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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Sus scrofa (Pig)
Status
Reviewed-Annotation score: Annotation score: 4 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.By similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SSC-190873. Gap junction degradation.
R-SSC-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SSC-3928662. EPHB-mediated forward signaling.
R-SSC-418990. Adherens junctions interactions.
R-SSC-437239. Recycling pathway of L1.
R-SSC-4420097. VEGFA-VEGFR2 Pathway.
R-SSC-445095. Interaction between L1 and Ankyrins.
R-SSC-446353. Cell-extracellular matrix interactions.
R-SSC-5250924. B-WICH complex positively regulates rRNA expression.
R-SSC-5626467. RHO GTPases activate IQGAPs.
R-SSC-5663213. RHO GTPases Activate WASPs and WAVEs.
R-SSC-5663220. RHO GTPases Activate Formins.
R-SSC-5696394. DNA Damage Recognition in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiSus scrofa (Pig)
Taxonomic identifieri9823 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus
Proteomesi
  • UP000008227 Componenti: Chromosome 3

Subcellular locationi

  • Cytoplasmcytoskeleton

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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367078Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000291869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Modified residuei73 – 731Tele-methylhistidineBy similarity
Modified residuei84 – 841N6-methyllysineBy 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).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).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

PaxDbiQ6QAQ1.
PeptideAtlasiQ6QAQ1.
PRIDEiQ6QAQ1.

Expressioni

Gene expression databases

GenevisibleiQ6QAQ1. SS.

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. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with TBC1D21.By similarity

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000008105.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ADXelectron microscopy4.00H6-375[»]
5AFUelectron microscopy3.50H6-375[»]
ProteinModelPortaliQ6QAQ1.
SMRiQ6QAQ1. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ6QAQ1.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin.
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.

Q6QAQ1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,737
Last modified:June 26, 2007 - v2
Checksum:i6AFD05CA94E360E2
GO

Sequence cautioni

The sequence AAS55927.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550069 mRNA. Translation: AAS55927.1. Different initiation.
RefSeqiXP_003124328.1. XM_003124280.4.
UniGeneiSsc.10316.

Genome annotation databases

EnsembliENSSSCT00000008324; ENSSSCP00000008105; ENSSSCG00000007585.
GeneIDi414396.
KEGGissc:414396.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY550069 mRNA. Translation: AAS55927.1. Different initiation.
RefSeqiXP_003124328.1. XM_003124280.4.
UniGeneiSsc.10316.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
5ADXelectron microscopy4.00H6-375[»]
5AFUelectron microscopy3.50H6-375[»]
ProteinModelPortaliQ6QAQ1.
SMRiQ6QAQ1. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9823.ENSSSCP00000008105.

Proteomic databases

PaxDbiQ6QAQ1.
PeptideAtlasiQ6QAQ1.
PRIDEiQ6QAQ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSSSCT00000008324; ENSSSCP00000008105; ENSSSCG00000007585.
GeneIDi414396.
KEGGissc:414396.

Organism-specific databases

CTDi60.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ6QAQ1.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-SSC-190873. Gap junction degradation.
R-SSC-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-SSC-3928662. EPHB-mediated forward signaling.
R-SSC-418990. Adherens junctions interactions.
R-SSC-437239. Recycling pathway of L1.
R-SSC-4420097. VEGFA-VEGFR2 Pathway.
R-SSC-445095. Interaction between L1 and Ankyrins.
R-SSC-446353. Cell-extracellular matrix interactions.
R-SSC-5250924. B-WICH complex positively regulates rRNA expression.
R-SSC-5626467. RHO GTPases activate IQGAPs.
R-SSC-5663213. RHO GTPases Activate WASPs and WAVEs.
R-SSC-5663220. RHO GTPases Activate Formins.
R-SSC-5696394. DNA Damage Recognition in GG-NER.

Gene expression databases

GenevisibleiQ6QAQ1. SS.

Family and domain databases

InterProiIPR004000. Actin.
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]
ProtoNetiSearch...

Publicationsi

  1. "Identification of differentially expressed genes in porcine embryos."
    Lee H.Y., Cui X.S., Jeong Y.J., Shin M.L., Hwang K.C., Kim N.H.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Entry informationi

Entry nameiACTB_PIG
AccessioniPrimary (citable) accession number: Q6QAQ1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: July 6, 2016
This is version 94 of the entry and version 2 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 (By similarity).By similarity

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.