EuRBPDB

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TCGA tumor abbreviations
  • ACCAdrenocortical carcinoma
  • BLCABladder Urothelial Carcinoma
  • BRCABreast invasive carcinoma
  • CESCCervical squamous cell carcinoma and endocervical adenocarcinoma
  • CHOLCholangio carcinoma
  • COADColon adenocarcinoma
  • DLBCLymphoid Neoplasm Diffuse Large B-cell Lymphoma
  • ESCAEsophageal carcinoma
  • GBMGlioblastoma multiforme
  • HNSCHead and Neck squamous cell carcinoma
  • KICHKidney Chromophobe
  • KIRCKidney renal clear cell carcinoma
  • KIRPKidney renal papillary cell carcinoma
  • LAMLAcute Myeloid Leukemia
  • LGGBrain Lower Grade Glioma
  • LIHCLiver hepatocellular carcinoma
  • LUADLung adenocarcinoma
  • LUSCLung squamous cell carcinoma
  • MESOMesothelioma
  • OVOvarian serous cystadenocarcinoma
  • PAADPancreatic adenocarcinoma
  • PCPGPheochromocytoma and Paraganglioma
  • PRADProstate adenocarcinoma
  • READRectum adenocarcinoma
  • SARCSarcoma
  • SKCMSkin Cutaneous Melanoma
  • STADStomach adenocarcinoma
  • TGCTThyroid carcinoma
  • THCAThyroid carcinoma
  • THYMThymoma
  • UCECUterine Corpus Endometrial Carcinoma
  • UCSUterine Carcinosarcoma
  • UVMUveal Melanoma

Note: Click here to get the extension of tumor abbreviations.


  • Cancer Related Information
  • Basic Information

Cancer associated literatures
PIDTitleArticle TimeAuthorDoi
16465428Expression and prognostic roles of PABPC1 in esophageal cancer: correlation with tumor progression and postoperative survival.Oncol Rep2006 MarTakashima N-
25065644Exosome-mediated extracellular release of polyadenylate-binding protein 1 in human metastatic duodenal cancer cells.Proteomics2014 OctOhshima Kdoi: 10.1002/pmic.201300477
26097561PABPC1 exerts carcinogenesis in gastric carcinoma by targeting miR-34c.Int J Clin Exp Pathol2015 Apr 1Zhu J-

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr8100721481Missense_MutationnovelG35W0.15PABP
BLCAchr8100712440SilentnovelV298V0.65
BLCAchr8100706972SilentNAI454I0.15
BLCAchr8100704337Missense_MutationnovelQ624H0.26
BLCAchr8100709185SilentNAI428I0.16
BLCAchr8100709583Missense_MutationnovelR374H0.26
BLCAchr8100705625Missense_MutationnovelA551T0.33
BLCAchr8100706683Missense_MutationnovelL524V0.03
BLCAchr8100709470In_Frame_DelnovelG407_A411del0.2
BRCAchr8100706914Missense_MutationnovelP474A0.1
BRCAchr8100705641Missense_MutationNAL545F0.48
BRCAchr81007030493'UTRnovel0.05
BRCAchr8100718192Silentrs146343662R94R0.45
BRCAchr8100706925Missense_MutationNAS470F0.27
BRCAchr8100706971Missense_Mutationrs749697639R455C0.09
BRCAchr8100704316Silentrs146621651T631T0.13
CESCchr8100705586Splice_Regionnovel0.27
CESCchr8100718279Splice_Regionrs751412519A65A0.45
CESCchr8100712695Missense_MutationNAR278H0.4
COADchr8100721518SilentNAV22V0.38
COADchr81007031473'UTRnovel0.2
COADchr8100712695Missense_MutationNAR278H0.34
COADchr8100704980SilentnovelI588I0.34
COADchr8100712390Missense_MutationnovelS315F0.09
COADchr81007032733'UTRnovel0.23
COADchr8100715540Nonsense_MutationNAE189*0.35
COADchr81007032733'UTRnovel0.33
COADchr81007216285'UTRnovel0.25
COADchr81007032443'UTRnovel0.27
COADchr8100706767Missense_MutationNAA496T0.15
COADchr8100704996Missense_MutationNAG583D0.25
COADchr8100712705Missense_MutationNAE275K0.42
COADchr81007032733'UTRnovel0.56
COADchr81007030443'UTRnovel0.27
COADchr8100705032Nonsense_MutationnovelQ571delinsP*K0.08
COADchr8100718227Missense_MutationNAR83C0.14
DLBCchr8100717772Splice_SitenovelX168_splice0.35
DLBCchr8100718194Missense_MutationnovelR94G0.37
DLBCchr8100709732Splice_SiteNAX325_splice0.34
DLBCchr81007216475'UTRnovel0.47
ESCAchr81007220005'UTRnovel0.44
ESCAchr81007032033'UTRnovel0.09
ESCAchr81007220435'UTRnovel0.21
ESCAchr81007032083'UTRnovel0.12
ESCAchr8100721464SilentnovelI40I0.09
ESCAchr8100712788Missense_MutationnovelA247D0.33
GBMchr8100709709Missense_MutationnovelS332I0.32
GBMchr8100718279Splice_Regionrs751412519A65A0.15
HNSCchr8100706731Missense_MutationnovelV508F0.1
HNSCchr8100721509SilentnovelA25A0.14
KIRCchr8100712446SilentNAL296L0.16
KIRCchr8100706907Missense_MutationNAV476D0.19
KIRCchr8100706964In_Frame_DelnovelA458del0.08
KIRPchr8100705665SilentnovelV537V0.34
LAMLchr8100706992Missense_MutationnovelQ448K0.11
LGGchr8100712408Missense_Mutationrs772757487R309H0.33
LGGchr8100721555Frame_Shift_InsnovelM10Nfs*660.27
LIHCchr81007032503'UTRnovel0.13
LIHCchr8100721485SilentnovelP33P0.43
LIHCchr8100706679Missense_MutationNAN525S0.12
LIHCchr81007030443'UTRnovel0.27
LIHCchr8100709600SilentnovelA368A0.72
LUADchr8100709534SilentNAR390R0.12
LUADchr8100709674Missense_Mutationrs760039491E344K0.09
LUADchr8100706903Missense_MutationnovelM477I0.2
LUADchr8100706732SilentNAT507T0.21
LUADchr8100706958Missense_MutationNAP459L0.13
LUSCchr8100709602Missense_MutationnovelA368P0.15
LUSCchr8100706945Missense_MutationnovelF463L0.16
LUSCchr8100706697Missense_MutationNAN519S0.54
LUSCchr8100721529Missense_MutationnovelH19Y0.22PABP
OVchr8100712415Missense_MutationnovelD307Y0.09
OVchr8100709524Missense_MutationNAN394H0.14
OVchr8100706911SilentnovelR475R0.08
OVchr8100718096SilentnovelL126L0.04
READchr8100715540Nonsense_MutationNAE189*0.35
READchr8100717779Missense_MutationnovelR166H0.28
SARCchr8100709703Missense_MutationnovelG334E0.31
SARCchr8100709704Missense_MutationnovelG334R0.31
SKCMchr8100715499Missense_MutationnovelM202I0.29
SKCMchr8100717854Missense_MutationnovelG141E0.06
SKCMchr8100706701Missense_MutationNAR518C0.3
SKCMchr8100717859SilentNAG139G0.38
SKCMchr8100718099SilentnovelI125I0.16
SKCMchr8100721485Silentrs148248545P33P0.77
SKCMchr8100704935SilentNAL603L0.38
SKCMchr8100709637Missense_MutationnovelR356K0.21
SKCMchr8100704934Missense_Mutationrs753302028R604C0.36
SKCMchr8100705046Silentrs775197453L566L0.18
SKCMchr8100721567Missense_MutationNAP6L0.59
STADchr8100713175Missense_MutationnovelA217V0.1
STADchr8100706732SilentNAT507T0.13
STADchr8100721455SilentNAC43C0.17
STADchr8100706932Missense_Mutationrs763825223P468S0.08
STADchr8100717859SilentNAG139G0.11
STADchr8100705049SilentNAR565R0.07
STADchr81007216135'UTRnovel0.41
STADchr8100721570Missense_MutationNAA5V0.18
TGCTchr81007029983'UTRnovel0.27
THCAchr8100709721Frame_Shift_InsnovelE328Vfs*290.09
THYMchr81007219675'UTRnovel0.11
UCECchr8100706701Missense_MutationNAR518C0.33
UCECchr8100718258Missense_MutationNAM72I0.2
UCECchr81007029653'UTRnovel0.31
UCECchr8100709579Missense_MutationNAQ375H0.21
UCECchr8100717783Missense_MutationnovelD165Y0.27
UCECchr8100717779Missense_MutationnovelR166H0.05
UCECchr8100709132Splice_SiteNAX446_splice0.24
UCECchr81007029253'UTRnovel0.31
UCECchr8100718193Missense_MutationNAR94H0.21
UCECchr8100709614Missense_MutationnovelY364H0.05
UCECchr81007032733'UTRnovel0.21
UCECchr8100717783Missense_MutationnovelD165Y0.41
UCECchr8100718276Missense_MutationnovelE66D0.61
UCECchr8100705618Missense_MutationnovelA553V0.06
UCECchr81007033013'UTRnovel0.19
UCECchr8100715540Nonsense_MutationNAE189*0.63
UCECchr8100717835SilentnovelT147T0.68
UCECchr8100718214Missense_MutationnovelS87F0.62
UCECchr81007032443'UTRnovel0.3
UCECchr81007031483'UTRnovel0.52
UCECchr8100706758Missense_Mutationrs375849218A499T0.19
UCECchr8100721583Translation_Start_SitenovelM1?0.29
UCECchr8100706984Missense_MutationnovelM450I0.27
UCECchr8100705673Missense_MutationnovelP535S0.38
UCECchr8100718275Missense_MutationnovelR67C0.46
UCECchr81007032733'UTRnovel0.36
UCECchr8100709595Missense_Mutationrs777648449R370H0.22
UCECchr8100717783Missense_MutationnovelD165Y0.27
UCECchr81007031093'UTRnovel0.11
UCECchr8100706701Missense_MutationNAR518C0.4
UCECchr8100712372Missense_MutationnovelT321N0.41
UCECchr8100718175Missense_MutationnovelN100S0.1
UCECchr8100706918SilentnovelQ472Q0.23
UCECchr81007032443'UTRnovel0.16
UCECchr81007032813'UTRnovel0.24
UCECchr81007031473'UTRnovel0.62
UCECchr8100712433Missense_MutationNAL301I0.5
UCECchr8100715489Missense_MutationNAR206C0.38
UCECchr8100715590Missense_Mutationrs748141355R172Q0.35
UCECchr8100712408Missense_Mutationrs772757487R309H0.41
UCECchr8100717779Missense_MutationnovelR166H0.24
UCECchr8100718211Missense_MutationnovelQ88R0.37
UCECchr81007032693'UTRnovel0.33
UCECchr81007032443'UTRnovel0.34
UCECchr8100704925Splice_SitenovelX606_splice0.29
UCECchr8100709605Missense_MutationnovelL367V0.24
UCECchr8100712409Missense_Mutationrs776112793R309C0.17
UCSchr8100717802Missense_MutationnovelM158I0.07
UCSchr8100715481Missense_MutationnovelK208N0.08

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
KIRCAMP0.10420.15559
PRADAMP0.26633.7005e-05
SARCAMP0.27630.18425
TGCTAMP0.64670.13696
THCADEL0.0080.038162

Survival Analysis
CancerP-value Q-value
THYM0.049

Kaplan-Meier Survival Analysis

KIRC0.0032

Kaplan-Meier Survival Analysis

SARC0.00076

Kaplan-Meier Survival Analysis

ACC0.0023

Kaplan-Meier Survival Analysis

UCS0.04

Kaplan-Meier Survival Analysis

HNSC0.0068

Kaplan-Meier Survival Analysis

KIRP0.0001

Kaplan-Meier Survival Analysis

PAAD0.013

Kaplan-Meier Survival Analysis

PCPG0.023

Kaplan-Meier Survival Analysis

BLCA0.025

Kaplan-Meier Survival Analysis

CESC0.04

Kaplan-Meier Survival Analysis

KICH0.025

Kaplan-Meier Survival Analysis

GBM0.0073

Kaplan-Meier Survival Analysis

LIHC0.0023

Kaplan-Meier Survival Analysis

LGG0.00012

Kaplan-Meier Survival Analysis

CHOL0.046

Kaplan-Meier Survival Analysis

LUAD0.023

Kaplan-Meier Survival Analysis

UVM0.018

Kaplan-Meier Survival Analysis

OV0.029

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBDs
  • RBPome
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Pathways
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000070756 (Gene tree)
Gene ID
26986
Gene Symbol
PABPC1
Alias
PABP1|PABPL1|PAB1|PABPC2
Full Name
poly(A) binding protein cytoplasmic 1
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
37,183 bases
Position
chr8:100,685,816-100,722,998
Accession
8554
RBP type
canonical RBP
Summary
This gene encodes a poly(A) binding protein. The protein shuttles between the nucleus and cytoplasm and binds to the 3' poly(A) tail of eukaryotic messenger RNAs via RNA-recognition motifs. The binding of this protein to poly(A) promotes ribosome recruitment and translation initiation; it is also required for poly(A) shortening which is the first step in mRNA decay. The gene is part of a small gene family including three protein-coding genes and several pseudogenes.[provided by RefSeq, Aug 2010]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000428021PABPPF00658.182.9e-3211
ENSP00000428840PABPPF00658.183.6e-3211
ENSP00000478108PABPPF00658.186.9e-3211
ENSP00000429594PABPPF00658.189.2e-3211
ENSP00000429395PABPPF00658.189.8e-3211
ENSP00000313007PABPPF00658.181.1e-3111
ENSP00000428030PABPPF00658.189e-2111
ENSP00000478108RRM_5PF13893.63.2e-0812
ENSP00000478108RRM_5PF13893.63.2e-0822
ENSP00000313007RRM_5PF13893.65.7e-0812
ENSP00000313007RRM_5PF13893.65.7e-0822
ENSP00000429594RRM_5PF13893.67.7e-0812
ENSP00000429594RRM_5PF13893.67.7e-0822
ENSP00000313007RRM_1PF00076.222.5e-9014
ENSP00000313007RRM_1PF00076.222.5e-9024
ENSP00000313007RRM_1PF00076.222.5e-9034
ENSP00000313007RRM_1PF00076.222.5e-9044
ENSP00000478108RRM_1PF00076.229.8e-8414
ENSP00000478108RRM_1PF00076.229.8e-8424
ENSP00000478108RRM_1PF00076.229.8e-8434
ENSP00000478108RRM_1PF00076.229.8e-8444
ENSP00000429395RRM_1PF00076.224.9e-7914
ENSP00000429395RRM_1PF00076.224.9e-7924
ENSP00000429395RRM_1PF00076.224.9e-7934
ENSP00000429395RRM_1PF00076.224.9e-7944
ENSP00000429594RRM_1PF00076.222.6e-7514
ENSP00000429594RRM_1PF00076.222.6e-7524
ENSP00000429594RRM_1PF00076.222.6e-7534
ENSP00000429594RRM_1PF00076.222.6e-7544
ENSP00000427914RRM_1PF00076.225e-5313
ENSP00000427914RRM_1PF00076.225e-5323
ENSP00000427914RRM_1PF00076.225e-5333
ENSP00000429892RRM_1PF00076.221.6e-4213
ENSP00000429892RRM_1PF00076.221.6e-4223
ENSP00000429892RRM_1PF00076.221.6e-4233
ENSP00000429119RRM_1PF00076.222.2e-2812
ENSP00000429119RRM_1PF00076.222.2e-2822
ENSP00000430159RRM_1PF00076.226e-2512
ENSP00000430159RRM_1PF00076.226e-2522
ENSP00000430012RRM_1PF00076.222.2e-2311
ENSP00000429790RRM_1PF00076.221.6e-1911
ENSP00000428937RRM_1PF00076.223.7e-1411
ENSP00000428749RRM_1PF00076.223.4e-0711
ENSP00000429032RRM_1PF00076.223.5e-0511
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
22681889The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts4SURIC & HEK2932012 MayBaltz AGDOI: 10.1016/j.molcel.2012.05.021
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & HEK2932019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & HEK2932018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
29431736Capturing the interactome of newly transcribed RNAPolyT-RICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNARICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & Hela2018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & MCF10A2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
30528433The Human RNA-Binding Proteome and Its Dynamics during Translational ArrestXRNAX & MCF72018 Dec 6Trendel JDOI: 10.1016/j.cell.2018.11.004
30607034Comprehensive identification of RNA protein interactions in any organism using orthogonal organic phase separation (OOPS)OOPS & U2OS2019 Jan 3Queiroz RMLDOI: 10.1038/s41587-018-0001-2
27453046Comprehensive Identification of RNA-Binding Domains in Human CellsRIC & Hela2016 Aug 18Castello ADOI: 10.1016/j.molcel.2016.06.029
30352994Discovery of RNA-binding proteins and characterization of their dynamic responses by enhanced RNA interactome captureRIC & Jurkat2018 Oct 23Perez-Perri JIDOI:10.1038/s41467-018-06557-8

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
14717712Human PABP binds AU-rich RNA via RNA-binding domains 3 and 4.Eur J Biochem2004 JanSladic RT-
9195926Translation initiation factors eIF-iso4G and eIF-4B interact with the poly(A)-binding protein and increase its RNA binding activity.J Biol Chem1997 Jun 27Le H-
1675426The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities.Mol Cell Biol1991 JulBurd CG-
31037644Viral Regulation of RNA Granules in Infected Cells.Virol Sin2019 AprZhang Qdoi: 10.1007/s12250-019-00122-3
8609610Xenopus poly(A) binding protein: functional domains in RNA binding and protein-protein interaction.J Mol Biol1996 Feb 16Kuhn U-
22128154Makorin ring zinc finger protein 1 (MKRN1), a novel poly(A)-binding protein-interacting protein, stimulates translation in nerve cells.J Biol Chem2012 Jan 6Miroci Hdoi: 10.1074/jbc.M111.315291
21262214The Bin3 RNA methyltransferase is required for repression of caudal translation in the Drosophila embryo.Dev Biol2011 Apr 1Singh Ndoi: 10.1016/j.ydbio.2011.01.017
26545814Biochemical identification of new proteins involved in splicing repression at the Drosophila P-element exonic splicing silencer.Genes Dev2015 Nov 1Horan Ldoi: 10.1101/gad.268847.115.
30014536Distinct modes of stress granule assembly mediated by the KH-type RNA-binding protein Rnc1.Genes Cells2018 SepSatoh Rdoi: 10.1111/gtc.12624
23046583Expression of Fused in sarcoma mutations in mice recapitulates the neuropathology of FUS proteinopathies and provides insight into disease pathogenesis.Mol Neurodegener2012 Oct 10Verbeeck Cdoi: 10.1186/1750-1326-7-53.
22536444PKCα binds G3BP2 and regulates stress granule formation following cellular stress.PLoS One2012Kobayashi Tdoi: 10.1371/journal.pone.0035820
11051545A mechanism for translationally coupled mRNA turnover: interaction between the poly(A) tail and a c-fos RNA coding determinant via a protein complex.Cell2000 Sep 29Grosset C-
27836661Phosphorylation of poly(rC) binding protein 1 (PCBP1) contributes to stabilization of mu opioid receptor (MOR) mRNA via interaction with AU-rich element RNA-binding protein 1 (AUF1) and poly A binding protein (PABP).Gene2017 Jan 20Hwang CKdoi: 10.1016/j.gene.2016.11.003
3110598Primary structure of human nuclear ribonucleoprotein particle C proteins: conservation of sequence and domain structures in heterogeneous nuclear RNA, mRNA, and pre-rRNA-binding proteins.Mol Cell Biol1987 MaySwanson MS-
16407409Identification of the junctional plaque protein plakophilin 3 in cytoplasmic particles containing RNA-binding proteins and the recruitment of plakophilins 1 and 3 to stress granules.Mol Biol Cell2006 MarHofmann I-
10747998The phosphorylation state of poly(A)-binding protein specifies its binding to poly(A) RNA and its interaction with eukaryotic initiation factor (eIF) 4F, eIFiso4F, and eIF4B.J Biol Chem2000 Jun 9Le H-
15353001RNA-binding proteins to assess gene expression states of co-cultivated cells in response to tumor cells.Mol Cancer2004 Sep 7Penalva LO-
16714065Stability of casein mRNA is ensured by structural interactions between the 3'-untranslated region and poly(A) tail via the HuR and poly(A)-binding protein complex.Biochim Biophys Acta2006 Mar-AprNagaoka K-
21139564Multiple elements in the eIF4G1 N-terminus promote assembly of eIF4G1PABP mRNPs in vivo.EMBO J2011 Jan 19Park EHdoi: 10.1038/emboj.2010.312
20418951Molecular basis of eRF3 recognition by the MLLE domain of poly(A)-binding protein.PLoS One2010 Apr 14Kozlov Gdoi: 10.1371/journal.pone.0010169.
23881279Plakophilin-associated RNA-binding proteins in prostate cancer and their implications in tumor progression and metastasis.Virchows Arch2013 SepYang Cdoi: 10.1007/s00428-013-1452-y
28611064Cytoplasmic poly(A)-binding protein 1 (PABPC1) interacts with the RNA-binding protein hnRNPLL and thereby regulates immunoglobulin secretion in plasma cells.J Biol Chem2017 Jul 21Peng Ydoi: 10.1074/jbc.M117.794834
16356927The autoregulatory translational control element of poly(A)-binding protein mRNA forms a heteromeric ribonucleoprotein complex.Nucleic Acids Res2005 Dec 14Patel GP-
17606619eIF4G, eIFiso4G, and eIF4B bind the poly(A)-binding protein through overlapping sites within the RNA recognition motif domains.J Biol Chem2007 Aug 31Cheng S-
28756945SIRT1 Functions as a Negative Regulator of Eukaryotic Poly(A)RNA Transport.Curr Biol2017 Aug 7Shan Pdoi: 10.1016/j.cub.2017.06.040
7506090Stimulation of globin synthesis by 11-amino acid peptide.Biochem Mol Biol Int1993 OctRubin HN-
9245750Visualization of poly(A)-binding protein complex formation with poly(A) RNA using atomic force microscopy.J Struct Biol1997 JulSmith BL-
8253214Evolutionary clustering and functional similarity of RNA-binding proteins.FEBS Lett1993 Dec 6Fukami-Kobayashi K-
10954604Levels of free PABP are limited by newly polyadenylated mRNA in early Spisula embryogenesis.Nucleic Acids Res2000 Sep 1de Melo Neto OP-
15525674Staufen recruitment into stress granules does not affect early mRNA transport in oligodendrocytes.Mol Biol Cell2005 JanThomas MG-
17212783IMP1 interacts with poly(A)-binding protein (PABP) and the autoregulatory translational control element of PABP-mRNA through the KH III-IV domain.FEBS J2006 DecPatel GP-
21233286Novel mRNA-containing cytoplasmic granules in ALK-transformed cells.Mol Biol Cell2011 Mar 15Fawal Mdoi: 10.1091/mbc.E10-07-0569
25721894Genetic ablation of ataxin-2 increases several global translation factors in their transcript abundance but decreases translation rate.Neurogenetics2015 JulFittschen Mdoi: 10.1007/s10048-015-0441-5
9732454The mouse gene encoding the testis-specific isoform of Poly(A) binding protein (Pabp2) is an expressed retroposon: intimations that gene expression in spermatogenic cells facilitates the creation of new genes.J Mol Evol1998 SepKleene KC-
10499800Recognition of polyadenylate RNA by the poly(A)-binding protein.Cell1999 Sep 17Deo RC-
9582337The human poly(A)-binding protein 1 shuttles between the nucleus and the cytoplasm.J Biol Chem1998 May 22Afonina E-
8524242iPABP, an inducible poly(A)-binding protein detected in activated human T cells.Mol Cell Biol1995 DecYang H-
7908267The mRNA poly(A)-binding protein: localization, abundance, and RNA-binding specificity.Exp Cell Res1994 AprGorlach M-
11850402PABP1 identified as an arginine methyltransferase substrate using high-density protein arrays.EMBO Rep2002 MarLee J-
11287654X-ray structure of the human hyperplastic discs protein: an ortholog of the C-terminal domain of poly(A)-binding protein.Proc Natl Acad Sci U S A2001 Apr 10Deo RC-
15769879Yeast poly(A)-binding protein Pab1 shuttles between the nucleus and the cytoplasm and functions in mRNA export.RNA2005 AprBrune C-
15254188Calicivirus 3C-like proteinase inhibits cellular translation by cleavage of poly(A)-binding protein.J Virol2004 AugKuyumcu-Martinez M-
18692164Effects of poly(A)-binding protein on the interactions of translation initiation factor eIF4F and eIF4F.4B with internal ribosome entry site (IRES) of tobacco etch virus RNA.Biochim Biophys Acta2008 OctKhan MAdoi: 10.1016/j.bbagrm.2008.07.004
18490513Neural RNA-binding protein Musashi1 inhibits translation initiation by competing with eIF4G for PABP.J Cell Biol2008 May 19Kawahara Hdoi: 10.1083/jcb.200708004.
17726047Poly(A) binding protein, C-terminally truncated by the hepatitis A virus proteinase 3C, inhibits viral translation.Nucleic Acids Res2007Zhang B-
17445855Foot-and-mouth disease virus infection induces proteolytic cleavage of PTB, eIF3a,b, and PABP RNA-binding proteins.Virology2007 Aug 1Rodriguez Pulido M-
17358048Solution structure of the PABC domain from wheat poly (A)-binding protein: an insight into RNA metabolic and translational control in plants.Biochemistry2007 Apr 10Siddiqui N-
22837200Site-specific cleavage of the host poly(A) binding protein by the encephalomyocarditis virus 3C proteinase stimulates viral replication.J Virol2012 OctKobayashi Mdoi: 10.1128/JVI.00896-12
21508314A yeast model for polyalanine-expansion aggregation and toxicity.Mol Biol Cell2011 Jun 15Konopka CAdoi: 10.1091/mbc.E11-01-0037
21336257Anti-proliferative protein Tob negatively regulates CPEB3 target by recruiting Caf1 deadenylase.EMBO J2011 Apr 6Hosoda Ndoi: 10.1038/emboj.2011.37
21098120La-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.Mol Cell Biol2011 FebYang Rdoi: 10.1128/MCB.01162-10
23148093The association of a La module with the PABP-interacting motif PAM2 is a recurrent evolutionary process that led to the neofunctionalization of La-related proteins.RNA2013 JanMerret Rdoi: 10.1261/rna.035469.112
25225333Plakophilins 1 and 3 bind to FXR1 and thereby influence the mRNA stability of desmosomal proteins.Mol Cell Biol2014 Dec 1Fischer-Keso Rdoi: 10.1128/MCB.00766-14
25189382microRNA and human inducible nitric oxide synthase.Vitam Horm2014Guo Zdoi: 10.1016/B978-0-12-800254-4.00002-7.
25110030Poly(A)-binding proteins are required for diverse biological processes in metazoans.Biochem Soc Trans2014 AugSmith RWdoi: 10.1042/BST20140111.
24648398AKAP3 synthesis is mediated by RNA binding proteins and PKA signaling during mouse spermiogenesis.Biol Reprod2014 JunXu Kdoi: 10.1095/biolreprod.113.116111
23938467Linking spermatid ribonucleic acid (RNA) binding protein and retrogene diversity to reproductive success.Mol Cell Proteomics2013 NovChapman KMdoi: 10.1074/mcp.M113.030585
26912148BTG2 bridges PABPC1 RNA-binding domains and CAF1 deadenylase to control cell proliferation.Nat Commun2016 Feb 25Stupfler Bdoi: 10.1038/ncomms10811.
26013164Structure and Mechanism of Dimer-Monomer Transition of a Plant Poly(A)-Binding Protein upon RNA Interaction: Insights into Its Poly(A) Tail Assembly.J Mol Biol2015 Jul 31Domingues MNdoi: 10.1016/j.jmb.2015.05.017
28559344Viral and cellular mRNA-specific activators harness PABP and eIF4G to promote translation initiation downstream of cap binding.Proc Natl Acad Sci U S A2017 Jun 13Smith RWPdoi: 10.1073/pnas.1610417114
28653621A tail of translational regulation.Elife2017 Jun 27Gray GAdoi: 10.7554/eLife.29104.
28895529LARP4 mRNA codon-tRNA match contributes to LARP4 activity for ribosomal protein mRNA poly(A) tail length protection.Elife2017 Sep 12Mattijssen Sdoi: 10.7554/eLife.28889.
30040867Comparative proteomics of the two T. brucei PABPs suggests that PABP2 controls bulk mRNA.PLoS Negl Trop Dis2018 Jul 24Zoltner Mdoi: 10.1371/journal.pntd.0006679
24965446Host factors that interact with the pestivirus N-terminal protease, Npro, are components of the ribonucleoprotein complex.J Virol2014 SepJefferson Mdoi: 10.1128/JVI.00984-14
18977752Translation initiation factor 4B homodimerization, RNA binding, and interaction with Poly(A)-binding protein are enhanced by zinc.J Biol Chem2008 Dec 26Cheng Sdoi: 10.1074/jbc.M807716200
21402597Cellular cap-binding proteins associate with influenza virus mRNAs.J Gen Virol2011 JulBier Kdoi: 10.1099/vir.0.029231-0
19751846Isolation and functional characterization of eIF4F components and poly(A)-binding protein from Plasmodium falciparum.Parasitol Int2009 DecTuteja Rdoi: 10.1016/j.parint.2009.09.001
27749929Rabies Virus Infection Induces the Formation of Stress Granules Closely Connected to the Viral Factories.PLoS Pathog2016 Oct 17Nikolic Jdoi: 10.1371/journal.ppat.1005942
12162957Poly(A)-binding protein is associated with neuronal BC1 and BC200 ribonucleoprotein particles.J Mol Biol2002 Aug 16Muddashetty R-
16154588Inhibitory effect of naked neural BC1 RNA or BC200 RNA on eukaryotic in vitro translation systems is reversed by poly(A)-binding protein (PABP).J Mol Biol2005 Oct 14Kondrashov AV-
18957126Selective translational repression of HIV-1 RNA by Sam68DeltaC occurs by altering PABP1 binding to unspliced viral RNA.Retrovirology2008 Oct 28Marsh Kdoi: 10.1186/1742-4690-5-97.
17387282Poly(A)-binding protein binds to A-rich sequences via RNA-binding domains 1+2 and 3+4.RNA Biol2006 OctKhanam T-
28095120The bent conformation of poly(A)-binding protein induced by RNA-binding is required for its translational activation function.RNA Biol2017 Mar 4Hong KYdoi: 10.1080/15476286.2017.1280224
10373504An mRNA stability complex functions with poly(A)-binding protein to stabilize mRNA in vitro.Mol Cell Biol1999 JulWang Z-
12952955Identification of a C-terminal poly(A)-binding protein (PABP)-PABP interaction domain: role in cooperative binding to poly (A) and efficient cap distal translational repression.J Biol Chem2003 Nov 21Melo EO-
19641745Identification and bioinformatics characterization of translation initiation complex eIF4F components and poly(A)-binding protein from Plasmodium falciparum.Commun Integr Biol2009 MayTuteja R-
21957477Is there a classical nonsense-mediated decay pathway in trypanosomes?PLoS One2011Delhi Pdoi: 10.1371/journal.pone.0025112
20723624Poly(A) tail affects equilibrium and thermodynamic behavior of tobacco etch virus mRNA with translation initiation factors eIF4F, eIF4B and PABP.Biochim Biophys Acta2010 SepYumak Hdoi: 10.1016/j.bbagrm.2010.08.003
24674072Standard in vitro assays for protein-nucleic acid interactions--gel shift assays for RNA and DNA binding.Methods Enzymol2014Mitchell SFdoi: 10.1016/B978-0-12-420119-4.00015-X.
29447394Human La binds mRNAs through contacts to the poly(A) tail.Nucleic Acids Res2018 May 4Vinayak Jdoi: 10.1093/nar/gky090.
29782795RNA Modulates the Interaction between Influenza A Virus NS1 and Human PABP1.Biochemistry2018 Jul 3Arias-Mireles BHdoi: 10.1021/acs.biochem.8b00218
8631310Overexpression of poly(A) binding protein prevents maturation-specific deadenylation and translational inactivation in Xenopus oocytes.EMBO J1996 Feb 15Wormington M-
12820898Fructose modulates GLUT5 mRNA stability in differentiated Caco-2 cells: role of cAMP-signalling pathway and PABP (polyadenylated-binding protein)-interacting protein (Paip) 2.Biochem J2003 Oct 1Gouyon F-
12086624Recognition of eIF4G by rotavirus NSP3 reveals a basis for mRNA circularization.Mol Cell2002 JunGroft CM-
11997512Paip1 interacts with poly(A) binding protein through two independent binding motifs.Mol Cell Biol2002 JunRoy G-
11836384Efficient cleavage of ribosome-associated poly(A)-binding protein by enterovirus 3C protease.J Virol2002 MarKuyumcu-Martinez NM-
11438674Dual interactions of the translational repressor Paip2 with poly(A) binding protein.Mol Cell Biol2001 AugKhaleghpour K-
10799579Host protein interactions with the 3' end of bovine coronavirus RNA and the requirement of the poly(A) tail for coronavirus defective genome replication.J Virol2000 JunSpagnolo JF-
16834569The ARE-associated factor AUF1 binds poly(A) in vitro in competition with PABP.Biochem J2006 Dec 1Sagliocco F-
15498576Interaction of rat poly(A)-binding protein with poly(A)- and non-poly(A) sequences is preferentially mediated by RNA recognition motifs 3+4.FEBS Lett2004 Oct 22Mullin C-
15355595The roles of cytoplasmic poly(A)-binding proteins in regulating gene expression: a developmental perspective.Brief Funct Genomic Proteomic2004 AugGorgoni B-
15085179Poly(A)-binding-protein-mediated regulation of hDcp2 decapping in vitro.EMBO J2004 May 5Khanna R-
14645908PABP1 and eIF4GI associate with influenza virus NS1 protein in viral mRNA translation initiation complexes.J Gen Virol2003 DecBurgui I-
23077296Interplay between polyadenylate-binding protein 1 and Kaposi's sarcoma-associated herpesvirus ORF57 in accumulation of polyadenylated nuclear RNA, a viral long noncoding RNA.J Virol2013 JanMassimelli MJdoi: 10.1128/JVI.01693-12
19716330Mammalian miRNA RISC recruits CAF1 and PABP to affect PABP-dependent deadenylation.Mol Cell2009 Sep 24Fabian MRdoi: 10.1016/j.molcel.2009.08.004
19218215Poly(A)-binding protein binds to the non-polyadenylated 3' untranslated region of dengue virus and modulates translation efficiency.J Gen Virol2009 MarPolacek Cdoi: 10.1099/vir.0.007021-0.
19078965General RNA-binding proteins have a function in poly(A)-binding protein-dependent translation.EMBO J2009 Jan 7Svitkin YVdoi: 10.1038/emboj.2008.259
18467502Inhibition of tristetraprolin deadenylation by poly(A) binding protein.Am J Physiol Gastrointest Liver Physiol2008 SepRowlett RMdoi: 10.1152/ajpgi.00508.2007
18439994Large P body-like RNPs form in C. elegans oocytes in response to arrested ovulation, heat shock, osmotic stress, and anoxia and are regulated by the major sperm protein pathway.Dev Biol2008 Jun 1Jud MCdoi: 10.1016/j.ydbio.2008.02.059
18321554Modulation of enteroviral proteinase cleavage of poly(A)-binding protein (PABP) by conformation and PABP-associated factors.Virology2008 May 25Rivera CIdoi: 10.1016/j.virol.2008.02.002
17942745Stimulation of picornavirus replication by the poly(A) tail in a cell-free extract is largely independent of the poly(A) binding protein (PABP).RNA2007 DecSvitkin YV-
17761883Cap-independent translation is required for starvation-induced differentiation in yeast.Science2007 Aug 31Gilbert WV-
17766253A specific role for the C-terminal region of the Poly(A)-binding protein in mRNA decay.Nucleic Acids Res2007Simon E-
17652158The exon-junction-complex-component metastatic lymph node 51 functions in stress-granule assembly.J Cell Sci2007 Aug 15Baguet A-
22836166Mass spectrometric identification of proteins that interact through specific domains of the poly(A) binding protein.Mol Genet Genomics2012 SepRichardson Rdoi: 10.1007/s00438-012-0709-5
17150895Crystallization of auto-regulatory A-rich repeats found in the 5'-UTR of human PABP mRNA.Nucleic Acids Symp Ser (Oxf)2006Kikuchi K-
22745225Tracking expression and subcellular localization of RNA and protein species using high-throughput single cell imaging flow cytometry.RNA2012 AugBorah Sdoi: 10.1261/rna.033126.112
22577345The ezrin metastatic phenotype is associated with the initiation of protein translation.Neoplasia2012 AprBriggs JW-
22276125Role of the RNA-binding protein Nrd1 in stress granule formation and its implication in the stress response in fission yeast.PLoS One2012Satoh Rdoi: 10.1371/journal.pone.0029683
22022268A viral nuclear noncoding RNA binds re-localized poly(A) binding protein and is required for late KSHV gene expression.PLoS Pathog2011 OctBorah Sdoi: 10.1371/journal.ppat.1002300
21782810Pabp binds to the osk 3'UTR and specifically contributes to osk mRNA stability and oocyte accumulation.Dev Biol2011 Sep 15Vazquez-Pianzola Pdoi: 10.1016/j.ydbio.2011.07.009
21539810Crystal structure of the middle domain of human poly(A)-binding protein-interacting protein 1.Biochem Biophys Res Commun2011 May 20Lei Jdoi: 10.1016/j.bbrc.2011.04.088
20435044PUF3 acceleration of deadenylation in vivo can operate independently of CCR4 activity, possibly involving effects on the PAB1-mRNP structure.J Mol Biol2010 Jun 18Lee Ddoi: 10.1016/j.jmb.2010.04.034
20400847Crossing the borders: poly(A)-binding proteins working on both sides of the fence.RNA Biol2010 May-JunLemay JF-
28089630The Aspergillus nidulans Pbp1 homolog is required for normal sexual development and secondary metabolism.Fungal Genet Biol2017 MarSoukup AAdoi: 10.1016/j.fgb.2017.01.004
25111021Poly-A binding protein-1 localization to a subset of TDP-43 inclusions in amyotrophic lateral sclerosis occurs more frequently in patients harboring an expansion in C9orf72.J Neuropathol Exp Neurol2014 SepMcGurk Ldoi: 10.1097/NEN.0000000000000102.
24293655Poly(A) RNA and Paip2 act as allosteric regulators of poly(A)-binding protein.Nucleic Acids Res2014 FebLee SHdoi: 10.1093/nar/gkt1170
23687047ATAXIN-2 activates PERIOD translation to sustain circadian rhythms in Drosophila.Science2013 May 17Lim Cdoi: 10.1126/science.1234785.
23630313The DEAD-box helicase DDX3 substitutes for the cap-binding protein eIF4E to promote compartmentalized translation initiation of the HIV-1 genomic RNA.Nucleic Acids Res2013 JulSoto-Rifo Rdoi: 10.1093/nar/gkt306
27418677PABP enhances release factor recruitment and stop codon recognition during translation termination.Nucleic Acids Res2016 Sep 19Ivanov Adoi: 10.1093/nar/gkw635
26644407LARP4 Is Regulated by Tumor Necrosis Factor Alpha in a Tristetraprolin-Dependent Manner.Mol Cell Biol2015 Dec 7Mattijssen Sdoi: 10.1128/MCB.00804-15
26581983Host MicroRNA miR-197 Plays a Negative Regulatory Role in the Enterovirus 71 Infectious Cycle by Targeting the RAN Protein.J Virol2015 Nov 18Tang WFdoi: 10.1128/JVI.02143-15
29176600Cleavage of poly(A)-binding protein by duck hepatitis A virus 3C protease.Sci Rep2017 Nov 24Sun Ddoi: 10.1038/s41598-017-16484-1.
29295980Inhibition of Poly(A)-binding protein with a synthetic RNA mimic reduces pain sensitization in mice.Nat Commun2018 Jan 2Barragan-Iglesias Pdoi: 10.1038/s41467-017-02449-5.
29359180Nuclear, Cytosolic, and Surface-Localized Poly(A)-Binding Proteins of Plasmodium yoelii.mSphere2018 Jan 10Minns AMdoi: 10.1128/mSphere.00435-17
29362417Characterization of the multimeric structure of poly(A)-binding protein on a poly(A) tail.Sci Rep2018 Jan 23Sawazaki Rdoi: 10.1038/s41598-018-19659-6.
30820564LARP4A recognizes polyA RNA via a novel binding mechanism mediated by disordered regions and involving the PAM2w motif, revealing interplay between PABP, LARP4A and mRNA.Nucleic Acids Res2019 May 7Cruz-Gallardo Idoi: 10.1093/nar/gkz144.
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000522658PABPC1-220736-ENSP00000428840183 (aa)-H0YB75
ENST00000523636PABPC1-223818-ENSP00000428948165 (aa)-H0YB86
ENST00000521067PABPC1-217492-ENSP0000042893761 (aa)-E5RFD8
ENST00000517921PABPC1-203885--- (aa)--
ENST00000518293PABPC1-206608-ENSP0000043071642 (aa)-H0YC10
ENST00000522720PABPC1-221593-ENSP0000042979075 (aa)-E5RHG7
ENST00000519363PABPC1-210453-ENSP0000042903238 (aa)-E5RJM8
ENST00000522387PABPC1-2192331-ENSP00000429395604 (aa)-E7ERJ7
ENST00000518196PABPC1-205631-ENSP00000430159108 (aa)-E5RGH3
ENST00000517403PABPC1-202560-ENSP00000428190187 (aa)-H0YAW6
ENST00000523555PABPC1-222522-ENSP00000429892174 (aa)-H0YBN4
ENST00000518716PABPC1-207694--- (aa)--
ENST00000519004PABPC1-2082401-ENSP00000429594591 (aa)-E7EQV3
ENST00000318607PABPC1-2013485XM_005250861ENSP00000313007636 (aa)XP_005250918P11940
ENST00000519100PABPC1-209851-ENSP00000427914284 (aa)-H0YAR2
ENST00000519622PABPC1-212667-ENSP00000427805131 (aa)-H0YAP2
ENST00000519848PABPC1-213676--- (aa)--
ENST00000520868PABPC1-216971-ENSP00000428021169 (aa)-H0YAS6
ENST00000521865PABPC1-218628-ENSP00000429119129 (aa)-E5RJB9
ENST00000520142PABPC1-214754-ENSP00000430012118 (aa)-E5RH24
ENST00000519596PABPC1-211771--- (aa)--
ENST00000520804PABPC1-215493-ENSP0000042874943 (aa)-E5RGC4
ENST00000517990PABPC1-204487-ENSP00000428030136 (aa)-H0YAS7
ENST00000610907PABPC1-2241569-ENSP00000478108522 (aa)-A0A087WTT1
Gene Model
Click here to download ENSG00000070756's gene model file
Pathways
Pathway IDPathway NameSource
hsa03013RNA transportKEGG
hsa03015mRNA surveillance pathwayKEGG
hsa03018RNA degradationKEGG
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000070756's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000070756PABPC18436.508ENSG00000234414RBMY1A17738.710
ENSG00000070756PABPC19243.137ENSG00000196361ELAVL39236.145
ENSG00000070756PABPC18436.508ENSG00000114503NCBP26431.818
ENSG00000070756PABPC110088.372ENSG00000101104PABPC1L9886.822
ENSG00000070756PABPC18236.000ENSG00000076053RBM76832.927
ENSG00000070756PABPC19973.832ENSG00000254535PABPC4L9972.162
ENSG00000070756PABPC19988.333ENSG00000184388PABPC1L2B9880.102
ENSG00000070756PABPC18935.821ENSG00000102317RBM36241.935
ENSG00000070756PABPC18447.059ENSG00000100461RBM236241.667
ENSG00000070756PABPC16433.333ENSG00000104177MYEF28135.211
ENSG00000070756PABPC15234.211ENSG00000048740CELF25635.714
ENSG00000070756PABPC19840.909ENSG00000143368SF3B49333.333
ENSG00000070756PABPC17639.759ENSG00000161082CELF56639.759
ENSG00000070756PABPC15635.526ENSG00000149187CELF16036.047
ENSG00000070756PABPC19237.500ENSG00000179950PUF607131.469
ENSG00000070756PABPC19988.333ENSG00000186288PABPC1L2A9880.102
ENSG00000070756PABPC19936.538ENSG00000151923TIAL19844.828
ENSG00000070756PABPC18434.921ENSG00000213516RBMXL15040.260
ENSG00000070756PABPC19241.379ENSG00000066044ELAVL18741.379
ENSG00000070756PABPC19241.772ENSG00000180098TRNAU1AP6731.034
ENSG00000070756PABPC16434.667ENSG00000115875SRSF75334.667
ENSG00000070756PABPC199100.000ENSG00000090621PABPC49897.619
ENSG00000070756PABPC18738.462ENSG00000188529SRSF106539.062
ENSG00000070756PABPC19935.577ENSG00000116001TIA18842.553
ENSG00000070756PABPC19974.766ENSG00000174740PABPC59864.690
ENSG00000070756PABPC19897.561ENSG00000151846PABPC310091.994
ENSG00000070756PABPC18139.344ENSG00000084072PPIE5139.474
ENSG00000070756PABPC18931.624ENSG00000138668HNRNPD8631.304
ENSG00000070756PABPC15037.500ENSG00000101489CELF46831.193
ENSG00000070756PABPC19531.132ENSG00000115053NCL9133.333
ENSG00000070756PABPC18436.508ENSG00000242389RBMY1E7738.710
ENSG00000070756PABPC18436.508ENSG00000244395RBMY1D7738.710
ENSG00000070756PABPC16736.585ENSG00000159409CELF36635.616
ENSG00000070756PABPC18436.508ENSG00000242875RBMY1B7738.710
ENSG00000070756PABPC19541.935ENSG00000107105ELAVL28937.349
ENSG00000070756PABPC18438.095ENSG00000099622CIRBP9438.889
ENSG00000070756PABPC18449.020ENSG00000131051RBM397340.278
ENSG00000070756PABPC18434.921ENSG00000147274RBMX8139.683
ENSG00000070756PABPC18941.667ENSG00000106344RBM289830.827
ENSG00000070756PABPC16731.646ENSG00000161547SRSF26132.432
ENSG00000070756PABPC18030.952ENSG00000144642RBMS35630.952
ENSG00000070756PABPC16141.429ENSG00000099783HNRNPM6538.028
ENSG00000070756PABPC19540.323ENSG00000162374ELAVL48836.145
ENSG00000070756PABPC17136.364ENSG00000140488CELF67438.554
ENSG00000070756PABPC18332.258ENSG00000153250RBMS17831.579
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000070756PABPC1100100.000ENSAMEG00000000348PABPC110098.899Ailuropoda_melanoleuca
ENSG00000070756PABPC199100.000ENSAPLG00000001129PABPC110097.906Anas_platyrhynchos
ENSG00000070756PABPC1100100.000ENSACAG00000016470PABPC110093.016Anolis_carolinensis
ENSG00000070756PABPC1100100.000ENSANAG00000033352-10099.843Aotus_nancymaae
ENSG00000070756PABPC199100.000ENSANAG00000027730-10093.553Aotus_nancymaae
ENSG00000070756PABPC110090.164ENSANAG00000026678-10080.346Aotus_nancymaae
ENSG00000070756PABPC110089.720ENSANAG00000019222-10083.542Aotus_nancymaae
ENSG00000070756PABPC19991.379ENSANAG00000036324-9975.130Aotus_nancymaae
ENSG00000070756PABPC19991.176ENSANAG00000035841-9977.671Aotus_nancymaae
ENSG00000070756PABPC110097.674ENSAMXG00000018395-10090.752Astyanax_mexicanus
ENSG00000070756PABPC19997.024ENSBTAG00000052977-9694.553Bos_taurus
ENSG00000070756PABPC1100100.000ENSBTAG00000046358PABPC1100100.000Bos_taurus
ENSG00000070756PABPC19990.566ENSCJAG00000045282-10084.545Callithrix_jacchus
ENSG00000070756PABPC1100100.000ENSCJAG00000015833PABPC110099.843Callithrix_jacchus
ENSG00000070756PABPC1100100.000ENSCJAG00000041162-9494.820Callithrix_jacchus
ENSG00000070756PABPC1100100.000ENSCAFG00000000567PABPC1100100.000Canis_familiaris
ENSG00000070756PABPC1100100.000ENSCAFG00020000440PABPC1100100.000Canis_lupus_dingo
ENSG00000070756PABPC1100100.000ENSCHIG00000023714PABPC1100100.000Capra_hircus
ENSG00000070756PABPC1100100.000ENSTSYG00000004229PABPC1100100.000Carlito_syrichta
ENSG00000070756PABPC110089.815ENSTSYG00000033737-9089.213Carlito_syrichta
ENSG00000070756PABPC19998.214ENSTSYG00000037130-10083.856Carlito_syrichta
ENSG00000070756PABPC199100.000ENSCAPG00000013098PABPC19898.378Cavia_aperea
ENSG00000070756PABPC1100100.000ENSCPOG00000012917PABPC198100.000Cavia_porcellus
ENSG00000070756PABPC19692.424ENSCCAG00000031750-9788.525Cebus_capucinus
ENSG00000070756PABPC1100100.000ENSCCAG00000037733-10099.286Cebus_capucinus
ENSG00000070756PABPC19994.444ENSCCAG00000037208PABPC310090.282Cebus_capucinus
ENSG00000070756PABPC110090.654ENSCCAG00000031444-10088.529Cebus_capucinus
ENSG00000070756PABPC19997.222ENSCCAG00000027395-10078.840Cebus_capucinus
ENSG00000070756PABPC110090.164ENSCCAG00000028512-10078.978Cebus_capucinus
ENSG00000070756PABPC19997.222ENSCATG00000029313PABPC310092.925Cercocebus_atys
ENSG00000070756PABPC19587.500ENSCATG00000045341-10077.316Cercocebus_atys
ENSG00000070756PABPC1100100.000ENSCATG00000039184PABPC1100100.000Cercocebus_atys
ENSG00000070756PABPC19892.683ENSCATG00000044984-10079.344Cercocebus_atys
ENSG00000070756PABPC110099.454ENSCLAG00000009676PABPC110099.825Chinchilla_lanigera
ENSG00000070756PABPC1100100.000ENSCSAG00000012017PABPC1100100.000Chlorocebus_sabaeus
ENSG00000070756PABPC199100.000ENSCHOG00000008178PABPC19987.087Choloepus_hoffmanni
ENSG00000070756PABPC1100100.000ENSCPBG00000005782PABPC110097.799Chrysemys_picta_bellii
ENSG00000070756PABPC199100.000ENSCANG00000041712PABPC310091.981Colobus_angolensis_palliatus
ENSG00000070756PABPC19595.050ENSCANG00000036233-9997.030Colobus_angolensis_palliatus
ENSG00000070756PABPC1100100.000ENSCANG00000021524PABPC19799.172Colobus_angolensis_palliatus
ENSG00000070756PABPC110095.628ENSCANG00000013549-10096.127Colobus_angolensis_palliatus
ENSG00000070756PABPC1100100.000ENSCGRG00001022067-10099.686Cricetulus_griseus_chok1gshd
ENSG00000070756PABPC19893.396ENSCGRG00001007983Pabpc69985.417Cricetulus_griseus_chok1gshd
ENSG00000070756PABPC19892.683ENSCGRG00000005826-9083.037Cricetulus_griseus_crigri
ENSG00000070756PABPC199100.000ENSCGRG00000006487-10099.124Cricetulus_griseus_crigri
ENSG00000070756PABPC19893.396ENSCGRG00000019560Pabpc69985.417Cricetulus_griseus_crigri
ENSG00000070756PABPC1100100.000ENSDNOG00000008718PABPC1100100.000Dasypus_novemcinctus
ENSG00000070756PABPC198100.000ENSDNOG00000006598-10090.638Dasypus_novemcinctus
ENSG00000070756PABPC110077.778ENSDNOG00000030956-9969.103Dasypus_novemcinctus
ENSG00000070756PABPC1100100.000ENSDORG00000013935Pabpc110099.843Dipodomys_ordii
ENSG00000070756PABPC199100.000ENSETEG00000002793-8499.614Echinops_telfairi
ENSG00000070756PABPC199100.000ENSETEG00000019213-10088.000Echinops_telfairi
ENSG00000070756PABPC19958.491ENSEASG00005014126-9849.841Equus_asinus_asinus
ENSG00000070756PABPC1100100.000ENSEASG00005002810PABPC1100100.000Equus_asinus_asinus
ENSG00000070756PABPC1100100.000ENSECAG00000020699PABPC1100100.000Equus_caballus
ENSG00000070756PABPC19266.942ENSECAG00000038200-9550.392Equus_caballus
ENSG00000070756PABPC1100100.000ENSEEUG00000002701PABPC110098.772Erinaceus_europaeus
ENSG00000070756PABPC19661.972ENSELUG00000005247-8857.751Esox_lucius
ENSG00000070756PABPC1100100.000ENSFCAG00000001874PABPC1100100.000Felis_catus
ENSG00000070756PABPC199100.000ENSFALG00000005841PABPC110097.906Ficedula_albicollis
ENSG00000070756PABPC19994.393ENSFDAG00000018480PABPC39890.476Fukomys_damarensis
ENSG00000070756PABPC1100100.000ENSFDAG00000005583PABPC1100100.000Fukomys_damarensis
