TWF2

Twinfilin actin binding protein 2
Rendering based on PDB 2VAC​.
Available structures PDB Ortholog search: PDBe, RCSB List of PDB id codes 2VAC​, 2W0I​
Identifiers
Symbols	TWF2 ; A6RP; A6r; MSTP011; PTK9L
External IDs	OMIM: 607433 MGI: 1346078 HomoloGene: 5272 GeneCards: TWF2 Gene
Gene ontology Molecular function • actin monomer binding • protein kinase C binding • ATP binding • phosphatidylinositol-4,5-bisphosphate binding • poly(A) RNA binding Cellular component • cytoplasm • cytoskeleton • myofibril • lamellipodium • filopodium • growth cone • stereocilium • perinuclear region of cytoplasm • extracellular exosome Biological process • positive regulation of lamellipodium assembly • positive regulation of neuron projection development • cell projection organization • negative regulation of actin filament polymerization • regulation of microvillus length • regulation of actin cytoskeleton organization • sequestering of actin monomers • positive regulation of axon extension • barbed-end actin filament capping • cellular response to retinoic acid • cellular response to growth factor stimulus Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	11344	23999
Ensembl	ENSG00000247596	ENSMUSG00000023277
UniProt	Q6IBS0	Q9Z0P5
RefSeq (mRNA)	NM_007284	NM_011876
RefSeq (protein)	NP_009215	NP_036006
Location (UCSC)	Chr 3: 52.23 – 52.24 Mb	Chr 9: 106.2 – 106.22 Mb
PubMed search

Twinfilin-2 is a protein that in humans is encoded by the TWF2 gene.^[1][2][3]

The protein encoded by this gene was identified by its interaction with the catalytic domain of protein kinase C-zeta. The encoded protein contains an actin-binding site and an ATP-binding site. It is most closely related to twinfilin (PTK9), a conserved actin monomer-binding protein.^[3]

References

1. Rohwer A, Kittstein W, Marks F, Gschwendt M (Aug 1999). "Cloning, expression and characterization of an A6-related protein". Eur J Biochem 263 (2): 518–25. doi:10.1046/j.1432-1327.1999.00537.x. PMID 10406962.
2. Vartiainen MK, Sarkkinen EM, Matilainen T, Salminen M, Lappalainen P (Sep 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.
3. "Entrez Gene: TWF2 twinfilin, actin-binding protein, homolog 2 (Drosophila)".

Further reading

• Yamada S, Uchimura E, Ueda T, et al. (2007). "Identification of twinfilin-2 as a factor involved in neurite outgrowth by RNAi-based screen.". Biochem. Biophys. Res. Commun. 363 (4): 926–30. doi:10.1016/j.bbrc.2007.09.069. PMID 17910947.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID 15592455.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• 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. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Wiemann S, Weil B, Wellenreuther R, et al. (2001). "Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs.". Genome Res. 11 (3): 422–35. doi:10.1101/gr.GR1547R. PMC 311072. PMID 11230166.