Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P60711 (ACTB_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin

Cleaved into the following chain:

  1. Actin, cytoplasmic 1, N-terminally processed
Gene names
Name:Actb
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Subunit structure

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 By similarity.

Subcellular location

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

Post-translational modification

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.

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.

Sequence similarities

Belongs to the actin family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Wasf1Q5BJU72EBI-349272,EBI-7269229

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin, cytoplasmic 1
PRO_0000367081
Initiator methionine11Removed; alternate By similarity
Chain2 – 375374Actin, cytoplasmic 1, N-terminally processed
PRO_0000000781

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed By similarity
Modified residue441Methionine (R)-sulfoxide By similarity
Modified residue471Methionine (R)-sulfoxide By similarity
Modified residue731Tele-methylhistidine By similarity
Modified residue841N6-methyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P60711 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 6AFD05CA94E360E2

FASTA37541,737
        10         20         30         40         50         60 
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 

        70         80         90        100        110        120 
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 

       130        140        150        160        170        180 
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 

       190        200        210        220        230        240 
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 

       250        260        270        280        290        300 
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 

       310        320        330        340        350        360 
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 

       370 
EYDESGPSIV HRKCF 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of the rat cytoplasmic beta-actin gene."
Nudel U., Zakut R., Shani M., Neuman S., Levy Z., Yaffe D.
Nucleic Acids Res. 11:1759-1771(1983) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary.
[3]Lubec G., Afjehi-Sadat L., Chen W.-Q., Kang S.U.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-39; 51-62; 85-113; 184-191; 197-206; 239-254; 292-312; 316-326; 329-335 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
V01217 Genomic DNA. Translation: CAA24528.1.
BC063166 mRNA. Translation: AAH63166.1.
RefSeqNP_112406.1. NM_031144.3.
UniGeneRn.94978.

3D structure databases

ProteinModelPortalP60711.
SMRP60711. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249680. 12 interactions.
IntActP60711. 17 interactions.
MINTMINT-132123.

PTM databases

PhosphoSiteP60711.

2D gel databases

World-2DPAGE0004:P60711.

Proteomic databases

PaxDbP60711.
PRIDEP60711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000042459; ENSRNOP00000044296; ENSRNOG00000034254.
GeneID81822.
KEGGrno:81822.
UCSCRGD:628837. rat.

Organism-specific databases

CTD60.
RGD628837. Actb.

Phylogenomic databases

eggNOGCOG5277.
GeneTreeENSGT00710000106384.
HOGENOMHOG000233340.
HOVERGENHBG003771.
InParanoidP60711.
KOK05692.
OMANGIADRM.
OrthoDBEOG72RMZ1.
PhylomeDBP60711.
TreeFamTF354237.

Enzyme and pathway databases

ReactomeREACT_195021. Developmental Biology.

Gene expression databases

ArrayExpressP60711.
GenevestigatorP60711.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio615747.

Entry information

Entry nameACTB_RAT
AccessionPrimary (citable) accession number: P60711
Secondary accession number(s): P02570 expand/collapse secondary AC list , P70514, P99021, Q11211, Q64316
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families