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Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.By similarity

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.By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • protein kinase binding Source: RGD

GO - Biological processi

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-190873 Gap junction degradation
R-RNO-196025 Formation of annular gap junctions
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-418990 Adherens junctions interactions
R-RNO-437239 Recycling pathway of L1
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-445095 Interaction between L1 and Ankyrins
R-RNO-446353 Cell-extracellular matrix interactions
R-RNO-5250924 B-WICH complex positively regulates rRNA expression
R-RNO-5626467 RHO GTPases activate IQGAPs
R-RNO-5663213 RHO GTPases Activate WASPs and WAVEs
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-5674135 MAP2K and MAPK activation
R-RNO-5689603 UCH proteinases
R-RNO-5696394 DNA Damage Recognition in GG-NER
R-RNO-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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi628837 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, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000007811 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00003670812 – 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 processedBy similarity1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysineBy similarity1

Post-translational modificationi

ISGylated.By similarity
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
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
Actin, cytoplasmic 1, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected.By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

PaxDbiP60711
PRIDEiP60711

2D gel databases

World-2DPAGEi0004:P60711

PTM databases

CarbonylDBiP60711
iPTMnetiP60711
PhosphoSitePlusiP60711

Expressioni

Gene expression databases

BgeeiENSRNOG00000034254 Expressed in 9 organ(s), highest expression level in lung
ExpressionAtlasiP60711 baseline and differential
GenevisibleiP60711 RN

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, 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 (By similarity). Interacts with TBC1D21. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes. Interacts with FAM107A (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
Wasf1Q5BJU72EBI-349272,EBI-7269229

GO - Molecular functioni

Protein-protein interaction databases

BioGridi249680, 12 interactors
CORUMiP60711
IntActiP60711, 18 interactors
MINTiP60711
STRINGi10116.ENSRNOP00000044296

Structurei

3D structure databases

ProteinModelPortaliP60711
SMRiP60711
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOGENOMiHOG000233340
HOVERGENiHBG003771
InParanoidiP60711
KOiK05692
PhylomeDBiP60711
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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P60711-1 [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

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0G2K3K2A0A0G2K3K2_RAT
Actin, cytoplasmic 1
Actb
378Annotation score:

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01217 Genomic DNA Translation: CAA24528.1
BC063166 mRNA Translation: AAH63166.1
RefSeqiNP_112406.1, NM_031144.3
UniGeneiRn.94978

Genome annotation databases

EnsembliENSRNOT00000042459; ENSRNOP00000044296; ENSRNOG00000034254
GeneIDi81822
KEGGirno:81822
UCSCiRGD:628837 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V01217 Genomic DNA Translation: CAA24528.1
BC063166 mRNA Translation: AAH63166.1
RefSeqiNP_112406.1, NM_031144.3
UniGeneiRn.94978

3D structure databases

ProteinModelPortaliP60711
SMRiP60711
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi249680, 12 interactors
CORUMiP60711
IntActiP60711, 18 interactors
MINTiP60711
STRINGi10116.ENSRNOP00000044296

PTM databases

CarbonylDBiP60711
iPTMnetiP60711
PhosphoSitePlusiP60711

2D gel databases

World-2DPAGEi0004:P60711

Proteomic databases

PaxDbiP60711
PRIDEiP60711

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000042459; ENSRNOP00000044296; ENSRNOG00000034254
GeneIDi81822
KEGGirno:81822
UCSCiRGD:628837 rat

Organism-specific databases

CTDi60
RGDi628837 Actb

Phylogenomic databases

eggNOGiKOG0676 Eukaryota
COG5277 LUCA
GeneTreeiENSGT00760000118957
HOGENOMiHOG000233340
HOVERGENiHBG003771
InParanoidiP60711
KOiK05692
PhylomeDBiP60711
TreeFamiTF354237

Enzyme and pathway databases

ReactomeiR-RNO-190873 Gap junction degradation
R-RNO-196025 Formation of annular gap junctions
R-RNO-2029482 Regulation of actin dynamics for phagocytic cup formation
R-RNO-3928662 EPHB-mediated forward signaling
R-RNO-418990 Adherens junctions interactions
R-RNO-437239 Recycling pathway of L1
R-RNO-4420097 VEGFA-VEGFR2 Pathway
R-RNO-445095 Interaction between L1 and Ankyrins
R-RNO-446353 Cell-extracellular matrix interactions
R-RNO-5250924 B-WICH complex positively regulates rRNA expression
R-RNO-5626467 RHO GTPases activate IQGAPs
R-RNO-5663213 RHO GTPases Activate WASPs and WAVEs
R-RNO-5663220 RHO GTPases Activate Formins
R-RNO-5674135 MAP2K and MAPK activation
R-RNO-5689603 UCH proteinases
R-RNO-5696394 DNA Damage Recognition in GG-NER
R-RNO-8856828 Clathrin-mediated endocytosis

Miscellaneous databases

PROiPR:P60711

Gene expression databases

BgeeiENSRNOG00000034254 Expressed in 9 organ(s), highest expression level in lung
ExpressionAtlasiP60711 baseline and differential
GenevisibleiP60711 RN

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
ProtoNetiSearch...

Entry informationi

Entry nameiACTB_RAT
AccessioniPrimary (citable) accession number: P60711
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: October 10, 2018
This is version 142 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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Main funding by: National Institutes of Health

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