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Protein

Actin, cytoplasmic 2

Gene

ACTG1

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.

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
  • 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.

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)5 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_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_032438332P → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894545Ensembl.1
Natural variantiVAR_032439370V → A in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation. 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

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.

Binary interactionsi

Show more details

GO - Molecular functioni

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

Protein-protein interaction databases

BioGridi106586. 143 interactors.
CORUMiP63261.
IntActiP63261. 103 interactors.
MINTiMINT-4998686.
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.
OMAiANGIHET.
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_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_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_032438332P → A in DFNA20. 1 PublicationCorresponds to variant dbSNP:rs104894545Ensembl.1
Natural variantiVAR_032439370V → A in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation. 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: September 27, 2017
This is version 160 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 17
    Human chromosome 17: 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