CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013849
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Twinfilin-1 
Protein Synonyms/Alias
  
Gene Name
 Twf1 
Gene Synonyms/Alias
 Ptk9 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
192DAFQALEKLSKRQLNacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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 (By similarity). 
Sequence Annotation
 DOMAIN 2 139 ADF-H 1.
 DOMAIN 175 313 ADF-H 2.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 143 143 Phosphoserine (By similarity).
 MOD_RES 309 309 Phosphotyrosine (By similarity).
 MOD_RES 349 349 Phosphothreonine (By similarity).  
Keyword
 Acetylation; Actin-binding; Complete proteome; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 350 AA 
Protein Sequence
MSHQTGIQAS EDVKEIFARA RNGKYRLLKI SIENEQLVVG SCSPPSDSWE QDYDPFVLPL 60
LEDKQPCYVL FRLDSQNAQG YEWIFIAWSP DHSHVRQKML YAATRATLKK EFGGGHIKDE 120
VFGTVKEDVS LHGYRKYLLS QSSPAPLTAA EEELRQIKIS EVQTDVSVDT KHQTLQGVAF 180
PISRDAFQAL EKLSKRQLNY VQLEIDIKNE TIILANTENT ELKDLPKRIP KDSARYHFFL 240
YKHSHEGDYL ESIVFIYSMP GYTCSIRERM LYSSCKSPLL DIVERQLQMD VIRKIEIDNG 300
DELTADFLYD EVHPKQHAHK QSFAKPKGPA GKRGIRRLIR GPAEAEATTD 350 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IEA:Compara.
 GO:0005911; C:cell-cell junction; IEA:Compara.
 GO:0030175; C:filopodium; IEA:Compara.
 GO:0030016; C:myofibril; IEA:Compara.
 GO:0048471; C:perinuclear region of cytoplasm; IEA:Compara.
 GO:0032587; C:ruffle membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:Compara.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Compara.
 GO:0004713; F:protein tyrosine kinase activity; IEA:Compara.
 GO:0051016; P:barbed-end actin filament capping; IEA:Compara.
 GO:0043538; P:regulation of actin phosphorylation; IEA:Compara.
 GO:0042989; P:sequestering of actin monomers; IEA:Compara. 
Interpro
 IPR002108; Actin-bd_cofilin/tropomyosin. 
Pfam
 PF00241; Cofilin_ADF 
SMART
 SM00102; ADF 
PROSITE
 PS51263; ADF_H 
PRINTS