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Reviewed, UniProtKB/Swiss-Prot P60711 (ACTB_RAT)

Last modified November 24, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Actin, cytoplasmic 1
Alternative name(s):
    Beta-actin
Cleaved into the following chain:
    1- Recommended name:
            Actin, cytoplasmic 1, N-terminally processed
Gene names
Name: Actb
OrganismRattus norvegicus (Rat)
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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and 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 MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD By similarity.

Subcellular location

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

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processaxonogenesis

Inferred from direct assay. Source: RGD

   Cellular componentaxon

Inferred from direct assay. Source: RGD

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein kinase binding

Inferred from physical interaction. Source: RGD

Complete GO annotation...

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; in Actin, cytoplasmic 1; alternate By similarity
Modified residue21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed By similarity
Modified residue531Phosphotyrosine By similarity
Modified residue731Tele-methylhistidine By similarity
Modified residue911Phosphotyrosine By similarity
Modified residue1661Phosphotyrosine By similarity
Modified residue1691Phosphotyrosine By similarity
Modified residue1981Phosphotyrosine By similarity
Modified residue2181Phosphotyrosine By similarity
Modified residue2941Phosphotyrosine By similarity
Modified residue3181Phosphothreonine By similarity

Sequences

Sequence LengthMass (Da)Tools
P60711-1 [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: 6300777] [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: 15489334] [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, MASS SPECTROMETRY.
Strain: Sprague-Dawley.
Tissue: Brain, Hippocampus and Spinal cord.
+Additional computationally mapped references.

Cross-references

Sequence databases

V01217 Genomic DNA. Translation: CAA24528.1.
BC063166 mRNA. Translation: AAH63166.1.
IPIIPI00189819.
RefSeqNP_112406.1.
UniGeneRn.94978

3D structure databases

SMRP60711. Positions 4-371.
ModBaseSearch...

Protein-protein interaction databases

IntActP60711. 9 interactions.
STRINGP60711.

PTM databases

PhosphoSiteP60711.

Proteomic databases

PRIDEP60711.

Genome annotation databases

EnsemblENSRNOT00000042459; ENSRNOP00000044296; ENSRNOG00000034254; Rattus norvegicus. [Genome view]
GeneID81822.
KEGGrno:81822.
UCSCNM_031144. rat.

Organism-specific databases

CTD81822.
RGD628837. Actb.

Phylogenomic databases

HOVERGENP60711.
OMALETANTS

Gene expression databases

ArrayExpressP60711.
GenevestigatorP60711.
GermOnlineENSRNOG00000034254. Rattus norvegicus.

Family and domain databases

InterProIPR004000. Actin-like.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. Actin_like. 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 Resources

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: November 24, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents