UniProt Accession

 PROF1_HUMAN; P07737; Q53Y44 

Genbank Protein ID

 J03191; GU727630; BT007001; AK312168; CR407670; CH471108; CH471108; CH471108; BC002475; BC006768; BC013439; BC015164; BC057828 

Genbank Nucleotide ID

 AAA36486.1; ADU87632.1; AAP35647.1; BAG35102.1; CAG28598.1; EAW90381.1; EAW90383.1; EAW90384.1; AAH02475.1; AAH06768.1; AAH13439.1; AAH15164.1; AAH57828.1 

Protein Name

 Profilin-1 

Protein Synonyms/Alias

 Epididymis tissue protein Li 184a; Profilin I 

Gene Name

 PFN1 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
38	VWAAVPGKTFVNITP	ubiquitination	[1, 2, 3]
54	EVGVLVGKDRSSFYV	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11]
70	GLTLGGQKCSVIRDS	ubiquitination	[1, 2, 3, 6, 7, 8, 9, 10, 11]
91	FSMDLRTKSTGGAPT	ubiquitination	[1, 2, 3, 7, 9, 10, 11]
105	TFNVTVTKTDKTLVL	acetylation	[12, 13, 14]
105	TFNVTVTKTDKTLVL	ubiquitination	[1, 2, 3, 6, 7, 8, 9, 10, 11]
108	VTVTKTDKTLVLLMG	acetylation	[13]
108	VTVTKTDKTLVLLMG	ubiquitination	[1, 2, 7, 11]
116	TLVLLMGKEGVHGGL	ubiquitination	[2]
126	VHGGLINKKCYEMAS	acetylation	[13]
126	VHGGLINKKCYEMAS	ubiquitination	[1, 2, 3, 6, 7, 8, 9, 11]
127	HGGLINKKCYEMASH	ubiquitination	[2]

Reference

 [1] 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]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] 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]
 [4] Quantitative analysis of global ubiquitination in HeLa cells by mass spectrometry.
 Meierhofer D, Wang X, Huang L, Kaiser P.
 J Proteome Res. 2008 Oct;7(10):4566-76. [PMID: 18781797]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] 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]
 [10] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [11] 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]
 [12] 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]
 [13] 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]
 [14] 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 actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Inhibits androgen receptor (AR) and HTT aggregation and binding of G-actin is essential for its inhibition of AR. 

Sequence Annotation

 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 85 85 Phosphoserine.
 MOD_RES 105 105 N6-acetyllysine.
 MOD_RES 108 108 N6-acetyllysine.
 MOD_RES 129 129 Phosphotyrosine.
 MOD_RES 138 138 Phosphoserine; by ROCK1.
 CROSSLNK 54 54 Glycyl lysine isopeptide (Lys-Gly)  

Keyword

 3D-structure; Acetylation; Actin-binding; Amyotrophic lateral sclerosis; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Disease mutation; Isopeptide bond; Neurodegeneration; Phosphoprotein; Reference proteome; Ubl conjugation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 140 AA 

Protein Sequence

Gene Ontology

 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0045202; C:synapse; IEA:Compara.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Compara.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0008219; P:cell death; IEA:UniProtKB-KW.
 GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
 GO:0001843; P:neural tube closure; IEA:Compara.
 GO:0030168; P:platelet activation; TAS:Reactome.
 GO:0002576; P:platelet degranulation; TAS:Reactome.
 GO:0051054; P:positive regulation of DNA metabolic process; IEA:Compara.
 GO:0051496; P:positive regulation of stress fiber assembly; IEA:Compara.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0050434; P:positive regulation of viral transcription; IEA:Compara. 

Interpro

 IPR005454; Profilin_chordates.
 IPR027310; Profilin_CS.
 IPR005455; Profilin_eukaryotes/bac. 

Pfam

 PF00235; Profilin 

SMART

 SM00392; PROF 

PROSITE

 PS00414; PROFILIN 

PRINTS

 PR01639; PROFILINMAML.