Ankyrin repeat domain-containing protein 54 (ANKRD54)
The protein contains 300 amino acids for an estimated molecular weight of 32505 Da.
Plays an important role in regulating intracellular signaling events associated with erythroid terminal differentiation. (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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No binding partner found
The reference OMIM entry for this protein is 613383
Ankyrin repeat domain-containing protein 54; ankrd54
Lyn-interacting ankyrin repeat protein; liar
CLONING
Samuels et al. (2009) cloned mouse Ankrd54, which they called Liar. The deduced 299-amino acid protein has an N-terminal ATP-binding P loop, followed by a nuclear localization signal, 4 ankyrin (see 612641) repeats, and a C-terminal nuclear export signal. It has several potential serine phosphorylation sites. Mouse and human LIAR share 92% amino acid identity. Northern blot analysis detected variable Liar expression in all mouse tissues examined, with highest expression in testis. Variable mRNA and protein expression was also detected in all erythropoietic cell lines examined. In situ hybridization of mouse embryos at embryonic day 10 revealed Liar expression in brachial arches, maxillary process, fore and hind limb buds, and gastrointestinal tract.GENE FUNCTION
Samuels et al. (2009) showed that mouse Lyn (165120) and Liar interacted in a yeast 2-hybrid screen. Liar was not a substrate for Lyn kinase activity. Domain analysis revealed that the SH3 domain of Lyn and the ankyrin repeat domain of Liar were required for the interaction. Lyn and Liar formed a multiprotein complex with Hs1 (HCLS1; 601306) in mouse erythroid cells. Samuels et al. (2009) observed a transient translocation and accumulation of Liar within the nuclear compartment that was associated with terminal differentiation in mouse erythroid cells, and expression of Liar decreased following differentiation. Overexpression of Liar inhibited erythroid differentiation and altered erythropoietin (EPO; 133170) signaling via Erk2 (MAPK1; 176948), Stat5 (STAT5A; 601511), Akt (see 164730), and Lyn.MAPPING
By genomic sequence analysis, Samuels et al. (2009) mapped the ANKRD54 gene to chromosome 22q13.1. They mapped the mouse Ankrd54 gene to a region of chromosome 15 that shares homology of synteny with human chro0mosome 22q13.1. ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
June 20, 2017: Protein entry updated
Automatic update: comparative model was added.
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 613383 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed