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P68133

- ACTS_HUMAN

UniProt

P68133 - ACTS_HUMAN

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Protein
Actin, alpha skeletal muscle
Gene
ACTA1, ACTA
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. ADP binding Source: UniProtKB
  2. ATP binding Source: UniProtKB
  3. myosin binding Source: UniProtKB
  4. protein binding Source: UniProtKB
  5. structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  1. cell growth Source: Ensembl
  2. muscle contraction Source: UniProtKB
  3. muscle filament sliding Source: Reactome
  4. response to extracellular stimulus Source: Ensembl
  5. response to lithium ion Source: Ensembl
  6. response to mechanical stimulus Source: Ensembl
  7. response to steroid hormone Source: Ensembl
  8. skeletal muscle fiber adaptation Source: Ensembl
  9. skeletal muscle fiber development Source: UniProtKB
  10. skeletal muscle thin filament assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_16969. Striated Muscle Contraction.
SignaLinkiP68133.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:129. ACTA1.

Subcellular locationi

GO - Cellular componenti

  1. actin cytoskeleton Source: UniProtKB
  2. actin filament Source: UniProtKB
  3. blood microparticle Source: UniProt
  4. cytosol Source: Reactome
  5. extracellular space Source: UniProt
  6. extracellular vesicular exosome Source: UniProtKB
  7. sarcomere Source: UniProtKB
  8. stress fiber Source: UniProtKB
  9. striated muscle thin filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Nemaline myopathy 3 (NEM3) [MIM:161800]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.10 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31D → Y in NEM3; some patients have core lesions on muscle biopsy. 1 Publication
VAR_062424
Natural varianti27 – 271D → N in NEM3.
VAR_062425
Natural varianti37 – 371V → L in NEM3. 1 Publication
VAR_062426
Natural varianti40 – 401P → L in NEM3. 1 Publication
VAR_062427
Natural varianti42 – 421H → Y in NEM3; severe. 2 Publications
VAR_015579
Natural varianti43 – 431Q → R in NEM3. 1 Publication
VAR_062428
Natural varianti44 – 441G → V in NEM3.
VAR_062429
Natural varianti45 – 451V → F in NEM3.
VAR_062430
Natural varianti66 – 661I → N in NEM3. 1 Publication
VAR_062431
Natural varianti68 – 681T → I in NEM3. 1 Publication
VAR_062432
Natural varianti74 – 741E → K in NEM3. 1 Publication
VAR_062433
Natural varianti75 – 751H → L in NEM3. 1 Publication
VAR_062434
Natural varianti75 – 751H → R in NEM3. 1 Publication
VAR_062435
Natural varianti77 – 771I → L in NEM3. 1 Publication
VAR_062436
Natural varianti79 – 791T → A in NEM3. 1 Publication
VAR_062437
Natural varianti85 – 851E → K in NEM3. 1 Publication
VAR_062438
Natural varianti96 – 961L → P in NEM3; autosomal recessive. 1 Publication
VAR_011681
Natural varianti116 – 1161A → T in NEM3.
VAR_062439
Natural varianti117 – 1171N → S in NEM3; autosomal dominant. 3 Publications
VAR_011682
Natural varianti117 – 1171N → T in NEM3.
VAR_062440
Natural varianti118 – 1181R → H in NEM3.
VAR_062441
Natural varianti134 – 1341M → V in NEM3; autosomal dominant. 2 Publications
VAR_013470
Natural varianti136 – 1361V → A in NEM3. 1 Publication
VAR_062442
Natural varianti138 – 1381I → M in NEM3; autosomal recessive. 2 Publications
VAR_011683
Natural varianti140 – 1401A → P in NEM3.
VAR_062443
Natural varianti142 – 1421L → P in NEM3.
VAR_062444
Natural varianti148 – 1481G → D in NEM3. 1 Publication
VAR_062445
Natural varianti150 – 1501T → N in NEM3.
VAR_062446
Natural varianti156 – 1561D → N in NEM3.
VAR_062447
Natural varianti165 – 1651V → 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 Publications
VAR_062448
Natural varianti172 – 1721A → G in NEM3.
VAR_062449
Natural varianti181 – 1811D → G in NEM3. 1 Publication
VAR_062450
Natural varianti181 – 1811D → H in NEM3.
VAR_062451
Natural varianti181 – 1811D → N in NEM3.
VAR_062452
Natural varianti184 – 1841G → D in NEM3; mild. 2 Publications
VAR_015580
Natural varianti185 – 1851R → C in NEM3; severe. 1 Publication
VAR_015582
Natural varianti185 – 1851R → D in NEM3; requires 2 nucleotide substitutions.
VAR_062453
Natural varianti185 – 1851R → G in NEM3; autosomal dominant; severe. 3 Publications
VAR_015581
Natural varianti185 – 1851R → S in NEM3.
VAR_062454
Natural varianti198 – 1981R → L in NEM3.
VAR_062455
Natural varianti199 – 1991G → S in NEM3. 1 Publication
VAR_062456
Natural varianti226 – 2261E → G in NEM3. 1 Publication
VAR_062457
Natural varianti226 – 2261E → Q in NEM3.
VAR_062458
Natural varianti227 – 2271N → V in NEM3; requires 2 nucleotide substitutions.
VAR_062459
Natural varianti229 – 2291M → I in NEM3. 1 Publication
VAR_062460
Natural varianti229 – 2291M → T in NEM3.
VAR_062461
Natural varianti229 – 2291M → V in NEM3. 1 Publication
VAR_062462
Natural varianti243 – 2431E → K in NEM3.
VAR_062463
Natural varianti248 – 2481Q → K in NEM3.
VAR_062464
Natural varianti248 – 2481Q → R in NEM3. 1 Publication
VAR_062465
Natural varianti253 – 2531G → D in NEM3. 1 Publication
VAR_062466
Natural varianti258 – 2581R → H in NEM3; severe. 1 Publication
VAR_015583
Natural varianti258 – 2581R → L in NEM3.
VAR_062467
Natural varianti261 – 2611E → V in NEM3; autosomal recessive. 1 Publication
VAR_011685
Natural varianti265 – 2651Q → L in NEM3; severe. 1 Publication
VAR_015584
Natural varianti270 – 2701G → C in NEM3; autosomal dominant. 3 Publications
VAR_011686
Natural varianti270 – 2701G → D in NEM3. 1 Publication
VAR_062468
Natural varianti270 – 2701G → R in NEM3.
VAR_062469
Natural varianti271 – 2711M → R in NEM3; autosomal dominant. 1 Publication
VAR_013471
Natural varianti274 – 2741A → E in NEM3.
VAR_062470
Natural varianti281 – 2811Y → H in NEM3. 1 Publication
VAR_062471
Natural varianti282 – 2821N → K in NEM3; severe. 2 Publications
VAR_015585
Natural varianti285 – 2851M → K in NEM3.
VAR_062472
Natural varianti288 – 2881D → G in NEM3; severe. 2 Publications
VAR_015586
Natural varianti336 – 3361E → A in NEM3. 1 Publication
VAR_062473
Natural varianti338 – 3381K → E in NEM3. 1 Publication
VAR_062474
Natural varianti338 – 3381K → I in NEM3.
VAR_062475
Natural varianti350 – 3501S → L in NEM3.
VAR_062476
Natural varianti359 – 3591I → L in NEM3; autosomal dominant; severe. 2 Publications
VAR_015587
Natural varianti372 – 3721V → F in NEM3; severe. 1 Publication
VAR_011687
Natural varianti374 – 3741R → S in NEM3.
VAR_062477
Natural varianti375 – 3751K → E in NEM3. 1 Publication
VAR_062478
Natural varianti375 – 3751K → Q in NEM3. 1 Publication
VAR_062479
Myopathy, actin, congenital, with excess of thin myofilaments (MPCETM) [MIM:161800]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti17 – 171G → R in MPCETM. 1 Publication
VAR_011680
Natural varianti165 – 1651V → L in MPCETM. 2 Publications
VAR_011684
Myopathy, congenital, with fiber-type disproportion (CFTD) [MIM:255310]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti223 – 2231L → P in CFTD. 1 Publication
VAR_032917
Natural varianti294 – 2941D → 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 Publications
VAR_032918
Natural varianti334 – 3341P → S in CFTD. 1 Publication
VAR_032919

Keywords - Diseasei

Disease mutation, Nemaline myopathy

Organism-specific databases

MIMi161800. phenotype.
255310. phenotype.
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form By similarity
PRO_0000000844
Chaini3 – 377375Actin, alpha skeletal muscle
PRO_0000000845Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate By similarity
Modified residuei46 – 461Methionine (R)-sulfoxide By similarity
Modified residuei49 – 491Methionine (R)-sulfoxide By similarity
Modified residuei63 – 631N6-malonyllysine1 Publication
Modified residuei75 – 751Tele-methylhistidine By similarity
Modified residuei86 – 861N6-methyllysine1 Publication

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.
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.

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

MaxQBiP68133.
PRIDEiP68133.

PTM databases

PhosphoSiteiP68133.

Expressioni

Gene expression databases

ArrayExpressiP68133.
BgeeiP68133.
CleanExiHS_ACTA1.
GenevestigatoriP68133.

Organism-specific databases

HPAiCAB000045.
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.2 Publications

Protein-protein interaction databases

BioGridi106573. 95 interactions.
IntActiP68133. 14 interactions.
MINTiMINT-135471.
STRINGi9606.ENSP00000355645.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
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:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T44X-ray2.00A8-377[»]
ProteinModelPortaliP68133.
SMRiP68133. Positions 6-377.

Miscellaneous databases

EvolutionaryTraceiP68133.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

Phylogenomic databases

HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68133.
KOiK10354.
OMAiILMETGM.
OrthoDBiEOG72RMZ1.
PhylomeDBiP68133.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin-related.
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

MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG    50
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP 100
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 150
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 200
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 250
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 300
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 350
LSTFQQMWIT KQEYDEAGPS IVHRKCF 377
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti3 – 31D → Y in NEM3; some patients have core lesions on muscle biopsy. 1 Publication
VAR_062424
Natural varianti17 – 171G → R in MPCETM. 1 Publication
VAR_011680
Natural varianti27 – 271D → N in NEM3.
VAR_062425
Natural varianti37 – 371V → L in NEM3. 1 Publication
VAR_062426
Natural varianti40 – 401P → L in NEM3. 1 Publication
VAR_062427
Natural varianti42 – 421H → Y in NEM3; severe. 2 Publications
VAR_015579
Natural varianti43 – 431Q → R in NEM3. 1 Publication
VAR_062428
Natural varianti44 – 441G → V in NEM3.
VAR_062429
Natural varianti45 – 451V → F in NEM3.
VAR_062430
Natural varianti66 – 661I → N in NEM3. 1 Publication
VAR_062431
Natural varianti68 – 681T → I in NEM3. 1 Publication
VAR_062432
Natural varianti74 – 741E → K in NEM3. 1 Publication
VAR_062433
Natural varianti75 – 751H → L in NEM3. 1 Publication
VAR_062434
Natural varianti75 – 751H → R in NEM3. 1 Publication
VAR_062435
Natural varianti77 – 771I → L in NEM3. 1 Publication
VAR_062436
Natural varianti79 – 791T → A in NEM3. 1 Publication
VAR_062437
Natural varianti85 – 851E → K in NEM3. 1 Publication
VAR_062438
Natural varianti96 – 961L → P in NEM3; autosomal recessive. 1 Publication
VAR_011681
Natural varianti116 – 1161A → T in NEM3.
VAR_062439
Natural varianti117 – 1171N → S in NEM3; autosomal dominant. 3 Publications
VAR_011682
Natural varianti117 – 1171N → T in NEM3.
VAR_062440
Natural varianti118 – 1181R → H in NEM3.
VAR_062441
Natural varianti134 – 1341M → V in NEM3; autosomal dominant. 2 Publications
VAR_013470
Natural varianti136 – 1361V → A in NEM3. 1 Publication
VAR_062442
Natural varianti138 – 1381I → M in NEM3; autosomal recessive. 2 Publications
VAR_011683
Natural varianti140 – 1401A → P in NEM3.
VAR_062443
Natural varianti142 – 1421L → P in NEM3.
VAR_062444
Natural varianti148 – 1481G → D in NEM3. 1 Publication
VAR_062445
Natural varianti150 – 1501T → N in NEM3.
VAR_062446
Natural varianti156 – 1561D → N in NEM3.
VAR_062447
Natural varianti165 – 1651V → L in MPCETM. 2 Publications
VAR_011684
Natural varianti165 – 1651V → 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 Publications
VAR_062448
Natural varianti172 – 1721A → G in NEM3.
VAR_062449
Natural varianti181 – 1811D → G in NEM3. 1 Publication
VAR_062450
Natural varianti181 – 1811D → H in NEM3.
VAR_062451
Natural varianti181 – 1811D → N in NEM3.
VAR_062452
Natural varianti184 – 1841G → D in NEM3; mild. 2 Publications
VAR_015580
Natural varianti185 – 1851R → C in NEM3; severe. 1 Publication
VAR_015582
Natural varianti185 – 1851R → D in NEM3; requires 2 nucleotide substitutions.
VAR_062453
Natural varianti185 – 1851R → G in NEM3; autosomal dominant; severe. 3 Publications
VAR_015581
Natural varianti185 – 1851R → S in NEM3.
VAR_062454
Natural varianti198 – 1981R → L in NEM3.
VAR_062455
Natural varianti199 – 1991G → S in NEM3. 1 Publication
VAR_062456
Natural varianti223 – 2231L → P in CFTD. 1 Publication
VAR_032917
Natural varianti226 – 2261E → G in NEM3. 1 Publication
VAR_062457
Natural varianti226 – 2261E → Q in NEM3.
VAR_062458
Natural varianti227 – 2271N → V in NEM3; requires 2 nucleotide substitutions.
VAR_062459
Natural varianti229 – 2291M → I in NEM3. 1 Publication
VAR_062460
Natural varianti229 – 2291M → T in NEM3.
VAR_062461
Natural varianti229 – 2291M → V in NEM3. 1 Publication
VAR_062462
Natural varianti243 – 2431E → K in NEM3.
VAR_062463
Natural varianti248 – 2481Q → K in NEM3.
VAR_062464
Natural varianti248 – 2481Q → R in NEM3. 1 Publication
VAR_062465
Natural varianti253 – 2531G → D in NEM3. 1 Publication
VAR_062466
Natural varianti258 – 2581R → H in NEM3; severe. 1 Publication
VAR_015583
Natural varianti258 – 2581R → L in NEM3.
VAR_062467
Natural varianti261 – 2611E → V in NEM3; autosomal recessive. 1 Publication
VAR_011685
Natural varianti265 – 2651Q → L in NEM3; severe. 1 Publication
VAR_015584
Natural varianti270 – 2701G → C in NEM3; autosomal dominant. 3 Publications
VAR_011686
Natural varianti270 – 2701G → D in NEM3. 1 Publication
VAR_062468
Natural varianti270 – 2701G → R in NEM3.
VAR_062469
Natural varianti271 – 2711M → R in NEM3; autosomal dominant. 1 Publication
VAR_013471
Natural varianti274 – 2741A → E in NEM3.
VAR_062470
Natural varianti281 – 2811Y → H in NEM3. 1 Publication
VAR_062471
Natural varianti282 – 2821N → K in NEM3; severe. 2 Publications
VAR_015585
Natural varianti285 – 2851M → K in NEM3.
VAR_062472
Natural varianti288 – 2881D → G in NEM3; severe. 2 Publications
VAR_015586
Natural varianti294 – 2941D → 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 Publications
VAR_032918
Natural varianti334 – 3341P → S in CFTD. 1 Publication
VAR_032919
Natural varianti336 – 3361E → A in NEM3. 1 Publication
VAR_062473
Natural varianti338 – 3381K → E in NEM3. 1 Publication
VAR_062474
Natural varianti338 – 3381K → I in NEM3.
VAR_062475
Natural varianti350 – 3501S → L in NEM3.
VAR_062476
Natural varianti359 – 3591I → L in NEM3; autosomal dominant; severe. 2 Publications
VAR_015587
Natural varianti372 – 3721V → F in NEM3; severe. 1 Publication
VAR_011687
Natural varianti374 – 3741R → S in NEM3.
VAR_062477
Natural varianti375 – 3751K → E in NEM3. 1 Publication
VAR_062478
Natural varianti375 – 3751K → Q in NEM3. 1 Publication
VAR_062479

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.3. human.

Polymorphism databases

DMDMi61218043.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS1578.1.
PIRi A31251. ATHU.
RefSeqi NP_001091.1. NM_001100.3.
UniGenei Hs.1288.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T44 X-ray 2.00 A 8-377 [» ]
ProteinModelPortali P68133.
SMRi P68133. Positions 6-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106573. 95 interactions.
IntActi P68133. 14 interactions.
MINTi MINT-135471.
STRINGi 9606.ENSP00000355645.

Chemistry

DrugBanki DB00003. Dornase Alfa.

PTM databases

PhosphoSitei P68133.

Polymorphism databases

DMDMi 61218043.

Proteomic databases

MaxQBi P68133.
PRIDEi P68133.

Protocols and materials databases

DNASUi 58.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000366684 ; ENSP00000355645 ; ENSG00000143632 .
GeneIDi 58.
KEGGi hsa:58.
UCSCi uc001htm.3. human.

Organism-specific databases

CTDi 58.
GeneCardsi GC01M229567.
GeneReviewsi ACTA1.
HGNCi HGNC:129. ACTA1.
HPAi CAB000045.
HPA041271.
MIMi 102610. gene.
161800. phenotype.
255310. phenotype.
neXtProti NX_P68133.
Orphaneti 171439. 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.
PharmGKBi PA24455.
GenAtlasi Search...

Phylogenomic databases

HOGENOMi HOG000233340.
HOVERGENi HBG003771.
InParanoidi P68133.
KOi K10354.
OMAi ILMETGM.
OrthoDBi EOG72RMZ1.
PhylomeDBi P68133.
TreeFami TF354237.

Enzyme and pathway databases

Reactomei REACT_16969. Striated Muscle Contraction.
SignaLinki P68133.

Miscellaneous databases

ChiTaRSi ACTA1. human.
EvolutionaryTracei P68133.
GeneWikii Actin,_alpha_1.
GenomeRNAii 58.
NextBioi 245.
PROi P68133.
SOURCEi Search...

Gene expression databases

ArrayExpressi P68133.
Bgeei P68133.
CleanExi HS_ACTA1.
Genevestigatori P68133.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view ]
PANTHERi PTHR11937. PTHR11937. 1 hit.
Pfami PF00022. Actin. 1 hit.
[Graphical view ]
PRINTSi PR00190. ACTIN.
SMARTi SM00268. ACTIN. 1 hit.
[Graphical view ]
PROSITEi PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of cDNA clones for human skeletal muscle alpha actin."
    Hanauer A., Levin M., Heilig R., Daegelen D., Kahn A., Mandel J.-L.
    Nucleic Acids Res. 11:3503-3516(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Skeletal muscle.
  2. "Nucleotide sequence and expression of the human skeletal alpha-actin gene: evolution of functional regulatory domains."
    Taylor A., Erba H.P., Muscat G.E.O., Kedes L.
    Genomics 3:323-336(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy."
    Nowak K.J., Wattanasirichaigoon D., Goebel H.H., Wilce M., Pelin K., Donner K., Jacob R.L., Hubner C., Oexle K., Anderson J.R., Verity C.M., North K.N.
    Nat. Genet. 23:208-212(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS NEM3 TYR-42; PRO-96; SER-117; VAL-134; ASP-184; CYS-185; HIS-258; VAL-261; LEU-265; LYS-282; GLY-288 AND PHE-372, VARIANTS MPCETM ARG-17 AND LEU-165.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  8. Cited for: INTERACTION WITH TTID.
  9. "The ubiquitin-specific protease USP25 interacts with three sarcomeric proteins."
    Bosch-Comas A., Lindsten K., Gonzalez-Duarte R., Masucci M.G., Marfany G.
    Cell. Mol. Life Sci. 63:723-734(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH USP25.
  10. Cited for: MALONYLATION AT LYS-63.
  11. Cited for: METHYLATION AT LYS-86, DEMETHYLATION BY ALKBH4.
  12. Cited for: VARIANTS NEM3 SER-117; MET-138; GLY-185; CYS-270 AND LEU-359.
  13. "Muscle disease caused by mutations in the skeletal muscle alpha-actin gene (ACTA1)."
    Sparrow J.C., Nowak K.J., Durling H.J., Beggs A.H., Wallgren-Pettersson C., Romero N., Nonaka I., Laing N.G.
    Neuromuscul. Disord. 13:519-531(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON VARIANTS.
  14. "Mild phenotype of nemaline myopathy with sleep hypoventilation due to a mutation in the skeletal muscle alpha-actin (ACTA1) gene."
    Jungbluth H., Sewry C.A., Brown S.C., Nowak K.J., Laing N.G., Wallgren-Pettersson C., Pelin K., Manzur A.Y., Mercuri E., Dubowitz V., Muntoni F.
    Neuromuscul. Disord. 11:35-40(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NEM3 VAL-134 AND ARG-271.
  15. Cited for: VARIANTS NEM3 LEU-37; LEU-40; TYR-42; ARG-43; ASN-66; LEU-75; ARG-75; LEU-77; ALA-79; LYS-85; ALA-136; ASP-148; GLY-181; ASP-184; GLY-185; SER-199; GLY-226; VAL-229; ILE-229; ARG-248; ASP-253; CYS-270; HIS-281; LYS-282; GLY-288 AND GLN-375.
  16. Cited for: VARIANTS CFTD PRO-223; VAL-294 AND SER-334.
  17. "Evidence for a dominant-negative effect in ACTA1 nemaline myopathy caused by abnormal folding, aggregation and altered polymerization of mutant actin isoforms."
    Ilkovski B., Nowak K.J., Domazetovska A., Maxwell A.L., Clement S., Davies K.E., Laing N.G., North K.N., Cooper S.T.
    Hum. Mol. Genet. 13:1727-1743(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NEM3 ILE-68; LYS-74; SER-117; MET-138; LEU-165; MET-165; GLY-185; CYS-270 AND LEU-359.
  18. Cited for: VARIANTS NEM3 TYR-3 AND ALA-336.
  19. "Follow-up of nemaline myopathy in two patients with novel mutations in the skeletal muscle alpha-actin gene (ACTA1)."
    Ohlsson M., Tajsharghi H., Darin N., Kyllerman M., Oldfors A.
    Neuromuscul. Disord. 14:471-475(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS NEM3 ASP-270 AND GLU-375.
  20. "Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: clinical and pathological variability within a kindred."
    Hutchinson D.O., Charlton A., Laing N.G., Ilkovski B., North K.N.
    Neuromuscul. Disord. 16:113-121(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NEM3 MET-165.
  21. Cited for: VARIANT NEM3 GLU-338.
  22. "The pathogenesis of ACTA1-related congenital fiber type disproportion."
    Clarke N.F., Ilkovski B., Cooper S., Valova V.A., Robinson P.J., Nonaka I., Feng J.-J., Marston S., North K.
    Ann. Neurol. 61:552-561(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CFTD VAL-294.
  23. Cited for: CHARACTERIZATION OF VARIANT NEM3 MET-165.

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: September 3, 2014
This is version 117 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

External Data

Dasty 3

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