UniProt Accession

 ACTB_HUMAN; P60709; P02570; P70514; P99021; Q11211; Q64316; Q75MN2; Q96B34; Q96HG5 

Genbank Protein ID

 X00351; M10277; X63432; AY582799; AC006483; BC001301; BC002409; BC004251; BC008633; BC012854; BC013380; BC014861; BC016045; V00478 

Genbank Nucleotide ID

 CAA25099.1; AAA51567.1; CAA45026.1; AAS79319.1; AAP22343.1; AAH01301.1; AAH02409.1; AAH04251.1; AAH08633.1; AAH12854.1; AAH13380.1; AAH14861.1; AAH16045.1; CAA23745.1 

Protein Name

 Actin, cytoplasmic 1 

Protein Synonyms/Alias

 Beta-actin; Actin, cytoplasmic 1, N-terminally processed 

Gene Name

 ACTB 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
18	DNGSGMCKAGFAGDD	ubiquitination	[1]
50	VMVGMGQKDSYVGDE	acetylation	[2]
50	VMVGMGQKDSYVGDE	ubiquitination	[1, 3, 4, 5, 6]
61	VGDEAQSKRGILTLK	acetylation	[2, 7, 8]
61	VGDEAQSKRGILTLK	ubiquitination	[1, 3, 4, 5, 6]
68	KRGILTLKYPIEHGI	sumoylation	[9]
113	TEAPLNPKANREKMT	sumoylation	[10]
113	TEAPLNPKANREKMT	ubiquitination	[1, 3, 4, 5, 6, 11, 12]
191	DLTDYLMKILTERGY	acetylation	[2, 8]
191	DLTDYLMKILTERGY	ubiquitination	[1, 3, 4, 5, 6]
213	REIVRDIKEKLCYVA	ubiquitination	[1, 4, 6]
215	IVRDIKEKLCYVALD	ubiquitination	[1, 4, 5, 13]
238	ASSSSLEKSYELPDG	ubiquitination	[5, 13]
284	TTFNSIMKCDVDIRK	sumoylation	[9]
284	TTFNSIMKCDVDIRK	ubiquitination	[13]
291	KCDVDIRKDLYANTV	acetylation	[14]
291	KCDVDIRKDLYANTV	ubiquitination	[1, 3, 4, 5, 6, 11, 12, 13, 15]
315	GIADRMQKEITALAP	ubiquitination	[1, 3, 4, 5, 6]
326	ALAPSTMKIKIIAPP	acetylation	[8]
326	ALAPSTMKIKIIAPP	ubiquitination	[1, 3, 4, 6]
328	APSTMKIKIIAPPER	acetylation	[8]
328	APSTMKIKIIAPPER	ubiquitination	[1, 3, 4, 5, 6]

Reference

 [1] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] Substrate and functional diversity of lysine acetylation revealed by a proteomics survey.
 Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y.
 Mol Cell. 2006 Aug;23(4):607-18. [PMID: 16916647]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] SUMOylation of nuclear actin.
 Hofmann WA, Arduini A, Nicol SM, Camacho CJ, Lessard JL, Fuller-Pace FV, de Lanerolle P.
 J Cell Biol. 2009 Jul 27;186(2):193-200. [PMID: 19635839]
 [10] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [11] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [12] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [13] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [14] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [15] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048] 

Functional Description

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

Sequence Annotation

 MOD_RES 1 1 N-acetylmethionine (By similarity).
 MOD_RES 2 2 N-acetylaspartate; in Actin, cytoplasmic
 MOD_RES 44 44 Methionine sulfoxide (By similarity).
 MOD_RES 73 73 Tele-methylhistidine (By similarity).
 MOD_RES 218 218 Nitrated tyrosine (By similarity).  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton; Deafness; Direct protein sequencing; Disease mutation; Dystonia; Mental retardation; Methylation; Nitration; Nucleotide-binding; Oxidation; Polymorphism; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 375 AA 

Protein Sequence

Gene Ontology

 GO:0030424; C:axon; IEA:Compara.
 GO:0030863; C:cortical cytoskeleton; IEA:Compara.
 GO:0005856; C:cytoskeleton; TAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0070062; C:extracellular vesicular exosome; IDA:UniProtKB.
 GO:0070688; C:MLL5-L complex; IDA:UniProtKB.
 GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
 GO:0014069; C:postsynaptic density; IEA:Compara.
 GO:0030529; C:ribonucleoprotein complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0005200; F:structural constituent of cytoskeleton; TAS:UniProtKB.
 GO:0051084; P:'de novo' posttranslational protein folding; TAS:Reactome.
 GO:0034332; P:adherens junction organization; TAS:Reactome.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0007596; P:blood coagulation; TAS:Reactome.
 GO:0034329; P:cell junction assembly; TAS:Reactome.
 GO:0006928; P:cellular component movement; TAS:UniProtKB.
 GO:0016044; P:cellular membrane organization; TAS:Reactome.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome. 

Interpro

 IPR004000; Actin-related.
 IPR020902; Actin/actin-like_CS.
 IPR004001; Actin_CS. 

Pfam

 PF00022; Actin 

SMART

 SM00268; ACTIN 

PROSITE

 PS00406; ACTINS_1
 PS00432; ACTINS_2
 PS01132; ACTINS_ACT_LIKE 

PRINTS

 PR00190; ACTIN.