CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006409
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Profilin-2 
Protein Synonyms/Alias
 Profilin II 
Gene Name
 PFN2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
91CTMDIRTKSQGGEPTubiquitination[1, 2, 3]
127HGGGLNKKAYSMAKYubiquitination[4, 5]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] 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]
 [5] 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
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. 
Sequence Annotation
 MOD_RES 99 99 Phosphotyrosine (By similarity).  
Keyword
 3D-structure; Actin-binding; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 140 AA 
Protein Sequence
MAGWQSYVDN LMCDGCCQEA AIVGYCDAKY VWAATAGGVF QSITPIEIDM IVGKDREGFF 60
TNGLTLGAKK CSVIRDSLYV DGDCTMDIRT KSQGGEPTYN VAVGRAGRVL VFVMGKEGVH 120
GGGLNKKAYS MAKYLRDSGF 140 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; NAS:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0043195; C:terminal bouton; IEA:Compara.
 GO:0003779; F:actin binding; NAS:UniProtKB.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; NAS:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; IEA:InterPro.
 GO:0030837; P:negative regulation of actin filament polymerization; IEA:Compara.
 GO:0030838; P:positive regulation of actin filament polymerization; IEA:Compara.
 GO:0008064; P:regulation of actin polymerization or depolymerization; NAS:UniProtKB.
 GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Compara. 
Interpro
 IPR005454; Profilin_chordates.
 IPR027310; Profilin_CS.
 IPR005455; Profilin_eukaryotes/bac. 
Pfam
 PF00235; Profilin 
SMART
 SM00392; PROF 
PROSITE
 PS00414; PROFILIN 
PRINTS
 PR00392; PROFILIN.
 PR01639; PROFILINMAML.