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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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.

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.

Caution

Was originally thought to be part of the MLL5-L complex, at least composed of KMT2E, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT (PubMed:19377461). However, the corresponding article has been retracted (PubMed:24336203).2 Publications

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • protein kinase binding Source: ARUK-UCL
  • structural constituent of cytoskeleton Source: UniProtKB
  • structural constituent of postsynaptic actin cytoskeleton Source: SynGO
  • Tat protein binding Source: BHF-UCL

GO - Biological processi

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148 Translocation of GLUT4 to the plasma membrane
R-HSA-190873 Gap junction degradation
R-HSA-196025 Formation of annular gap junctions
R-HSA-2029482 Regulation of actin dynamics for phagocytic cup formation
R-HSA-3214847 HATs acetylate histones
R-HSA-389957 Prefoldin mediated transfer of substrate to CCT/TriC
R-HSA-390450 Folding of actin by CCT/TriC
R-HSA-3928662 EPHB-mediated forward signaling
R-HSA-3928665 EPH-ephrin mediated repulsion of cells
R-HSA-418990 Adherens junctions interactions
R-HSA-437239 Recycling pathway of L1
R-HSA-4420097 VEGFA-VEGFR2 Pathway
R-HSA-445095 Interaction between L1 and Ankyrins
R-HSA-446353 Cell-extracellular matrix interactions
R-HSA-5250924 B-WICH complex positively regulates rRNA expression
R-HSA-5626467 RHO GTPases activate IQGAPs
R-HSA-5663213 RHO GTPases Activate WASPs and WAVEs
R-HSA-5663220 RHO GTPases Activate Formins
R-HSA-5674135 MAP2K and MAPK activation
R-HSA-5689603 UCH proteinases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-6802946 Signaling by moderate kinase activity BRAF mutants
R-HSA-6802948 Signaling by high-kinase activity BRAF mutants
R-HSA-6802949 Signaling by RAS mutants
R-HSA-6802952 Signaling by BRAF and RAF fusions
R-HSA-6802955 Paradoxical activation of RAF signaling by kinase inactive BRAF
R-HSA-8856828 Clathrin-mediated endocytosis
R-HSA-983231 Factors involved in megakaryocyte development and platelet production
SignaLinkiP60709

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

EuPathDBiHostDB:ENSG00000075624.13
HGNCiHGNC:132 ACTB
MIMi102630 gene
neXtProtiNX_P60709

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Dystonia, juvenile-onset (DJO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.
See also OMIM:607371
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003EnsemblClinVar.1
Baraitser-Winter syndrome 1 (BRWS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:243310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331EnsemblClinVar.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332EnsemblClinVar.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333EnsemblClinVar.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334EnsemblClinVar.1

Keywords - Diseasei

Deafness, Disease mutation, Dystonia, Mental retardation

Organism-specific databases

DisGeNETi60
MalaCardsiACTB
MIMi243310 phenotype
607371 phenotype
OpenTargetsiENSG00000075624
Orphaneti2995 Baraitser-Winter syndrome
79107 Developmental malformations - deafness - dystonia
PharmGKBiPA24457

Chemistry databases

ChEMBLiCHEMBL2062353

Polymorphism and mutation databases

BioMutaiACTB
DMDMi46397333

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003670731 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateCombined sources2 Publications
ChainiPRO_00000007712 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedCombined sources1 Publication1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Cross-linki50Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG11 Publication
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysine1 Publication1
Cross-linki270Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG11 Publication

Post-translational modificationi

ISGylated.1 Publication
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 (By similarity).By similarity
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.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-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).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Oxidation, Ubl conjugation

Proteomic databases

EPDiP60709
PaxDbiP60709
PeptideAtlasiP60709
PRIDEiP60709
ProteomicsDBi57224
TopDownProteomicsiP60709

2D gel databases

DOSAC-COBS-2DPAGEiP60709
REPRODUCTION-2DPAGEiP60709
SWISS-2DPAGEiP60709
UCD-2DPAGEiP60709

PTM databases

CarbonylDBiP60709
iPTMnetiP60709
PhosphoSitePlusiP60709
SwissPalmiP60709

Expressioni

Gene expression databases

BgeeiENSG00000075624
CleanExiHS_ACTB
ExpressionAtlasiP60709 baseline and differential
GenevisibleiP60709 HS

Organism-specific databases

HPAiCAB002621
HPA041264
HPA041271

Interactioni

Subunit structurei

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). 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 IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57 SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts with TBC1D21 (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (PubMed:11687588).By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • protein kinase binding Source: ARUK-UCL
  • Tat protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106575, 314 interactors
CORUMiP60709
DIPiDIP-29686N
IntActiP60709, 216 interactors
MINTiP60709
STRINGi9606.ENSP00000349960

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
6ANUelectron microscopy7.00A/B/C/D/E/F1-375[»]
ProteinModelPortaliP60709
SMRiP60709
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60709

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOVERGENiHBG003771
InParanoidiP60709
KOiK05692
OMAiMERGYPF
OrthoDBiEOG091G08LD
PhylomeDBiP60709
TreeFamiTF354237

Family and domain databases

InterProiView protein in InterPro
IPR004000 Actin
IPR020902 Actin/actin-like_CS
IPR004001 Actin_CS
PANTHERiPTHR11937 PTHR11937, 1 hit
PfamiView protein in Pfam
PF00022 Actin, 1 hit
PRINTSiPR00190 ACTIN
SMARTiView protein in SMART
SM00268 ACTIN, 1 hit
PROSITEiView protein in PROSITE
PS00406 ACTINS_1, 1 hit
PS00432 ACTINS_2, 1 hit
PS01132 ACTINS_ACT_LIKE, 1 hit

Sequencei

Sequence statusi: Complete.

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

P60709-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,737
Last modified:April 1, 1988 - v1
Checksum:i6AFD05CA94E360E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97A → P in AAH16045 (PubMed:15489334).Curated1
Sequence conflicti116R → L in AAH12854 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331EnsemblClinVar.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332EnsemblClinVar.1
Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003EnsemblClinVar.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333EnsemblClinVar.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334EnsemblClinVar.1
Natural variantiVAR_048185243P → L. Corresponds to variant dbSNP:rs11546899Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA Translation: CAA25099.1
M10277 Genomic DNA Translation: AAA51567.1
X63432 mRNA Translation: CAA45026.1
AY582799 Genomic DNA Translation: AAS79319.1
AC006483 Genomic DNA Translation: AAP22343.1
BC001301 mRNA Translation: AAH01301.1
BC002409 mRNA Translation: AAH02409.1
BC004251 mRNA Translation: AAH04251.1
BC008633 mRNA Translation: AAH08633.1
BC012854 mRNA Translation: AAH12854.1
BC013380 mRNA Translation: AAH13380.1
BC014861 mRNA Translation: AAH14861.1
BC016045 mRNA Translation: AAH16045.1
V00478 mRNA Translation: CAA23745.1
CCDSiCCDS5341.1
PIRiA25168 ATHUB
RefSeqiNP_001092.1, NM_001101.3
UniGeneiHs.520640

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624
ENST00000493945; ENSP00000494269; ENSG00000075624
ENST00000646664; ENSP00000494750; ENSG00000075624
GeneIDi60
KEGGihsa:60

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiACTB_HUMAN
AccessioniPrimary (citable) accession number: P60709
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: June 20, 2018
This is version 172 of the entry and version 1 of the sequence. See 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

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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