UniProt Accession

 COF1_HUMAN; P23528; B3KUQ1; Q53Y87; Q9UCA2 

Genbank Protein ID

 D00682; U21909; X95404; BT006846; AK097690; CH471076; BC011005; BC012265; BC012318; BC018256 

Genbank Nucleotide ID

 BAA00589.1; AAA64501.1; CAA64685.1; AAP35492.1; BAG53513.1; EAW74449.1; AAH11005.1; AAH12265.1; AAH12318.1; AAH18256.1 

Protein Name

 Cofilin-1 

Protein Synonyms/Alias

 18 kDa phosphoprotein; p18; Cofilin, non-muscle isoform 

Gene Name

 CFL1 

Gene Synonyms/Alias

 CFL 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
13	AVSDGVIKVFNDMKV	acetylation	[1]
13	AVSDGVIKVFNDMKV	ubiquitination	[2, 3, 4, 5]
19	IKVFNDMKVRKSSTP	acetylation	[1]
19	IKVFNDMKVRKSSTP	ubiquitination	[3, 4, 5, 6, 7]
30	SSTPEEVKKRKKAVL	acetylation	[8]
33	PEEVKKRKKAVLFCL	ubiquitination	[4]
34	EEVKKRKKAVLFCLS	ubiquitination	[4]
45	FCLSEDKKNIILEEG	ubiquitination	[6]
53	NIILEEGKEILVGDV	ubiquitination	[4, 6]
73	DPYATFVKMLPDKDC	acetylation	[1]
73	DPYATFVKMLPDKDC	ubiquitination	[3, 5, 6, 7]
92	YDATYETKESKKEDL	acetylation	[1]
92	YDATYETKESKKEDL	ubiquitination	[2, 4, 5, 6, 7]
95	TYETKESKKEDLVFI	ubiquitination	[4, 7]
96	YETKESKKEDLVFIF	ubiquitination	[4, 6, 7]
112	APESAPLKSKMIYAS	ubiquitination	[2, 3, 4, 5, 6, 7, 9]
114	ESAPLKSKMIYASSK	acetylation	[1]
114	ESAPLKSKMIYASSK	ubiquitination	[3, 4, 5, 6, 7]
121	KMIYASSKDAIKKKL	acetylation	[1]
121	KMIYASSKDAIKKKL	ubiquitination	[4, 7, 10]
127	SKDAIKKKLTGIKHE	ubiquitination	[3, 5]
132	KKKLTGIKHELQANC	acetylation	[11, 12]
132	KKKLTGIKHELQANC	ubiquitination	[4]
144	ANCYEEVKDRCTLAE	acetylation	[1]
144	ANCYEEVKDRCTLAE	ubiquitination	[4, 6, 7, 10]
164	AVISLEGKPL*****	ubiquitination	[6, 7]

Reference

 [1] 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]
 [2] 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]
 [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] 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]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] 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]
 [7] 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]
 [8] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [9] 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]
 [10] 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]
 [11] 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]
 [12] Proteome-wide prediction of acetylation substrates.
 Basu A, Rose KL, Zhang J, Beavis RC, Ueberheide B, Garcia BA, Chait B, Zhao Y, Hunt DF, Segal E, Allis CD, Hake SB.
 Proc Natl Acad Sci U S A. 2009 Aug 18;106(33):13785-90. [PMID: 19666589] 

Functional Description

 Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. 

Sequence Annotation

 DOMAIN 4 153 ADF-H.
 MOTIF 30 34 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 3 3 Phosphoserine; by NRK.
 MOD_RES 8 8 Phosphoserine (By similarity).
 MOD_RES 13 13 N6-acetyllysine.
 MOD_RES 25 25 Phosphothreonine.
 MOD_RES 68 68 Phosphotyrosine.
 MOD_RES 73 73 N6-acetyllysine.
 MOD_RES 140 140 Phosphotyrosine.
 MOD_RES 144 144 N6-acetyllysine.
 MOD_RES 156 156 Phosphoserine.  

Keyword

 3D-structure; Acetylation; Actin-binding; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Membrane; Nucleus; Phosphoprotein; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 166 AA 

Protein Sequence

Gene Ontology

 GO:0030864; C:cortical actin cytoskeleton; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
 GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
 GO:0030042; P:actin filament depolymerization; IEA:InterPro.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0000910; P:cytokinesis; IEA:Compara.
 GO:0030010; P:establishment of cell polarity; IEA:Compara.
 GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
 GO:0045087; P:innate immune response; TAS:Reactome.
 GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
 GO:0001755; P:neural crest cell migration; IEA:Compara.
 GO:0001842; P:neural fold formation; IEA:Compara.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0030836; P:positive regulation of actin filament depolymerization; IEA:Compara.
 GO:0006468; P:protein phosphorylation; IEA:Compara.
 GO:0022604; P:regulation of cell morphogenesis; IMP:UniProtKB.
 GO:0043200; P:response to amino acid stimulus; IEA:Compara.
 GO:0009615; P:response to virus; IEP:UniProtKB.
 GO:0007266; P:Rho protein signal transduction; TAS:ProtInc. 

Interpro

 IPR002108; Actin-bd_cofilin/tropomyosin.
 IPR017904; ADF/Cofilin/Destrin.
 IPR027234; Cofilin_1/2. 

Pfam

 PF00241; Cofilin_ADF 

SMART

 SM00102; ADF 

PROSITE

 PS51263; ADF_H 

PRINTS

 PR00006; COFILIN.