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P60711

- ACTB_RAT

UniProt

P60711 - ACTB_RAT

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Protein

Actin, cytoplasmic 1

Gene
Actb
Organism
Rattus norvegicus (Rat)
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: UniProtKB
  3. protein kinase binding Source: RGD

GO - Biological processi

  1. axonogenesis Source: RGD
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_196232. Factors involved in megakaryocyte development and platelet production.
REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
REACT_198384. HATs acetylate histones.
REACT_199176. Translocation of GLUT4 to the plasma membrane.

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
ProteomesiUP000002494: Chromosome 12

Organism-specific databases

RGDi628837. Actb.

Subcellular locationi

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

GO - Cellular componenti

  1. axon Source: RGD
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: Ensembl
  4. MLL5-L complex Source: Ensembl
  5. NuA4 histone acetyltransferase complex Source: Ensembl
  6. postsynaptic density Source: RGD
  7. protein complex Source: RGD
  8. 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 1PRO_0000367081Add
BLAST
Initiator methioninei1 – 11Removed; alternate By similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000781Add
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 processed By similarity
Modified residuei44 – 441Methionine (R)-sulfoxide By similarity
Modified residuei47 – 471Methionine (R)-sulfoxide By similarity
Modified residuei73 – 731Tele-methylhistidine By similarity
Modified residuei84 – 841N6-methyllysine By similarity

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.
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

PaxDbiP60711.
PRIDEiP60711.

2D gel databases

World-2DPAGE0004:P60711.

PTM databases

PhosphoSiteiP60711.

Expressioni

Gene expression databases

ArrayExpressiP60711.
GenevestigatoriP60711.

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 By similarity.

Binary interactionsi

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

Protein-protein interaction databases

BioGridi249680. 12 interactions.
IntActiP60711. 18 interactions.
MINTiMINT-132123.

Structurei

3D structure databases

ProteinModelPortaliP60711.
SMRiP60711. Positions 6-375.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00710000106384.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP60711.
KOiK05692.
OMAiDARAPIM.
OrthoDBiEOG72RMZ1.
PhylomeDBiP60711.
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.

P60711-1 [UniParc]FASTAAdd to Basket

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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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
V01217 Genomic DNA. Translation: CAA24528.1 .
BC063166 mRNA. Translation: AAH63166.1 .
RefSeqi NP_112406.1. NM_031144.3.
UniGenei Rn.94978.

3D structure databases

ProteinModelPortali P60711.
SMRi P60711. Positions 6-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249680. 12 interactions.
IntActi P60711. 18 interactions.
MINTi MINT-132123.

PTM databases

PhosphoSitei P60711.

2D gel databases

World-2DPAGE 0004:P60711.

Proteomic databases

PaxDbi P60711.
PRIDEi P60711.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSRNOT00000042459 ; ENSRNOP00000044296 ; ENSRNOG00000034254 .
GeneIDi 81822.
KEGGi rno:81822.
UCSCi RGD:628837. rat.

Organism-specific databases

CTDi 60.
RGDi 628837. Actb.

Phylogenomic databases

eggNOGi COG5277.
GeneTreei ENSGT00710000106384.
HOGENOMi HOG000233340.
HOVERGENi HBG003771.
InParanoidi P60711.
KOi K05692.
OMAi DARAPIM.
OrthoDBi EOG72RMZ1.
PhylomeDBi P60711.
TreeFami TF354237.

Enzyme and pathway databases

Reactomei REACT_196232. Factors involved in megakaryocyte development and platelet production.
REACT_196755. Regulation of actin dynamics for phagocytic cup formation.
REACT_198384. HATs acetylate histones.
REACT_199176. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

NextBioi 615747.

Gene expression databases

ArrayExpressi P60711.
Genevestigatori P60711.

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. "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.

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: September 3, 2014
This is version 106 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

External Data

Dasty 3

Similar proteinsi