PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
7607214-8	1995	In addition, PCBP-2 bound poly(rU), whereas very little binding to poly(rA) was observed for both proteins.	Ruthenium	31-33	poly(rC) binding protein 2	Homo sapiens	13-19
10781945-5	2000	Finally, a candidate specificity factor for polycytosine-mediated cytoplasmic polyadenylation has been purified and identified as the Xenopus homologue of human alpha-CP2.	polycytosine	44-56	poly(rC) binding protein 2	Homo sapiens	161-170
10455157-3	1999	The two major cytoplasmic poly(C)-binding proteins in mammalian cells, alphaCP-1 and alphaCP-2, are implicated in a spectrum of post-transcriptional controls.	Poly C	26-33	poly(rC) binding protein 2	Homo sapiens	85-94
9234743-3	1997	One of the protein activities in this multiprotein complex is a poly(C)-binding activity which consists of two proteins, alphaCP1 and alphaCP2.	Poly C	64-71	poly(rC) binding protein 2	Homo sapiens	134-142
34948101-7	2021	Moreover, a higher level of p53 protein in the presence of rapamycin or doxorubicin and the combination of both antibiotics was noticed in PCBP2-overexpressed cells compared to control cells.	Sirolimus	59-68	poly(rC) binding protein 2	Homo sapiens	139-144
34948101-7	2021	Moreover, a higher level of p53 protein in the presence of rapamycin or doxorubicin and the combination of both antibiotics was noticed in PCBP2-overexpressed cells compared to control cells.	Doxorubicin	72-83	poly(rC) binding protein 2	Homo sapiens	139-144
32679248-3	2020	PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.	Iron	121-125	poly(rC) binding protein 2	Homo sapiens	76-81
34418457-10	2021	Moreover, actinomycin D assay showed that overexpression of PCBP2 enhanced the RNA stability of AC104958.2.	Dactinomycin	10-23	poly(rC) binding protein 2	Homo sapiens	60-65
34233389-1	2021	Poly(rC)-binding protein 2 (PCBP2) is an RNA-binding protein that is characterized by its ability to interact with poly(C) with high affinity in a sequence-specific manner.	Poly C	115-122	poly(rC) binding protein 2	Homo sapiens	0-26
34233389-1	2021	Poly(rC)-binding protein 2 (PCBP2) is an RNA-binding protein that is characterized by its ability to interact with poly(C) with high affinity in a sequence-specific manner.	Poly C	115-122	poly(rC) binding protein 2	Homo sapiens	28-33
34233389-3	2021	The specific structure and localization of PCBP2 lay the foundation for its multiple roles in transcriptional, posttranscriptional, and translational processes, even in iron metabolism.	Iron	169-173	poly(rC) binding protein 2	Homo sapiens	43-48
34108034-0	2021	H3K27ac-induced lncRNA PAXIP1-AS1 promotes cell proliferation, migration, EMT and apoptosis in ovarian cancer by targeting miR-6744-5p/PCBP2 axis.	h3k27ac	0-7	poly(rC) binding protein 2	Homo sapiens	135-140
33037085-4	2021	In this study, it was observed that the expression levels of PCBP2 mRNA and protein were diametric in breast normal and cancer cell lines, paraffin-embedded and fresh tissue specimens, consistent with data from The Cancer Genome Atlas (TCGA) and the Clinical Proteomic Tumor Analysis Consortium (CPTAC).	Paraffin	139-147	poly(rC) binding protein 2	Homo sapiens	61-66
33511005-5	2021	Mechanistically, lnc030 cooperates with poly(rC) binding protein 2(PCBP2) to stabilize squalene epoxidase (SQLE) mRNA, resulting in an increase of cholesterol synthesis.	Cholesterol	147-158	poly(rC) binding protein 2	Homo sapiens	40-66
33511005-5	2021	Mechanistically, lnc030 cooperates with poly(rC) binding protein 2(PCBP2) to stabilize squalene epoxidase (SQLE) mRNA, resulting in an increase of cholesterol synthesis.	Cholesterol	147-158	poly(rC) binding protein 2	Homo sapiens	67-72
32679248-3	2020	PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.	Iron	121-125	poly(rC) binding protein 2	Homo sapiens	76-81
32679248-3	2020	PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.	Iron	121-125	poly(rC) binding protein 2	Homo sapiens	76-81
32679248-3	2020	PCBP1 is involved in the iron storage pathway that involves ferritin, while PCBP2 is involved in processes that include: iron transfer from the iron importer, divalent metal ion transporter 1; iron export mediated by ferroportin-1; and heme degradation via heme oxygenase 1.	Heme	236-240	poly(rC) binding protein 2	Homo sapiens	76-81
32679248-4	2020	MAJOR CONCLUSIONS: Both PCBP1 and PCBP2 possess iron-binding activity and form hetero/homo dimer complexes.	Iron	48-52	poly(rC) binding protein 2	Homo sapiens	34-39
32480040-12	2020	Confocal microscopy co-localization studies and proximity ligation assays both demonstrated decreased interaction of ADI1 with PCBP1 and PCBP2 under conditions of iron depletion using DFO.	Iron	163-167	poly(rC) binding protein 2	Homo sapiens	137-142
32480040-12	2020	Confocal microscopy co-localization studies and proximity ligation assays both demonstrated decreased interaction of ADI1 with PCBP1 and PCBP2 under conditions of iron depletion using DFO.	Deferoxamine	184-187	poly(rC) binding protein 2	Homo sapiens	137-142
32480040-0	2020	Acireductone dioxygenase 1 (ADI1) is regulated by cellular iron by a mechanism involving the iron chaperone, PCBP1, with PCBP2 acting as a potential co-chaperone.	Iron	59-63	poly(rC) binding protein 2	Homo sapiens	121-126
32324262-10	2020	LINC02535 cooperated with PCBP2 to enhance the stability of RRM1 messenger RNA (mRNA).	linc02535	0-9	poly(rC) binding protein 2	Homo sapiens	26-31
32712297-3	2020	In the current study, we elaborate on the direct partners in calibrating the capability of FPN in exporting iron out of cells, such as ceruloplasmin (CP), hephaestin (HP) and poly(rC)-binding protein 2 (PCBP2).	Iron	108-112	poly(rC) binding protein 2	Homo sapiens	203-208
31693182-1	2020	The purpose of this study was to investigate the role of Poly (C)-binding protein 2 (PCBP2) and the related signaling pathway in glioma progression.	poly If	57-61	poly(rC) binding protein 2	Homo sapiens	85-90
32768236-7	2020	Host cell poly(C) binding protein 2 (PCBP2) was determined to bind and interact with PLP1.	Poly C	10-17	poly(rC) binding protein 2	Homo sapiens	37-42
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Heme	114-118	poly(rC) binding protein 2	Homo sapiens	51-56
31961070-5	2020	Zn2+ reversibly inhibited the nucleotide-binding ability of PCBP2 in vitro.	Zinc	0-4	poly(rC) binding protein 2	Homo sapiens	60-65
31961070-6	2020	These findings suggest that both PCBP2 and PCBP1 may control the stability of sortilin transcripts by sensing intracellular Zn2+ levels in immune cells.	Zinc	124-128	poly(rC) binding protein 2	Homo sapiens	33-38
31914575-12	2020	The result of GMDR showed that there were interaction effects of the hnRNP E2 low expression, HPV16 E2 low expression and HPV16 E6 high expression in both CIN II/III and SCC groups.	gmdr	14-18	poly(rC) binding protein 2	Homo sapiens	69-77
31421070-0	2019	How iron is handled in the course of heme catabolism: Integration of heme oxygenase with intracellular iron transport mechanisms mediated by poly (rC)-binding protein-2.	Iron	4-8	poly(rC) binding protein 2	Homo sapiens	141-168
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Heme	114-118	poly(rC) binding protein 2	Homo sapiens	161-166
31421070-0	2019	How iron is handled in the course of heme catabolism: Integration of heme oxygenase with intracellular iron transport mechanisms mediated by poly (rC)-binding protein-2.	Heme	37-41	poly(rC) binding protein 2	Homo sapiens	141-168
31421070-0	2019	How iron is handled in the course of heme catabolism: Integration of heme oxygenase with intracellular iron transport mechanisms mediated by poly (rC)-binding protein-2.	Iron	103-107	poly(rC) binding protein 2	Homo sapiens	141-168
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	28-32	poly(rC) binding protein 2	Homo sapiens	44-71
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	28-32	poly(rC) binding protein 2	Homo sapiens	73-78
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	137-141	poly(rC) binding protein 2	Homo sapiens	44-71
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	137-141	poly(rC) binding protein 2	Homo sapiens	73-78
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Heme	148-152	poly(rC) binding protein 2	Homo sapiens	44-71
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Heme	148-152	poly(rC) binding protein 2	Homo sapiens	73-78
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	137-141	poly(rC) binding protein 2	Homo sapiens	44-71
31421070-5	2019	Recently, the intracellular iron chaperone, poly (rC)-binding protein 2 (PCBP2), has been identified, which can be involved in accepting iron after heme catabolism as well as intracellular iron transport.	Iron	137-141	poly(rC) binding protein 2	Homo sapiens	73-78
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Iron	153-157	poly(rC) binding protein 2	Homo sapiens	51-56
31421070-6	2019	In fact, HO1, NADPH-cytochrome P450 reductase, and PCBP2 form a functional unit that integrates the catabolism of heme with the binding and transport of iron by PCBP2.	Iron	153-157	poly(rC) binding protein 2	Homo sapiens	161-166
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	50-76
30055235-8	2019	We summarize DMT1 expression depending on the types of cell or tissue and the function and mechanism of one of the iron chaperones, PCBP2.	Iron	115-119	poly(rC) binding protein 2	Homo sapiens	132-137
29866654-0	2018	Poly(C)-Binding Protein Pcbp2 Enables Differentiation of Definitive Erythropoiesis by Directing Functional Splicing of the Runx1 Transcript.	Poly C	0-7	poly(rC) binding protein 2	Homo sapiens	24-29
29744291-6	2018	Cyclin-dependent kinase 2 (CDK2) was positively regulated by PCBP2 via a direct 3" UTR binding pathway as determined using a ribonucleoprotein immunoprecipitation assay and a biotin pulldown assay.	Biotin	175-181	poly(rC) binding protein 2	Homo sapiens	61-66
28655775-0	2017	The iron chaperone poly(rC)-binding protein 2 forms a metabolon with the heme oxygenase 1/cytochrome P450 reductase complex for heme catabolism and iron transfer.	Iron	4-8	poly(rC) binding protein 2	Homo sapiens	19-45
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	50-76
30448895-7	2019	Notably, the UTRs of HAstVs contain putative binding sites for the serine/arginine-rich factors SRSF2, SRSF5, SRSF6, SRSF3, and the multifunctional hnRNPE2 protein.	Serine	67-73	poly(rC) binding protein 2	Homo sapiens	148-155
30448895-7	2019	Notably, the UTRs of HAstVs contain putative binding sites for the serine/arginine-rich factors SRSF2, SRSF5, SRSF6, SRSF3, and the multifunctional hnRNPE2 protein.	Arginine	74-82	poly(rC) binding protein 2	Homo sapiens	148-155
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	78-83
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	78-83
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	50-76
28655775-3	2017	Recently, we demonstrated that the iron chaperone poly(rC)-binding protein 2 (PCBP2) can directly receive ferrous iron from DMT1 or transfer iron to the iron exporter, ferroportin 1.	Iron	114-118	poly(rC) binding protein 2	Homo sapiens	78-83
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	3-7	poly(rC) binding protein 2	Homo sapiens	84-89
28655775-8	2017	In heme-loaded cells, heme prompted HO1-CPR complex formation and decreased the HO1/PCBP2 interaction.	Heme	22-26	poly(rC) binding protein 2	Homo sapiens	84-89
28655775-9	2017	Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1.	Heme	142-146	poly(rC) binding protein 2	Homo sapiens	117-122
