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P60709 (ACTB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin

Cleaved into the following chain:

  1. Actin, cytoplasmic 1, N-terminally processed
Gene names
Name:ACTB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

Subunit structure

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. Ref.11 Ref.12 Ref.14 Ref.15 Ref.16 Ref.18 Ref.21

Subcellular location

Cytoplasmcytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Ref.15

Post-translational modification

ISGylated. Ref.13

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.

Involvement in disease

Dystonia, juvenile-onset (DYTJ) [MIM:607371]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20

Baraitser-Winter syndrome 1 (BRWS1) [MIM:243310]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.23

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.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Disease mutation
Dystonia
Mental retardation
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Oxidation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

Fc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

adherens junction organization

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

blood coagulation

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 16130169PubMed 6202424. Source: UniProtKB

cellular protein metabolic process

Traceable author statement. Source: Reactome

chromatin organization

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

substantia nigra development

Inferred from expression pattern PubMed 22926577. Source: UniProt

   Cellular_componentMLL5-L complex

Inferred from direct assay Ref.21. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from direct assay PubMed 10966108. Source: UniProtKB

axon

Inferred from electronic annotation. Source: Ensembl

blood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

ribonucleoprotein complex

Inferred from direct assay Ref.15. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Tat protein binding

Inferred from physical interaction PubMed 16687403. Source: BHF-UCL

kinesin binding

Inferred from physical interaction PubMed 18680169. Source: UniProtKB

nitric-oxide synthase binding

Inferred from physical interaction PubMed 17502619. Source: BHF-UCL

structural constituent of cytoskeleton

Traceable author statement PubMed 6202424. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin, cytoplasmic 1
PRO_0000367073
Initiator methionine11Removed; alternate Ref.7 Ref.8
Chain2 – 375374Actin, cytoplasmic 1, N-terminally processed
PRO_0000000771

Amino acid modifications

Modified residue11N-acetylmethionine Ref.19
Modified residue21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed Ref.8 Ref.17 Ref.19
Modified residue441Methionine (R)-sulfoxide By similarity
Modified residue471Methionine (R)-sulfoxide By similarity
Modified residue731Tele-methylhistidine By similarity
Modified residue841N6-methyllysine Ref.22

Natural variations

Natural variant121N → D in BRWS1. Ref.23
Corresponds to variant rs281875331 [ dbSNP | Ensembl ].
VAR_067810
Natural variant651L → V in BRWS1. Ref.23
Corresponds to variant rs281875332 [ dbSNP | Ensembl ].
VAR_067811
Natural variant1831R → W in DYTJ; modifies cell response to latrunculin A. Ref.20
VAR_030026
Natural variant1961R → C in BRWS1. Ref.23
Corresponds to variant rs281875333 [ dbSNP | Ensembl ].
VAR_067812
Natural variant1961R → H in BRWS1. Ref.23
Corresponds to variant rs281875334 [ dbSNP | Ensembl ].
VAR_067813
Natural variant2431P → L.
Corresponds to variant rs11546899 [ dbSNP | Ensembl ].
VAR_048185

Experimental info

Sequence conflict971A → P in AAH16045. Ref.6
Sequence conflict1161R → L in AAH12854. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P60709 [UniParc].

Last modified April 1, 1988. Version 1.
Checksum: 6AFD05CA94E360E2

FASTA37541,737
        10         20         30         40         50         60 
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 

        70         80         90        100        110        120 
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 

       130        140        150        160        170        180 
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 

       190        200        210        220        230        240 
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 

       250        260        270        280        290        300 
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 

       310        320        330        340        350        360 
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 

       370 
EYDESGPSIV HRKCF 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
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]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"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.
[19]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND ASP-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"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 DYTJ TRP-183, CHARACTERIZATION OF VARIANT DYTJ TRP-183.
[21]"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.
[22]"ALKBH4-dependent demethylation of actin regulates actomyosin dynamics."
Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y., Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C., Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.
Nat. Commun. 4:1832-1832(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-84, DEMETHYLATION BY ALKBH4.
[23]"De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome."
Riviere J.B., van Bon B.W., Hoischen A., Kholmanskikh S.S., O'Roak B.J., Gilissen C., Gijsen S., Sullivan C.T., Christian S.L., Abdul-Rahman O.A., Atkin J.F., Chassaing N., Drouin-Garraud V., Fry A.E., Fryns J.P., Gripp K.W., Kempers M., Kleefstra T. expand/collapse author list , Mancini G.M., Nowaczyk M.J., van Ravenswaaij-Arts C.M., Roscioli T., Marble M., Rosenfeld J.A., Siu V.M., de Vries B.B., Shendure J., Verloes A., Veltman J.A., Brunner H.G., Ross M.E., Pilz D.T., Dobyns W.B.
Nat. Genet. 44:440-444(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BRWS1 ASP-12; VAL-65; CYS-196 AND HIS-196.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRATHUB. A25168.
RefSeqNP_001092.1. NM_001101.3.
UniGeneHs.520640.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
ProteinModelPortalP60709.
SMRP60709. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106575. 184 interactions.
DIPDIP-29686N.
IntActP60709. 165 interactions.
MINTMINT-220312.

Chemistry

ChEMBLCHEMBL2062353.

PTM databases

PhosphoSiteP60709.

Polymorphism databases

DMDM46397333.

2D gel databases

DOSAC-COBS-2DPAGEP60709.
P60709_OR_P63261.
REPRODUCTION-2DPAGEP60709.
SWISS-2DPAGEP60709.
UCD-2DPAGEP60709.

Proteomic databases

PaxDbP60709.
PeptideAtlasP60709.
PRIDEP60709.

Protocols and materials databases

DNASU60.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331789; ENSP00000349960; ENSG00000075624.
GeneID60.
KEGGhsa:60.
UCSCuc003soq.4. human.

Organism-specific databases

CTD60.
GeneCardsGC07M005566.
HGNCHGNC:132. ACTB.
HPACAB002621.
HPA041264.
HPA041271.
MIM102630. gene.
243310. phenotype.
607371. phenotype.
neXtProtNX_P60709.
Orphanet2995. Baraitser-Winter syndrome.
79107. Developmental malformations - deafness - dystonia.
PharmGKBPA24457.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5277.
HOVERGENHBG003771.
InParanoidP60709.
KOK05692.
OMANGIADRM.
OrthoDBEOG72RMZ1.
PhylomeDBP60709.
TreeFamTF354237.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_11123. Membrane Trafficking.
REACT_17015. Metabolism of proteins.
REACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP60709.

Gene expression databases

ArrayExpressP60709.
BgeeP60709.
CleanExHS_ACTB.
GenevestigatorP60709.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTB. human.
EvolutionaryTraceP60709.
GeneWikiBeta-actin.
GenomeRNAi60.
NextBio253.
PROP60709.
SOURCESearch...

Entry information

Entry nameACTB_HUMAN
AccessionPrimary (citable) accession number: P60709
Secondary accession number(s): P02570 expand/collapse secondary AC list , P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: April 16, 2014
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM