P63261 · ACTG_HUMAN
- ProteinActin, cytoplasmic 2
- GeneACTG1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids375 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells. May play a role in the repair of noise-induced stereocilia gaps thereby maintains hearing sensitivity following loud noise damage (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 2
- 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 accessionP63261
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Deafness, autosomal dominant, 20 (DFNA20)
- Note
- DescriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
- See alsoMIM:604717
Natural variants in DFNA20
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_032434 | 89 | T>I | in DFNA20; dbSNP:rs28999111 | |
VAR_032435 | 118 | K>M | in DFNA20; dbSNP:rs104894544 | |
VAR_067824 | 118 | K>N | in DFNA20; dbSNP:rs267606630 | |
VAR_067825 | 122 | I>V | in DFNA20; dbSNP:rs281875330 | |
VAR_079878 | 187 | D>H | in DFNA20 | |
VAR_067826 | 241 | E>K | in DFNA20; dbSNP:rs267606631 | |
VAR_032436 | 264 | P>L | in DFNA20; dbSNP:rs104894546 | |
VAR_032437 | 278 | T>I | in DFNA20; dbSNP:rs28999112 | |
VAR_079879 | 316 | E>K | in DFNA20; uncertain significance | |
VAR_032438 | 332 | P>A | in DFNA20; dbSNP:rs104894545 | |
VAR_032439 | 370 | V>A | in DFNA20; dbSNP:rs104894547 |
Baraitser-Winter syndrome 2 (BRWS2)
- 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:614583
Natural variants in BRWS2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067814 | 120 | T>I | in BRWS2; dbSNP:rs281875325 | |
VAR_067815 | 135 | A>V | in BRWS2; dbSNP:rs11549190 | |
VAR_067816 | 155 | S>F | in BRWS2; dbSNP:rs281875326 | |
VAR_067817 | 203 | T>K | in BRWS2; dbSNP:rs281875327 | |
VAR_067818 | 254 | R>W | in BRWS2; dbSNP:rs281875328 | |
VAR_067819 | 256 | R>W | in BRWS2; dbSNP:rs281875329 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_079849 | 70 | found in a patient with isolated coloboma; decreased incorporation into F-actin; decreased interaction with cofilin; loss of interaction with TWF1, CAPZB and profilin | |||
Sequence: P → L | ||||||
Natural variant | VAR_032434 | 89 | in DFNA20; dbSNP:rs28999111 | |||
Sequence: T → I | ||||||
Natural variant | VAR_032435 | 118 | in DFNA20; dbSNP:rs104894544 | |||
Sequence: K → M | ||||||
Natural variant | VAR_067824 | 118 | in DFNA20; dbSNP:rs267606630 | |||
Sequence: K → N | ||||||
Natural variant | VAR_067814 | 120 | in BRWS2; dbSNP:rs281875325 | |||
Sequence: T → I | ||||||
Natural variant | VAR_067825 | 122 | in DFNA20; dbSNP:rs281875330 | |||
Sequence: I → V | ||||||
Natural variant | VAR_067815 | 135 | in BRWS2; dbSNP:rs11549190 | |||
Sequence: A → V | ||||||
Natural variant | VAR_067816 | 155 | in BRWS2; dbSNP:rs281875326 | |||
Sequence: S → F | ||||||
Natural variant | VAR_048186 | 160 | in dbSNP:rs11549206 | |||
Sequence: T → I | ||||||
Natural variant | VAR_079878 | 187 | in DFNA20 | |||
Sequence: D → H | ||||||
Natural variant | VAR_067817 | 203 | in BRWS2; dbSNP:rs281875327 | |||
Sequence: T → K | ||||||
Natural variant | VAR_067826 | 241 | in DFNA20; dbSNP:rs267606631 | |||
Sequence: E → K | ||||||
Natural variant | VAR_067818 | 254 | in BRWS2; dbSNP:rs281875328 | |||
Sequence: R → W | ||||||
Natural variant | VAR_067819 | 256 | in BRWS2; dbSNP:rs281875329 | |||
Sequence: R → W | ||||||
Natural variant | VAR_032436 | 264 | in DFNA20; dbSNP:rs104894546 | |||
Sequence: P → L | ||||||
Natural variant | VAR_032437 | 278 | in DFNA20; dbSNP:rs28999112 | |||
Sequence: T → I | ||||||
Natural variant | VAR_079879 | 316 | in DFNA20; uncertain significance | |||
Sequence: E → K | ||||||
Natural variant | VAR_032438 | 332 | in DFNA20; dbSNP:rs104894545 | |||
Sequence: P → A | ||||||
Natural variant | VAR_032439 | 370 | in DFNA20; dbSNP:rs104894547 | |||
Sequence: V → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 558 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_0000367100 | 1-375 | UniProt | Actin, cytoplasmic 2 | |||
Sequence: MEEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | |||||||
Modified residue | 2 | UniProt | N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial | ||||
Sequence: E | |||||||
Chain | PRO_0000000831 | 2-375 | UniProt | Actin, cytoplasmic 2, N-terminally processed | |||
Sequence: EEEIAALVIDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF | |||||||
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
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. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.