28655775-9	2017	Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1.	Iron	178-190	poly(rC) binding protein 2	Homo sapiens	167-172
28655775-9	2017	Furthermore, in vitro reconstitution experiments with purified recombinant proteins indicated that HO1 could bind to PCBP2 in the presence of heme, whereas loading of PCBP2 with ferrous iron caused PCBP2 to lose its affinity for HO1.	Iron	178-190	poly(rC) binding protein 2	Homo sapiens	167-172
28655775-10	2017	These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.	Iron	36-40	poly(rC) binding protein 2	Homo sapiens	76-81
28655775-10	2017	These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.	Heme	55-59	poly(rC) binding protein 2	Homo sapiens	76-81
28655775-10	2017	These results indicate that ferrous iron released from heme can be bound by PCBP2 and suggest a model for an integrated heme catabolism and iron transport metabolon.	Iron	140-144	poly(rC) binding protein 2	Homo sapiens	76-81
27209304-1	2016	PCBP2, a member of the poly(C)-binding protein (PCBP) family, plays a pivotal role in posttranscriptional and translational regulation by interacting with single-stranded poly(C) motifs in target mRNAs.	Poly C	23-30	poly(rC) binding protein 2	Homo sapiens	0-5
27748915-1	2016	Poly(C)-binding protein 2 (PCBP2) is a member of the PCBP family, and plays an important role in post-transcriptional and translational regulation of various signaling molecules through direct binding to single-stranded poly(C) motifs.	Poly C	220-227	poly(rC) binding protein 2	Homo sapiens	0-25
27748915-1	2016	Poly(C)-binding protein 2 (PCBP2) is a member of the PCBP family, and plays an important role in post-transcriptional and translational regulation of various signaling molecules through direct binding to single-stranded poly(C) motifs.	Poly C	220-227	poly(rC) binding protein 2	Homo sapiens	27-32
27748915-7	2016	Moreover, we found that high expression of PCBP2 may contribute to sorafenib resistance in HCC cells, involving dysregulated expression of Bax and Bcl-2 proteins.	Sorafenib	67-76	poly(rC) binding protein 2	Homo sapiens	43-48
27209304-11	2016	In vitro, PCBP2-specific siRNA-transfected neuron showed significantly decrease of neuronal apoptosis and expression of cell cycle related proteins following glutamate stimulation.	Glutamic Acid	158-167	poly(rC) binding protein 2	Homo sapiens	10-15
26722446-1	2015	PCBP2, a member of the poly(C)-binding protein (PCBP) family, is involved in posttranscriptional and translational regulation by interacting with single-stranded poly(C) motifs in target mRNAs.	Poly C	23-30	poly(rC) binding protein 2	Homo sapiens	0-5
27573788-6	2016	Induction of miRNA-328 expression during cell differentiation antagonizes the blockade by hnRNP E2 which results in the upregulation of CD11b expression and ROS production in monocytic cells.	ros	157-160	poly(rC) binding protein 2	Homo sapiens	90-98
27302059-0	2016	Iron Export through the Transporter Ferroportin 1 Is Modulated by the Iron Chaperone PCBP2.	Iron	0-4	poly(rC) binding protein 2	Homo sapiens	85-90
27302059-5	2016	Subsequently, PCBP2 receives iron from DMT1 and then disengages from the transporter.	Iron	29-33	poly(rC) binding protein 2	Homo sapiens	14-19
27302059-6	2016	In this study, we investigated the function of PCBP2 in iron export.	Iron	56-60	poly(rC) binding protein 2	Homo sapiens	47-52
27302059-11	2016	The silencing of PCBP2 expression suppressed FPN1-dependent iron export from cells.	Iron	60-64	poly(rC) binding protein 2	Homo sapiens	17-22
27302059-12	2016	These results suggest that FPN1 exports iron received from the iron chaperone PCBP2.	Iron	40-44	poly(rC) binding protein 2	Homo sapiens	78-83
27302059-13	2016	Therefore, it was found that PCBP2 modulates cellular iron export, which is an important physiological process.	Iron	54-58	poly(rC) binding protein 2	Homo sapiens	29-34
