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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.

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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367066Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000757Add
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

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 interactions.
STRINGi9913.ENSBTAP00000008132.

Structurei

Secondary structure

1
375
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Beta strandi8 – 125Combined sources
Beta strandi14 – 218Combined sources
Beta strandi24 – 263Combined sources
Beta strandi30 – 323Combined sources
Beta strandi35 – 384Combined sources
Beta strandi45 – 473Combined sources
Beta strandi51 – 544Combined sources
Helixi56 – 605Combined sources
Helixi62 – 643Combined sources
Beta strandi65 – 684Combined sources
Beta strandi70 – 723Combined sources
Helixi79 – 9113Combined sources
Turni92 – 943Combined sources
Helixi98 – 1003Combined sources
Beta strandi103 – 1075Combined sources
Helixi113 – 12513Combined sources
Beta strandi130 – 1367Combined sources
Helixi137 – 1448Combined sources
Beta strandi148 – 1558Combined sources
Beta strandi160 – 1667Combined sources
Helixi172 – 1743Combined sources
Beta strandi176 – 1794Combined sources
Helixi182 – 19615Combined sources
Helixi203 – 21614Combined sources
Helixi223 – 2319Combined sources
Beta strandi234 – 2363Combined sources
Beta strandi238 – 2414Combined sources
Beta strandi243 – 2453Combined sources
Beta strandi247 – 2515Combined sources
Helixi253 – 2564Combined sources
Helixi259 – 2624Combined sources
Helixi264 – 2674Combined sources
Helixi274 – 2829Combined sources
Helixi287 – 2948Combined sources
Beta strandi297 – 3015Combined sources
Helixi302 – 3043Combined sources
Helixi309 – 32012Combined sources
Turni333 – 3364Combined sources
Helixi338 – 34710Combined sources
Helixi350 – 3545Combined sources
Beta strandi356 – 3583Combined sources
Helixi359 – 3657Combined sources
Helixi369 – 3735Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 6-375.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti126 – 1261T → A in AAI42414 (Ref. 3) Curated
Sequence conflicti204 – 2063AER → GRA in AAM98378 (PubMed:14559974).Curated
Sequence conflicti281 – 2811S → F in AAM98378 (PubMed:14559974).Curated

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
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. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-57682N.
IntActiP60712. 4 interactions.
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.

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: July 6, 2016
This is version 115 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.