ACTB
entrez
60
canonical
uniprot
P60709
canonical
ensembl
ENSG00000075624
resolver
ensp
ENSP00000494269
resolver
ensp
ENSP00000494750
resolver
ensp
ENSP00000495995
resolver
ensp
ENSP00000501862
resolver
ensp
ENSP00000502821
resolver
ensp
ENSP00000569479
resolver
ensp
ENSP00000569480
resolver
ensp
ENSP00000569484
resolver
ensp
ENSP00000569488
resolver
ensp
ENSP00000589365
resolver
ensp
ENSP00000620638
resolver
enst
ENST00000493945
resolver
enst
ENST00000642480
resolver
enst
ENST00000646664
resolver
enst
ENST00000674681
resolver
enst
ENST00000675515
resolver
enst
ENST00000899420
resolver
enst
ENST00000899421
resolver
enst
ENST00000899425
resolver
enst
ENST00000899429
resolver
enst
ENST00000919306
resolver
enst
ENST00000950579
resolver
genesymbol
ACTB
resolver
genesymbol
PS1TP5BP1
resolver
hgnc
HGNC:132
resolver
uniprot
P02570
resolver
uniprot
P70514
resolver
uniprot
P99021
resolver
uniprot
Q11211
resolver
uniprot
Q1KLZ0
resolver
uniprot
Q64316
resolver
uniprot
Q75MN2
resolver
uniprot
Q96B34
resolver
uniprot
Q96HG5
resolver
uniprot_entry
ACTB_HUMAN
resolver
uniprot_entry
Q1KLZ0_HUMAN
resolver
uniprot_sec
P02570
resolver
uniprot_sec
P70514
resolver
uniprot_sec
P99021
resolver
uniprot_sec
Q11211
resolver
uniprot_sec
Q64316
resolver
uniprot_sec
Q75MN2
resolver
uniprot_sec
Q96B34
resolver
uniprot_sec
Q96HG5
resolver
amino_acid_sequence
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
uniprot
proteins
disease_involvement
DISEASE: Dystonia-deafness syndrome 1 (DDS1) [MIM:607371]: An 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. {ECO:0000269|PubMed:16685646, ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:28487785, ECO:0000269|PubMed:29788902, ECO:0000269|PubMed:35005077}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A 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. {ECO:0000269|PubMed:22366783, ECO:0000269|PubMed:30733661}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thrombocytopenia 8, with dysmorphic features and developmental delay (THC8) [MIM:620475]: A 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. {ECO:0000269|PubMed:10411937, ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:30315159, ECO:0000269|PubMed:30733661}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Becker nevus syndrome (BNS) [MIM:604919]: A 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. {ECO:0000269|PubMed:28347698}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Congenital smooth muscle hamartoma, with or without hemihypertrophy (CSMH) [MIM:620470]: A 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. {ECO:0000269|PubMed:32170967}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
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). 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 (PubMed:39321809, PubMed:38609661). 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). {ECO:0000250|UniProtKB:Q6QAQ1, ECO:0000269|PubMed:25255767, ECO:0000269|PubMed:29581253, ECO:0000269|PubMed:29925947, ECO:0000269|PubMed:38609661, ECO:0000269|PubMed:39321809}.
uniprot
proteins
mass_dalton
41737
uniprot
proteins
mutagenesis
MUTAGEN 69; /note="Y->A: Decreased interaction with SETD3."; /evidence="ECO:0000269|PubMed:30785395"; MUTAGEN 71; /note="I->A: Decreased interaction with SETD3."; /evidence="ECO:0000269|PubMed:30785395"; MUTAGEN 71; /note="I->A: Impaired methylation by SETD3."; /evidence="ECO:0000269|PubMed:30626964"; MUTAGEN 73; /note="H->A: Abolished methylation by SETD3."; /evidence="ECO:0000269|PubMed:30785395"; MUTAGEN 73; /note="H->K: Weak methylation by a A-256 or V-256 SETD3 mutant. High methylation by a F-256 and A-274 SETD3 mutant."; /evidence="ECO:0000269|PubMed:31388018, ECO:0000269|PubMed:32503840"; MUTAGEN 74; /note="G->A: Impaired methylation by SETD3."; /evidence="ECO:0000269|PubMed:30626964"; MUTAGEN 79; /note="W->E: Does not affect methylation by SETD3."; /evidence="ECO:0000269|PubMed:30626964"; MUTAGEN 80; /note="D->A: Decreased interaction with SETD3."; /evidence="ECO:0000269|PubMed:30785395"; MUTAGEN 81; /note="D->A: Decreased interaction with SETD3."; /evidence="ECO:0000269|PubMed:30785395"; MUTAGEN 82; /note="M->A: Decreased interaction with SETD3."; /evidence="ECO:0000269|PubMed:30785395
uniprot
proteins
post_translational_modification
PTM: ISGylated. {ECO:0000269|PubMed:16139798}.; 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. {ECO:0000269|PubMed:29343822}.; PTM: 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). {ECO:0000269|PubMed:23673617}.; PTM: 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). {ECO:0000250|UniProtKB:P60710, ECO:0000269|PubMed:30526847, ECO:0000269|PubMed:30626964, ECO:0000269|PubMed:30785395, ECO:0000269|PubMed:31388018}.; PTM: [Actin, cytoplasmic 1]: N-terminal cleavage of acetylated methionine of immature cytoplasmic actin by ACTMAP. {ECO:0000269|PubMed:36173861}.; PTM: [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). {ECO:0000269|PubMed:29581253}.; PTM: (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). {ECO:0000305|PubMed:19015515, ECO:0000305|PubMed:26228148}.
uniprot
proteins
protein_family
Actin family
uniprot
proteins
pubmed
10411937
uniprot
proteins
pubmed
11687588
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12853948
uniprot
proteins
pubmed
14592989
uniprot
proteins
pubmed
14654843
uniprot
proteins
pubmed
15328537
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16139798
uniprot
proteins
pubmed
16685646
uniprot
proteins
pubmed
17289661
uniprot
proteins
pubmed
1734024
uniprot
proteins
pubmed
17823310
uniprot
proteins
pubmed
18765789
uniprot
proteins
pubmed
19015515
uniprot
proteins
pubmed
19377461
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
21555369
uniprot
proteins
pubmed
21969592
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22366783
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23673617
uniprot
proteins
pubmed
24336203
uniprot
proteins
pubmed
25255767
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26228148
uniprot
proteins
pubmed
28347698
uniprot
proteins
pubmed
28487785
uniprot
proteins
pubmed
28604741
uniprot
proteins
pubmed
29343822
uniprot
proteins
pubmed
29581253
uniprot
proteins
pubmed
29788902
uniprot
proteins
pubmed
29925947
uniprot
proteins
pubmed
2994062
uniprot
proteins
pubmed
30028079
uniprot
proteins
pubmed
30315159
uniprot
proteins
pubmed
30451859
uniprot
proteins
pubmed
30526847
uniprot
proteins
pubmed
30626964
uniprot
proteins
pubmed
30733661
uniprot
proteins
pubmed
30785395
uniprot
proteins
pubmed
31388018
uniprot
proteins
pubmed
31911441
uniprot
proteins
pubmed
32170967
uniprot
proteins
pubmed
32503840
uniprot
proteins
pubmed
35005077
uniprot
proteins
pubmed
36173861
uniprot
proteins
pubmed
38609661
uniprot
proteins
pubmed
39321809
uniprot
proteins
pubmed
6322116
uniprot
proteins
pubmed
6842590
uniprot
proteins
sequence_length
375
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:17289661}. Nucleus {ECO:0000269|PubMed:11687588, ECO:0000269|PubMed:29925947}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000269|PubMed:17289661}.
uniprot
proteins