Talin-2 (TLN2)
The protein contains 2542 amino acids for an estimated molecular weight of 271613 Da.
As a major component of focal adhesion plaques that links integrin to the actin cytoskeleton, may play an important role in cell adhesion. Recruits PIP5K1C to focal adhesion plaques and strongly activates its kinase activity (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.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
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.
This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.
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Biological Process
Cell adhesion
Cell-cell adhesion
Cell-cell junction assembly
Obsolete cytoskeletal anchoring at plasma membrane
The reference OMIM entry for this protein is 607349
Talin 2; tln2
Kiaa0320
CLONING
By randomly sequencing clones from a brain cDNA library, Nagase et al. (1997) obtained a partial cDNA encoding TLN2, which they called KIAA0320. RT-PCR detected expression in heart, brain, kidney, thymus, testis, and small intestine. Using genomic and cDNA/EST sequences, Monkley et al. (2001) assembled the complete coding sequence for TLN2. The deduced 2,532-amino acid protein contains a FERM domain. In TLN1 (186745), the FERM domain binds the cytodomains of beta-1 (135630) and beta-3 (173470) integrins, as well as to F-actin (see 102610) and other proteins. TLN2 shares 74% identity with TLN1, and the N- and C-terminal regions of TLN2 are highly conserved across species. Analysis of EST databases indicated that both TLN1 and TLN2 are expressed in brain, lung, heart, eye, mammary gland, colon, stomach, lymphocytes, germ cells, liver, spleen, bone, and many tumors. Northern blot analysis of adult mouse tissues revealed multiple Tln2 transcripts, with highest expression in heart and undetectable expression in spleen.GENE FUNCTION
DiPaolo et al. (2002) and Ling et al. (2002) presented evidence that talin, through its FERM domain, interacts with the C-terminal tail of the 90-kD PIP5K1C (606102) isoform. DiPaolo et al. (2002) determined that, in rat brain, the predominant talin that interacts with PIP5K1C is Tln2. The authors showed that this interaction induces clustering of PIP5K1C and talin at focal adhesions and increases the local production of phosphatidylinositol-4,5-bisphosphate.GENE STRUCTURE
Monkley et al. (2001) determined that the TLN2 gene contains 55 exons and spans about 190 kb. Chu et al. (2014) identified the gene encoding microRNA-190A (MIR190A; 615845) within an intron of the TLN2 gene. However, they found that MIR190A expression was independent of TLN2 expression.MAPPING
By radiation hybrid analysis, Nagase et al. (1997) mapped the TLN2 gene to chromosome 15. By genomic sequence analysis, Monkley et al. (2001) mapped the TLN2 gene to chromosome 15q15-q21. Chu et al. (2014) mapped the TLN2 gene to chromosome 15q22.2 by genomic sequence analysis. ... 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 607349 was added.