Reviewed, UniProtKB/Swiss-Prot P60710 (ACTB_MOUSE)

Names and origin

Protein names

Recommended name:
    Actin, cytoplasmic 1
Alternative name(s):
    Beta-actin
Cleaved into the following chain:
    1- Recommended name:
            Actin, cytoplasmic 1, N-terminally processed

Gene names

Name:

Actb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 mRNP granule complex, at least composed of ACTB, ACTN4, DHX9, ERG, HNRNPA1, HNRNPA2B1, HNRNPAB, HNRNPD, HNRNPL, HNRNPR, HNRNPU, HSPA1, HSPA8, IGF2BP1, ILF2, ILF3, NCBP1, NCL, PABPC1, PABPC4, PABPN1, RPLP0, RPS3, RPS3A, RPS4X, RPS8, RPS9, SYNCRIP, TROVE2, YBX1 and untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, MARCB1/BAF47, 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. Component of the MLL5-L complex, at least composed of MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD By similarity.
Subcellular location	Cytoplasm › cytoskeleton. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs By similarity.
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 component	Cytoplasm Cytoskeleton
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Nitration Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Cellular component	cortical cytoskeleton Inferred from direct assay. Source: MGI cytosol Inferred from direct assay. Source: MGI soluble fraction Inferred from direct assay. Source: MGI
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Actin, cytoplasmic 1		PRO_0000367076
	Initiator methionine	1	1	Removed; alternate Ref.3
	Chain	2 – 375	374	Actin, cytoplasmic 1, N-terminally processed		PRO_0000000775
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in Actin, cytoplasmic 1; alternate
	Modified residue	2	1	N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processed
	Modified residue	53	1	Phosphotyrosine By similarity
	Modified residue	73	1	Tele-methylhistidine
	Modified residue	91	1	Phosphotyrosine By similarity
	Modified residue	166	1	Phosphotyrosine By similarity
	Modified residue	169	1	Phosphotyrosine By similarity
	Modified residue	198	1	Phosphotyrosine By similarity
	Modified residue	218	1	Nitrated tyrosine; alternate
	Modified residue	218	1	Phosphotyrosine; alternate By similarity
	Modified residue	294	1	Phosphotyrosine By similarity
	Modified residue	318	1	Phosphothreonine By similarity
Experimental info
	Sequence conflict	38	1	P → S in CAA27396. Ref.5
	Sequence conflict	38	1	P → S in AAA37144. Ref.5
	Sequence conflict	52	1	S → F in BAE39957. Ref.2
	Sequence conflict	80	1	D → E in BAE35572. Ref.2
	Sequence conflict	109	1	P → T in BAE39957. Ref.2
	Sequence conflict	156	1	G → R in BAE39957. Ref.2
	Sequence conflict	178	1	L → V in BAE39957. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P60710-1 [UniParc]. Last modified April 1, 1988. Version 1. Checksum: 6AFD05CA94E360E2	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of a full-length cDNA for mouse cytoskeletal beta-actin mRNA." Tokunaga K., Taniguchi H., Yoda K., Shimizu M., Sakiyama S. Nucleic Acids Res. 14:2829-2829(1986) [PubMed: 3754329] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: BALB/c, C57BL/6J and NOD. Tissue: Bone marrow, Mammary gland and Thymus.
[3]	"Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin." Vandekerckhove J., Weber K. Eur. J. Biochem. 90:451-462(1978) [PubMed: 213279] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-375. Tissue: Thymus.
[4]	Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 19-39; 51-61; 85-113; 148-177; 184-191; 197-206; 216-254; 257-284; 291-326 AND 360-372, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus.
[5]	"Comparison of three actin-coding sequences in the mouse; evolutionary relationships between the actin genes of warm-blooded vertebrates." Alonso S., Minty A., Bourlet Y., Buckingham M. J. Mol. Evol. 23:11-22(1986) [PubMed: 3084797] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 27-375.
[6]	Vilbois F. Submitted (OCT-1998) to UniProtKB Cited for: ACETYLATION. Tissue: Muscle.
[7]	"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease." Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J. Biochemistry 45:8009-8022(2006) [PubMed: 16800626] [Abstract] Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-218, MASS SPECTROMETRY. Tissue: Brain.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X03672 mRNA. Translation: CAA27307.1. AK088691 mRNA. Translation: BAC40507.1. AK145191 mRNA. Translation: BAE26283.1. AK145196 mRNA. Translation: BAE26288.1. AK145308 mRNA. Translation: BAE26359.1. AK150711 mRNA. Translation: BAE29789.1. AK150879 mRNA. Translation: BAE29928.1. AK151010 mRNA. Translation: BAE30031.1. AK151136 mRNA. Translation: BAE30144.1. AK151145 mRNA. Translation: BAE30152.1. AK151159 mRNA. Translation: BAE30164.1. AK151166 mRNA. Translation: BAE30169.1. AK151190 mRNA. Translation: BAE30187.1. AK151202 mRNA. Translation: BAE30199.1. AK151226 mRNA. Translation: BAE30218.1. AK151277 mRNA. Translation: BAE30264.1. AK151350 mRNA. Translation: BAE30326.1. AK151398 mRNA. Translation: BAE30366.1. AK151995 mRNA. Translation: BAE30859.1. AK151999 mRNA. Translation: BAE30863.1. AK152615 mRNA. Translation: BAE31359.1. AK152651 mRNA. Translation: BAE31388.1. AK152844 mRNA. Translation: BAE31537.1. AK159759 mRNA. Translation: BAE35350.1. AK159834 mRNA. Translation: BAE35412.1. AK160029 mRNA. Translation: BAE35572.1. AK166349 mRNA. Translation: BAE38723.1. AK166498 mRNA. Translation: BAE38810.1. AK167117 mRNA. Translation: BAE39265.1. AK167960 mRNA. Translation: BAE39957.1. X03765 mRNA. Translation: CAA27396.1. M12481 mRNA. Translation: AAA37144.1.
IPI	IPI00110850.
PIR	ATMSB. A39104.
RefSeq	NP_031419.1.
UniGene	Mm.328431 Mm.391967 Mm.469717
3D structure databases
SMR	P60710. Positions 4-371.
ModBase	Search...
Protein-protein interaction databases
IntAct	P60710. 12 interactions.
STRING	P60710.
2-D gel databases
SWISS-2DPAGE	P99041.
REPRODUCTION-2DPAGE	P60710.
Proteomic databases
PRIDE	P60710.
Genome annotation databases
Ensembl	ENSMUST00000031564; ENSMUSP00000031564; ENSMUSG00000029580; Mus musculus. [Genome view]
GeneID	11461.
KEGG	mmu:11461.
UCSC	uc009ajk.1. mouse.
Organism-specific databases
CTD	11461.
MGI	MGI:87904. Actb.
Phylogenomic databases
HOVERGEN	P60710.
InParanoid	P60710.
OMA	ADSEDIQ.
Gene expression databases
ArrayExpress	P60710.
Bgee	P60710.
CleanEx	MM_ACTB.
Genevestigator	P60710.
GermOnline	ENSMUSG00000029580. Mus musculus.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR004001. Actin_CS. [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
NextBio	278784.
SOURCE	Search...

Entry information

Entry name

ACTB_MOUSE

Accession

Primary (citable) accession number: P60710
Secondary accession number(s): P02570 , P70514, P99021, Q11211, Q3TI89, Q3TVP6, Q64316, Q6ZWM3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	April 1, 1988
Last modified:	December 15, 2009
This is version 67 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)