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P60710 (ACTB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

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, 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. 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. Ref.7

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.

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

CxadrP977926EBI-353957,EBI-7429264

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin, cytoplasmic 1
PRO_0000367076
Initiator methionine11Removed; alternate Ref.3
Chain2 – 375374Actin, cytoplasmic 1, N-terminally processed
PRO_0000000775

Amino acid modifications

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

Experimental info

Sequence conflict381P → S in CAA27396. Ref.5
Sequence conflict381P → S in AAA37144. Ref.5
Sequence conflict521S → F in BAE39957. Ref.2
Sequence conflict801D → E in BAE35572. Ref.2
Sequence conflict1091P → T in BAE39957. Ref.2
Sequence conflict1561G → R in BAE39957. Ref.2
Sequence conflict1781L → V in BAE39957. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P60710 [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]"Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA."
Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S.
Nucleic Acids Res. 14:2829-2829(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: BALB/c, C57BL/6J and NOD.
Tissue: Bone marrow, Mammary gland and Thymus.
[3]"Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin."
Vandekerckhove J., Weber K.
Eur. J. Biochem. 90:451-462(1978) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-375.
Tissue: Thymus.
[4]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 19-39; 51-61; 85-113; 148-177; 184-191; 197-206; 216-254; 257-284; 291-326 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[5]"Comparison of three actin-coding sequences in the mouse; evolutionary relationships between the actin genes of warm-blooded vertebrates."
Alonso S., Minty A., Bourlet Y., Buckingham M.
J. Mol. Evol. 23:11-22(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-375.
[6]Vilbois F.
Submitted (OCT-1998) to UniProtKB
Cited for: ACETYLATION.
Tissue: Muscle.
[7]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[8]"MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: OXIDATION AT MET-44 AND MET-47, DEOXIDATION AT MET-44 AND MET-47.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRATMSB. A39104.
RefSeqNP_031419.1. NM_007393.3.
UniGeneMm.328431.
Mm.391967.
Mm.469717.

3D structure databases

ProteinModelPortalP60710.
SMRP60710. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid197944. 25 interactions.
DIPDIP-31574N.
IntActP60710. 40 interactions.
MINTMINT-1202772.

PTM databases

PhosphoSiteP60710.

2D gel databases

COMPLUYEAST-2DPAGEP60710.
REPRODUCTION-2DPAGEP60710.
SWISS-2DPAGEP99041.
UCD-2DPAGEP60710.

Proteomic databases

PRIDEP60710.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580.
GeneID11461.
KEGGmmu:11461.
UCSCuc009ajk.1. mouse.

Organism-specific databases

CTD60.
MGIMGI:87904. Actb.

Phylogenomic databases

GeneTreeENSGT00710000106384.
HOVERGENHBG003771.
InParanoidP60710.
KOK05692.
OMANGIADRM.
OrthoDBEOG72RMZ1.
PhylomeDBP60710.
TreeFamTF354237.

Enzyme and pathway databases

ReactomeREACT_147847. Translocation of Glut4 to the Plasma Membrane.

Gene expression databases

ArrayExpressP60710.
BgeeP60710.
CleanExMM_ACTB.
GenevestigatorP60710.

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

ChiTaRSACTB. mouse.
NextBio278784.
PROP60710.
SOURCESearch...

Entry information

Entry nameACTB_MOUSE
AccessionPrimary (citable) accession number: P60710
Secondary accession number(s): P02570 expand/collapse secondary AC list , P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 109 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

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot