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Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Mus musculus (Mouse)
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

GO - Biological processi

  • negative regulation of cyclin-dependent protein kinase activity Source: ARUK-UCL
  • negative regulation of protein binding Source: ARUK-UCL
  • postsynaptic actin cytoskeleton organization Source: MGI

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-190873 Gap junction degradation
R-MMU-196025 Formation of annular gap junctions
R-MMU-2029482 Regulation of actin dynamics for phagocytic cup formation
R-MMU-3928662 EPHB-mediated forward signaling
R-MMU-418990 Adherens junctions interactions
R-MMU-437239 Recycling pathway of L1
R-MMU-4420097 VEGFA-VEGFR2 Pathway
R-MMU-445095 Interaction between L1 and Ankyrins
R-MMU-446353 Cell-extracellular matrix interactions
R-MMU-5626467 RHO GTPases activate IQGAPs
R-MMU-5663213 RHO GTPases Activate WASPs and WAVEs
R-MMU-5663220 RHO GTPases Activate Formins
R-MMU-5674135 MAP2K and MAPK activation
R-MMU-5689603 UCH proteinases
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-8856828 Clathrin-mediated endocytosis

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:Actb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:87904 Actb

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003670761 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternate1 Publication
ChainiPRO_00000007752 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed1 Publication1
Modified residuei44Methionine (R)-sulfoxide1 Publication1
Modified residuei47Methionine (R)-sulfoxide1 Publication1
Modified residuei73Tele-methylhistidine1 Publication1
Modified residuei84N6-methyllysineBy similarity1

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.1 Publication
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

EPDiP60710
MaxQBiP60710
PaxDbiP60710
PeptideAtlasiP60710
PRIDEiP60710
TopDownProteomicsiP60710

2D gel databases

COMPLUYEAST-2DPAGEiP60710
REPRODUCTION-2DPAGEiP60710
SWISS-2DPAGEiP99041
UCD-2DPAGEiP60710

PTM databases

CarbonylDBiP60710
iPTMnetiP60710
PhosphoSitePlusiP60710
SwissPalmiP60710

Expressioni

Gene expression databases

BgeeiENSMUSG00000029580
CleanExiMM_ACTB
ExpressionAtlasiP60710 baseline and differential
GenevisibleiP60710 MM

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 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, MARCB1/BAF47, 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. Component of a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By similarity). Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (PubMed:12522145). Interacts with TBC1D21 (PubMed:21128978). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes (By similarity).By similarity2 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

BioGridi197944, 214 interactors
CORUMiP60710
DIPiDIP-31574N
IntActiP60710, 230 interactors
MINTiP60710
STRINGi10090.ENSMUSP00000098066

Structurei

3D structure databases

ProteinModelPortaliP60710
SMRiP60710
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOVERGENiHBG003771
InParanoidiP60710
KOiK05692
OMAiMERGYPF
OrthoDBiEOG091G08LD
PhylomeDBiP60710
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.

P60710-1 [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 conflicti38P → S in CAA27396 (PubMed:3084797).Curated1
Sequence conflicti38P → S in AAA37144 (PubMed:3084797).Curated1
Sequence conflicti52S → F in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti80D → E in BAE35572 (PubMed:16141072).Curated1
Sequence conflicti109P → T in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti156G → R in BAE39957 (PubMed:16141072).Curated1
Sequence conflicti178L → V in BAE39957 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X03672 mRNA Translation: CAA27307.1
AK088691 mRNA Translation: BAC40507.1
AK145191 mRNA Translation: BAE26283.1
AK145196 mRNA Translation: BAE26288.1
AK145308 mRNA Translation: BAE26359.1
AK150711 mRNA Translation: BAE29789.1
AK150879 mRNA Translation: BAE29928.1
AK151010 mRNA Translation: BAE30031.1
AK151136 mRNA Translation: BAE30144.1
AK151145 mRNA Translation: BAE30152.1
AK151159 mRNA Translation: BAE30164.1
AK151166 mRNA Translation: BAE30169.1
AK151190 mRNA Translation: BAE30187.1
AK151202 mRNA Translation: BAE30199.1
AK151226 mRNA Translation: BAE30218.1
AK151277 mRNA Translation: BAE30264.1
AK151350 mRNA Translation: BAE30326.1
AK151398 mRNA Translation: BAE30366.1
AK151995 mRNA Translation: BAE30859.1
AK151999 mRNA Translation: BAE30863.1
AK152615 mRNA Translation: BAE31359.1
AK152651 mRNA Translation: BAE31388.1
AK152844 mRNA Translation: BAE31537.1
AK159759 mRNA Translation: BAE35350.1
AK159834 mRNA Translation: BAE35412.1
AK160029 mRNA Translation: BAE35572.1
AK166349 mRNA Translation: BAE38723.1
AK166498 mRNA Translation: BAE38810.1
AK167117 mRNA Translation: BAE39265.1
AK167960 mRNA Translation: BAE39957.1
X03765 mRNA Translation: CAA27396.1
M12481 mRNA Translation: AAA37144.1
CCDSiCCDS19833.1
PIRiA39104 ATMSB
RefSeqiNP_031419.1, NM_007393.5
UniGeneiMm.328431
Mm.391967
Mm.469717

Genome annotation databases

EnsembliENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580
GeneIDi11461
KEGGimmu:11461
UCSCiuc009ajk.1 mouse

Similar proteinsi

Entry informationi

Entry nameiACTB_MOUSE
AccessioniPrimary (citable) accession number: P60710
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 25, 2018
This is version 151 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health