Details for: PABPC1
Gene ID: 26986
Gene Type: Protein-coding - A gene that serves as a template for producing a messenger RNA (mRNA) molecule, which is then translated into a functional protein.
Symbol: PABPC1
Ensembl ID: ENSG00000070756
Description: poly(A) binding protein cytoplasmic 1
Selected Context(s): Overall
Cell Significance Landscape
Associated with
Significant Cells
Cell Significance Index (CSI) scores for the chosen context(s)
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CSI 145.35rCSI 96.61%PRS 1.93
-
CSI 138.75rCSI 93.48%PRS 1.96
-
CSI 127.9rCSI 89.3%PRS 1.71
-
CSI 124.73rCSI 96.1%PRS 1.46
-
CSI 124.6rCSI 87.51%PRS 4.96
-
CSI 123.19rCSI 92.56%PRS 1.67
-
CSI 118.58rCSI 85.12%PRS 2.21
-
CSI 118.22rCSI 69.82%PRS 2.27
-
CSI 118.16rCSI 88.6%PRS 4.9
-
CSI 117.23rCSI 94.79%PRS 1.59
-
CSI 116.34rCSI 86.85%PRS 2.75
-
CSI 115.13rCSI 87.09%PRS 2.27
-
CSI 114.26rCSI 79.44%PRS 1.89
-
CSI 110.88rCSI 82.38%PRS 2.42
-
CSI 109.16rCSI 81.69%PRS 2.66
-
CSI 106.33rCSI 92.07%PRS 1.81
-
CSI 105.65rCSI 73.52%PRS 2.37
-
CSI 105.07rCSI 94.88%PRS 1.43
-
CSI 104.97rCSI 69.96%PRS 4.61
-
CSI 104.59rCSI 96.5%PRS 1.64
-
CSI 103.91rCSI 86.14%PRS 1.51
-
CSI 103.8rCSI 89.03%PRS 5.28
-
CSI 102.89rCSI 89.44%PRS 2
-
CSI 102.15rCSI 85.62%PRS 1.95
-
CSI 100.95rCSI 78.26%PRS 1.55
-
CSI 98.24rCSI 94.48%PRS 3.55
-
CSI 97.39rCSI 85.54%PRS 1.81
-
CSI 95.24rCSI 76.95%PRS 4.26
-
CSI 91.6rCSI 72.73%PRS 2.89
-
CSI 91.51rCSI 90.37%PRS 7.21
-
CSI 91.35rCSI 75.65%PRS 1.62
-
CSI 90.99rCSI 79.7%PRS 2.19
-
CSI 89.43rCSI 91.15%PRS 2.36
-
CSI 87.62rCSI 70.18%PRS 3.04
-
CSI 86.9rCSI 68.37%PRS 1.93
-
CSI 86.1rCSI 88.58%PRS 2.58
-
CSI 85.48rCSI 66.49%PRS 2.33
-
CSI 85.33rCSI 89.04%PRS 1.66
-
CSI 85.26rCSI 71.73%PRS 2.74
-
CSI 83.77rCSI 80.77%PRS 0.41
-
CSI 82.71rCSI 86.44%PRS 1.75
-
CSI 81.9rCSI 66.55%PRS 1.69
-
CSI 81.13rCSI 78.1%PRS 1.69
-
CSI 80.16rCSI 83.72%PRS 5.24
-
CSI 79.42rCSI 68.47%PRS 2.72
-
CSI 79.16rCSI 73.18%PRS 2.98
-
CSI 77.84rCSI 61.53%PRS 1.13
-
CSI 77.4rCSI 71.07%PRS 1.85
-
CSI 76.58rCSI 58.25%PRS 2.15
-
CSI 75.63rCSI 67.13%PRS 1.63
-
CSI 75.36rCSI 78.94%PRS 1.52
-
CSI 74.68rCSI 87.71%PRS 1.98
-
CSI 74.49rCSI 86.39%PRS 2.43
-
CSI 74.41rCSI 89.88%PRS 1.86
-
CSI 73.87rCSI 76.52%PRS 1.9
-
CSI 73.12rCSI 83.71%PRS 3.38
-
CSI 73.12rCSI 85.88%PRS 16.53
-
CSI 70.57rCSI 58.91%PRS 5.45
-
CSI 70.3rCSI 88.34%PRS 8.96
-
CSI 70.06rCSI 87.26%PRS 2.4
-
CSI 69.13rCSI 88.66%PRS 1.88
-
CSI 68.13rCSI 64.38%PRS 1.7
-
CSI 67.87rCSI 66.71%PRS 4.86
-
CSI 67.7rCSI 67.56%PRS 1.36
-
CSI 67.19rCSI 97.34%PRS 2.38
-
CSI 66.77rCSI 58.71%PRS 1.18
-
CSI 65.95rCSI 82.76%PRS 2.06
-
CSI 63.67rCSI 81.44%PRS 7.56
-
CSI 63.66rCSI 81.47%PRS 35.42
-
CSI 63.63rCSI 86.68%PRS 4.08
-
CSI 61.66rCSI 88.93%PRS 2.25
-
CSI 61.43rCSI 91.07%PRS 19.43
-
CSI 61.31rCSI 65.15%PRS 2.96
-
CSI 61.18rCSI 92.32%PRS 1.59
-
CSI 60.93rCSI 93.58%PRS 1.88
-
CSI 60.76rCSI 80.75%PRS 1.78
-
CSI 59.5rCSI 85.76%PRS 2.64
-
CSI 59.49rCSI 58.51%PRS 1.8
-
CSI 59.44rCSI 44.02%PRS 1.55
-
CSI 58.66rCSI 72.28%PRS 5.39
-
CSI 58.29rCSI 72.11%PRS 1.43
-
CSI 57.79rCSI 69.37%PRS 1.62
-
CSI 57.44rCSI 100%PRS 1.57
-
CSI 57rCSI 87.06%PRS 2.85
-
CSI 56.81rCSI 57.54%PRS 10.89
-
CSI 56.69rCSI 86.58%PRS 1.65
-
CSI 56.38rCSI 82.49%PRS 1.72
-
CSI 56.09rCSI 69.76%PRS 1.74
-
CSI 55.64rCSI 85.5%PRS 2.36
-
CSI 55.5rCSI 88.95%PRS 5.39
-
CSI 55.08rCSI 76.29%PRS 2.34
-
CSI 54.74rCSI 100%PRS 1.77
-
CSI 54.67rCSI 63.22%PRS 1.18
-
CSI 54.61rCSI 93.55%PRS 2.17
-
CSI 54.12rCSI 68.04%PRS 2.5
-
CSI 53.49rCSI 49.78%PRS 1.62
-
CSI 53.47rCSI 78.32%PRS 1.92
-
CSI 53.4rCSI 71.45%PRS 9.99
-
CSI 53.07rCSI 77.82%PRS 2.15
-
CSI 52.9rCSI 84.02%PRS 2.13
-
CSI -32.5rCSI -60.9%PRS 1.4%
-
CSI -25.9rCSI -58.0%PRS 1.1%
-
CSI -25.8rCSI -67.2%PRS 2.0%
-
CSI -24.3rCSI -91.5%PRS 3.9%
-
CSI -22.9rCSI -38.5%PRS 1.1%
-
CSI -21.9rCSI -68.5%PRS 1.3%
-
CSI -21.0rCSI -85.7%PRS 2.3%
-
CSI -18.9rCSI -90.6%PRS 2.9%
-
CSI -18.3rCSI -32.1%PRS 1.4%
-
CSI -16.1rCSI -37.7%PRS 3.0%
-
CSI -15.6rCSI -35.9%PRS 1.7%
-
CSI -13.5rCSI -21.8%PRS 1.3%
-
CSI -13.5rCSI -25.7%PRS 2.6%
-
CSI -12.7rCSI -22.0%PRS 1.3%
-
CSI -12.4rCSI -48.5%PRS 10.2%
-
CSI -12.0rCSI -57.6%PRS 0.8%
-
CSI -11.9rCSI -14.8%PRS 1.0%
-
CSI -11.7rCSI -45.5%PRS 2.9%
-
CSI -11.5rCSI -38.6%PRS 1.8%
-
CSI -11.2rCSI -38.3%PRS 2.4%
-
CSI -7.8rCSI -14.1%PRS 1.9%
-
CSI -7.2rCSI -12.7%PRS 2.2%
-
CSI -6.7rCSI -21.4%PRS 1.3%
-
CSI -5.0rCSI -25.1%PRS 13.1%
-
CSI -5.0rCSI -65.7%PRS 17.3%
-
CSI -4.8rCSI -17.4%PRS 1.0%
-
CSI -4.7rCSI -14.7%PRS 1.1%
-
CSI -4.6rCSI -20.4%PRS 1.7%
-
CSI -4.6rCSI -77.4%PRS 9.4%
-
CSI -4.6rCSI -9.4%PRS 2.0%
-
CSI -4.5rCSI -5.7%PRS 2.2%
-
CSI -3.4rCSI -8.2%PRS 2.1%
-
CSI -2.7rCSI -8.9%PRS 3.0%
-
CSI -2.7rCSI -4.7%PRS 1.0%
-
CSI -2.5rCSI -6.7%PRS 1.7%
-
CSI -2.5rCSI -13.4%PRS 13.0%
-
CSI -2.2rCSI -16.5%PRS 0.8%
-
CSI -1.6rCSI -10.3%PRS 1.4%
-
CSI -1.1rCSI -3.7%PRS 1.5%
-
CSI -1.0rCSI -4.9%PRS 3.4%
-
CSI -1.0rCSI -19.6%PRS 2.3%
-
CSI -0.9rCSI -3.7%PRS 4.8%
-
CSI -0.9rCSI -4.7%PRS 7.7%
-
CSI -0.9rCSI -3.7%PRS 2.0%
-
CSI -0.9rCSI -17.4%PRS 14.1%
-
CSI -0.8rCSI -15.8%PRS 2.2%
-
CSI -0.8rCSI -11.0%PRS 21.4%
-
CSI -0.5rCSI -1.2%PRS 1.8%
-
CSI -0.5rCSI -1.5%PRS 0.9%
-
CSI 0.2rCSI 2.3%PRS 25.1%
-
CSI 0.2rCSI 3.3%PRS 26.6%
-
CSI 0.5rCSI 6.3%PRS 11.7%
-
CSI 0.5rCSI 6.0%PRS 7.1%
-
CSI 0.5rCSI 10.8%PRS 42.5%
-
CSI 0.8rCSI 2.8%PRS 7.7%
-
CSI 0.9rCSI 1.2%PRS 1.9%
-
CSI 0.9rCSI 1.9%PRS 1.2%
-
CSI 1.0rCSI 29.4%PRS 30.5%
-
CSI 1.0rCSI 2.4%PRS 1.1%
-
CSI 1.0rCSI 16.6%PRS 18.7%
-
CSI 1.1rCSI 1.5%PRS 1.1%
-
CSI 1.3rCSI 7.4%PRS 9.7%
-
CSI 1.8rCSI 2.1%PRS 1.1%
-
CSI 2.1rCSI 5.8%PRS 2.3%
-
CSI 2.2rCSI 5.5%PRS 3.1%
-
CSI 2.2rCSI 5.6%PRS 1.3%
-
CSI 2.3rCSI 13.1%PRS 2.5%
-
CSI 2.3rCSI 45.2%PRS 6.0%
-
CSI 2.4rCSI 57.2%PRS 0.9%
-
CSI 2.4rCSI 15.5%PRS 4.7%
-
CSI 2.4rCSI 14.3%PRS 1.3%
-
CSI 2.5rCSI 60.5%PRS 1.3%
-
CSI 2.6rCSI 3.7%PRS 1.4%
-
CSI 2.7rCSI 42.9%PRS 41.0%
-
CSI 2.7rCSI 61.4%PRS 9.9%
-
CSI 2.8rCSI 7.2%PRS 2.6%
-
CSI 2.8rCSI 25.0%PRS 15.9%
-
CSI 2.8rCSI 72.4%PRS 10.3%
-
CSI 2.8rCSI 74.2%PRS 9.5%
-
CSI 2.9rCSI 31.7%PRS 11.5%
-
CSI 2.9rCSI 73.1%PRS 16.2%
-
CSI 3.0rCSI 88.7%PRS 4.2%
-
CSI 3.0rCSI 63.1%PRS 33.1%
-
CSI 3.0rCSI 8.1%PRS 2.5%
-
CSI 3.0rCSI 26.2%PRS 12.0%
-
CSI 3.2rCSI 75.4%PRS 1.1%
-
CSI 3.2rCSI 13.5%PRS 5.8%
-
CSI 3.3rCSI 4.7%PRS 2.5%
-
CSI 3.4rCSI 78.5%PRS 12.1%
-
CSI 3.4rCSI 19.7%PRS 2.6%
-
CSI 3.5rCSI 87.2%PRS 5.9%
-
CSI 3.6rCSI 11.5%PRS 2.1%
-
CSI 3.7rCSI 54.8%PRS 5.5%
-
CSI 3.7rCSI 29.8%PRS 1.7%
-
CSI 3.8rCSI 88.9%PRS 5.7%
-
CSI 4.0rCSI 11.7%PRS 1.4%
-
CSI 4.1rCSI 16.6%PRS 8.3%
-
CSI 4.3rCSI 7.6%PRS 2.3%
-
CSI 4.4rCSI 10.7%PRS 1.7%
-
CSI 4.4rCSI 93.2%PRS 10.8%
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this cell type. Calculated using techniques like effect size estimation and bootstrapping for reliability.
Network Configuration
Explore relationships of the current gene. Select an Interaction Source: 'ONTOLOGY' for shared pathways (GO/Reactome) or 'STRING' for protein-protein interactions. Further refine by selecting context genes and comparing Cell Significance Index (CSI) scores between baseline and target cell types and their specific contexts.
Legend:
- Query Gene
-
Node Color (Target Cell CSI, relative to current network):
- Very High
- High
- Medium
- Low
- Very Low
- CSI N/A
- Node Size: Proportional to Target Cell CSI magnitude
- STRING PPI Edge
- Shared Pathway Edge (ONTOLOGY)
Other Information
This section provides additional information about the gene, including a description generated by an AI language model and details about associated proteins.
Genular Protein ID: 2605181677
Symbol: PABP1_HUMAN
Name: N/A
UniProtKB Accession Codes:
Database IDs:
Citations:
PubMed ID: 2885805
Title: Human mRNA polyadenylate binding protein: evolutionary conservation of a nucleic acid binding motif.
PubMed ID: 2885805
PubMed ID: 16421571
Title: DNA sequence and analysis of human chromosome 8.
PubMed ID: 16421571
DOI: 10.1038/nature04406
PubMed ID: 15489334
Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
PubMed ID: 15489334
DOI: 10.1101/gr.2596504
PubMed ID: 7908267
Title: The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity.
PubMed ID: 7908267
PubMed ID: 9582337
Title: The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm.
PubMed ID: 9582337
PubMed ID: 9548260
Title: Interaction of polyadenylate-binding protein with the eIF4G homologue PAIP enhances translation.
PubMed ID: 9548260
DOI: 10.1038/33198
PubMed ID: 11051545
Title: A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.
PubMed ID: 11051545
PubMed ID: 11172725
Title: Translational repression by a novel partner of human poly(A) binding protein, Paip2.
PubMed ID: 11172725
PubMed ID: 11438674
Title: Dual interactions of the translational repressor Paip2 with poly(A) binding protein.
PubMed ID: 11438674
PubMed ID: 11850402
Title: PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.
PubMed ID: 11850402
PubMed ID: 11997512
Title: Paip1 interacts with poly(A) binding protein through two independent binding motifs.
PubMed ID: 11997512
PubMed ID: 11991638
Title: Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis.
PubMed ID: 11991638
PubMed ID: 12565831
Title: Affinity purification of ARE-binding proteins identifies polyA-binding protein 1 as a potential substrate in MK2-induced mRNA stabilization.
PubMed ID: 12565831
PubMed ID: 14654843
Title: Proteomic characterization of the human centrosome by protein correlation profiling.
PubMed ID: 14654843
DOI: 10.1038/nature02166
PubMed ID: 15314026
Title: UNR, a new partner of poly(A)-binding protein, plays a key role in translationally coupled mRNA turnover mediated by the c-fos major coding-region determinant.
PubMed ID: 15314026
DOI: 10.1101/gad.1219104
PubMed ID: 16356927
Title: The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex.
PubMed ID: 16356927
DOI: 10.1093/nar/gki1014
PubMed ID: 17212783
Title: IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain.
PubMed ID: 17212783
PubMed ID: 16804161
Title: Regulation of poly(A) binding protein function in translation: Characterization of the Paip2 homolog, Paip2B.
PubMed ID: 16804161
DOI: 10.1261/rna.106506
PubMed ID: 17932509
Title: Proteomic and functional analysis of Argonaute-containing mRNA-protein complexes in human cells.
PubMed ID: 17932509
PubMed ID: 17267499
Title: NFX1-123 and poly(A) binding proteins synergistically augment activation of telomerase in human papillomavirus type 16 E6-expressing cells.
PubMed ID: 17267499
DOI: 10.1128/jvi.02007-06
PubMed ID: 17289661
Title: Molecular composition of IMP1 ribonucleoprotein granules.
PubMed ID: 17289661
PubMed ID: 18799579
Title: Nuclear localization of cytoplasmic poly(A)-binding protein upon rotavirus infection involves the interaction of NSP3 with eIF4G and RoXaN.
PubMed ID: 18799579
DOI: 10.1128/jvi.00872-08
PubMed ID: 18596238
Title: The DEAD-box RNA helicase DDX3 associates with export messenger ribonucleoproteins as well as tip-associated protein and participates in translational control.
PubMed ID: 18596238
PubMed ID: 18447585
Title: A competition between stimulators and antagonists of Upf complex recruitment governs human nonsense-mediated mRNA decay.
PubMed ID: 18447585
PubMed ID: 18669648
Title: A quantitative atlas of mitotic phosphorylation.
PubMed ID: 18669648
PubMed ID: 19413330
Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.
PubMed ID: 19413330
DOI: 10.1021/ac9004309
PubMed ID: 19029303
Title: Control of c-myc mRNA stability by IGF2BP1-associated cytoplasmic RNPs.
PubMed ID: 19029303
DOI: 10.1261/rna.1175909
PubMed ID: 19608861
Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.
PubMed ID: 19608861
PubMed ID: 20102337
Title: Poly(A)-binding protein (PABP): a common viral target.
PubMed ID: 20102337
DOI: 10.1042/bj20091571
PubMed ID: 20430826
Title: The RNA binding protein Larp1 regulates cell division, apoptosis and cell migration.
PubMed ID: 20430826
DOI: 10.1093/nar/gkq294
PubMed ID: 20133758
Title: Human cytomegalovirus UL69 protein facilitates translation by associating with the mRNA cap-binding complex and excluding 4EBP1.
PubMed ID: 20133758
PubMed ID: 20573744
Title: A stimulatory role for the La-related protein 4B in translation.
PubMed ID: 20573744
DOI: 10.1261/rna.2146910
PubMed ID: 20068231
Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
PubMed ID: 20068231
PubMed ID: 21269460
Title: Initial characterization of the human central proteome.
PubMed ID: 21269460
PubMed ID: 21700224
Title: Human senataxin resolves RNA/DNA hybrids formed at transcriptional pause sites to promote Xrn2-dependent termination.
PubMed ID: 21700224
PubMed ID: 21883093
Title: Critical roles of RNA helicase DDX3 and its interactions with eIF4E/PABP1 in stress granule assembly and stress response.
PubMed ID: 21883093
DOI: 10.1042/bj20110739
PubMed ID: 22872150
Title: DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs.
PubMed ID: 22872150
PubMed ID: 23186163
Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.
PubMed ID: 23186163
DOI: 10.1021/pr300630k
PubMed ID: 23125361
Title: The mammalian TRIM-NHL protein TRIM71/LIN-41 is a repressor of mRNA function.
PubMed ID: 23125361
DOI: 10.1093/nar/gks1032
PubMed ID: 23279204
Title: Both G3BP1 and G3BP2 contribute to stress granule formation.
PubMed ID: 23279204
DOI: 10.1111/gtc.12023
PubMed ID: 23077296
Title: Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA.
PubMed ID: 23077296
DOI: 10.1128/jvi.01693-12
PubMed ID: 25220460
Title: The RNA helicase DHX34 activates NMD by promoting a transition from the surveillance to the decay-inducing complex.
PubMed ID: 25220460
PubMed ID: 25480299
Title: Uridylation by TUT4 and TUT7 marks mRNA for degradation.
PubMed ID: 25480299
PubMed ID: 24532714
Title: Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation.
PubMed ID: 24532714
PubMed ID: 24129315
Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.
PubMed ID: 24129315
PubMed ID: 25940091
Title: La-related protein 1 (LARP1) represses terminal oligopyrimidine (TOP) mRNA translation downstream of mTOR complex 1 (mTORC1).
PubMed ID: 25940091
PubMed ID: 25944712
Title: N-terminome analysis of the human mitochondrial proteome.
PubMed ID: 25944712
PubMed ID: 27573237
Title: Regulation of Human Endonuclease V Activity and Relocalization to Cytoplasmic Stress Granules.
PubMed ID: 27573237
PubMed ID: 27871484
Title: Identification of a nuclear exosome decay pathway for processed transcripts.
PubMed ID: 27871484
PubMed ID: 26735137
Title: Characterization of RyDEN (C19orf66) as an interferon-stimulated cellular inhibitor against dengue virus replication.
PubMed ID: 26735137
PubMed ID: 28733330
Title: The helicase, DDX3X, interacts with poly(A)-binding protein 1 (PABP1) and caprin-1 at the leading edge of migrating fibroblasts and is required for efficient cell spreading.
PubMed ID: 28733330
DOI: 10.1042/bcj20170354
PubMed ID: 28931820
Title: The non-canonical poly(A) polymerase FAM46C acts as an onco-suppressor in multiple myeloma.
PubMed ID: 28931820
PubMed ID: 28559491
Title: Antagonistic actions of two human Pan3 isoforms on global mRNA turnover.
PubMed ID: 28559491
PubMed ID: 29476152
Title: Recognition of RNA N6-methyladenosine by IGF2BP proteins enhances mRNA stability and translation.
PubMed ID: 29476152
PubMed ID: 31649314
Title: The Interactome analysis of the Respiratory Syncytial Virus protein M2-1 suggests a new role in viral mRNA metabolism post-transcription.
PubMed ID: 31649314
PubMed ID: 32245947
Title: An oncopeptide regulates m6A recognition by the m6A reader IGF2BP1 and tumorigenesis.
PubMed ID: 32245947
PubMed ID: 33876849
Title: The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation.
PubMed ID: 33876849
PubMed ID: 10499800
Title: Recognition of polyadenylate RNA by the poly(A)-binding protein.
PubMed ID: 10499800
PubMed ID: 11287632
Title: Structure and function of the C-terminal PABC domain of human poly(A)-binding protein.
PubMed ID: 11287632
PubMed ID: 20096703
Title: Molecular determinants of PAM2 recognition by the MLLE domain of poly(A)-binding protein.
PubMed ID: 20096703
PubMed ID: 21098120
Title: La-related protein 4 binds poly(A), interacts with the poly(A)-binding protein MLLE domain via a variant PAM2w motif, and can promote mRNA stability.
PubMed ID: 21098120
DOI: 10.1128/mcb.01162-10
Sequence Information:
- Length: 636
- Mass: 70671
- Checksum: 2EB1B02A346132EE
- Sequence:
MNPSAPSYPM ASLYVGDLHP DVTEAMLYEK FSPAGPILSI RVCRDMITRR SLGYAYVNFQ QPADAERALD TMNFDVIKGK PVRIMWSQRD PSLRKSGVGN IFIKNLDKSI DNKALYDTFS AFGNILSCKV VCDENGSKGY GFVHFETQEA AERAIEKMNG MLLNDRKVFV GRFKSRKERE AELGARAKEF TNVYIKNFGE DMDDERLKDL FGKFGPALSV KVMTDESGKS KGFGFVSFER HEDAQKAVDE MNGKELNGKQ IYVGRAQKKV ERQTELKRKF EQMKQDRITR YQGVNLYVKN LDDGIDDERL RKEFSPFGTI TSAKVMMEGG RSKGFGFVCF SSPEEATKAV TEMNGRIVAT KPLYVALAQR KEERQAHLTN QYMQRMASVR AVPNPVINPY QPAPPSGYFM AAIPQTQNRA AYYPPSQIAQ LRPSPRWTAQ GARPHPFQNM PGAIRPAAPR PPFSTMRPAS SQVPRVMSTQ RVANTSTQTM GPRPAAAAAA ATPAVRTVPQ YKYAAGVRNP QQHLNAQPQV TMQQPAVHVQ GQEPLTASML ASAPPQEQKQ MLGERLFPLI QAMHPTLAGK ITGMLLEIDN SELLHMLESP ESLRSKVDEA VAVLQAHQAK EAAQKAVNSA TGVPTV