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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: UniProtKB
  • Tat protein binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-418990. Adherens junctions interactions.
R-HSA-437239. Recycling pathway of L1.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-446353. Cell-extracellular matrix interactions.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60709.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:132. ACTB.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytoskeleton Source: UniProtKB
  • cytosol Source: Reactome
  • dense body Source: AgBase
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • MLL5-L complex Source: UniProtKB
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • plasma membrane Source: AgBase
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Dystonia, juvenile-onset (DJO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.
See also OMIM:607371
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti183 – 1831R → W in DJO; modifies cell response to latrunculin A. 1 Publication
VAR_030026
Baraitser-Winter syndrome 1 (BRWS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.
See also OMIM:243310
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121N → D in BRWS1. 1 Publication
Corresponds to variant rs281875331 [ dbSNP | Ensembl ].
VAR_067810
Natural varianti65 – 651L → V in BRWS1. 1 Publication
Corresponds to variant rs281875332 [ dbSNP | Ensembl ].
VAR_067811
Natural varianti196 – 1961R → C in BRWS1. 1 Publication
Corresponds to variant rs281875333 [ dbSNP | Ensembl ].
VAR_067812
Natural varianti196 – 1961R → H in BRWS1. 1 Publication
Corresponds to variant rs281875334 [ dbSNP | Ensembl ].
VAR_067813

Keywords - Diseasei

Deafness, Disease mutation, Dystonia, Mental retardation

Organism-specific databases

MalaCardsiACTB.
MIMi243310. phenotype.
607371. phenotype.
Orphaneti2995. Baraitser-Winter syndrome.
79107. Developmental malformations - deafness - dystonia.
PharmGKBiPA24457.

Chemistry

ChEMBLiCHEMBL2062353.

Polymorphism and mutation databases

BioMutaiACTB.
DMDMi46397333.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367073Add
BLAST
Initiator methionineiRemoved; alternateCombined sources2 Publications
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000771Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedCombined sources1 Publication
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Cross-linki50 – 50Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG11 Publication
Modified residuei73 – 731Tele-methylhistidineBy similarity
Modified residuei84 – 841N6-methyllysine1 Publication
Cross-linki270 – 270Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG11 Publication

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 (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.1 Publication
(Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Oxidation, Ubl conjugation

Proteomic databases

EPDiP60709.
PaxDbiP60709.
PeptideAtlasiP60709.
PRIDEiP60709.
TopDownProteomicsiP60709.

2D gel databases

DOSAC-COBS-2DPAGEP60709.
REPRODUCTION-2DPAGEP60709.
SWISS-2DPAGEP60709.
UCD-2DPAGEP60709.

PTM databases

iPTMnetiP60709.
PhosphoSiteiP60709.
SwissPalmiP60709.

Expressioni

Gene expression databases

BgeeiP60709.
CleanExiHS_ACTB.
ExpressionAtlasiP60709. baseline and differential.
GenevisibleiP60709. HS.

Organism-specific databases

HPAiCAB002621.
HPA041264.
HPA041271.

Interactioni

Subunit structurei

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). 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 similarity7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-353944,EBI-353944
ACTG1P632616EBI-353944,EBI-351292
CFL1P235284EBI-353944,EBI-352733
CFL2Q549N03EBI-353944,EBI-10201319
CFL2Q9Y2813EBI-353944,EBI-351218
DSTNP609814EBI-353944,EBI-745191
ERBB2P0462610EBI-353944,EBI-641062
FBXO25Q8TCJ0-23EBI-353944,EBI-6264551
HSPA8P111422EBI-353944,EBI-351896
Mkl1Q8K4J63EBI-353944,EBI-8291665From a different organism.
MYL12BO149503EBI-353944,EBI-1642165
NCF1P145983EBI-353944,EBI-395044
NSMAFQ926362EBI-353944,EBI-2947053
TAGLN2P378023EBI-353944,EBI-1056740
TINF2Q9BSI42EBI-353944,EBI-717399
WDYHV1Q96HA83EBI-353944,EBI-741158
YWHAZP631043EBI-353944,EBI-347088

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • Tat protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106575. 273 interactions.
DIPiDIP-29686N.
IntActiP60709. 192 interactions.
MINTiMINT-220312.
STRINGi9606.ENSP00000349960.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
ProteinModelPortaliP60709.
SMRiP60709. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60709.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOVERGENiHBG003771.
InParanoidiP60709.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
PhylomeDBiP60709.
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.

P60709-1 [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 conflicti97 – 971A → P in AAH16045 (PubMed:15489334).Curated
Sequence conflicti116 – 1161R → L in AAH12854 (PubMed:15489334).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121N → D in BRWS1. 1 Publication
Corresponds to variant rs281875331 [ dbSNP | Ensembl ].
VAR_067810
Natural varianti65 – 651L → V in BRWS1. 1 Publication
Corresponds to variant rs281875332 [ dbSNP | Ensembl ].
VAR_067811
Natural varianti183 – 1831R → W in DJO; modifies cell response to latrunculin A. 1 Publication
VAR_030026
Natural varianti196 – 1961R → C in BRWS1. 1 Publication
Corresponds to variant rs281875333 [ dbSNP | Ensembl ].
VAR_067812
Natural varianti196 – 1961R → H in BRWS1. 1 Publication
Corresponds to variant rs281875334 [ dbSNP | Ensembl ].
VAR_067813
Natural varianti243 – 2431P → L.
Corresponds to variant rs11546899 [ dbSNP | Ensembl ].
VAR_048185

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA. Translation: CAA25099.1.
M10277 Genomic DNA. Translation: AAA51567.1.
X63432 mRNA. Translation: CAA45026.1.
AY582799 Genomic DNA. Translation: AAS79319.1.
AC006483 Genomic DNA. Translation: AAP22343.1.
BC001301 mRNA. Translation: AAH01301.1.
BC002409 mRNA. Translation: AAH02409.1.
BC004251 mRNA. Translation: AAH04251.1.
BC008633 mRNA. Translation: AAH08633.1.
BC012854 mRNA. Translation: AAH12854.1.
BC013380 mRNA. Translation: AAH13380.1.
BC014861 mRNA. Translation: AAH14861.1.
BC016045 mRNA. Translation: AAH16045.1.
V00478 mRNA. Translation: CAA23745.1.
CCDSiCCDS5341.1.
PIRiA25168. ATHUB.
RefSeqiNP_001092.1. NM_001101.3.
UniGeneiHs.520640.

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624.
GeneIDi60.
KEGGihsa:60.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Mendelian genes actin, beta (ACTB)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA. Translation: CAA25099.1.
M10277 Genomic DNA. Translation: AAA51567.1.
X63432 mRNA. Translation: CAA45026.1.
AY582799 Genomic DNA. Translation: AAS79319.1.
AC006483 Genomic DNA. Translation: AAP22343.1.
BC001301 mRNA. Translation: AAH01301.1.
BC002409 mRNA. Translation: AAH02409.1.
BC004251 mRNA. Translation: AAH04251.1.
BC008633 mRNA. Translation: AAH08633.1.
BC012854 mRNA. Translation: AAH12854.1.
BC013380 mRNA. Translation: AAH13380.1.
BC014861 mRNA. Translation: AAH14861.1.
BC016045 mRNA. Translation: AAH16045.1.
V00478 mRNA. Translation: CAA23745.1.
CCDSiCCDS5341.1.
PIRiA25168. ATHUB.
RefSeqiNP_001092.1. NM_001101.3.
UniGeneiHs.520640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
ProteinModelPortaliP60709.
SMRiP60709. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106575. 273 interactions.
DIPiDIP-29686N.
IntActiP60709. 192 interactions.
MINTiMINT-220312.
STRINGi9606.ENSP00000349960.

Chemistry

ChEMBLiCHEMBL2062353.

PTM databases

iPTMnetiP60709.
PhosphoSiteiP60709.
SwissPalmiP60709.

Polymorphism and mutation databases

BioMutaiACTB.
DMDMi46397333.

2D gel databases

DOSAC-COBS-2DPAGEP60709.
REPRODUCTION-2DPAGEP60709.
SWISS-2DPAGEP60709.
UCD-2DPAGEP60709.

Proteomic databases

EPDiP60709.
PaxDbiP60709.
PeptideAtlasiP60709.
PRIDEiP60709.
TopDownProteomicsiP60709.

Protocols and materials databases

DNASUi60.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624.
GeneIDi60.
KEGGihsa:60.

Organism-specific databases

CTDi60.
GeneCardsiACTB.
HGNCiHGNC:132. ACTB.
HPAiCAB002621.
HPA041264.
HPA041271.
MalaCardsiACTB.
MIMi102630. gene.
243310. phenotype.
607371. phenotype.
neXtProtiNX_P60709.
Orphaneti2995. Baraitser-Winter syndrome.
79107. Developmental malformations - deafness - dystonia.
PharmGKBiPA24457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
HOVERGENiHBG003771.
InParanoidiP60709.
KOiK05692.
OMAiMCKAGCA.
OrthoDBiEOG72RMZ1.
PhylomeDBiP60709.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-418990. Adherens junctions interactions.
R-HSA-437239. Recycling pathway of L1.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-446353. Cell-extracellular matrix interactions.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60709.

Miscellaneous databases

ChiTaRSiACTB. human.
EvolutionaryTraceiP60709.
GeneWikiiBeta-actin.
GenomeRNAii60.
NextBioi253.
PROiP60709.
SOURCEiSearch...

Gene expression databases

BgeeiP60709.
CleanExiHS_ACTB.
ExpressionAtlasiP60709. baseline and differential.
GenevisibleiP60709. HS.

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

« Hide 'large scale' publications
  1. "Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human beta-actin cDNA."
    Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L.
    Nucleic Acids Res. 12:1687-1696(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular structure of the human cytoplasmic beta-actin gene: interspecies homology of sequences in the introns."
    Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T.
    Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Direct proof that the primary site of action of cytochalasin on cell motility processes is actin."
    Ohmori H., Toyama S., Toyama S.
    J. Cell Biol. 116:933-941(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. NIEHS SNPs program
    Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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: Brain, Eye, Kidney, Muscle, Pancreas, Placenta and Skin.
  7. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
    Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
    Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-28.
    Tissue: Platelet.
  8. Bienvenut W.V.
    Submitted (JUN-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-95; 148-177; 184-191; 197-206; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ASP-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  9. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 19-62; 85-113; 184-191; 197-206; 216-254; 291-312; 316-326 AND 360-372, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  10. "Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions."
    Hanukoglu I., Tanese N., Fuchs E.
    J. Mol. Biol. 163:673-678(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 252-375.
  11. "Exportin 6: a novel nuclear export receptor that is specific for profilin.actin complexes."
    Stueven T., Hartmann E., Goerlich D.
    EMBO J. 22:5928-5940(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, INTERACTION WITH XPO6.
  12. "Emerin caps the pointed end of actin filaments: evidence for an actin cortical network at the nuclear inner membrane."
    Holaska J.M., Kowalski A.K., Wilson K.L.
    PLoS Biol. 2:1354-1362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EMD.
  13. Cited for: ISGYLATION.
  14. "HGAL, a lymphoma prognostic biomarker, interacts with the cytoskeleton and mediates the effects of IL-6 on cell migration."
    Lu X., Chen J., Malumbres R., Cubedo Gil E., Helfman D.M., Lossos I.S.
    Blood 110:4268-4277(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GCSAM.
  15. Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
  16. "Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
    Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
    Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Connecting actin monomers by iso-peptide bond is a toxicity mechanism of the Vibrio cholerae MARTX toxin."
    Kudryashov D.S., Durer Z.A., Ytterberg A.J., Sawaya M.R., Pashkov I., Prochazkova K., Yeates T.O., Loo R.R., Loo J.A., Satchell K.J., Reisler E.
    Proc. Natl. Acad. Sci. U.S.A. 105:18537-18542(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROSS-LINK BETWEEN LYS-50 AND GLU-270 BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Nuclear ErbB2 enhances translation and cell growth by activating transcription of ribosomal RNA genes."
    Li L.Y., Chen H., Hsieh Y.H., Wang Y.N., Chu H.J., Chen Y.H., Chen H.Y., Chien P.J., Ma H.T., Tsai H.C., Lai C.C., Sher Y.P., Lien H.C., Tsai C.H., Hung M.C.
    Cancer Res. 71:4269-4279(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERBB2.
  20. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ASP-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ASP-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: CROSS-LINK BY V.CHOLERAE TOXIN RTXA (MICROBIAL INFECTION).
  24. "A mutation of beta -actin that alters depolymerization dynamics is associated with autosomal dominant developmental malformations, deafness, and dystonia."
    Procaccio V., Salazar G., Ono S., Styers M.L., Gearing M., Davila A., Jimenez R., Juncos J., Gutekunst C.-A., Meroni G., Fontanella B., Sontag E., Sontag J.-M., Faundez V., Wainer B.H.
    Am. J. Hum. Genet. 78:947-960(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DJO TRP-183, CHARACTERIZATION OF VARIANT DJO TRP-183.
  25. "GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis."
    Fujiki R., Chikanishi T., Hashiba W., Ito H., Takada I., Roeder R.G., Kitagawa H., Kato S.
    Nature 459:455-459(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL5-L COMPLEX.
  26. Cited for: METHYLATION AT LYS-84, DEMETHYLATION BY ALKBH4.
  27. Cited for: VARIANTS BRWS1 ASP-12; VAL-65; CYS-196 AND HIS-196.

Entry informationi

Entry nameiACTB_HUMAN
AccessioniPrimary (citable) accession number: P60709
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: May 11, 2016
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.