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Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

GO - Molecular functioni

  • ADP binding Source: UniProtKB
  • ATP binding Source: UniProtKB
  • myosin binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143632-MONOMER.
ReactomeiR-HSA-390522. Striated Muscle Contraction.
SignaLinkiP68133.
SIGNORiP68133.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene namesi
Name:ACTA1
Synonyms:ACTA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:129. ACTA1.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • actin filament Source: UniProtKB
  • blood microparticle Source: UniProtKB
  • cell body Source: AgBase
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • filopodium Source: AgBase
  • lamellipodium Source: AgBase
  • sarcomere Source: UniProtKB
  • stress fiber Source: UniProtKB
  • striated muscle thin filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Nemaline myopathy 3 (NEM3)12 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of nemaline myopathy. Nemaline myopathies are muscular disorders characterized by muscle weakness of varying severity and onset, and abnormal thread-like or rod-shaped structures in muscle fibers on histologic examination.
See also OMIM:161800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0624243D → Y in NEM3; some patients have core lesions on muscle biopsy. 1 PublicationCorresponds to variant rs121909527dbSNPEnsembl.1
Natural variantiVAR_06242527D → N in NEM3. 1
Natural variantiVAR_06242637V → L in NEM3. 1 Publication1
Natural variantiVAR_06242740P → L in NEM3. 1 Publication1
Natural variantiVAR_01557942H → Y in NEM3; severe. 2 Publications1
Natural variantiVAR_06242843Q → R in NEM3. 1 Publication1
Natural variantiVAR_06242944G → V in NEM3. 1
Natural variantiVAR_06243045V → F in NEM3. Corresponds to variant rs398123562dbSNPEnsembl.1
Natural variantiVAR_06243166I → N in NEM3. 1 Publication1
Natural variantiVAR_06243268T → I in NEM3. 1 Publication1
Natural variantiVAR_06243374E → K in NEM3. 1 Publication1
Natural variantiVAR_06243475H → L in NEM3. 1 Publication1
Natural variantiVAR_06243575H → R in NEM3. 1 Publication1
Natural variantiVAR_06243677I → L in NEM3. 1 Publication1
Natural variantiVAR_06243779T → A in NEM3. 1 Publication1
Natural variantiVAR_06243885E → K in NEM3. 1 Publication1
Natural variantiVAR_01168196L → P in NEM3; autosomal recessive. 1 PublicationCorresponds to variant rs121909519dbSNPEnsembl.1
Natural variantiVAR_062439116A → T in NEM3. 1
Natural variantiVAR_011682117N → S in NEM3; autosomal dominant. 3 PublicationsCorresponds to variant rs121909520dbSNPEnsembl.1
Natural variantiVAR_062440117N → T in NEM3. 1
Natural variantiVAR_062441118R → H in NEM3. 1
Natural variantiVAR_013470134M → V in NEM3; autosomal dominant. 2 Publications1
Natural variantiVAR_062442136V → A in NEM3. 1 Publication1
Natural variantiVAR_011683138I → M in NEM3; autosomal recessive. 2 PublicationsCorresponds to variant rs121909526dbSNPEnsembl.1
Natural variantiVAR_062443140A → P in NEM3. 1
Natural variantiVAR_062444142L → P in NEM3. 1
Natural variantiVAR_062445148G → D in NEM3. 1 Publication1
Natural variantiVAR_062446150T → N in NEM3. 1
Natural variantiVAR_062447156D → N in NEM3. 1
Natural variantiVAR_062448165V → M in NEM3; results in sequestration of sarcomeric and Z line proteins into intranuclear aggregates; there is some evidence of muscle regeneration suggesting a compensatory effect. 3 PublicationsCorresponds to variant rs121909522dbSNPEnsembl.1
Natural variantiVAR_062449172A → G in NEM3. 1
Natural variantiVAR_062450181D → G in NEM3. 1 Publication1
Natural variantiVAR_062451181D → H in NEM3. 1
Natural variantiVAR_062452181D → N in NEM3. 1
Natural variantiVAR_015580184G → D in NEM3; mild. 2 Publications1
Natural variantiVAR_015582185R → C in NEM3; severe. 1 Publication1
Natural variantiVAR_062453185R → D in NEM3; requires 2 nucleotide substitutions. 1
Natural variantiVAR_015581185R → G in NEM3; autosomal dominant; severe. 3 Publications1
Natural variantiVAR_062454185R → S in NEM3. 1
Natural variantiVAR_062455198R → L in NEM3. 1
Natural variantiVAR_062456199G → S in NEM3. 1 Publication1
Natural variantiVAR_062457226E → G in NEM3. 1 Publication1
Natural variantiVAR_062458226E → Q in NEM3. 1
Natural variantiVAR_062459227N → V in NEM3; requires 2 nucleotide substitutions. 1
Natural variantiVAR_062460229M → I in NEM3. 1 Publication1
Natural variantiVAR_062461229M → T in NEM3. 1
Natural variantiVAR_062462229M → V in NEM3. 1 PublicationCorresponds to variant rs794727714dbSNPEnsembl.1
Natural variantiVAR_062463243E → K in NEM3. Corresponds to variant rs367543051dbSNPEnsembl.1
Natural variantiVAR_062464248Q → K in NEM3. 1
Natural variantiVAR_062465248Q → R in NEM3. 1 Publication1
Natural variantiVAR_062466253G → D in NEM3. 1 Publication1
Natural variantiVAR_015583258R → H in NEM3; severe. 1 Publication1
Natural variantiVAR_062467258R → L in NEM3. 1
Natural variantiVAR_011685261E → V in NEM3; autosomal recessive. 1 PublicationCorresponds to variant rs121909523dbSNPEnsembl.1
Natural variantiVAR_015584265Q → L in NEM3; severe. 1 Publication1
Natural variantiVAR_011686270G → C in NEM3; autosomal dominant. 3 PublicationsCorresponds to variant rs121909525dbSNPEnsembl.1
Natural variantiVAR_062468270G → D in NEM3. 1 Publication1
Natural variantiVAR_062469270G → R in NEM3. 1
Natural variantiVAR_013471271M → R in NEM3; autosomal dominant. 1 Publication1
Natural variantiVAR_062470274A → E in NEM3. 1
Natural variantiVAR_062471281Y → H in NEM3. 1 Publication1
Natural variantiVAR_015585282N → K in NEM3; severe. 2 Publications1
Natural variantiVAR_062472285M → K in NEM3. 1
Natural variantiVAR_015586288D → G in NEM3; severe; formation of rod-like structure. 3 Publications1
Natural variantiVAR_076427328K → N in NEM3; no effect on actin structure; higher sensitivty to calcium. 1 PublicationCorresponds to variant rs398122936dbSNPEnsembl.1
Natural variantiVAR_062473336E → A in NEM3. 1 PublicationCorresponds to variant rs121909528dbSNPEnsembl.1
Natural variantiVAR_062474338K → E in NEM3. 1 Publication1
Natural variantiVAR_062475338K → I in NEM3. 1
Natural variantiVAR_062476350S → L in NEM3. 1
Natural variantiVAR_076428358W → C in NEM3; found in a patient with a rare combination of NEM3 and dilated cardiomyopathy. 1 PublicationCorresponds to variant rs587777354dbSNPEnsembl.1
Natural variantiVAR_015587359I → L in NEM3; autosomal dominant; severe. 2 PublicationsCorresponds to variant rs121909524dbSNPEnsembl.1
Natural variantiVAR_011687372V → F in NEM3; severe. 1 Publication1
Natural variantiVAR_062477374R → S in NEM3. 1
Natural variantiVAR_062478375K → E in NEM3. 1 Publication1
Natural variantiVAR_062479375K → Q in NEM3. 1 Publication1
Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA congenital muscular disorder characterized at histological level by areas of sarcoplasm devoid of normal myofibrils and mitochondria, and replaced with dense masses of thin filaments. Central cores, rods, ragged red fibers, and necrosis are absent.
See also OMIM:161800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01168017G → R in MPCETM. 1 PublicationCorresponds to variant rs121909521dbSNPEnsembl.1
Natural variantiVAR_011684165V → L in MPCETM. 2 PublicationsCorresponds to variant rs121909522dbSNPEnsembl.1
Myopathy, congenital, with fiber-type disproportion (CFTD)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA genetically heterogeneous disorder in which there is relative hypotrophy of type 1 muscle fibers compared to type 2 fibers on skeletal muscle biopsy. However, these findings are not specific and can be found in many different myopathic and neuropathic conditions.
See also OMIM:255310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_032917223L → P in CFTD. 1 PublicationCorresponds to variant rs121909530dbSNPEnsembl.1
Natural variantiVAR_032918294D → V in CFTD; results in decreased motility due to abnormal interactions between actin and tropomyosin with tropomyosin stabilized in the 'off' position; the mutant protein incorporates into actin filaments and does not result in increased actin aggregation or disruption of the sarcomere. 2 PublicationsCorresponds to variant rs121909529dbSNPEnsembl.1
Natural variantiVAR_032919334P → S in CFTD. 1 PublicationCorresponds to variant rs121909531dbSNPEnsembl.1
Myopathy, scapulohumeroperoneal (SHPM)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant muscular disorder characterized by progressive muscle weakness with initial scapulo-humeral-peroneal and distal distribution. Over time, muscle weakness progresses to proximal muscle groups. Clinical characteristics include scapular winging, mild lower facial weakness, foot drop due to foot eversion and dorsiflexion weakness, and selective muscle atrophy. Age at onset and disease progression are variable.
See also OMIM:616852
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_076426197E → D in SHPM; no effect on cytoskeleton structure. 1 Publication1

Keywords - Diseasei

Disease mutation, Nemaline myopathy

Organism-specific databases

DisGeNETi58.
MalaCardsiACTA1.
MIMi161800. phenotype.
255310. phenotype.
616852. phenotype.
OpenTargetsiENSG00000143632.
Orphaneti171439. Childhood-onset nemaline myopathy.
2020. Congenital fiber-type disproportion myopathy.
98904. Congenital myopathy with excess of thin filaments.
171433. Intermediate nemaline myopathy.
171430. Severe congenital nemaline myopathy.
171436. Typical nemaline myopathy.
PharmGKBiPA24455.

Polymorphism and mutation databases

BioMutaiACTA1.
DMDMi61218043.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000008441 – 2Removed in mature formBy similarity2
ChainiPRO_00000008453 – 377Actin, alpha skeletal muscleAdd BLAST375

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei3N-acetylaspartateBy similarity1
Modified residuei46Methionine (R)-sulfoxideBy similarity1
Modified residuei49Methionine (R)-sulfoxideBy similarity1
Cross-linki52Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-272); by Vibrio toxins RtxA and VgrG1By similarity
Modified residuei63N6-malonyllysine1 Publication1
Modified residuei86N6-methyllysine1 Publication1
Cross-linki272Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-52); by Vibrio toxins RtxA and VgrG1By similarity

Post-translational modificationi

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 promote actin repolymerization (By similarity).By similarity
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.1 Publication
(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).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Oxidation

Proteomic databases

EPDiP68133.
MaxQBiP68133.
PaxDbiP68133.
PeptideAtlasiP68133.
PRIDEiP68133.

PTM databases

iPTMnetiP68133.
PhosphoSitePlusiP68133.
SwissPalmiP68133.

Expressioni

Gene expression databases

BgeeiENSG00000143632.
CleanExiHS_ACTA1.
ExpressionAtlasiP68133. baseline and differential.
GenevisibleiP68133. HS.

Organism-specific databases

HPAiCAB000045.
HPA041264.
HPA041271.

Interactioni

Subunit structurei

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. Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (By similarity). Interacts with TTID. Interacts (via its C-terminus) with USP25; the interaction occurs for all USP25 isoforms but is strongest for isoform USP25m in muscle differentiating cells.By similarity2 Publications

GO - Molecular functioni

  • myosin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106573. 126 interactors.
IntActiP68133. 16 interactors.
MINTiMINT-135471.
STRINGi9606.ENSP00000355645.

Structurei

Secondary structure

1377
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 134
Beta strandi19 – 213
Beta strandi30 – 334
Turni59 – 613
Helixi81 – 9313
Helixi100 – 1023
Beta strandi105 – 1095
Helixi115 – 12713
Beta strandi132 – 1387
Helixi139 – 1468
Beta strandi154 – 1574
Beta strandi162 – 1654
Helixi174 – 1763
Beta strandi178 – 1803
Helixi186 – 19712
Helixi205 – 21814
Helixi225 – 23410
Beta strandi240 – 2434
Beta strandi249 – 2524
Helixi255 – 26410
Helixi266 – 2683
Helixi277 – 2848
Turni289 – 2913
Helixi292 – 2976
Beta strandi299 – 3024
Helixi312 – 3209
Turni335 – 3384
Turni340 – 3423
Helixi347 – 3504
Helixi354 – 3574
Beta strandi358 – 3603
Helixi361 – 3666
Helixi371 – 3755

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T44X-ray2.00A8-377[»]
ProteinModelPortaliP68133.
SMRiP68133.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68133.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68133.
KOiK10354.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.
PhylomeDBiP68133.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P68133-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP
110 120 130 140 150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT
160 170 180 190 200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI
260 270 280 290 300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
310 320 330 340 350
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS
360 370
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0624243D → Y in NEM3; some patients have core lesions on muscle biopsy. 1 PublicationCorresponds to variant rs121909527dbSNPEnsembl.1
Natural variantiVAR_01168017G → R in MPCETM. 1 PublicationCorresponds to variant rs121909521dbSNPEnsembl.1
Natural variantiVAR_06242527D → N in NEM3. 1
Natural variantiVAR_06242637V → L in NEM3. 1 Publication1
Natural variantiVAR_06242740P → L in NEM3. 1 Publication1
Natural variantiVAR_01557942H → Y in NEM3; severe. 2 Publications1
Natural variantiVAR_06242843Q → R in NEM3. 1 Publication1
Natural variantiVAR_06242944G → V in NEM3. 1
Natural variantiVAR_06243045V → F in NEM3. Corresponds to variant rs398123562dbSNPEnsembl.1
Natural variantiVAR_06243166I → N in NEM3. 1 Publication1
Natural variantiVAR_06243268T → I in NEM3. 1 Publication1
Natural variantiVAR_06243374E → K in NEM3. 1 Publication1
Natural variantiVAR_06243475H → L in NEM3. 1 Publication1
Natural variantiVAR_06243575H → R in NEM3. 1 Publication1
Natural variantiVAR_06243677I → L in NEM3. 1 Publication1
Natural variantiVAR_06243779T → A in NEM3. 1 Publication1
Natural variantiVAR_06243885E → K in NEM3. 1 Publication1
Natural variantiVAR_01168196L → P in NEM3; autosomal recessive. 1 PublicationCorresponds to variant rs121909519dbSNPEnsembl.1
Natural variantiVAR_062439116A → T in NEM3. 1
Natural variantiVAR_011682117N → S in NEM3; autosomal dominant. 3 PublicationsCorresponds to variant rs121909520dbSNPEnsembl.1
Natural variantiVAR_062440117N → T in NEM3. 1
Natural variantiVAR_062441118R → H in NEM3. 1
Natural variantiVAR_013470134M → V in NEM3; autosomal dominant. 2 Publications1
Natural variantiVAR_062442136V → A in NEM3. 1 Publication1
Natural variantiVAR_011683138I → M in NEM3; autosomal recessive. 2 PublicationsCorresponds to variant rs121909526dbSNPEnsembl.1
Natural variantiVAR_062443140A → P in NEM3. 1
Natural variantiVAR_062444142L → P in NEM3. 1
Natural variantiVAR_062445148G → D in NEM3. 1 Publication1
Natural variantiVAR_062446150T → N in NEM3. 1
Natural variantiVAR_062447156D → N in NEM3. 1
Natural variantiVAR_011684165V → L in MPCETM. 2 PublicationsCorresponds to variant rs121909522dbSNPEnsembl.1
Natural variantiVAR_062448165V → M in NEM3; results in sequestration of sarcomeric and Z line proteins into intranuclear aggregates; there is some evidence of muscle regeneration suggesting a compensatory effect. 3 PublicationsCorresponds to variant rs121909522dbSNPEnsembl.1
Natural variantiVAR_062449172A → G in NEM3. 1
Natural variantiVAR_062450181D → G in NEM3. 1 Publication1
Natural variantiVAR_062451181D → H in NEM3. 1
Natural variantiVAR_062452181D → N in NEM3. 1
Natural variantiVAR_015580184G → D in NEM3; mild. 2 Publications1
Natural variantiVAR_015582185R → C in NEM3; severe. 1 Publication1
Natural variantiVAR_062453185R → D in NEM3; requires 2 nucleotide substitutions. 1
Natural variantiVAR_015581185R → G in NEM3; autosomal dominant; severe. 3 Publications1
Natural variantiVAR_062454185R → S in NEM3. 1
Natural variantiVAR_076426197E → D in SHPM; no effect on cytoskeleton structure. 1 Publication1
Natural variantiVAR_062455198R → L in NEM3. 1
Natural variantiVAR_062456199G → S in NEM3. 1 Publication1
Natural variantiVAR_032917223L → P in CFTD. 1 PublicationCorresponds to variant rs121909530dbSNPEnsembl.1
Natural variantiVAR_062457226E → G in NEM3. 1 Publication1
Natural variantiVAR_062458226E → Q in NEM3. 1
Natural variantiVAR_062459227N → V in NEM3; requires 2 nucleotide substitutions. 1
Natural variantiVAR_062460229M → I in NEM3. 1 Publication1
Natural variantiVAR_062461229M → T in NEM3. 1
Natural variantiVAR_062462229M → V in NEM3. 1 PublicationCorresponds to variant rs794727714dbSNPEnsembl.1
Natural variantiVAR_062463243E → K in NEM3. Corresponds to variant rs367543051dbSNPEnsembl.1
Natural variantiVAR_062464248Q → K in NEM3. 1
Natural variantiVAR_062465248Q → R in NEM3. 1 Publication1
Natural variantiVAR_062466253G → D in NEM3. 1 Publication1
Natural variantiVAR_015583258R → H in NEM3; severe. 1 Publication1
Natural variantiVAR_062467258R → L in NEM3. 1
Natural variantiVAR_011685261E → V in NEM3; autosomal recessive. 1 PublicationCorresponds to variant rs121909523dbSNPEnsembl.1
Natural variantiVAR_015584265Q → L in NEM3; severe. 1 Publication1
Natural variantiVAR_011686270G → C in NEM3; autosomal dominant. 3 PublicationsCorresponds to variant rs121909525dbSNPEnsembl.1
Natural variantiVAR_062468270G → D in NEM3. 1 Publication1
Natural variantiVAR_062469270G → R in NEM3. 1
Natural variantiVAR_013471271M → R in NEM3; autosomal dominant. 1 Publication1
Natural variantiVAR_062470274A → E in NEM3. 1
Natural variantiVAR_062471281Y → H in NEM3. 1 Publication1
Natural variantiVAR_015585282N → K in NEM3; severe. 2 Publications1
Natural variantiVAR_062472285M → K in NEM3. 1
Natural variantiVAR_015586288D → G in NEM3; severe; formation of rod-like structure. 3 Publications1
Natural variantiVAR_032918294D → V in CFTD; results in decreased motility due to abnormal interactions between actin and tropomyosin with tropomyosin stabilized in the 'off' position; the mutant protein incorporates into actin filaments and does not result in increased actin aggregation or disruption of the sarcomere. 2 PublicationsCorresponds to variant rs121909529dbSNPEnsembl.1
Natural variantiVAR_076427328K → N in NEM3; no effect on actin structure; higher sensitivty to calcium. 1 PublicationCorresponds to variant rs398122936dbSNPEnsembl.1
Natural variantiVAR_032919334P → S in CFTD. 1 PublicationCorresponds to variant rs121909531dbSNPEnsembl.1
Natural variantiVAR_062473336E → A in NEM3. 1 PublicationCorresponds to variant rs121909528dbSNPEnsembl.1
Natural variantiVAR_062474338K → E in NEM3. 1 Publication1
Natural variantiVAR_062475338K → I in NEM3. 1
Natural variantiVAR_062476350S → L in NEM3. 1
Natural variantiVAR_076428358W → C in NEM3; found in a patient with a rare combination of NEM3 and dilated cardiomyopathy. 1 PublicationCorresponds to variant rs587777354dbSNPEnsembl.1
Natural variantiVAR_015587359I → L in NEM3; autosomal dominant; severe. 2 PublicationsCorresponds to variant rs121909524dbSNPEnsembl.1
Natural variantiVAR_011687372V → F in NEM3; severe. 1 Publication1
Natural variantiVAR_062477374R → S in NEM3. 1
Natural variantiVAR_062478375K → E in NEM3. 1 Publication1
Natural variantiVAR_062479375K → Q in NEM3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00068 mRNA. Translation: AAB59376.1.
M20543 Genomic DNA. Translation: AAA60296.1.
AF182035 Genomic DNA. Translation: AAF02694.1.
CR536516 mRNA. Translation: CAG38754.1.
CR541796 mRNA. Translation: CAG46595.1.
AL160004 Genomic DNA. Translation: CAI19050.1.
CH471098 Genomic DNA. Translation: EAW69898.1.
BC012597 mRNA. Translation: AAH12597.1.
CCDSiCCDS1578.1.
PIRiA31251. ATHU.
RefSeqiNP_001091.1. NM_001100.3.
UniGeneiHs.1288.

