Twinfilin-2 (TWF2)
The protein contains 349 amino acids for an estimated molecular weight of 39548 Da.
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 (By similarity). (updated: March 4, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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| Variant | Description |
|---|---|
| dbSNP:rs35114109 | |
| dbSNP:rs35711542 | |
| a lung neuroendocrine carcinoma sample |
Biological Process
Actin filament depolymerization
Barbed-end actin filament capping
Cell projection organization
Cellular response to growth factor stimulus
Cellular response to retinoic acid
Negative regulation of actin filament polymerization
Positive regulation of axon extension
Positive regulation of lamellipodium assembly
Positive regulation of neuron projection development
Regulation of actin cytoskeleton organization
Regulation of lamellipodium assembly
Regulation of microvillus length
Sequestering of actin monomers
The reference OMIM entry for this protein is 607433
Twinfilin, drosophila, homolog of, 2; twf2
Protein tyrosine kinase 9-like; ptk9l
A6-related protein; a6rp
CLONING
Using the catalytic domain of rat Pkc-zeta (176982) as bait in a yeast 2-hybrid screen, Rohwer et al. (1999) cloned PTK9L, which they called A6RP, from a human keratinocyte cell line cDNA library. The deduced 349-amino acid protein has a calculated molecular mass of 39.5 kD. PTK9L contains a consensus sequence for actin-depolymerizing proteins and 2 ATP-binding motifs. It shares 64% amino acid identity with the human A6 protein (PTK9), 97% identity with mouse Ptk9l, 34% identity with C. elegans A6, and 26% identity with yeast twinfilin (see 610932). RT-PCR and Western blot analysis detected PTK9L in all human and mouse tissues and cells tested. Immunofluorescence localization revealed spotty accumulation of PTK9L in the cytoplasm close to nuclei.GENE FUNCTION
Rohwer et al. (1999) found that PTK9L was phosphorylated by PKC-zeta, but not significantly by other PKC isoenzymes. It was also phosphorylated by casein kinase II (see 115442) and most effectively by the tyrosine kinase SRC (190090). In accordance with its potential ATP-binding site, PTK9L was able to bind ATP.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the PTK9L gene to chromosome 3 (TMAP stSG1676). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 607433 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed