WW domain-binding protein 2 (WBP2)
The protein contains 261 amino acids for an estimated molecular weight of 28087 Da.
Acts as transcriptional coactivator of estrogen and progesterone receptors (ESR1 and PGR) upon hormone activation (PubMed:16772533). In presence of estrogen, binds to ESR1-responsive promoters (PubMed:16772533). Required for YAP1 coactivation function on PGR activity (PubMed:16772533). Synergizes with WBP2 in enhancing PGR activity (PubMed:16772533). Modulates expression of post-synaptic scaffolding proteins via regulation of ESR1, ESR2 and PGR (By similarity). (updated: Jan. 31, 2018)
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.
Biological Process
Cellular response to estrogen stimulus
Establishment of protein localization
Positive regulation of gene expression, epigenetic
Positive regulation of histone H3-K14 acetylation
Positive regulation of intracellular estrogen receptor signaling pathway
Positive regulation of transcription by RNA polymerase II
Positive regulation of transcription, DNA-templated
Progesterone receptor signaling pathway
Response to estrogen
Response to progesterone
The reference OMIM entry for this protein is 606962
Ww domain-binding protein 2; wbp2
DESCRIPTION
The globular WW domain is composed of 38 to 40 semiconserved amino acids shared by proteins of diverse functions including structural, regulatory, and signaling proteins. The domain is involved in mediating protein-protein interactions through the binding of polyproline ligands. Thus, its function is similar to that of the Src homology-3 (SH3) domain.CLONING
Using a functional screen of a mouse cDNA expression library, Chen and Sudol (1995) cloned 2 ligands, which they designated Wbp1 (606961) and Wpb2, that bound to the WW domain of human Yes kinase-associated protein (YAP; 606608). Sequence comparison showed no homology between the 2 proteins except in a short proline-rich region containing the invariant residues PPPPY, which the authors designated the PY motif. Wbp1 contains a single PY motif, whereas Wbp2 contains 2 in the forward orientation and 1 in the reverse orientation. A structural similarity between the WW and SH3 domains is a hydrophobic core of conserved aromatic residues surrounded by beta loops containing charged amino acids. Northern blot analysis of multiple human tissues detected Northern blot analysis of multiple human tissues revealed ubiquitous expression of a 2.0-kb WBP2 transcript. Using the partial mouse cDNA as probe, Chen et al. (1997) cloned WBP2 from a human lung fibroblast cDNA library. The cDNA encodes a deduced 268-amino acid protein that shares 94% sequence identity with the mouse protein.GENE FUNCTION
Since Wbp1 contains only a single PY motif, Chen and Sudol (1995) used this as a model protein to characterize interaction between the PY and WW domains. By mutagenesis followed by Western ligand blot analysis, they established that all residues of the PY motif engage in binding the WW domain, and that P2, P3, and Y5 are crucial but not entirely sufficient for optimal binding. Chen et al. (1997) confirmed and refined the consensus PY motif as XPPXW.MAPPING
By FISH, Chen et al. (1997) mapped the WBP2 gene to chromosome 17q25. ... More on the omim web site
Feb. 10, 2018: 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
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 606962 was added.