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Protein

Actin, cytoplasmic 2

Gene

ACTG1

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.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • profilin binding Source: UniProtKB
  • structural constituent of cytoskeleton Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-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-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-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-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
SignaLinkiP63261
SIGNORiP63261

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin
Cleaved into the following chain:
Gene namesi
Name:ACTG1
Synonyms:ACTG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

EuPathDBiHostDB:ENSG00000184009.9
HGNCiHGNC:144 ACTG1
MIMi102560 gene
neXtProtiNX_P63261

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

Deafness, autosomal dominant, 20 (DFNA20)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
See also OMIM:604717
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_03243489T → I in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs28999111Ensembl.1
Natural variantiVAR_032435118K → M in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894544Ensembl.1
Natural variantiVAR_067824118K → N in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs267606630Ensembl.1
Natural variantiVAR_067825122I → V in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs281875330Ensembl.1
Natural variantiVAR_079878187D → H in DFNA20. 1 Publication1
Natural variantiVAR_067826241E → K in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs267606631Ensembl.1
Natural variantiVAR_032436264P → L in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894546Ensembl.1
Natural variantiVAR_032437278T → I in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs28999112Ensembl.1
Natural variantiVAR_079879316E → K in DFNA20; unknown pathological significance. 1 Publication1
Natural variantiVAR_032438332P → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894545Ensembl.1
Natural variantiVAR_032439370V → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894547Ensembl.1
Baraitser-Winter syndrome 2 (BRWS2)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:614583
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067814120T → I in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875325Ensembl.1
Natural variantiVAR_067815135A → V in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs11549190Ensembl.1
Natural variantiVAR_067816155S → F in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875326Ensembl.1
Natural variantiVAR_067817203T → K in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875327Ensembl.1
Natural variantiVAR_067818254R → W in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875328Ensembl.1
Natural variantiVAR_067819256R → W in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875329Ensembl.1
Defects in ACTG1 has been found in a patient with isolated coloboma, a defect of the eye characterized by the absence of ocular structures due to abnormal morphogenesis of the optic cup and stalk, and the fusion of the fetal fissure (optic fissure). Isolated colobomas may be associated with an abnormally small eye (microphthalmia) or small cornea.1 Publication

Keywords - Diseasei

Deafness, Disease mutation, Mental retardation, Non-syndromic deafness

Organism-specific databases

DisGeNETi71
GeneReviewsiACTG1
MalaCardsiACTG1
MIMi604717 phenotype
614583 phenotype
OpenTargetsiENSG00000184009
Orphaneti90635 Autosomal dominant non-syndromic sensorineural deafness type DFNA
2995 Baraitser-Winter syndrome
PharmGKBiPA24468

Polymorphism and mutation databases

BioMutaiACTG1
DMDMi54036678

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003671001 – 375Actin, cytoplasmic 2Add BLAST375
Initiator methionineiRemoved; alternateCombined sources3 Publications
ChainiPRO_00000008312 – 375Actin, cytoplasmic 2, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partialCombined sources2 Publications1
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 VgrG1By similarity
Modified residuei73Tele-methylhistidine1 Publication1
Modified residuei84N6-methyllysine1 Publication1
Cross-linki270Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG1By similarity

Post-translational modificationi

The methylhistidine determined by Bienvenut et al is assumed to be the tele-methylhistidine isomer by similarity to the mouse ortholog.
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

Proteomic databases

EPDiP63261
MaxQBiP63261
PaxDbiP63261
PeptideAtlasiP63261
PRIDEiP63261
TopDownProteomicsiP63261

2D gel databases

DOSAC-COBS-2DPAGEiP63261
OGPiP63261
REPRODUCTION-2DPAGEiP63261
SWISS-2DPAGEiP63261

PTM databases

iPTMnetiP63261
PhosphoSitePlusiP63261
SwissPalmiP63261

Miscellaneous databases

PMAP-CutDBiP63261

Expressioni

Gene expression databases

BgeeiENSG00000184009
CleanExiHS_ACTB
HS_ACTG1
ExpressionAtlasiP63261 baseline and differential
GenevisibleiP63261 HS

Organism-specific databases

HPAiHPA041264
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. Interacts with TWF1, CAPZB, cofilin and profilin (PubMed:28493397).1 Publication

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • profilin binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi106586144 interactors.
CORUMiP63261
IntActiP63261 107 interactors.
MINTiP63261
STRINGi9606.ENSP00000331514

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5JLHelectron microscopy3.90A/B/C/D/E2-375[»]
ProteinModelPortaliP63261
SMRiP63261
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOVERGENiHBG003771
InParanoidiP63261
KOiK05692
OMAiMIGRECS
OrthoDBiEOG091G08LD
PhylomeDBiP63261
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.

P63261-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEEIAALVI 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):41,793
Last modified:July 21, 1986 - v1
Checksum:i54D08F986964EFD5
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti316E → K in AAA51580 (PubMed:3472224).Curated1
Sequence conflicti344S → F in AAA51580 (PubMed:3472224).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07984970P → L Found in a patient with isolated coloboma; decreased incorporation into F-actin; decreased interaction with cofilin; loss of interaction with TWF1, CAPZB and profilin. 1 Publication1
Natural variantiVAR_03243489T → I in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs28999111Ensembl.1
Natural variantiVAR_032435118K → M in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894544Ensembl.1
Natural variantiVAR_067824118K → N in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs267606630Ensembl.1
Natural variantiVAR_067814120T → I in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875325Ensembl.1
Natural variantiVAR_067825122I → V in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs281875330Ensembl.1
Natural variantiVAR_067815135A → V in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs11549190Ensembl.1
Natural variantiVAR_067816155S → F in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875326Ensembl.1
Natural variantiVAR_048186160T → I. Corresponds to variant dbSNP:rs11549206Ensembl.1
Natural variantiVAR_079878187D → H in DFNA20. 1 Publication1
Natural variantiVAR_067817203T → K in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875327Ensembl.1
Natural variantiVAR_067826241E → K in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs267606631Ensembl.1
Natural variantiVAR_067818254R → W in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875328Ensembl.1
Natural variantiVAR_067819256R → W in BRWS2. 1 PublicationCorresponds to variant dbSNP:rs281875329Ensembl.1
Natural variantiVAR_032436264P → L in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894546Ensembl.1
Natural variantiVAR_032437278T → I in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs28999112Ensembl.1
Natural variantiVAR_079879316E → K in DFNA20; unknown pathological significance. 1 Publication1
Natural variantiVAR_032438332P → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894545Ensembl.1
Natural variantiVAR_032439370V → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894547Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04098 mRNA Translation: CAA27723.1
M19283 Genomic DNA Translation: AAA51579.1
AK291937 mRNA Translation: BAF84626.1
BT019856 mRNA Translation: AAV38659.1
BC000292 mRNA Translation: AAH00292.1
BC001920 mRNA Translation: AAH01920.1
BC007442 mRNA Translation: AAH07442.1
BC009848 mRNA Translation: AAH09848.1
BC010999 mRNA Translation: AAH10999.1
BC012050 mRNA Translation: AAH12050.1
BC015005 mRNA Translation: AAH15005.1
BC015695 mRNA Translation: AAH15695.1
BC015779 mRNA Translation: AAH15779.1
BC018774 mRNA Translation: AAH18774.1
BC053572 mRNA Translation: AAH53572.1
M16247 mRNA Translation: AAA51580.1
CCDSiCCDS11782.1
PIRiA28098 ATHUG
JC5818
RefSeqiNP_001186883.1, NM_001199954.1
NP_001605.1, NM_001614.3
UniGeneiHs.514581
Hs.713764

Genome annotation databases

EnsembliENST00000331925; ENSP00000331514; ENSG00000184009
ENST00000573283; ENSP00000458435; ENSG00000184009
ENST00000575087; ENSP00000459124; ENSG00000184009
ENST00000575842; ENSP00000458162; ENSG00000184009
ENST00000576544; ENSP00000461672; ENSG00000184009
ENST00000615544; ENSP00000477968; ENSG00000184009
GeneIDi71
KEGGihsa:71
UCSCiuc002kak.3 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiACTG_HUMAN
AccessioniPrimary (citable) accession number: P63261
Secondary accession number(s): A8K7C2
, P02571, P14104, P99022, Q5U032, Q96E67
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: April 25, 2018
This is version 166 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