Actin, cytoplasmic 1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P60709 (ACTB_HUMAN)

Last modified November 25, 2008. Version 66. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

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

Gene names

Name:

ACTB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. 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 a complex composed at least of ACTB, AP2M1, AP2A1, AP2A2, MEGF10 and VIM. Interacts with XPO6.
Subcellular location	Cytoplasm › cytoskeleton.
Involvement in disease	Defects in ACTB are a cause of juvenile-onset dystonia [MIM:607371]. Dystonia is a movement disorder with a neurological basis, due to disordered tonicity of muscle. It is characterized by sustained involuntary muscle contractions that cause abnormal postures and repetitive movements. It may affect muscles throughout the body (generalized), in certain parts of the body (segmental), or may be confined to particular muscles or muscle groups (focal). Individuals with juvenile-onset dystonia due to ACTB mutations present a complicated phenotype that includes progressive generalized dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.
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.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Disease	Deafness Disease mutation
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	cell motion Traceable author statement. Source: UniProtKB sensory perception of sound Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	NuA4 histone acetyltransferase complex Inferred from direct assay. Source: UniProtKB cytoskeleton Traceable author statement. Source: UniProtKB
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase binding Inferred from physical interaction. Source: UniProtKB structural constituent of cytoskeleton Traceable author statement. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
CFL2	Q9Y281	1	EBI-353944,EBI-351218
MDM2	Q00987	1	EBI-353944,EBI-389668
SMAD3	P84022	1	EBI-353944,EBI-347161

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Propeptide

Removed in mature form

PRO_0000000770

Chain

2 – 375

374

Actin, cytoplasmic 1

PRO_0000000771

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

N-acetylaspartate

Modified residue

Phosphotyrosine

Modified residue

Tele-methylhistidine By similarity

Modified residue

Phosphotyrosine

Modified residue

166

Phosphotyrosine

Modified residue

198

Phosphotyrosine

Modified residue

218

Phosphotyrosine

Modified residue

294

Phosphotyrosine

Modified residue

318

Phosphothreonine

Natural variations

Natural variant

183

R → W in juvenile-onset dystonia; modifies cell response to latrunculin A.

VAR_030026

Experimental info

Sequence conflict

A → P in AAH16045. Ref.6

Sequence conflict

116

R → L in AAH12854. Ref.6

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Sequences

Sequence

Length

Mass (Da)

Tools

P60709-1 [UniParc].

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

375

41,737

        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

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References

	« Hide 'large scale' referencesShow '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: 6322116] [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: 2994062] [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: 1734024] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"NIEHS-SNPs, environmental genome project, NIEHS ES15478, Department of Genome Sciences, Seattle, WA (URL: http://egp.gs.washington.edu)." Livingston R.J., Rieder M.J., Chung M.-W., Ritchie T.K., Olson A.N., Nguyen C.P., Nguyen D.A., Poel C.L., Robertson P.D., Schackwitz W.S., Sherwood J.K., Sherwood A.M., Leithauser B.J., Nickerson D.A. 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. Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: 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: 12665801] [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, ACETYLATION AT ASP-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[9]	Lubec G., Afjehi-Sadat L. Submitted (MAR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 29-39; 85-95; 239-254 AND 292-312, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[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: 6842590] [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: 14592989] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH RAN; XPO6 AND PFN1, INTERACTION WITH XPO6.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-166; TYR-218 AND TYR-294, MASS SPECTROMETRY.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-53; TYR-91; TYR-198 AND TYR-294, MASS SPECTROMETRY. Tissue: Lung.
[14]	"MEGF10 is a mammalian ortholog of CED-1 that interacts with clathrin assembly protein complex 2 medium chain and induces large vacuole formation." Suzuki E., Nakayama M. Exp. Cell Res. 313:3729-3742(2007) [PubMed: 17643423] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH AP2M1; AP2A1; AP2A2; MEGF10 AND VIM.
[15]	"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: 18765789] [Abstract] Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[16]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Platelet.
[17]	"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: 16685646] [Abstract] Cited for: VARIANT JUVENILE-ONSET DYSTONIA TRP-183, CHARACTERIZATION OF VARIANT JUVENILE-ONSET DYSTONIA TRP-183.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

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.
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.

PIR

ATHUB. A25168.

RefSeq

NP_001092.1.

UniGene

Hs.520640
Hs.702191

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BYH	electron microscopy	12.00	A	2-375	[»]
3D2U	X-ray	2.21	C/G	170-178	[»]

SMR

P60709. Positions 4-371.

ModBase

Search...

Protein-protein interaction databases

IntAct

P60709.

PTM databases

PhosphoSite

P60709.

Polymorphism databases

NIEHS-SNPs

Search...

2-D gel databases

SWISS-2DPAGE

P60709.

Aarhus/Ghent-2DPAGE

7316. IEF.

DOSAC-COBS-2DPAGE

P60709.

REPRODUCTION-2DPAGE

P60709.

Siena-2DPAGE

P60709.

Proteomic databases

PeptideAtlas

P60709.

Genome annotation databases

Ensembl

ENSG00000075624. Homo sapiens. [Contig view]

GeneID

60.

KEGG

hsa:60.

Organism-specific databases

HGNC

HGNC:132. ACTB.

HPA

CAB002621.

MIM

102630. gene.
607371. phenotype.

Orphanet

256. Early onset torsion dystonia.

PharmGKB

PA24457.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P60709.

Gene expression databases

ArrayExpress

P60709.

CleanEx

HS_ACTB.

GermOnline

ENSG00000075624. Homo sapiens.

Family and domain databases

InterPro

IPR004001. Actin_CS.
IPR004000. Actin_like.
[Graphical view]

PANTHER

PTHR11937. Actin_like. 1 hit.

Pfam

PF00022. Actin. 1 hit.
[Graphical view]

PRINTS

PR00190. ACTIN.

SMART

SM00268. ACTIN. 1 hit.
[Graphical view]

PROSITE

PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P60709.

NextBio

253.

SOURCE

Search...

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Entry information

Entry name

ACTB_HUMAN

Accession

Primary (citable) accession number: P60709
Secondary accession number(s): P02570

Q96B34

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	November 25, 2008
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 7

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Natural variations

Experimental info

Sequences

References

Web resources

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents