Polyadenylate-binding protein-interacting protein 1 (PAIP1)
The protein contains 479 amino acids for an estimated molecular weight of 53525 Da.
Acts as a coactivator in the regulation of translation initiation of poly(A)-containing mRNAs. Its stimulatory activity on translation is mediated via its action on PABPC1. Competes with PAIP2 for binding to PABPC1. Its association with EIF4A and PABPC1 may potentiate contacts between mRNA termini. May also be involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. (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.
- 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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The reference OMIM entry for this protein is 605184
Polyadenylate-binding protein-interacting protein 1; paip1
Poly(a)-binding protein-interacting protein 1
Pabp-interacting protein 1
DESCRIPTION
In initiation of translation in eukaryotes, binding of the small ribosomal subunit to mRNA requires recognition of the 5-prime cap structure by the cap-binding complex eIF4F. eIF4F consists of eIF4E (133440), eIF4A (see 602641), and eIF4G (see 600495). Translation initiation is further regulated by the mRNA 3-prime poly(A) tail and the poly(A)-binding protein (PABC1; 604679). PAIP1 interacts with PABC1 and some eIF4 complexes.CLONING
By Far Western blot analysis of HeLa cell extracts and a placenta cDNA library using a PABC1 probe, Craig et al. (1998) identified a cDNA encoding PAIP1 (PABC1-interacting protein-1). Sequence analysis of the deduced 480-amino acid PAIP1 protein predicted that it shares 39% amino acid similarity with the central portion of eIF4G, which contains an eIF4A-binding region. PAIP1 also contains a proline-rich N terminus. SDS-PAGE analysis determined that PAIP1 is expressed as a 70-kD protein.GENE FUNCTION
Binding analysis by Craig et al. (1998) showed that PAIP1 binds strongly to poly(A) only in the presence of PABC1. Immunoprecipitation and Western blot analysis demonstrated that in HeLa extracts, the C terminus of PAIP1 interacts with PABC1, and PAIP1 interacts with eIF4A but not eIF4G complexes. AU-rich elements and protein-coding determinants direct rapid removal of poly(A) tails as a necessary first step in mRNA decay. Grosset et al. (2000) determined that 5 proteins form a multiprotein complex associated with the major protein-coding-region determinant of instability (mCRD) of the FOS gene (164810): PABP, HNRNPD (601324), PAIP1, NSAP1, and UNR (191510). Overexpression of these proteins stabilized mCRD-containing mRNA by impeding deadenylation. ... 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 605184 was added.
Feb. 24, 2016: Protein entry updated
Automatic update: model status changed