Actin, cytoplasmic 2
N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP.
Actin, cytoplasmic 2, 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).
Methylated at His-73 by SETD3.
(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. Each actin can bind to 4 others. Interacts with TWF1, CAPZB, cofilin and profilin (PubMed:28493397).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P63261 | ACTB P60709 | 16 | EBI-351292, EBI-353944 | |
BINARY | P63261 | ACTG1 P63261 | 8 | EBI-351292, EBI-351292 | |
BINARY | P63261 | CAP2 P40123 | 13 | EBI-351292, EBI-1051165 | |
BINARY | P63261 | CCDC22 O60826 | 3 | EBI-351292, EBI-3943153 | |
BINARY | P63261 | CDC37 Q16543 | 3 | EBI-351292, EBI-295634 | |
BINARY | P63261 | CFL1 P23528 | 10 | EBI-351292, EBI-352733 | |
BINARY | P63261 | CFL2 Q549N0 | 5 | EBI-351292, EBI-10201319 | |
BINARY | P63261 | CFL2 Q9Y281 | 10 | EBI-351292, EBI-351218 | |
BINARY | P63261 | DSTN P60981 | 8 | EBI-351292, EBI-745191 | |
BINARY | P63261 | EHHADH Q08426 | 4 | EBI-351292, EBI-2339219 | |
BINARY | P63261 | HTT P42858 | 16 | EBI-351292, EBI-466029 | |
BINARY | P63261 | MLH1 P40692 | 7 | EBI-351292, EBI-744248 | |
BINARY | P63261 | NTAQ1 Q96HA8 | 7 | EBI-351292, EBI-741158 | |
BINARY | P63261 | PS1TP5BP1 Q1KLZ0 | 3 | EBI-351292, EBI-9978131 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length375
- Mass (Da)41,793
- Last updated1986-07-21 v1
- Checksum54D08F986964EFD5
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
J3KT65 | J3KT65_HUMAN | ACTG1 | 198 | ||
A0A804GS07 | A0A804GS07_HUMAN | ACTG1 | 366 | ||
A0A7P0TBL1 | A0A7P0TBL1_HUMAN | ACTG1 | 59 | ||
K7EM38 | K7EM38_HUMAN | ACTG1 | 133 | ||
I3L4N8 | I3L4N8_HUMAN | ACTG1 | 351 | ||
I3L3R2 | I3L3R2_HUMAN | ACTG1 | 164 | ||
I3L3I0 | I3L3I0_HUMAN | ACTG1 | 214 | ||
I3L1U9 | I3L1U9_HUMAN | ACTG1 | 214 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 344 | in Ref. 10; AAA51580 | ||||
Sequence: S → F |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X04098 EMBL· GenBank· DDBJ | CAA27723.1 EMBL· GenBank· DDBJ | mRNA | ||
M19283 EMBL· GenBank· DDBJ | AAA51579.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK291937 EMBL· GenBank· DDBJ | BAF84626.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019856 EMBL· GenBank· DDBJ | AAV38659.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000292 EMBL· GenBank· DDBJ | AAH00292.1 EMBL· GenBank· DDBJ | mRNA | ||
BC001920 EMBL· GenBank· DDBJ | AAH01920.1 EMBL· GenBank· DDBJ | mRNA | ||
BC007442 EMBL· GenBank· DDBJ | AAH07442.1 EMBL· GenBank· DDBJ | mRNA | ||
BC009848 EMBL· GenBank· DDBJ | AAH09848.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010999 EMBL· GenBank· DDBJ | AAH10999.1 EMBL· GenBank· DDBJ | mRNA | ||
BC012050 EMBL· GenBank· DDBJ | AAH12050.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015005 EMBL· GenBank· DDBJ | AAH15005.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015695 EMBL· GenBank· DDBJ | AAH15695.1 EMBL· GenBank· DDBJ | mRNA | ||
BC015779 EMBL· GenBank· DDBJ | AAH15779.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018774 EMBL· GenBank· DDBJ | AAH18774.1 EMBL· GenBank· DDBJ | mRNA | ||
BC053572 EMBL· GenBank· DDBJ | AAH53572.1 EMBL· GenBank· DDBJ | mRNA | ||
M16247 EMBL· GenBank· DDBJ | AAA51580.1 EMBL· GenBank· DDBJ | mRNA |