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P60710

- ACTB_MOUSE

UniProt

P60710 - ACTB_MOUSE

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Protein
Actin, cytoplasmic 1
Gene
Actb
Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_209040. Gap junction degradation.
REACT_220352. Formation of annular gap junctions.
REACT_226917. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:Actb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 5

Organism-specific databases

MGIiMGI:87904. Actb.

Subcellular locationi

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

GO - Cellular componenti

  1. MLL5-L complex Source: Ensembl
  2. NuA4 histone acetyltransferase complex Source: Ensembl
  3. cortical cytoskeleton Source: MGI
  4. cytosol Source: MGI
  5. extracellular vesicular exosome Source: Ensembl
  6. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1
PRO_0000367076Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processed
PRO_0000000775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity
Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed1 Publication
Modified residuei44 – 441Methionine (R)-sulfoxide
Modified residuei47 – 471Methionine (R)-sulfoxide
Modified residuei73 – 731Tele-methylhistidine1 Publication
Modified residuei84 – 841N6-methyllysine By similarity

Post-translational modificationi

ISGylated.1 Publication
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.

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

MaxQBiP60710.
PRIDEiP60710.

2D gel databases

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

PTM databases

PhosphoSiteiP60710.

Expressioni

Gene expression databases

ArrayExpressiP60710.
BgeeiP60710.
CleanExiMM_ACTB.
GenevestigatoriP60710.

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, 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.

Binary interactionsi

WithEntry#Exp.IntActNotes
CxadrP977926EBI-353957,EBI-7429264

Protein-protein interaction databases

BioGridi197944. 26 interactions.
DIPiDIP-31574N.
IntActiP60710. 41 interactions.
MINTiMINT-1202772.

Structurei

3D structure databases

ProteinModelPortaliP60710.
SMRiP60710. Positions 6-375.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

Phylogenomic databases

GeneTreeiENSGT00710000106384.
HOVERGENiHBG003771.
InParanoidiP60710.
KOiK05692.
OMAiSIVHLKC.
OrthoDBiEOG72RMZ1.
PhylomeDBiP60710.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin-related.
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.

P60710-1 [UniParc]FASTAAdd to Basket

« Hide

MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK    50
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE 100
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG 150
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF 200
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI 250
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 300
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS 350
TFQQMWISKQ EYDESGPSIV HRKCF 375
Length:375
Mass (Da):41,737
Last modified:April 1, 1988 - v1
Checksum:i6AFD05CA94E360E2
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381P → S in CAA27396. 1 Publication
Sequence conflicti38 – 381P → S in AAA37144. 1 Publication
Sequence conflicti52 – 521S → F in BAE39957. 1 Publication
Sequence conflicti80 – 801D → E in BAE35572. 1 Publication
Sequence conflicti109 – 1091P → T in BAE39957. 1 Publication
Sequence conflicti156 – 1561G → R in BAE39957. 1 Publication
Sequence conflicti178 – 1781L → V in BAE39957. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS19833.1.
PIRiA39104. ATMSB.
RefSeqiNP_031419.1. NM_007393.3.
UniGeneiMm.328431.
Mm.391967.
Mm.469717.

Genome annotation databases

EnsembliENSMUST00000100497; ENSMUSP00000098066; ENSMUSG00000029580.
GeneIDi11461.
KEGGimmu:11461.
UCSCiuc009ajk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS19833.1.
PIRi A39104. ATMSB.
RefSeqi NP_031419.1. NM_007393.3.
UniGenei Mm.328431.
Mm.391967.
Mm.469717.

3D structure databases

ProteinModelPortali P60710.
SMRi P60710. Positions 6-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197944. 26 interactions.
DIPi DIP-31574N.
IntActi P60710. 41 interactions.
MINTi MINT-1202772.

PTM databases

PhosphoSitei P60710.

2D gel databases

COMPLUYEAST-2DPAGE P60710.
REPRODUCTION-2DPAGE P60710.
SWISS-2DPAGE P99041.
UCD-2DPAGE P60710.

Proteomic databases

MaxQBi P60710.
PRIDEi P60710.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000100497 ; ENSMUSP00000098066 ; ENSMUSG00000029580 .
GeneIDi 11461.
KEGGi mmu:11461.
UCSCi uc009ajk.1. mouse.

Organism-specific databases

CTDi 60.
MGIi MGI:87904. Actb.

Phylogenomic databases

GeneTreei ENSGT00710000106384.
HOVERGENi HBG003771.
InParanoidi P60710.
KOi K05692.
OMAi SIVHLKC.
OrthoDBi EOG72RMZ1.
PhylomeDBi P60710.
TreeFami TF354237.

Enzyme and pathway databases

Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_198649. Factors involved in megakaryocyte development and platelet production.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_209040. Gap junction degradation.
REACT_220352. Formation of annular gap junctions.
REACT_226917. HATs acetylate histones.

Miscellaneous databases

ChiTaRSi ACTB. mouse.
NextBioi 278784.
PROi P60710.
SOURCEi Search...

Gene expression databases

ArrayExpressi P60710.
Bgeei P60710.
CleanExi MM_ACTB.
Genevestigatori P60710.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view ]
PANTHERi PTHR11937. PTHR11937. 1 hit.
Pfami PF00022. Actin. 1 hit.
[Graphical view ]
PRINTSi PR00190. ACTIN.
SMARTi SM00268. ACTIN. 1 hit.
[Graphical view ]
PROSITEi PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, METHYLATION AT HIS-73.
    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. 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.

Entry informationi

Entry nameiACTB_MOUSE
AccessioniPrimary (citable) accession number: P60710
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: September 3, 2014
This is version 113 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi