variant | |||
Sequence: G → A | ||||||
Natural variant | VAR_088865 | 146 | in CSMH; somatic variant | |||
Sequence: G → D | ||||||
Natural variant | VAR_088866 | 146 | in CSMH; somatic variant | |||
Sequence: G → S | ||||||
Natural variant | VAR_088867 | 146 | in CSMH; somatic variant | |||
Sequence: G → V | ||||||
Natural variant | VAR_088868 | 147 | in BNS and CSMH; also found in isolated non-syndromic Becker nevi; somatic variant | |||
Sequence: R → C | ||||||
Natural variant | VAR_088869 | 147 | in CSMH; also found in isolated non-syndromic Becker nevi; somatic variant | |||
Sequence: R → S | ||||||
Natural variant | VAR_088870 | 171 | in THC8; likely pathogenic | |||
Sequence: L → F | ||||||
Natural variant | VAR_030026 | 183 | in DDS1; likely pathogenic; results in reduced actin polymerization rate and increased depolymerization; results in higher ATP hydrolysis compared to the wild type; does not affect thermal stability; modifies cell response to latrunculin A; dbSNP:rs104894003 | |||
Sequence: R → W | ||||||
Natural variant | VAR_067812 | 196 | in BRWS1; dbSNP:rs281875333 | |||
Sequence: R → C | ||||||
Natural variant | VAR_067813 | 196 | in BRWS1; dbSNP:rs281875334 | |||
Sequence: R → H | ||||||
Natural variant | VAR_048185 | 243 | in dbSNP:rs11546899 | |||
Sequence: P → L | ||||||
Natural variant | VAR_088871 | 313 | in THC8; uncertain significance | |||
Sequence: M → R | ||||||
Natural variant | VAR_088872 | 338-341 | in THC8; likely pathogenic | |||
Sequence: Missing | ||||||
Natural variant | VAR_088873 | 364 | in THC8; uncertain significance; results in reduced actin polymerization rate without affecting depolymerization; has no effect on ATP hydrolysis rate; does not affect thermal stability | |||
Sequence: E → K |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 504 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed; alternate | ||||
Sequence: M | |||||||
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000367073 | 1-375 | UniProt | Actin, cytoplasmic 1 | |||
Sequence: MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | |||||||
Modified residue | 2 | UniProt | N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed | ||||
Sequence: D | |||||||
Chain | PRO_0000000771 | 2-375 | UniProt | Actin, cytoplasmic 1, N-terminally processed | |||
Sequence: DDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | |||||||
Modified residue (large scale data) | 14 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 33 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 44 | UniProt | Methionine (R)-sulfoxide | ||||
Sequence: M | |||||||
Modified residue | 47 | UniProt | Methionine (R)-sulfoxide | ||||
Sequence: M | |||||||
Cross-link | 50 | UniProt | (Microbial infection) Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG1 | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 60 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 73 | UniProt | Tele-methylhistidine | ||||
Sequence: H | |||||||
Modified residue | 84 | UniProt | N6-methyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 89 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 106 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 166 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 188 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 199 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 201 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 218 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 233 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 239 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 240 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 249 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 270 | UniProt | (Microbial infection) Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG1 | ||||
Sequence: E | |||||||
Modified residue (large scale data) | 294 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 297 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 303 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 304 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 324 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 362 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 368 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
ISGylated.
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.
Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes (PubMed:23673617).
Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617).
Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (PubMed:23673617).
Methylated at His-73 by SETD3 (PubMed:30526847, PubMed:30626964, PubMed:30785395, PubMed:31388018).
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).
Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).
Actin, cytoplasmic 1
N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.
Actin, cytoplasmic 1, N-terminally processed
N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins (PubMed:29581253).
In contrast, filament nucleation by the Arp2/3 complex is not affected (PubMed:29581253).
In contrast, filament nucleation by the Arp2/3 complex is not affected (PubMed:29581253).
(Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515).
The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148).
The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148).
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Interaction
Subunit
Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (PubMed:16685646, PubMed:28604741).
Each actin can bind to 4 others (PubMed:16685646, PubMed:28604741).
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).
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 (PubMed:18765789).
In muscle cells, the BAF complex also contains DPF3 (PubMed:18765789).
Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989).
Interacts with PFN1 (PubMed:10411937, PubMed:25255767).
Interacts with XPO6 and EMD (PubMed:15328537).
Interacts with ERBB2 (PubMed:21555369).
Interacts with GCSAM (PubMed:17823310).
Interacts with TBC1D21 (By similarity).
Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588).
Interacts with FAM107A (PubMed:21969592, PubMed:28604741).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The filament contains 8 copies of ACTR1A and 1 ACTB (By similarity).
Interacts with TPRN which forms ring-like structures in the stereocilium taper region; the interaction may stabilize stereocilia in inner ear hair cells (By similarity).
Interacts with AMOTL2 (via N-terminus), the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (By similarity).
Each actin can bind to 4 others (PubMed:16685646, PubMed:28604741).
Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (PubMed:17289661).
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 (PubMed:18765789).
In muscle cells, the BAF complex also contains DPF3 (PubMed:18765789).
Found in a complex with XPO6, Ran, ACTB and PFN1 (PubMed:14592989).
Interacts with PFN1 (PubMed:10411937, PubMed:25255767).
Interacts with XPO6 and EMD (PubMed:15328537).
Interacts with ERBB2 (PubMed:21555369).
Interacts with GCSAM (PubMed:17823310).
Interacts with TBC1D21 (By similarity).
Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity).
Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588).
Interacts with FAM107A (PubMed:21969592, PubMed:28604741).
Part of the ACTR1A/ACTB filament around which the dynactin complex is built. The filament contains 8 copies of ACTR1A and 1 ACTB (By similarity).
Interacts with TPRN which forms ring-like structures in the stereocilium taper region; the interaction may stabilize stereocilia in inner ear hair cells (By similarity).
Interacts with AMOTL2 (via N-terminus), the interaction facilitates binding of cell junction complexes to actin fibers in endothelial cells (By similarity).
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,737
- Last updated1988-04-01 v1
- Checksum6AFD05CA94E360E2
Computationally mapped potential isoform sequences
There are 12 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y793 | A0A2R8Y793_HUMAN | ACTB | 309 | ||
A0A6Q8PFE4 | A0A6Q8PFE4_HUMAN | ACTB | 332 | ||
E7EVS6 | E7EVS6_HUMAN | ACTB | 334 | ||
A0A6Q8PGD7 | A0A6Q8PGD7_HUMAN | ACTB | 40 | ||
A0A6Q8PH58 | A0A6Q8PH58_HUMAN | ACTB | 151 | ||
A0A2R8YEA7 | A0A2R8YEA7_HUMAN | ACTB | 157 | ||
A0A2R8YGF8 | A0A2R8YGF8_HUMAN | ACTB | 165 | ||
C9JZR7 | C9JZR7_HUMAN | ACTB | 102 | ||
A0A2R8YFE2 | A0A2R8YFE2_HUMAN | ACTB | 79 | ||
C9JTX5 | C9JTX5_HUMAN | ACTB | 80 | ||
C9JUM1 | C9JUM1_HUMAN | ACTB | 96 | ||
G5E9R0 | G5E9R0_HUMAN | ACTB | 125 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 97 | in Ref. 6; AAH16045 | ||||
Sequence: A → P | ||||||
Sequence conflict | 116 | in Ref. 6; AAH12854 | ||||
Sequence: R → L |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X00351 EMBL· GenBank· DDBJ | CAA25099.1 EMBL· GenBank· DDBJ | mRNA | ||
M10277 EMBL· GenBank· DDBJ | AAA51567.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X63432 EMBL· GenBank· DDBJ | CAA45026.1 EMBL· GenBank· DDBJ | mRNA | ||
AY582799 EMBL· GenBank· DDBJ | AAS79319.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AC006483 EMBL· GenBank· DDBJ | AAP22343.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC001301 EMBL· GenBank· DDBJ | AAH01301.1 EMBL· GenBank· DDBJ | mRNA | ||
BC002409 EMBL· GenBank· DDBJ | AAH02409.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004251 EMBL· GenBank· DDBJ | AAH04251.1 EMBL· GenBank· DDBJ | mRNA | ||
BC008633 EMBL· GenBank· DDBJ | AAH08633.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012854 EMBL· GenBank· DDBJ | AAH12854.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013380 EMBL· GenBank· DDBJ | AAH13380.1 EMBL· GenBank· DDBJ | mRNA | ||
BC014861 EMBL· GenBank· DDBJ | AAH14861.1 EMBL· GenBank· DDBJ | mRNA | ||
BC016045 EMBL· GenBank· DDBJ | AAH16045.1 EMBL· GenBank· DDBJ | mRNA | ||
V00478 EMBL· GenBank· DDBJ | CAA23745.1 EMBL· GenBank· DDBJ | mRNA |