27461833-0	2016	Poly (C)-binding protein 2 (PCBP2) promotes the progression of esophageal squamous cell carcinoma (ESCC) through regulating cellular proliferation and apoptosis.	Poly C	0-7	poly(rC) binding protein 2	Homo sapiens	28-33
27461833-1	2016	PCBP2 (Poly(C)-binding protein 2) is a member of PCBP family, which has many functions including mRNA stabilization, translational silence and translational enhancement performed by their poly(C)-binding ability.	Poly C	188-195	poly(rC) binding protein 2	Homo sapiens	0-5
27461833-1	2016	PCBP2 (Poly(C)-binding protein 2) is a member of PCBP family, which has many functions including mRNA stabilization, translational silence and translational enhancement performed by their poly(C)-binding ability.	Poly C	188-195	poly(rC) binding protein 2	Homo sapiens	7-32
26803058-8	2016	Overexpression of beta2-AR and PCBP2 was associated with advanced tumor stage and significantly worsened prognosis in patients with PDAC.	pdac	132-136	poly(rC) binding protein 2	Homo sapiens	31-36
26002461-9	2015	In addition, we showed that over-expression of PCBP2 ameliorates palmitate (PA)-induced insulin resistance, which was indicated by elevated phosphorylation of protein kinase B (AKT) and glycogen synthase kinase 3beta (GSK3beta).	Palmitates	65-74	poly(rC) binding protein 2	Homo sapiens	47-52
26002461-9	2015	In addition, we showed that over-expression of PCBP2 ameliorates palmitate (PA)-induced insulin resistance, which was indicated by elevated phosphorylation of protein kinase B (AKT) and glycogen synthase kinase 3beta (GSK3beta).	Palmitates	76-78	poly(rC) binding protein 2	Homo sapiens	47-52
26002461-13	2015	Accordingly, PA-induced intracellular lipid accumulation was suppressed in over-expression of PCBP2 HepG2 cells.	Palmitates	13-15	poly(rC) binding protein 2	Homo sapiens	94-99
25411354-4	2015	FAST-iCLIP of Poly-C binding protein 2 (PCBP2) showed that PCBP2-bound CU-rich motifs in different topologies to recognize mRNAs and noncoding RNAs with distinct biological functions.	Copper	71-73	poly(rC) binding protein 2	Homo sapiens	14-38
25411354-4	2015	FAST-iCLIP of Poly-C binding protein 2 (PCBP2) showed that PCBP2-bound CU-rich motifs in different topologies to recognize mRNAs and noncoding RNAs with distinct biological functions.	Copper	71-73	poly(rC) binding protein 2	Homo sapiens	40-45
25411354-4	2015	FAST-iCLIP of Poly-C binding protein 2 (PCBP2) showed that PCBP2-bound CU-rich motifs in different topologies to recognize mRNAs and noncoding RNAs with distinct biological functions.	Copper	71-73	poly(rC) binding protein 2	Homo sapiens	59-64
24854545-7	2014	Iron uptake and subsequent ferritin expression were suppressed by either DMT1 or PCBP2 knockdown.	Iron	0-4	poly(rC) binding protein 2	Homo sapiens	81-86
24854545-8	2014	Iron-associated DMT1 could interact with PCBP2 in vitro, whereas iron-chelated DMT1 could not.	Iron	0-4	poly(rC) binding protein 2	Homo sapiens	41-46
24854545-9	2014	These results indicate that ferrous iron imported by DMT1 is transferred directly to PCBP2.	Iron	36-40	poly(rC) binding protein 2	Homo sapiens	85-90
24607900-5	2014	We find that SIRT6, one of the NAD(+)-dependent class III deacetylase SIRTUINs, is down-regulated in human glioma tissues and that the level of SIRT6 is negatively correlated with PCBP2 level while H3K9ac enrichment on the promoter of PCBP2 is positively correlated with PCBP2 expression.	NAD	31-37	poly(rC) binding protein 2	Homo sapiens	180-185
24854545-10	2014	Moreover, we demonstrated that PCBP2 could bind to ferroportin, which exports ferrous iron out of the cell.	Iron	86-90	poly(rC) binding protein 2	Homo sapiens	31-36
24854545-11	2014	These findings suggest that PCBP2 can transfer ferrous iron from DMT1 to the appropriate intracellular sites or ferroportin and could function as an iron chaperone.	Iron	55-59	poly(rC) binding protein 2	Homo sapiens	28-33
24854545-11	2014	These findings suggest that PCBP2 can transfer ferrous iron from DMT1 to the appropriate intracellular sites or ferroportin and could function as an iron chaperone.	Iron	149-153	poly(rC) binding protein 2	Homo sapiens	28-33
24843120-2	2014	Poly(rC)-binding proteins PCBP1 and PCBP2 are multifunctional adaptor proteins that bind iron and deliver it to ferritin for storage or to prolyl and asparagyl hydroxylases to metallate the mononuclear iron center.	Poly C	0-8	poly(rC) binding protein 2	Homo sapiens	36-41
24843120-2	2014	Poly(rC)-binding proteins PCBP1 and PCBP2 are multifunctional adaptor proteins that bind iron and deliver it to ferritin for storage or to prolyl and asparagyl hydroxylases to metallate the mononuclear iron center.	Iron	89-93	poly(rC) binding protein 2	Homo sapiens	36-41
24843120-2	2014	Poly(rC)-binding proteins PCBP1 and PCBP2 are multifunctional adaptor proteins that bind iron and deliver it to ferritin for storage or to prolyl and asparagyl hydroxylases to metallate the mononuclear iron center.	Iron	202-206	poly(rC) binding protein 2	Homo sapiens	36-41
24843120-3	2014	Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A.	Iron	48-52	poly(rC) binding protein 2	Homo sapiens	29-34
24843120-3	2014	Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A.	Iron	104-108	poly(rC) binding protein 2	Homo sapiens	29-34
24843120-3	2014	Here, we show that PCBP1 and PCBP2 also deliver iron to deoxyhypusine hydroxylase (DOHH), the dinuclear iron enzyme required for hypusine modification of the translation factor eukaryotic initiation factor 5A.	hypusine	61-69	poly(rC) binding protein 2	Homo sapiens	29-34
24843120-4	2014	Cells depleted of PCBP1 or PCBP2 exhibited loss of DOHH activity and loss of the holo form of the enzyme in cells, particularly when cells were made mildly iron-deficient.	Iron	156-160	poly(rC) binding protein 2	Homo sapiens	27-32
24843120-10	2014	Thus, PCBP1 and PCBP2 may serve as iron chaperones to multiple classes of cytosolic nonheme iron enzymes and may have a particular role in restoring metal cofactors that are spontaneously lost in iron deficient cells.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	16-21
24843120-10	2014	Thus, PCBP1 and PCBP2 may serve as iron chaperones to multiple classes of cytosolic nonheme iron enzymes and may have a particular role in restoring metal cofactors that are spontaneously lost in iron deficient cells.	Iron	92-96	poly(rC) binding protein 2	Homo sapiens	16-21
24843120-10	2014	Thus, PCBP1 and PCBP2 may serve as iron chaperones to multiple classes of cytosolic nonheme iron enzymes and may have a particular role in restoring metal cofactors that are spontaneously lost in iron deficient cells.	Iron	92-96	poly(rC) binding protein 2	Homo sapiens	16-21
24607900-5	2014	We find that SIRT6, one of the NAD(+)-dependent class III deacetylase SIRTUINs, is down-regulated in human glioma tissues and that the level of SIRT6 is negatively correlated with PCBP2 level while H3K9ac enrichment on the promoter of PCBP2 is positively correlated with PCBP2 expression.	NAD	31-37	poly(rC) binding protein 2	Homo sapiens	235-240
24607900-5	2014	We find that SIRT6, one of the NAD(+)-dependent class III deacetylase SIRTUINs, is down-regulated in human glioma tissues and that the level of SIRT6 is negatively correlated with PCBP2 level while H3K9ac enrichment on the promoter of PCBP2 is positively correlated with PCBP2 expression.	NAD	31-37	poly(rC) binding protein 2	Homo sapiens	235-240
22951310-2	2012	In the present study, we have analyzed the interaction of Nsp1beta of Chinese highly pathogenic PRRSV (HP-PRRSV) with cellular poly(C)-binding 2 (PCBP2) by means of the yeast two-hybrid screening in a pulmonary alveolar macrophages (PAMs) cDNA library and co-immunoprecipitation (Co-IP) assay.	Poly C	127-134	poly(rC) binding protein 2	Homo sapiens	146-151
23585479-1	2013	PCBP2 is a member of the poly(C)-binding protein (PCBP) family, which plays an important role in posttranscriptional and translational regulation by interacting with single-stranded poly(C) motifs in target mRNAs.	Poly C	25-32	poly(rC) binding protein 2	Homo sapiens	0-5
23640898-2	2013	Poly r(C)-binding protein 1 (PCBP1) is an iron chaperone for ferritin; both PCBP1 and its paralog PCBP2 are required for iron delivery to the prolyl hydroxylase that regulates HIF1.	Iron	121-125	poly(rC) binding protein 2	Homo sapiens	98-103
23640898-3	2013	Here we show that PCBP2 is also an iron chaperone for ferritin.	Iron	35-39	poly(rC) binding protein 2	Homo sapiens	18-23
23640898-4	2013	Co-expression of PCBP2 and human ferritins in yeast activated the iron deficiency response and increased iron deposition into ferritin.	Iron	66-70	poly(rC) binding protein 2	Homo sapiens	17-22
23640898-5	2013	Depletion of PCBP2 in Huh7 cells diminished iron incorporation into ferritin.	Iron	44-48	poly(rC) binding protein 2	Homo sapiens	13-18
23640898-6	2013	Both PCBP1 and PCBP2 were co-immunoprecipitated with ferritin in HEK293 cells, and expression of both PCBPs was required for ferritin complex formation in cells.	pcbps	102-107	poly(rC) binding protein 2	Homo sapiens	15-20
21976648-4	2011	To further our understanding of the role of the viral nsp1 in these processes, using nsp1beta, a proteolytically processed functional product of nsp1 as bait, we have identified the cellular poly(C)-binding proteins 1 and 2 (PCBP1 and PCBP2) as two of its interaction partners.	Poly C	191-198	poly(rC) binding protein 2	Homo sapiens	235-240
22633452-0	2012	Iron homeostasis regulates the activity of the microRNA pathway through poly(C)-binding protein 2.	Iron	0-4	poly(rC) binding protein 2	Homo sapiens	72-97
22633452-5	2012	We show that cytosolic iron could regulate the activity of the miRNA pathway through poly(C)-binding protein 2 (PCBP2).	Iron	23-27	poly(rC) binding protein 2	Homo sapiens	85-110
22633452-5	2012	We show that cytosolic iron could regulate the activity of the miRNA pathway through poly(C)-binding protein 2 (PCBP2).	Iron	23-27	poly(rC) binding protein 2	Homo sapiens	112-117
22633452-7	2012	Cytosolic iron could modulate the association between PCBP2 and Dicer, as well as the multimerization of PCBP2 and its ability to bind to miRNA precursors, which can alter the processing of miRNA precursors.	Iron	10-14	poly(rC) binding protein 2	Homo sapiens	54-59
22633452-7	2012	Cytosolic iron could modulate the association between PCBP2 and Dicer, as well as the multimerization of PCBP2 and its ability to bind to miRNA precursors, which can alter the processing of miRNA precursors.	Iron	10-14	poly(rC) binding protein 2	Homo sapiens	105-110
19211566-0	2009	Depletion of the poly(C)-binding proteins alphaCP1 and alphaCP2 from K562 cells leads to p53-independent induction of cyclin-dependent kinase inhibitor (CDKN1A) and G1 arrest.	Poly C	17-24	poly(rC) binding protein 2	Homo sapiens	55-63
19230839-6	2009	While PCBP2 was more likely to reside in larger P-bodies, P-body size did not seem to be the sole determinant, and puromycin-induced enlargement of P-bodies only modestly increased the percentage of PCBP2-positive P-bodies.	Puromycin	115-124	poly(rC) binding protein 2	Homo sapiens	199-204
22055506-0	2011	Activation of the HIF prolyl hydroxylase by the iron chaperones PCBP1 and PCBP2.	Iron	48-52	poly(rC) binding protein 2	Homo sapiens	74-79
17475908-3	2007	In fact, high levels of p210-BCR/ABL are required for enhanced hnRNP-E2 expression, which depends on phosphorylation of hnRNP-E2 serines 173, 189, and 272 and threonine 213 by the BCR/ABL-activated MAPK(ERK1/2).	Serine	129-136	poly(rC) binding protein 2	Homo sapiens	63-71
18174314-6	2008	Upon exposure to heat and arsenic stress, PCBP2 became predominantly accumulated at the SG, but was still present in Dcp1a-positive P-bodies.	Arsenic	26-33	poly(rC) binding protein 2	Homo sapiens	42-47
17475908-4	2007	Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors.	Serine	0-6	poly(rC) binding protein 2	Homo sapiens	51-59
18687895-3	2008	PCBP2 is known to bind pyrimidine-rich repeats within the 3" UTR of mRNAs and has been implicated in control of RNA stability and translation and selective cap-independent transcription.	pyrimidine	23-33	poly(rC) binding protein 2	Homo sapiens	0-5
17581994-6	2007	Among the four different isoforms of PCBP in mammalian cells, PCBP2 is required for translation initiation on picornavirus genomes with type I internal ribosome entry site elements and also for RNA replication.	pcbp	37-41	poly(rC) binding protein 2	Homo sapiens	62-67
17475908-4	2007	Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors.	Threonine	7-16	poly(rC) binding protein 2	Homo sapiens	51-59
17475908-3	2007	In fact, high levels of p210-BCR/ABL are required for enhanced hnRNP-E2 expression, which depends on phosphorylation of hnRNP-E2 serines 173, 189, and 272 and threonine 213 by the BCR/ABL-activated MAPK(ERK1/2).	Serine	129-136	poly(rC) binding protein 2	Homo sapiens	120-128
17475908-4	2007	Serine/threonine to alanine substitution abolishes hnRNP-E2 phosphorylation and markedly decreases its stability in BCR/ABL-expressing myeloid precursors.	Alanine	20-27	poly(rC) binding protein 2	Homo sapiens	51-59
17475908-3	2007	In fact, high levels of p210-BCR/ABL are required for enhanced hnRNP-E2 expression, which depends on phosphorylation of hnRNP-E2 serines 173, 189, and 272 and threonine 213 by the BCR/ABL-activated MAPK(ERK1/2).	Threonine	159-168	poly(rC) binding protein 2	Homo sapiens	63-71
16831266-1	2006	BACKGROUND & OBJECTIVE: The abnormal expression of poly(rC)-binding protein E2 (hnRNP E2) induced by BCR/ABL plays an important role in blast crisis of chronic myeloid leukemia (CML).	Adenosine Monophosphate	12-15	poly(rC) binding protein 2	Homo sapiens	84-92
17526645-3	2007	To reveal the mechanisms of KH domain-D/RNA recognition and its functional importance, we have determined the crystal structures of PCBP2 KH1 domain in complex with a 12-nucleotide DNA corresponding to two repeats of the human C-rich strand telomeric DNA and its RNA equivalent.	12-nucleotide	167-180	poly(rC) binding protein 2	Homo sapiens	132-137
17426136-4	2007	To reveal the molecular basis of poly(C)-sequence recognition, we have determined the crystal structure, at 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence (5"-AACCCTA-3") corresponding to one repeat of the C-rich strand of human telomeric DNA.	Poly C	33-40	poly(rC) binding protein 2	Homo sapiens	129-134
17426136-4	2007	To reveal the molecular basis of poly(C)-sequence recognition, we have determined the crystal structure, at 1.6 A resolution, of PCBP2 KH3 domain in complex with a 7-nt DNA sequence (5"-AACCCTA-3") corresponding to one repeat of the C-rich strand of human telomeric DNA.	Carbon	38-39	poly(rC) binding protein 2	Homo sapiens	129-134
16186123-2	2005	To reveal the molecular basis of poly(C) sequence recognition, we have determined the crystal structure, at 1.7-A resolution, of PCBP2 KH1 in complex with a 7-nucleotide DNA sequence (5"-AACCCTA-3") corresponding to one repeat of the human C-rich strand telomeric DNA.	Poly C	33-40	poly(rC) binding protein 2	Homo sapiens	129-134
15967798-8	2005	Iron influx increased the association of alphaCP1 with ferritin mRNA and decreased the alphaCP2-ferritin mRNA interaction, whereas IL-1beta reduced the association of alphaCP1 and alphaCP2 with H-ferritin mRNA.	Iron	0-4	poly(rC) binding protein 2	Homo sapiens	87-95