CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024061
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Twinfilin-2 
Protein Synonyms/Alias
 A6-related protein; mA6RP; Twinfilin-1-like protein 
Gene Name
 Twf2 
Gene Synonyms/Alias
 Ptk9l 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
14IHATEELKEFFAKARacetylation[1]
98DNSPVRLKMLYAATRacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 
Functional Description
 Actin-binding protein involved in motile and morphological processes. Inhibits actin polymerization, likely by sequestering G-actin. By capping the barbed ends of filaments, it also regulates motility. Seems to play an important role in clathrin-mediated endocytosis and distribution of endocytic organelles. May play a role in regulating the mature length of the middle and short rows of stereocilia. 
Sequence Annotation
 DOMAIN 4 139 ADF-H 1.
 DOMAIN 177 313 ADF-H 2.
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 14 14 N6-acetyllysine (By similarity).
 MOD_RES 19 19 N6-acetyllysine (By similarity).
 MOD_RES 309 309 Phosphotyrosine.
 MOD_RES 349 349 Phosphoserine (By similarity).  
Keyword
 Acetylation; Actin-binding; Alternative promoter usage; Cell projection; Cilium biogenesis/degradation; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Direct protein sequencing; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 349 AA 
Protein Sequence
MAHQTGIHAT EELKEFFAKA RAGSIRLIKV IIEDEQLVLG ASQEPVGRWD QDYDRAVLPL 60
LDAQEPCYLL FRLDSQNAQG FEWLFLAWSP DNSPVRLKML YAATRATVKK EFGGGHIKDE 120
LFGTVKDDLS LAGYQKHLSS CAAPAPLTSA ERELQQIRIN EVKTEISVES KHQTLQGLAF 180
PLQPEAQRAL QQLKQKTVNY IQLKLDLERE TIELVHTEPT NVAQLPSRIP RDAARYHFFL 240
YKHTHEGDAL ESVVFIYSMP GYKCSIKERM LYSSCKSRLL DSVEQDFQLE IAKKIEIGDG 300
AELTAEFLYD EVHPKQHAFK QAFAKPKGPG GKRGHKRLIR GPGENGEDS 349 
Gene Ontology
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0030175; C:filopodium; IDA:BHF-UCL.
 GO:0030426; C:growth cone; IEA:Compara.
 GO:0030027; C:lamellipodium; IDA:BHF-UCL.
 GO:0030016; C:myofibril; IDA:BHF-UCL.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
 GO:0032420; C:stereocilium; IDA:BHF-UCL.
 GO:0003785; F:actin monomer binding; IDA:BHF-UCL.
 GO:0005524; F:ATP binding; ISA:MGI.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:BHF-UCL.
 GO:0005080; F:protein kinase C binding; ISA:MGI.
 GO:0051016; P:barbed-end actin filament capping; IDA:BHF-UCL.
 GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
 GO:0071363; P:cellular response to growth factor stimulus; IEA:Compara.
 GO:0071300; P:cellular response to retinoic acid; IEA:Compara.
 GO:0035556; P:intracellular signal transduction; ISA:MGI.
 GO:0030837; P:negative regulation of actin filament polymerization; IDA:BHF-UCL.
 GO:0045773; P:positive regulation of axon extension; IEA:Compara.
 GO:0010592; P:positive regulation of lamellipodium assembly; IEA:Compara.
 GO:0010976; P:positive regulation of neuron projection development; IEA:Compara.
 GO:0032532; P:regulation of microvillus length; IC:BHF-UCL.
 GO:0042989; P:sequestering of actin monomers; IDA:BHF-UCL. 
Interpro
 IPR002108; Actin-bd_cofilin/tropomyosin. 
Pfam
 PF00241; Cofilin_ADF 
SMART
 SM00102; ADF 
PROSITE
 PS51263; ADF_H 
PRINTS