Poly(A) RNA polymerase GLD2 (TENT2)
The protein contains 484 amino acids for an estimated molecular weight of 56028 Da.
Cytoplasmic poly(A) RNA polymerase that adds successive AMP monomers to the 3'-end of specific RNAs, forming a poly(A) tail. In contrast to the canonical nuclear poly(A) RNA polymerase, it only adds poly(A) to selected cytoplasmic mRNAs (PubMed:15070731). Does not play a role in replication-dependent histone mRNA degradation (PubMed:18172165). Adds a single nucleotide to the 3' end of specific miRNAs, monoadenylation stabilizes and prolongs the activity of some but not all miRNAs (PubMed:23200856). (updated: Sept. 12, 2018)
Protein identification was indicated in the following studies:
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
Biological Process
Dark adaptation
Hematopoietic progenitor cell differentiation
Hippocampus development
Histone mRNA catabolic process
MRNA polyadenylation
MRNA processing
Negative regulation of miRNA catabolic process
Neuron differentiation
Retina development in camera-type eye
RNA 3'-end processing
RNA polyadenylation
RNA stabilization
The reference OMIM entry for this protein is 614121
Poly(a) polymerase-associated domain-containing protein 4; papd4
Gld2
Terminal uridyltransferase 2; tut2
DESCRIPTION
PAPD4 is a poly(A) polymerase (PAP; EC 2.7.7.19). Gld2, the C. elegans ortholog of PAPD4, functions as a cytoplasmic PAP that regulates stem cell fate and is required for stem cells to complete meiosis (Kwak et al., 2004).CLONING
By searching a human database for sequences similar to C. elegans Gld2, followed by PCR of a human breast cancer cell line, Kwak et al. (2004) cloned PAPD4, which they called GLD2. The deduced 484-amino acid protein contains a catalytic domain within a central domain that shares higher similarity with C. elegans cytosolic Gld2 than with canonic nuclear PAP (PAPOLA; 605553). Kwak et al. (2004) also cloned mouse Gld2, which encodes a deduced 484-amino acid protein that shares 93% identity with human GLD2.GENE FUNCTION
Kwak et al. (2004) stated that C. elegans Gld2 has little PAP activity until it is directed to RNA via interaction with Gld3, an RNA-binding protein. They showed that Gld2 tethered to RNA via Ms2, a nonnative RNA-binding protein, efficiently catalyzed polyadenylation of reporter mRNA. Similarly, mouse and human GLD2 catalyzed polyadenylation of reporter mRNA to which they were tethered.MAPPING
Hartz (2011) mapped the PAPD4 gene to chromosome 5q14.1 based on an alignment of the PAPD4 sequence (GenBank GENBANK AK095818) with the genomic sequence (GRCh37). ... More on the omim web site
Oct. 20, 2018: Protein entry updated
Automatic update: OMIM entry 614121 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).