Fascin (FSCN1)
The protein contains 493 amino acids for an estimated molecular weight of 54530 Da.
Actin-binding protein that contains 2 major actin binding sites (PubMed:21685497, PubMed:23184945). Organizes filamentous actin into parallel bundles (PubMed:20393565, PubMed:21685497, PubMed:23184945). Plays a role in the organization of actin filament bundles and the formation of microspikes, membrane ruffles, and stress fibers (PubMed:22155786). Important for the formation of a diverse set of cell protrusions, such as filopodia, and for cell motility and migration (PubMed:20393565, PubMed:21685497, PubMed:23184945). Mediates reorganization of the actin cytoskeleton and axon growth cone collapse in response to NGF (PubMed:22155786). (updated: July 3, 2019)
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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
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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Biological Process
Actin cytoskeleton organization
Actin filament bundle assembly
Anatomical structure morphogenesis
Cell migration
Cell motility
Cell population proliferation
Cell-cell junction assembly
Cytokine-mediated signaling pathway
Establishment of apical/basal cell polarity
Establishment or maintenance of cell polarity
Microspike assembly
Parallel actin filament bundle assembly
Positive regulation of extracellular matrix disassembly
Positive regulation of filopodium assembly
Positive regulation of lamellipodium assembly
Positive regulation of podosome assembly
Regulation of actin cytoskeleton organization
Regulation of microvillus assembly
The reference OMIM entry for this protein is 602689
Fascin actin-bundling protein 1; fscn1
Fascin, sea urchin, homolog of, 1
Singed, drosophila, homolog of; snl
Actin-bundling protein, 55-kd
P55
CLONING
Sea urchin fascin, one of the first actin-bundling proteins extensively characterized, can crosslink actin filaments in vitro (Bryan and Kane, 1982). The cloning of a fascin cDNA by Bryan et al. (1993) showed that fascin is homologous to the Drosophila singed gene product. Duh et al. (1994) isolated cDNAs encoding the human homolog of sea urchin fascin and Drosophila singed, called HSN by them, from a human teratocarcinoma cDNA library. The HSN mRNA was expressed at various levels in all human tissues analyzed and at high levels in actively growing renal carcinoma cell lines and in activated but not in resting lymphocytes, suggesting a functional role for HSN in proliferation. The HSN gene is predicted to encode a 493-amino acid protein with a molecular mass of 55 kD. Based on peptide sequence identity and immunocrossreactivity, Duh et al. (1994) indicated that the HSN protein is the 55-kD actin-bundling protein purified from HeLa cells (Yamashiro-Matsumura and Matsumura, 1985).GENE FUNCTION
Yamashiro-Matsumura and Matsumura (1986) suggested that the 55-kD HSN protein is involved in the assembly of actin filament bundles present in microspikes, membrane ruffles, and stress fibers. Yamakita et al. (1996) demonstrated that the actin-binding and -bundling activities of SNL are inhibited by phosphorylation. SNL is phosphorylated in vivo upon treatment with 12-O-tetradecanoylphorbol-13-acetate, a tumor promoter. The phosphorylation gradually increases, concomitant with the disappearance of SNL from stress fibers, microspikes, and membrane ruffles. Ono et al. (1997) identified serine-39 as the major site of SNL phosphorylation. This site is highly conserved among all fascin homologs. Substitution of serine-39 with alanine eliminated the phosphorylation-dependent regulation of the actin-binding activity of SNL, indicating that phosphorylation at this site regulates the actin-binding ability of SNL. Ono et al. (1997) found that the C-terminal half of SNL contains an actin-binding domain. Using immunofluorescence microscopy and Western blot analysis, Mosialos et al. (1996) demonstrated that an anti-p55 antibody reacted with nearly all purified dendritic cells but not with other blood leukocytes. Expression of p55 colocalized with actin. Immunohistochemistry indicated that p55 is expressed in dendritic cells in lymph node T-cell zones. Sonderbye et al. (1997) used flow cytometric and immunohistochemical analyses to show that expression of fascin is rare in CD34 (142230)-positive progenitor cells but that cytoplasmic expression increases with differentiation in culture until nearly all dendritic cells are fascin-positive. Using immunohistochemistry, Pinkus et al. (1997) found that nearly all Reed-Sternberg cells in Hodgkin disease (236000), except in the nodular lymphocyte predominance type, express fascin. They proposed that fascin expression may be helpful in distinguishing Hodgkin from non-Hodgkin lymphoma and suggested that Reed-Sternberg cells may have a dendritic cell derivation. By in vivo selection, transcriptomic analysis, functional verification, and clinical validation, Minn et al. (2005) identified a set of genes that marks and mediates breast cancer metastasis to the lungs. Some of these genes serve dual functions, providing growth advantages both in the primary tumor and in the lung microenvironment. Others contribute to aggressive growth selectivity in the lung. Two that were not functionally validated ... More on the omim web site
July 4, 2019: Protein entry updated
Automatic update: Entry updated from uniprot information.
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 602689 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed