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General information about the entry
Entry name ACTB_HUMAN
Primary accession number P02570
Secondary accession numbers P70514 P99021 Q11211 Q64316
Entered in Swiss-Prot in Release 01, July 1986
Sequence was last modified in Release 07, April 1988
Annotations were last modified in    Release 41, February 2003
Name and origin of the protein
Protein name Actin, cytoplasmic 1
Synonym Beta-actin
Gene name
ACTB
From
Homo sapiens (Human) [TaxID: 9606]
Mus musculus (Mouse) [TaxID: 10090]
Rattus norvegicus (Rat) [TaxID: 10116]
Bos taurus (Bovine) [TaxID: 9913]
Ovis aries (Sheep) [TaxID: 9940]
Equus caballus (Horse) [TaxID: 9796]
Trichosurus vulpecula (Brush-tailed possum) [TaxID: 9337]
Gallus gallus (Chicken) [TaxID: 9031]
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo.
References
[1]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=85298307; PubMed=2994062; [NCBI, ExPASy, EBI, Israel, Japan]
Nakajima-Iijima S., Hamada H., Reddy P., Kakunaga T.;
"Molecular structure of the human cytoplasmic beta-actin gene: interspecies homology of sequences in the introns.";
Proc. Natl. Acad. Sci. U.S.A. 82:6133-6137(1985).
[2]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=84144061; PubMed=6322116; [NCBI, ExPASy, EBI, Israel, Japan]
Ponte P., Ng S.Y., Engel J., Gunning P., Kedes L.;
"Evolutionary conservation in the untranslated regions of actin mRNAs: DNA sequence of a human beta-actin cDNA.";
Nucleic Acids Res. 12:1687-1696(1984).
[3]
SEQUENCE OF 252-375 FROM NUCLEIC ACID.
SPECIES=Human;
MEDLINE=83189093; PubMed=6842590; [NCBI, ExPASy, EBI, Israel, Japan]
Hanukoglu I., Tanese N., Fuchs E.;
"Complementary DNA sequence of a human cytoplasmic actin. Interspecies divergence of 3' non-coding regions.";
J. Mol. Biol. 163:673-678(1983).
[4]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Rat;
MEDLINE=83168920; PubMed=6300777; [NCBI, ExPASy, EBI, Israel, Japan]
Nudel U., Zakut R., Shani M., Neuman S., Levy Z., Yaffe D.;
"The nucleotide sequence of the rat cytoplasmic beta-actin gene.";
Nucleic Acids Res. 11:1759-1771(1983).
[5]
SEQUENCE OF 2-375.
SPECIES=Bovine, and Mouse;
TISSUE=Brain, and Thymus;
MEDLINE=79045349; PubMed=213279; [NCBI, ExPASy, EBI, Israel, Japan]
Vandekerckhove J., Weber K.;
"Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin.";
Eur. J. Biochem. 90:451-462(1978).
[6]
SEQUENCE OF 77-228 AND 345-375 FROM NUCLEIC ACID.
SPECIES=Bovine;
MEDLINE=84032385; PubMed=6195151; [NCBI, ExPASy, EBI, Israel, Japan]
Degen J.L., Neubauer M.G., Friezner Degen S.J., Seyfried C.E., Morris D.R.;
"Regulation of protein synthesis in mitogen-activated bovine lymphocytes. Analysis of actin-specific and total mRNA accumulation and utilization.";
J. Biol. Chem. 258:12153-12162(1983).
[7]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Mouse;
MEDLINE=86176768; PubMed=3754329; [NCBI, ExPASy, EBI, Israel, Japan]
Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S.;
"Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA.";
Nucleic Acids Res. 14:2829-2829(1986).
[8]
SEQUENCE OF 27-375 FROM NUCLEIC ACID.
SPECIES=Mouse;
MEDLINE=86200234; PubMed=3084797; [NCBI, ExPASy, EBI, Israel, Japan]
Alonso S., Minty A., Bourlet Y., Buckingham M.;
"Comparison of three actin-coding sequences in the mouse; evolutionary relationships between the actin genes of warm-blooded vertebrates.";
J. Mol. Evol. 23:11-22(1986).
[9]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Sheep;
Rothwell M.C., Miller W.L.;
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
[10]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Horse;
Swiderski C.E., Horohov D.W.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[11]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=T.vulpecula;
Wedlock D.N., Hickson R., Buddle B.M.;
"Isolation of the full-length cDNA for beta-actin from the common brushtail possum.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[12]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Chicken;
MEDLINE=84169478; PubMed=6324080; [NCBI, ExPASy, EBI, Israel, Japan]
Kost T.A., Theodorakis N., Hughes S.H.;
"The nucleotide sequence of the chick cytoplasmic beta-actin gene.";
Nucleic Acids Res. 11:8287-8301(1983).
[13]
SEQUENCE FROM NUCLEIC ACID.
SPECIES=Chicken;
Wang H., Morais R.;
Submitted (XXX-1994) to the EMBL/GenBank/DDBJ databases.
[14]
ACETYLATION.
SPECIES=Mouse;
TISSUE=Muscle;
Vilbois F.;
Submitted (OCT-1998) to the SWISS-PROT data bank.
[15]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF COMPLEX WITH PROFILIN.
SPECIES=Bovine;
MEDLINE=94019858; PubMed=8413665; [NCBI, ExPASy, EBI, Israel, Japan]
Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U.;
"The structure of crystalline profilin-beta-actin.";
Nature 365:810-816(1993).
[16]
X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF COMPLEX WITH PROFILIN.
SPECIES=Bovine;
MEDLINE=97078817; PubMed=8918942; [NCBI, ExPASy, EBI, Israel, Japan]
Chik J.K., Lindberg U., Schutt C.E.;
"The structure of an open state of beta-actin at 2.65-A resolution.";
J. Mol. Biol. 263:607-623(1996).
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: 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.
  • SUBCELLULAR LOCATION: Cytoplasmic.
  • 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 CO-EXIST IN MOST CELL TYPES AS COMPONENTS OF THE CYTOSKELETON AND AS MEDIATORS OF INTERNAL CELL MOTILITY.
  • SIMILARITY: BELONGS TO THE ACTIN FAMILY.
Copyright
This SWISS-PROT entry is copyright. It is produced through a collaboration between the Swiss Institute of Bioinformatics and the EMBL outstation - the European Bioinformatics Institute. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/ or send an email to license@isb-sib.ch).
Cross-references
EMBL
V00478; CAA23745.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
V01217; CAA24528.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
M10277; AAA51567.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
X63432; CAA45026.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00351; CAA25099.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03672; CAA27307.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00622; AAA30352.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
K00623; AAA30353.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
X00182; CAA25004.1; ALT_SEQ.[EMBL / GenBank / DDBJ] [CoDingSequence]
L08165; AAA48615.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF076190; AAC26519.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF035774; AAB88212.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
U39357; AAB60717.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
X03765; CAA27396.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
M12481; AAA37144.1; -.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A25168; ATHUB.
A02999; ATRTC.
A39104; ATMSB.
A14185; ATBOB.
A20888; ATCHB.
S23707; S23707.
PDB
2BTF; 22-JUN-94.[ExPASy / RCSB]
1HLU; 15-OCT-97.[ExPASy / RCSB]
Detailed list of linked structures.
SWISS-2DPAGE P02570; HUMAN.
P99021; MOUSE.
Aarhus/Ghent-2DPAGE 7316; IEF.
Siena-2DPAGE P02570; -.
Genew HGNC:132; ACTB.
CleanEx HGNC:132; ACTB.
MIM 102630 [NCBI / EBI].
GeneCards ACTB.
GeneLynx ACTB; Homo sapiens.
MGD MGI:87904; Actb.
GeneLynx ACTB; Mus musculus.
SOURCE ACTB; Homo sapiens.
ACTB; Mus musculus.
Ensembl P02570; Homo sapiens. [Entry / Contig view]
P02570; Mus musculus. [Entry / Contig view]
InterPro IPR004001; Actin.
IPR004000; Actin_like.
Graphical view of domain structure.
Pfam PF00022; actin; 1.
PRINTS PR00190; ACTIN.
SMART SM00268; ACTIN; 1.
PROSITE PS00406; ACTINS_1; 1.
PS00432; ACTINS_2; 1.
PS01132; ACTINS_ACT_LIKE; 1.
ProDom [Domain structure / List of seq. sharing at least 1 domain].
BLOCKS P02570.
ProtoNet P02570.
ProtoMap P02570.
PRESAGE P02570.
DIP P02570.
ModBase P02570.
Keywords
Multigene family; Structural protein; Methylation; Acetylation; Cytoskeleton; 3D-structure.
Features
<
KeyFrom   To Length Description
PROPEP   1     1  1     REMOVED IN MATURE FORM.
CHAIN   2   375  374     ACTIN, CYTOPLASMIC 1.
MOD_RES   1     1        ACETYLATION.
MOD_RES   2     2        ACETYLATION.
MOD_RES   73    73        METHYLATION.
CONFLICT   38    38        P -> S (IN REF. 8).
STRAND   8    12  5     
STRAND   16    21  6     
TURN   22    23  2     
STRAND   29    32  4     
STRAND   35    37  3     
STRAND   53    54  2     
HELIX   55    64  10     
STRAND   66    68  3     
STRAND   71    72  2     
STRAND   75    76  2     
HELIX   79    91  13     
TURN   92    94  3     
HELIX   98   100  3     
STRAND   103   107  5     
TURN   109   110  2     
HELIX   113   127  15     
STRAND   131   136  6     
HELIX   137   145  9     
TURN   146   146  1     
STRAND   150   155  6     
STRAND   160   166  7     
TURN   167   168  2     
STRAND   169   170  2     
HELIX   172   174  3     
STRAND   176   178  3     
HELIX   182   195  14     
TURN   196   196  1