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Details on Person UniProt:P60711 Actb
| Class:Id | ReferenceGeneProduct:49580 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Sat February 7 2015;chain:1-375 added on Sat February 7 2015;chain:2-375 added on Sat February 7 2015;initiator methionine:1 for 49580 removed on Fri Nov 03 2023;initiator methionine: for 49580 added on Fri Nov 03 2023;initiator methionine: for 49580 removed on Fri Aug 15 2025;initiator methionine:1 for 49580 added on Fri Aug 15 2025 |
| _displayName | UniProt:P60711 Actb |
| _timestamp | 2025-08-15 21:12:44 |
| chain | chain:1-375 initiator methionine:1 chain:2-375 |
| checksum | 6AFD05CA94E360E2 |
| comment | FUNCTION Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells (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 (By similarity). 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 (By similarity). Plays a role in the assembly of the gamma-tubulin ring complex (gTuRC), which regulates the minus-end nucleation of alpha-beta tubulin heterodimers that grow into microtubule protafilaments (By similarity). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). The dynactin multiprotein complex activates the molecular motor dynein for ultra-processive transport along microtubules (By similarity).CATALYTIC ACTIVITY ATP + H2O = ADP + phosphate + H(+)SUBUNIT Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix (By similarity). Each actin can bind to 4 others (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs (By similarity). 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 (By similarity). In muscle cells, the BAF complex also contains DPF3 (By similarity). Found in a complex with XPO6, Ran, ACTB and PFN1 (By similarity). Interacts with PFN1 (By similarity). Interacts with XPO6 and EMD (By similarity). Interacts with ERBB2 (By similarity). Interacts with GCSAM (By similarity). 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 (By similarity). Interacts with FAM107A (By similarity). Associates with the gamma-tubulin ring complex (gTuRC) consisting of TUBGCP2, TUBGCP3, TUBGCP4, TUBGCP5 and TUBGCP6 and gamma-tubulin TUBG1 or TUBG2; within the complex, interacts with TUBGCP3 and TUBGCP6 to form a luminal bridge with MZT1 that stabilizes the initial structure during complex assembly (By similarity). Part of the ACTR1A/ACTB filament around which the dynactin complex is built (By similarity). 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).INTERACTION Localized in cytoplasmic mRNP granules containing untranslated mRNAs.TISSUE SPECIFICITY Expressed in the epididymis (at protein level).PTM N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.PTM ISGylated.PTM 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.PTM 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.PTM Methylated at His-73 by SETD3 (PubMed:30526847). Methylation at His-73 is required for smooth muscle contraction of the laboring uterus during delivery (By similarity).PTM N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected.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.SIMILARITY Belongs to the actin family. |
| description | recommendedName: Actin, cytoplasmic 1 ecNumber evidence="4"3.6.4.- alternativeName: Beta-actin component recommendedName: Actin, cytoplasmic 1, N-terminally processed /component |
| geneName | Actb |
| identifier | P60711 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation ATP-binding Cytoplasm Cytoskeleton Direct protein sequencing Hydrolase Methylation Nucleotide-binding Nucleus Oxidation Reference proteome Ubl conjugation |
| modified | [InstanceEdit:84067] Schmidt, EE, 2003-12-18 04:29:09 [InstanceEdit:143527] Schmidt, EE, 2004-11-12 07:45:10 [InstanceEdit:217385] Schmidt, EE, 2008-03-27 06:23:53 [InstanceEdit:354386] Schmidt, EE, 2008-06-18 04:45:12 [InstanceEdit:384350] Kanapin, AA, 2008-11-26 14:00:39 [InstanceEdit:392885] Kanapin, AA, 2009-03-09 12:07:18 [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 [InstanceEdit:423310] Kanapin, AA [InstanceEdit:435478] Kanapin, AA [InstanceEdit:435871] Kanapin, AA [InstanceEdit:447347] Kanapin, AA [InstanceEdit:525883] Kanapin, AA [InstanceEdit:613449] Kanapin, AA [InstanceEdit:797602] Kanapin, AA [InstanceEdit:937368] Yung, CK [InstanceEdit:1042053] Yung, CK [InstanceEdit:1220657] Yung, CK [InstanceEdit:1300696] Yung, CK [InstanceEdit:1301627] Yung, CK [InstanceEdit:1551960] Weiser, JD [InstanceEdit:1995863] Weiser, JD [InstanceEdit:2132304] Weiser, JD [InstanceEdit:2265580] Weiser, JD [InstanceEdit:3445779] Weiser, JD [InstanceEdit:4341137] Weiser, JD [InstanceEdit:5263031] Weiser, JD [InstanceEdit:5433710] Weiser, JD [InstanceEdit:5618415] Weiser, JD [InstanceEdit:5634237] Weiser, JD [InstanceEdit:5673015] Weiser, JD [InstanceEdit:9037114] Weiser, JD [InstanceEdit:9607352] Weiser, JD [InstanceEdit:9627708] Weiser, JD [InstanceEdit:9637257] Weiser, JD [InstanceEdit:9657908] Weiser, JD [InstanceEdit:9676415] Weiser, JD [InstanceEdit:9819394] Weiser, Joel [InstanceEdit:9834092] Weiser, Joel [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | Actb |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| secondaryIdentifier | ACTB_RAT P02570 P70514 P99021 Q11211 Q64316 |
| sequenceLength | 375 |
| species | [Species:48895] Rattus norvegicus |
| (referenceEntity) | [EntityWithAccessionedSequence:443585] Beta actin_Rat [cytosol] [Rattus norvegicus] |
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No pathways have been reviewed or authored by UniProt:P60711 Actb (49580)
