TWF2

TWF2
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2VAC, 2W0I
Identifiers
Aliases	TWF2 , A6RP, A6r, PTK9L, MSTP011, twinfilin actin binding protein 2
External IDs	OMIM: 607433; MGI: 1346078; HomoloGene: 5272; GeneCards: TWF2; OMA:TWF2 - orthologs
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3p21.2 Start 52,228,612 bp [1] End 52,246,788 bp [1]
Gene location (Mouse) Chr. Chromosome 9 (mouse) [2] Band 9|9 F1 Start 106,080,307 bp [2] End 106,092,588 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in apex of heart muscle of thigh granulocyte gastrocnemius muscle monocyte glutes left ventricle triceps brachii muscle blood mucosa of transverse colon Top expressed in intercostal muscle granulocyte soleus muscle vestibular sensory epithelium interventricular septum thoracic diaphragm medial head of gastrocnemius muscle masseter muscle muscle of thigh digastric muscle More reference expression data BioGPS n/a
Gene ontology Molecular function actin monomer binding protein binding actin binding phosphatidylinositol-4,5-bisphosphate binding ATP binding protein kinase C binding RNA binding cadherin binding actin filament binding Cellular component cell projection filopodium growth cone intracellular anatomical structure stereocilium perinuclear region of cytoplasm extracellular exosome cytoskeleton lamellipodium cytoplasm myofibril actin filament Biological process cellular response to retinoic acid regulation of actin cytoskeleton organization negative regulation of actin filament polymerization cellular response to growth factor stimulus cell projection organization positive regulation of neuron projection development positive regulation of axon extension positive regulation of lamellipodium assembly regulation of microvillus length sequestering of actin monomers barbed-end actin filament capping regulation of lamellipodium assembly actin filament depolymerization 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 – 52.25 Mb Chr 9: 106.08 – 106.09 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Twinfilin-2 is a protein that in humans is encoded by the TWF2 gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000247596 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000023277 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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.
7. "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. S2CID   7200157.
• 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. Bibcode:2002PNAS...9916899M. 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.