Poly(rC)-binding protein 1 (PCBP1)
The protein contains 356 amino acids for an estimated molecular weight of 37498 Da.
Single-stranded nucleic acid binding protein that binds preferentially to oligo dC. In case of infection by poliovirus, plays a role in initiation of viral RNA replication in concert with the viral protein 3CD (PubMed:12414943). (updated: Oct. 25, 2017)
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.
- Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
- 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.
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Biological Process
Gene expression
MRNA splicing, via spliceosome
Positive regulation of transcription by RNA polymerase II
Regulation of gene expression
Regulation of RNA metabolic process
RNA metabolic process
RNA splicing
Viral RNA genome replication
The reference OMIM entry for this protein is 601209
Poly(rc)-binding protein 1; pcbp1
CLONING
Leffers et al. (1995) described the cloning and characterization of 2 cDNAs for poly(rC)-binding proteins, called PCBP1 and PCBP2 (601210) by them. The authors analyzed an EST database for sequences that were predicted to encode a protein with K-homologous (KH) domains. The 60- to 70-amino acid KH motifs are found in several putative nucleic acid binding proteins such as FMR1 (309550) and HNRNPK (600712) and are thought to be involved in RNA binding. Using primers from 1 EST the authors produced a probe that was used to screen a cDNA library of transformed human amnion cells. The cDNA they isolated for PCBP1 encodes a putative 356-amino acid protein that contains 3 KH domains. It is 83% identical to PCBP2 at the DNA level and 90% homologous at the amino acid level. The PCBP1 protein is about 85% similar to the mouse hnRNP-X/mCTBP protein (Hahm et al., 1993). Chkheidze and Liebhaber (2003) determined that endogenous HeLa cell PCBP1 colocalized to nuclear speckles with SC35 (600813). They identified a nuclear localization signal within a 9-amino acid segment between KH2 and KH3. Deletion of this segment blocked nuclear accumulation of PCBP1.GENE FUNCTION
When expressed with a vaccinia virus system in transformed amnion cells, Leffers et al. (1995) found that both PCBP1 and PCBP2 bound poly(rC) when not phosphorylated; phosphorylated protein bound with much lower affinity. By yeast 2-hybrid analysis of a human brain cDNA library, Kosturko et al. (2006) found that mouse Hnrnpa2 (600124) interacted with human HNRNPE1. They confirmed the interaction with in vivo and in vitro protein interaction assays. Hnrnpe1 colocalized with Hnrnpa2 and A2RE mRNA in granules in dendrites of rat oligodendrocytes. Overexpression of HNRNPE1 or microinjection of exogenous HNRNPE1 in rat neural cells inhibited translation of A2RE mRNA, but not translation of mutated A2RE mRNA. Excess HNRNPE1 added to an in vitro translation system reduced translation efficiency of A2RE mRNA in an Hnrnpa2-dependent manner. Kosturko et al. (2006) hypothesized that binding of HNRNPE1 to HNRNPA2 inhibits A2RE mRNA translation during granule transport. Shi et al. (2008) identified PCBP1 in a genetic screen to identify human genes that, when expressed in yeast, could increase the amount of iron loaded into ferritin (see 134790). PCBP1 bound to ferritin in vivo, and bound iron and facilitated iron loading into ferritin in vitro. Depletion of PCBP1 in human cells inhibited ferritin iron loading and increased cytosolic iron pools. Thus, Shi et al. (2008) concluded that PCBP1 can function as a cytosolic iron chaperone in the delivery of iron to ferritin.MAPPING
Transcripts of both PCBPs were detected in all the human tissues analyzed. Tommerup and Leffers (1996) mapped PCBP1 to 2p13-p12 by fluorescence in situ hybridization. ... 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
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 601209 was added.
Jan. 25, 2016: Protein entry updated
Automatic update: model status changed