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Protein

Actin, cytoplasmic 1

Gene

Actb

Organism
Rattus norvegicus (Rat)
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.

GO - Molecular functioni

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

GO - Biological processi

  • axonogenesis Source: RGD
  • cellular response to electrical stimulus Source: RGD
  • retina development in camera-type eye Source: RGD
Complete GO annotation...

Keywords - Ligandi

ATP-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-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 12

Organism-specific databases

RGDi628837. Actb.

Subcellular locationi

  • Cytoplasmcytoskeleton

  • Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

  • axon Source: RGD
  • cytoskeleton Source: AgBase
  • cytosol Source: Reactome
  • dense body Source: AgBase
  • focal adhesion Source: AgBase
  • plasma membrane Source: AgBase
  • postsynaptic density Source: RGD
  • protein complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003670811 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00000007812 – 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).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).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

PaxDbiP60711.
PRIDEiP60711.

2D gel databases

World-2DPAGE0004:P60711.

PTM databases

iPTMnetiP60711.
PhosphoSitePlusiP60711.

Expressioni

Gene expression databases

BgeeiENSRNOG00000034254.
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. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with TBC1D21.By similarity

Binary interactionsi

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

GO - Molecular functioni

  • protein kinase binding Source: RGD

Protein-protein interaction databases

BioGridi249680. 11 interactors.
IntActiP60711. 18 interactors.
MINTiMINT-132123.
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

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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

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.

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. 11 interactors.
IntActiP60711. 18 interactors.
MINTiMINT-132123.
STRINGi10116.ENSRNOP00000044296.

PTM databases

iPTMnetiP60711.
PhosphoSitePlusiP60711.

2D gel databases

World-2DPAGE0004: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-5689603. UCH proteinases.
R-RNO-5696394. DNA Damage Recognition in GG-NER.
R-RNO-8856828. Clathrin-mediated endocytosis.

Miscellaneous databases

PROiP60711.

Gene expression databases

BgeeiENSRNOG00000034254.
ExpressionAtlasiP60711. baseline and differential.
GenevisibleiP60711. RN.

Family and domain databases

InterProiIPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiACTB_RAT
AccessioniPrimary (citable) accession number: P60711
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 2, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.