TWF1

Twinfilin-1 is a protein that in humans is encoded by the TWF1 gene. This gene encodes twinfilin, an actin monomer-binding protein conserved from yeast to mammals. Studies of the mouse counterpart suggest that this protein may be an actin monomer-binding protein, and its localization to cortical G-actin-rich structures may be regulated by the small GTPase RAC1.

TWF1
Identifiers
Aliases	TWF1, A6, PTK9, twinfilin actin binding protein 1
External IDs	OMIM: 610932; MGI: 1100520; HomoloGene: 48140; GeneCards: TWF1; OMA:TWF1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) Band 12q12 Start 43,793,723 bp End 43,806,328 bp
Gene location (Mouse) Chr. Chromosome 15 (mouse) Band 15|15 E3 Start 94,475,832 bp End 94,487,770 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in secondary oocyte palpebral conjunctiva seminal vesicula gingival epithelium epithelium of nasopharynx Achilles tendon oral cavity jejunal mucosa islet of Langerhans rectum Top expressed in utricle vestibular sensory epithelium stroma of bone marrow endothelial cell of lymphatic vessel Paneth cell vestibular membrane of cochlear duct transitional epithelium of urinary bladder cumulus cell olfactory epithelium ileum More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein-containing complex binding protein tyrosine kinase activity ATP binding actin monomer binding phosphatidylinositol-4,5-bisphosphate binding cadherin binding actin binding protein binding actin filament binding Cellular component intracellular anatomical structure cytoskeleton focal adhesion filopodium actin cytoskeleton cell-cell junction perinuclear region of cytoplasm myofibril ruffle membrane cytoplasm cytosol actin filament Biological process regulation of actin phosphorylation barbed-end actin filament capping sequestering of actin monomers negative regulation of actin filament polymerization positive regulation of cardiac muscle hypertrophy regulation of lamellipodium assembly positive regulation of neuron projection development peptidyl-tyrosine phosphorylation actin filament depolymerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 5756 19230 Ensembl ENSG00000151239 ENSMUSG00000022451 UniProt Q12792 Q91YR1 RefSeq (mRNA) NM_001242397 NM_002822 NM_198974 NM_008971 RefSeq (protein) NP_001229326 NP_002813 NP_032997 NP_001389738 NP_001389739 Location (UCSC) Chr 12: 43.79 – 43.81 Mb Chr 15: 94.48 – 94.49 Mb PubMed search
Wikidata
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Further reading

• Palmgren S, Vartiainen M, Lappalainen P (2002). "Twinfilin, a molecular mailman for actin monomers". J. Cell Sci. 115 (Pt 5): 881–6. doi:10.1242/jcs.115.5.881. PMID 11870207.
• Hassel S, Eichner A, Yakymovych M, et al. (2004). "Proteins associated with type II bone morphogenetic protein receptor (BMPR-II) and identified by two-dimensional gel electrophoresis and mass spectrometry". Proteomics. 4 (5): 1346–58. doi:10.1002/pmic.200300770. PMID 15188402. S2CID 6773754.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Vartiainen MK, Sarkkinen EM, Matilainen T, et al. (2003). "Mammals have two twinfilin isoforms whose subcellular localizations and tissue distributions are differentially regulated". J. Biol. Chem. 278 (36): 34347–55. doi:10.1074/jbc.M303642200. PMID 12807912.
• Galey D, Becker K, Haughey N, et al. (2003). "Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes". J. Neurovirol. 9 (3): 358–71. doi:10.1080/13550280390201119. PMID 12775419. S2CID 22016092.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Ojala PJ, Paavilainen VO, Vartiainen MK, et al. (2003). "The two ADF-H domains of twinfilin play functionally distinct roles in interactions with actin monomers". Mol. Biol. Cell. 13 (11): 3811–21. doi:10.1091/mbc.E02-03-0157. PMC 133594. PMID 12429826.
• Paavilainen VO, Merckel MC, Falck S, et al. (2003). "Structural conservation between the actin monomer-binding sites of twinfilin and actin-depolymerizing factor (ADF)/cofilin". J. Biol. Chem. 277 (45): 43089–95. doi:10.1074/jbc.M208225200. PMID 12207032.