Genome annotation databases

EnsembliENST00000366684; ENSP00000355645; ENSG00000143632.
GeneIDi58.
KEGGihsa:58.
UCSCiuc001htm.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J00068 mRNA. Translation: AAB59376.1.
M20543 Genomic DNA. Translation: AAA60296.1.
AF182035 Genomic DNA. Translation: AAF02694.1.
CR536516 mRNA. Translation: CAG38754.1.
CR541796 mRNA. Translation: CAG46595.1.
AL160004 Genomic DNA. Translation: CAI19050.1.
CH471098 Genomic DNA. Translation: EAW69898.1.
BC012597 mRNA. Translation: AAH12597.1.
CCDSiCCDS1578.1.
PIRiA31251. ATHU.
RefSeqiNP_001091.1. NM_001100.3.
UniGeneiHs.1288.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T44X-ray2.00A8-377[»]
ProteinModelPortaliP68133.
SMRiP68133.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106573. 126 interactors.
IntActiP68133. 16 interactors.
MINTiMINT-135471.
STRINGi9606.ENSP00000355645.

PTM databases

iPTMnetiP68133.
PhosphoSitePlusiP68133.
SwissPalmiP68133.

Polymorphism and mutation databases

BioMutaiACTA1.
DMDMi61218043.

Proteomic databases

EPDiP68133.
MaxQBiP68133.
PaxDbiP68133.
PeptideAtlasiP68133.
PRIDEiP68133.

Protocols and materials databases

DNASUi58.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366684; ENSP00000355645; ENSG00000143632.
GeneIDi58.
KEGGihsa:58.
UCSCiuc001htm.4. human.

Organism-specific databases

CTDi58.
DisGeNETi58.
GeneCardsiACTA1.
GeneReviewsiACTA1.
HGNCiHGNC:129. ACTA1.
HPAiCAB000045.
HPA041264.
HPA041271.
MalaCardsiACTA1.
MIMi102610. gene.
161800. phenotype.
255310. phenotype.
616852. phenotype.
neXtProtiNX_P68133.
OpenTargetsiENSG00000143632.
Orphaneti171439. Childhood-onset nemaline myopathy.
2020. Congenital fiber-type disproportion myopathy.
98904. Congenital myopathy with excess of thin filaments.
171433. Intermediate nemaline myopathy.
171430. Severe congenital nemaline myopathy.
171436. Typical nemaline myopathy.
PharmGKBiPA24455.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68133.
KOiK10354.
OMAiIXMESAG.
OrthoDBiEOG091G08LD.
PhylomeDBiP68133.
TreeFamiTF354237.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000143632-MONOMER.
ReactomeiR-HSA-390522. Striated Muscle Contraction.
SignaLinkiP68133.
SIGNORiP68133.

Miscellaneous databases

ChiTaRSiACTA1. human.
EvolutionaryTraceiP68133.
GeneWikiiActin,_alpha_1.
GenomeRNAii58.
PROiP68133.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143632.
CleanExiHS_ACTA1.
ExpressionAtlasiP68133. baseline and differential.
GenevisibleiP68133. HS.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACTS_HUMAN
AccessioniPrimary (citable) accession number: P68133
Secondary accession number(s): P02568, P99020, Q5T8M9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 2, 2016
This is version 141 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.