ACTA2
entrez
59
canonical
uniprot
P62736
canonical
ensembl
ENSG00000107796
resolver
ensp
ENSP00000224784
resolver
ensp
ENSP00000396730
resolver
ensp
ENSP00000398239
resolver
ensp
ENSP00000518893
resolver
ensp
ENSP00000518895
resolver
ensp
ENSP00000518896
resolver
ensp
ENSP00000518897
resolver
ensp
ENSP00000518898
resolver
ensp
ENSP00000573434
resolver
ensp
ENSP00000573435
resolver
ensp
ENSP00000573436
resolver
ensp
ENSP00000616996
resolver
ensp
ENSP00000616997
resolver
ensp
ENSP00000616998
resolver
ensp
ENSP00000616999
resolver
ensp
ENSP00000617001
resolver
ensp
ENSP00000617002
resolver
ensp
ENSP00000617004
resolver
ensp
ENSP00000617006
resolver
ensp
ENSP00000617007
resolver
ensp
ENSP00000617008
resolver
ensp
ENSP00000617009
resolver
ensp
ENSP00000617010
resolver
ensp
ENSP00000617011
resolver
ensp
ENSP00000617012
resolver
ensp
ENSP00000794599
resolver
enst
ENST00000224784
resolver
enst
ENST00000415557
resolver
enst
ENST00000458159
resolver
enst
ENST00000713597
resolver
enst
ENST00000713599
resolver
enst
ENST00000713600
resolver
enst
ENST00000713601
resolver
enst
ENST00000713602
resolver
enst
ENST00000903375
resolver
enst
ENST00000903377
resolver
enst
ENST00000946937
resolver
enst
ENST00000946938
resolver
enst
ENST00000946939
resolver
enst
ENST00000946940
resolver
enst
ENST00000946942
resolver
enst
ENST00000946943
resolver
enst
ENST00000946945
resolver
enst
ENST00000946947
resolver
enst
ENST00000946948
resolver
enst
ENST00000946949
resolver
enst
ENST00000946950
resolver
enst
ENST00000946951
resolver
enst
ENST00000946952
resolver
enst
ENST00000946953
resolver
genesymbol
ACTA2
resolver
genesymbol_syn
ACTSA
resolver
genesymbol_syn
ACTVS
resolver
hgnc
HGNC:130
resolver
uniprot
A0AAQ5BGG7
resolver
uniprot
A0AAQ5BGI6
resolver
uniprot
B2R8A4
resolver
uniprot
P03996
resolver
uniprot
P04108
resolver
uniprot
Q6FI19
resolver
uniprot_entry
A0AAQ5BGG7_HUMAN
resolver
uniprot_entry
A0AAQ5BGI6_HUMAN
resolver
uniprot_entry
ACTA_HUMAN
resolver
uniprot_sec
B2R8A4
resolver
uniprot_sec
P03996
resolver
uniprot_sec
P04108
resolver
uniprot_sec
Q6FI19
resolver
amino_acid_sequence
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
uniprot
proteins
disease_involvement
DISEASE: Note=ACTA2 mutations predispose patients to a variety of diffuse and diverse vascular diseases, premature onset coronary artery disease (CAD), premature ischemic strokes and Moyamoya disease. {ECO:0000269|PubMed:19409525}.; DISEASE: Aortic aneurysm, familial thoracic 6 (AAT6) [MIM:611788]: A disease characterized by permanent dilation of the thoracic aorta usually due to degenerative changes in the aortic wall. It is primarily associated with a characteristic histologic appearance known as 'medial necrosis' or 'Erdheim cystic medial necrosis' in which there is degeneration and fragmentation of elastic fibers, loss of smooth muscle cells, and an accumulation of basophilic ground substance. {ECO:0000269|PubMed:17994018, ECO:0000269|PubMed:19409525, ECO:0000269|PubMed:19639654}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Moyamoya disease 5 (MYMY5) [MIM:614042]: A progressive cerebral angiopathy characterized by bilateral intracranial carotid artery stenosis and telangiectatic vessels in the region of the basal ganglia. The abnormal vessels resemble a 'puff of smoke' (moyamoya) on cerebral angiogram. Affected individuals can develop transient ischemic attacks and/or cerebral infarction, and rupture of the collateral vessels can cause intracranial hemorrhage. Hemiplegia of sudden onset and epileptic seizures constitute the prevailing presentation in childhood, while subarachnoid bleeding occurs more frequently in adults. {ECO:0000269|PubMed:20970362}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Smooth muscle dysfunction syndrome (SMDYS) [MIM:613834]: An autosomal dominant syndrome characterized by dysfunction of smooth muscle cells throughout the body, leading to aortic and cerebrovascular disease, fixed dilated pupils, hypotonic bladder, malrotation, and hypoperistalsis of the gut and pulmonary hypertension. {ECO:0000269|PubMed:20734336, ECO:0000269|PubMed:27481187}. 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: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
uniprot
proteins
mass_dalton
42009
uniprot
proteins
post_translational_modification
PTM: Oxidation of Met-46 and Met-49 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 promotes actin repolymerization. {ECO:0000250|UniProtKB:P62737}.; PTM: Monomethylation at Lys-86 (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. {ECO:0000250|UniProtKB:P68032}.; PTM: Methylated at His-75 by SETD3. {ECO:0000269|PubMed:30626964}.; PTM: [Actin, aortic smooth muscle, intermediate form]: N-terminal cleavage of acetylated cysteine of intermediate muscle actin by ACTMAP. {ECO:0000250|UniProtKB:P62737}.; 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-52 of one monomer and Glu-272 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
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16548883
uniprot
proteins
pubmed
17994018
uniprot
proteins
pubmed
19015515
uniprot
proteins
pubmed
19409525
uniprot
proteins
pubmed
19639654
uniprot
proteins
pubmed
20734336
uniprot
proteins
pubmed
20970362
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
2295650
uniprot
proteins
pubmed
2612915
uniprot
proteins
pubmed
26228148
uniprot
proteins
pubmed
2701935
uniprot
proteins
pubmed
27481187
uniprot
proteins
pubmed
30626964
uniprot
proteins
pubmed
6330528
uniprot
proteins
sequence_length
377
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
uniprot
proteins