ENSG00000070756PABPC1100100.000ENSGALG00000030280PABPC110098.116Gallus_gallus
ENSG00000070756PABPC1100100.000ENSGAGG00000000869PABPC110098.428Gopherus_agassizii
ENSG00000070756PABPC19897.561ENSGGOG00000041637-10071.406Gorilla_gorilla
ENSG00000070756PABPC19997.222ENSGGOG00000013146PABPC310091.994Gorilla_gorilla
ENSG00000070756PABPC19987.912ENSGGOG00000039851-10069.494Gorilla_gorilla
ENSG00000070756PABPC1100100.000ENSGGOG00000006785-100100.000Gorilla_gorilla
ENSG00000070756PABPC19895.122ENSHGLG00000003042-9782.560Heterocephalus_glaber_female
ENSG00000070756PABPC1100100.000ENSHGLG00000007713-10099.843Heterocephalus_glaber_female
ENSG00000070756PABPC19895.122ENSHGLG00100000417-9788.547Heterocephalus_glaber_male
ENSG00000070756PABPC110099.454ENSHGLG00100007448-10099.825Heterocephalus_glaber_male
ENSG00000070756PABPC19768.421ENSIPUG00000019895-6050.000Ictalurus_punctatus
ENSG00000070756PABPC19754.400ENSIPUG00000010020-7057.246Ictalurus_punctatus
ENSG00000070756PABPC19573.196ENSIPUG00000024284-9550.000Ictalurus_punctatus
ENSG00000070756PABPC18161.290ENSIPUG00000007890-5153.659Ictalurus_punctatus
ENSG00000070756PABPC19265.049ENSIPUG00000020086-8364.706Ictalurus_punctatus
ENSG00000070756PABPC1100100.000ENSSTOG00000016395PABPC3100100.000Ictidomys_tridecemlineatus
ENSG00000070756PABPC19884.906ENSJJAG00000019230Pabpc610079.567Jaculus_jaculus
ENSG00000070756PABPC110091.667ENSJJAG00000014258Pabpc29984.404Jaculus_jaculus
ENSG00000070756PABPC1100100.000ENSJJAG00000015918Pabpc1100100.000Jaculus_jaculus
ENSG00000070756PABPC1100100.000ENSLACG00000004395PABPC19998.337Latimeria_chalumnae
ENSG00000070756PABPC1100100.000ENSLOCG00000009681PABPC110093.125Lepisosteus_oculatus
ENSG00000070756PABPC19887.805ENSLAFG00000007939-10069.025Loxodonta_africana
ENSG00000070756PABPC1100100.000ENSLAFG00000013994PABPC1100100.000Loxodonta_africana
ENSG00000070756PABPC110099.454ENSMFAG00000004725-10098.780Macaca_fascicularis
ENSG00000070756PABPC110093.478ENSMFAG00000016858PABPC310093.093Macaca_fascicularis
ENSG00000070756PABPC19590.000ENSMFAG00000034213-10073.019Macaca_fascicularis
ENSG00000070756PABPC1100100.000ENSMFAG00000044845PABPC1100100.000Macaca_fascicularis
ENSG00000070756PABPC19896.694ENSMMUG00000020835PABPC39394.558Macaca_mulatta
ENSG00000070756PABPC1100100.000ENSMMUG00000017786PABPC1100100.000Macaca_mulatta
ENSG00000070756PABPC19585.000ENSMMUG00000041053-10069.074Macaca_mulatta
ENSG00000070756PABPC199100.000ENSMMUG00000047411-10099.062Macaca_mulatta
ENSG00000070756PABPC199100.000ENSMNEG00000042936PABPC310093.564Macaca_nemestrina
ENSG00000070756PABPC110098.913ENSMNEG00000010564-9998.261Macaca_nemestrina
ENSG00000070756PABPC1100100.000ENSMNEG00000009340-100100.000Macaca_nemestrina
ENSG00000070756PABPC19892.683ENSMNEG00000007852-10069.497Macaca_nemestrina
ENSG00000070756PABPC19590.000ENSMLEG00000041649-9969.697Mandrillus_leucophaeus
ENSG00000070756PABPC19986.111ENSMLEG00000043225-8377.431Mandrillus_leucophaeus
ENSG00000070756PABPC1100100.000ENSMLEG00000027792-9998.294Mandrillus_leucophaeus
ENSG00000070756PABPC199100.000ENSMLEG00000042214PABPC310093.553Mandrillus_leucophaeus
ENSG00000070756PABPC199100.000ENSMGAG00000012239PABPC19997.906Meleagris_gallopavo
ENSG00000070756PABPC110092.105ENSMAUG00000017991Pabpc29986.651Mesocricetus_auratus
ENSG00000070756PABPC19892.453ENSMAUG00000003031Pabpc610080.031Mesocricetus_auratus
ENSG00000070756PABPC110099.454ENSMAUG00000003523Pabpc110095.447Mesocricetus_auratus
ENSG00000070756PABPC110097.674ENSMICG00000011830PABPC310092.138Microcebus_murinus
ENSG00000070756PABPC1100100.000ENSMICG00000009121PABPC1100100.000Microcebus_murinus
ENSG00000070756PABPC1100100.000ENSMOCG00000018191-100100.000Microtus_ochrogaster
ENSG00000070756PABPC110090.741ENSMOCG00000001354Pabpc29980.472Microtus_ochrogaster
ENSG00000070756PABPC110099.454ENSMOCG00000004921-10098.428Microtus_ochrogaster
ENSG00000070756PABPC19997.101ENSMODG00000012040-10092.602Monodelphis_domestica
ENSG00000070756PABPC1100100.000ENSMODG00000006222PABPC110099.058Monodelphis_domestica
ENSG00000070756PABPC110095.370ENSMODG00000017105-9992.506Monodelphis_domestica
ENSG00000070756PABPC110092.105MGP_CAROLIEiJ_G0021058Pabpc69984.954Mus_caroli
ENSG00000070756PABPC1100100.000MGP_CAROLIEiJ_G0019740Pabpc110099.691Mus_caroli
ENSG00000070756PABPC110090.741MGP_CAROLIEiJ_G0022217Pabpc29685.246Mus_caroli
ENSG00000070756PABPC110092.105ENSMUSG00000046173Pabpc69984.491Mus_musculus
ENSG00000070756PABPC1100100.000ENSMUSG00000022283Pabpc1100100.000Mus_musculus
ENSG00000070756PABPC110090.741ENSMUSG00000051732Pabpc29985.012Mus_musculus
ENSG00000070756PABPC110091.667MGP_PahariEiJ_G0018950Pabpc29586.183Mus_pahari
ENSG00000070756PABPC1100100.000MGP_PahariEiJ_G0019749Pabpc110099.214Mus_pahari
ENSG00000070756PABPC19283.333MGP_PahariEiJ_G0023374-9973.056Mus_pahari
ENSG00000070756PABPC110092.105MGP_SPRETEiJ_G0021962Pabpc69984.028Mus_spretus
ENSG00000070756PABPC110090.741MGP_SPRETEiJ_G0023126Pabpc210080.189Mus_spretus
ENSG00000070756PABPC1100100.000MGP_SPRETEiJ_G0020636Pabpc110099.686Mus_spretus
ENSG00000070756PABPC1100100.000ENSMPUG00000015163PABPC110099.650Mustela_putorius_furo
ENSG00000070756PABPC199100.000ENSMLUG00000012245PABPC110094.976Myotis_lucifugus
ENSG00000070756PABPC19880.952ENSMLUG00000030069-9963.443Myotis_lucifugus
ENSG00000070756PABPC19888.679ENSNGAG00000000987Pabpc69979.841Nannospalax_galili
ENSG00000070756PABPC19895.122ENSNGAG00000023773-10076.311Nannospalax_galili
ENSG00000070756PABPC19897.561ENSNGAG00000023820-10086.120Nannospalax_galili
ENSG00000070756PABPC1100100.000ENSNGAG00000000996Pabpc1100100.000Nannospalax_galili
ENSG00000070756PABPC19986.916ENSNGAG00000016040Pabpc29882.904Nannospalax_galili
ENSG00000070756PABPC110093.204ENSNLEG00000018338PABPC39991.038Nomascus_leucogenys
ENSG00000070756PABPC1100100.000ENSNLEG00000003142-100100.000Nomascus_leucogenys
ENSG00000070756PABPC19571.171ENSNLEG00000034154-9964.626Nomascus_leucogenys
ENSG00000070756PABPC19892.683ENSNLEG00000034666-9883.969Nomascus_leucogenys
ENSG00000070756PABPC19988.398ENSNLEG00000030011-9982.545Nomascus_leucogenys
ENSG00000070756PABPC1100100.000ENSOPRG00000009667PABPC310099.843Ochotona_princeps
ENSG00000070756PABPC110097.674ENSODEG00000013269-9689.228Octodon_degus
ENSG00000070756PABPC1100100.000ENSODEG00000003229PABPC19599.493Octodon_degus
ENSG00000070756PABPC1100100.000ENSOANG00000007307PABPC110099.057Ornithorhynchus_anatinus
ENSG00000070756PABPC1100100.000ENSOCUG00000023935-10099.686Oryctolagus_cuniculus
ENSG00000070756PABPC1100100.000ENSOCUG00000004354-10099.843Oryctolagus_cuniculus
ENSG00000070756PABPC110091.667ENSOGAG00000025522-10085.047Otolemur_garnettii
ENSG00000070756PABPC1100100.000ENSOGAG00000007921-10092.692Otolemur_garnettii
ENSG00000070756PABPC199100.000ENSOGAG00000033115-10092.163Otolemur_garnettii
ENSG00000070756PABPC110093.519ENSOGAG00000033369-10082.353Otolemur_garnettii
ENSG00000070756PABPC1100100.000ENSOARG00000000095PABPC1100100.000Ovis_aries
ENSG00000070756PABPC1100100.000ENSPPAG00000037498-99100.000Pan_paniscus
ENSG00000070756PABPC19985.165ENSPPAG00000037955-10082.201Pan_paniscus
ENSG00000070756PABPC110087.963ENSPPAG00000036729-9874.121Pan_paniscus
ENSG00000070756PABPC1100100.000ENSPPRG00000003755PABPC1100100.000Panthera_pardus
ENSG00000070756PABPC1100100.000ENSPTIG00000021083PABPC196100.000Panthera_tigris_altaica
ENSG00000070756PABPC19985.714ENSPTRG00000045319-10082.524Pan_troglodytes
ENSG00000070756PABPC19997.222ENSPTRG00000022593PABPC310091.706Pan_troglodytes
ENSG00000070756PABPC19094.737ENSPTRG00000047501-10089.256Pan_troglodytes
ENSG00000070756PABPC1100100.000ENSPTRG00000047939PABPC1100100.000Pan_troglodytes
ENSG00000070756PABPC199100.000ENSPANG00000032213PABPC310092.453Papio_anubis
ENSG00000070756PABPC19890.244ENSPANG00000032575-10093.671Papio_anubis
ENSG00000070756PABPC19590.000ENSPANG00000030537-9970.523Papio_anubis
ENSG00000070756PABPC1100100.000ENSPANG00000010645PABPC110098.148Papio_anubis
ENSG00000070756PABPC19777.143ENSPKIG00000002905-9477.344Paramormyrops_kingsleyae
ENSG00000070756PABPC19594.595ENSPKIG00000016835-9787.124Paramormyrops_kingsleyae
ENSG00000070756PABPC19777.143ENSPKIG00000002089-9477.344Paramormyrops_kingsleyae
ENSG00000070756PABPC19882.927ENSPKIG00000016850-7980.000Paramormyrops_kingsleyae
ENSG00000070756PABPC1100100.000ENSPSIG00000003719PABPC110098.428Pelodiscus_sinensis
ENSG00000070756PABPC19885.366ENSPMGG00000022485-9370.414Periophthalmus_magnuspinnatus
ENSG00000070756PABPC1100100.000ENSPEMG00000014998Pabpc110099.528Peromyscus_maniculatus_bairdii
ENSG00000070756PABPC110092.105ENSPEMG00000013149Pabpc29987.354Peromyscus_maniculatus_bairdii
ENSG00000070756PABPC1100100.000ENSPCIG00000000267-10098.584Phascolarctos_cinereus
ENSG00000070756PABPC19577.477ENSPPYG00000012833-9972.165Pongo_abelii
ENSG00000070756PABPC1100100.000ENSPPYG00000018790PABPC1100100.000Pongo_abelii
ENSG00000070756PABPC19997.222ENSPPYG00000005219PABPC310094.016Pongo_abelii
ENSG00000070756PABPC1100100.000ENSPCAG00000007096PABPC184100.000Procavia_capensis
ENSG00000070756PABPC110095.349ENSPCOG00000013197PABPC310091.667Propithecus_coquereli
ENSG00000070756PABPC1100100.000ENSPCOG00000020234PABPC1100100.000Propithecus_coquereli
ENSG00000070756PABPC1100100.000ENSPVAG00000016640PABPC110099.686Pteropus_vampyrus
ENSG00000070756PABPC1100100.000ENSRNOG00000008639Pabpc110099.528Rattus_norvegicus
ENSG00000070756PABPC110091.667ENSRNOG00000014527Pabpc29985.714Rattus_norvegicus
ENSG00000070756PABPC110092.105ENSRNOG00000017367Pabpc69981.779Rattus_norvegicus
ENSG00000070756PABPC19982.178ENSRBIG00000027660-9970.646Rhinopithecus_bieti
ENSG00000070756PABPC1100100.000ENSRBIG00000029759-10095.238Rhinopithecus_bieti
ENSG00000070756PABPC19294.215ENSRBIG00000000042-9974.885Rhinopithecus_bieti
ENSG00000070756PABPC19997.222ENSRBIG00000034396PABPC310092.453Rhinopithecus_bieti
ENSG00000070756PABPC19987.129ENSRROG00000044781-9972.016Rhinopithecus_roxellana
ENSG00000070756PABPC1100100.000ENSRROG00000042796-10099.296Rhinopithecus_roxellana
ENSG00000070756PABPC19997.222ENSRROG00000036871PABPC310092.453Rhinopithecus_roxellana
ENSG00000070756PABPC198100.000ENSRROG00000032349-10094.795Rhinopithecus_roxellana
ENSG00000070756PABPC19892.683ENSRROG00000028723-10072.642Rhinopithecus_roxellana
ENSG00000070756PABPC19279.279ENSRROG00000029758-9368.874Rhinopithecus_roxellana
ENSG00000070756PABPC19993.458ENSSBOG00000025499-10089.565Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC110087.850ENSSBOG00000021975-9585.390Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC19997.222ENSSBOG00000023677PABPC310088.906Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC110084.426ENSSBOG00000020745-9786.230Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC1100100.000ENSSBOG00000022216PABPC110099.648Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC19885.366ENSSBOG00000026437-10065.463Saimiri_boliviensis_boliviensis
ENSG00000070756PABPC110097.222ENSSHAG00000003431-9994.848Sarcophilus_harrisii
ENSG00000070756PABPC1100100.000ENSSHAG00000011267PABPC19996.357Sarcophilus_harrisii
ENSG00000070756PABPC110088.785ENSSFOG00015006617-10083.046Scleropages_formosus
ENSG00000070756PABPC17269.492ENSSFOG00015019638-7852.653Scleropages_formosus
ENSG00000070756PABPC19784.286ENSSLDG00000009165-9989.630Seriola_lalandi_dorsalis
ENSG00000070756PABPC199100.000ENSSARG00000004448PABPC110091.497Sorex_araneus
ENSG00000070756PABPC19599.174ENSSPUG00000018259-9882.245Sphenodon_punctatus
ENSG00000070756PABPC1100100.000ENSSPUG00000018267PABPC110098.428Sphenodon_punctatus
ENSG00000070756PABPC19878.049ENSSSCG00000036199-10049.060Sus_scrofa
ENSG00000070756PABPC1100100.000ENSSSCG00000006063PABPC1100100.000Sus_scrofa
ENSG00000070756PABPC110075.229ENSSSCG00000033638-9673.826Sus_scrofa
ENSG00000070756PABPC1100100.000ENSTGUG00000012067PABPC110097.959Taeniopygia_guttata
ENSG00000070756PABPC110098.361ENSTBEG00000009320PABPC18998.361Tupaia_belangeri
ENSG00000070756PABPC1100100.000ENSTTRG00000004689PABPC310096.226Tursiops_truncatus
ENSG00000070756PABPC1100100.000ENSUAMG00000024428PABPC1100100.000Ursus_americanus
ENSG00000070756PABPC19269.748ENSUAMG00000022453-9953.156Ursus_americanus
ENSG00000070756PABPC1100100.000ENSUMAG00000017554PABPC1100100.000Ursus_maritimus
ENSG00000070756PABPC19067.273ENSVPAG00000011006-9847.632Vicugna_pacos
ENSG00000070756PABPC199100.000ENSVPAG00000003865PABPC110099.815Vicugna_pacos
ENSG00000070756PABPC1100100.000ENSVVUG00000013156PABPC1100100.000Vulpes_vulpes
ENSG00000070756PABPC1100100.000ENSXETG00000006635pabpc19995.440Xenopus_tropicalis
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000184nuclear-transcribed mRNA catabolic process, nonsense-mediated decay-TASProcess
GO:0000398mRNA splicing, via spliceosome11991638.ICProcess
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding21873635.IBAFunction
GO:0003723RNA binding25225333.IDAFunction
GO:0003730mRNA 3'-UTR binding21873635.IBAFunction
GO:0003730mRNA 3'-UTR binding16126846.IDAFunction
GO:0005515protein binding11051545.11172725.11997512.12086624.12489690.14685257.15567442.15663938.16452507.16556936.16601676.16772376.16804161.17289661.17392519.17595167.17932509.18447585.18596238.19515850.19716330.20098421.20181956.20221403.20418951.20430826.20595389.20595394.20696395.21063388.21098120.21883093.21981923.22872150.23125361.23340509.23665581.23770097.23788676.24396066.24532714.24965446.25225333.26735137.27871484.28877994.28931820.IPIFunction
GO:0005634nucleus21873635.IBAComponent
GO:0005634nucleus21940797.IDAComponent
GO:0005737cytoplasm21873635.IBAComponent
GO:0005737cytoplasm9582337.TASComponent
GO:0005829cytosol21873635.IBAComponent
GO:0005829cytosol-IDAComponent
GO:0005829cytosol-TASComponent
GO:0005925focal adhesion21423176.HDAComponent
GO:0006378mRNA polyadenylation2885805.TASProcess
GO:0006413translational initiation-TASProcess
GO:0008022protein C-terminus binding15663938.IPIFunction
GO:0008143poly(A) binding21873635.IBAFunction
GO:0008143poly(A) binding16804161.21984414.IDAFunction
GO:0008143poly(A) binding2885805.TASFunction
GO:0008266poly(U) RNA binding21873635.IBAFunction
GO:0008266poly(U) RNA binding21984414.IDAFunction
GO:0008494translation activator activity11997512.TASFunction
GO:0010494cytoplasmic stress granule21873635.IBAComponent
GO:0010494cytoplasmic stress granule21883093.21940797.IDAComponent
GO:0016020membrane19946888.HDAComponent
GO:0030425dendrite-IEAComponent
GO:0031047gene silencing by RNA-ISSProcess
GO:0036464cytoplasmic ribonucleoprotein granule15121898.IDAComponent
GO:0043488regulation of mRNA stability-TASProcess
GO:0045070positive regulation of viral genome replication26735137.IMPProcess
GO:0045202synapse-IEAComponent
GO:0045727positive regulation of translation-IEAProcess
GO:0048255mRNA stabilization11997512.TASProcess
GO:0060213positive regulation of nuclear-transcribed mRNA poly(A) tail shortening-ISSProcess
GO:0070062extracellular exosome23533145.HDAComponent
GO:0071013catalytic step 2 spliceosome11991638.IDAComponent
GO:1900153positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay-ISSProcess
GO:1990124messenger ribonucleoprotein complex-IEAComponent
GO:1990904ribonucleoprotein complex21873635.IBAComponent
GO:1990904ribonucleoprotein complex17289661.IDAComponent
GO:2000623negative regulation of nuclear-transcribed mRNA catabolic process, nonsense-mediated decay18447585.IDAProcess
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