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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Bos taurus (Bovine)
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-BTA-392029. Prefoldin mediated transfer of substrate to CCT/TriC.
R-BTA-392030. Folding of actin by CCT/TriC.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

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)DescriptionActionsGraphical viewLength
ChainiPRO_00003670661 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateBy similarity
ChainiPRO_00000007572 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysineBy similarity1

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

PaxDbiP60712.
PeptideAtlasiP60712.
PRIDEiP60712.

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

DIPiDIP-57682N.
IntActiP60712. 4 interactors.
STRINGi9913.ENSBTAP00000008132.

Structurei

Secondary structure

1375
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 6Combined sources3
Beta strandi8 – 12Combined sources5
Beta strandi14 – 21Combined sources8
Beta strandi24 – 26Combined sources3
Beta strandi30 – 32Combined sources3
Beta strandi35 – 38Combined sources4
Beta strandi45 – 47Combined sources3
Beta strandi51 – 54Combined sources4
Helixi56 – 60Combined sources5
Helixi62 – 64Combined sources3
Beta strandi65 – 68Combined sources4
Beta strandi70 – 72Combined sources3
Helixi79 – 91Combined sources13
Turni92 – 94Combined sources3
Helixi98 – 100Combined sources3
Beta strandi103 – 107Combined sources5
Helixi113 – 125Combined sources13
Beta strandi130 – 136Combined sources7
Helixi137 – 144Combined sources8
Beta strandi148 – 155Combined sources8
Beta strandi160 – 166Combined sources7
Helixi172 – 174Combined sources3
Beta strandi176 – 179Combined sources4
Helixi182 – 196Combined sources15
Helixi203 – 216Combined sources14
Helixi223 – 231Combined sources9
Beta strandi234 – 236Combined sources3
Beta strandi238 – 241Combined sources4
Beta strandi243 – 245Combined sources3
Beta strandi247 – 251Combined sources5
Helixi253 – 256Combined sources4
Helixi259 – 262Combined sources4
Helixi264 – 267Combined sources4
Helixi274 – 282Combined sources9
Helixi287 – 294Combined sources8
Beta strandi297 – 301Combined sources5
Helixi302 – 304Combined sources3
Helixi309 – 320Combined sources12
Turni333 – 336Combined sources4
Helixi338 – 347Combined sources10
Helixi350 – 354Combined sources5
Beta strandi356 – 358Combined sources3
Helixi359 – 365Combined sources7
Helixi369 – 373Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HLUX-ray2.65A2-375[»]
2BTFX-ray2.55A2-375[»]
2OANX-ray2.61A/B/C/D1-375[»]
3U4LX-ray2.40A1-375[»]
3UB5X-ray2.20A2-375[»]
ProteinModelPortaliP60712.
SMRiP60712.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60712.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOVERGENiHBG003771.
InParanoidiP60712.
KOiK05692.

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.

P60712-1 [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:April 1, 1988 - v1
Checksum:i6AFD05CA94E360E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti126T → A in AAI42414 (Ref. 3) Curated1
Sequence conflicti204 – 206AER → GRA in AAM98378 (PubMed:14559974).Curated3
Sequence conflicti281S → F in AAM98378 (PubMed:14559974).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY141970 mRNA. Translation: AAM98378.1.
BT030480 mRNA. Translation: ABQ12920.1.
BC102948 mRNA. Translation: AAI02949.1.
BC142413 mRNA. Translation: AAI42414.1.
K00622 mRNA. Translation: AAA30352.1.
K00623 mRNA. Translation: AAA30353.1.
PIRiE14185. ATBOB.
RefSeqiNP_776404.2. NM_173979.3.
UniGeneiBt.14186.

Genome annotation databases

GeneIDi280979.
KEGGibta:280979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY141970 mRNA. Translation: AAM98378.1.
BT030480 mRNA. Translation: ABQ12920.1.
BC102948 mRNA. Translation: AAI02949.1.
BC142413 mRNA. Translation: AAI42414.1.
K00622 mRNA. Translation: AAA30352.1.
K00623 mRNA. Translation: AAA30353.1.
PIRiE14185. ATBOB.
RefSeqiNP_776404.2. NM_173979.3.
UniGeneiBt.14186.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1HLUX-ray2.65A2-375[»]
2BTFX-ray2.55A2-375[»]
2OANX-ray2.61A/B/C/D1-375[»]
3U4LX-ray2.40A1-375[»]
3UB5X-ray2.20A2-375[»]
ProteinModelPortaliP60712.
SMRiP60712.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-57682N.
IntActiP60712. 4 interactors.
STRINGi9913.ENSBTAP00000008132.

Proteomic databases

PaxDbiP60712.
PeptideAtlasiP60712.
PRIDEiP60712.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi280979.
KEGGibta:280979.

Organism-specific databases

CTDi60.

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOVERGENiHBG003771.
InParanoidiP60712.
KOiK05692.

Enzyme and pathway databases

ReactomeiR-BTA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-BTA-392029. Prefoldin mediated transfer of substrate to CCT/TriC.
R-BTA-392030. Folding of actin by CCT/TriC.

Miscellaneous databases

EvolutionaryTraceiP60712.

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...

Entry informationi

Entry nameiACTB_BOVIN
AccessioniPrimary (citable) accession number: P60712
Secondary accession number(s): A5D961
, A5PKA1, P02570, P70514, P99021, Q11211, Q3SZD2, Q64316, Q8MIJ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: November 30, 2016
This is version 118 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

3D-structure, Complete proteome, Direct protein sequencing, 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.