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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
21956899High nuclear RBM3 expression is associated with an improved prognosis in colorectal cancer.Proteomics Clin Appl2011 DecHjelm Bdoi: 10.1002/prca.201100020.
30758670Prevalence and clinical significance of RBM3 immunostaining in non-small cell lung cancers.J Cancer Res Clin Oncol2019 AprMelling Ndoi: 10.1007/s00432-019-02850-1
26331352RNA binding protein RBM3 increases β-catenin signaling to increase stem cell characteristics in colorectal cancer cells.Mol Carcinog2016 NovVenugopal Adoi: 10.1002/mc.22404
24380696High RNA-binding motif protein 3 expression is an independent prognostic marker in operated prostate cancer and tightly linked to ERG activation and PTEN deletions.Eur J Cancer2014 MarGrupp Kdoi: 10.1016/j.ejca.2013.12.003
19277990Down-regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity.J Cell Biochem2009 May 1Zeng Ydoi: 10.1002/jcb.22114.
19734850Nuclear expression of the RNA-binding protein RBM3 is associated with an improved clinical outcome in breast cancer.Mod Pathol2009 DecJgi Adoi: 10.1038/modpathol.2009.124
23565664Decreased expression of RNA-binding motif protein 3 correlates with tumour progression and poor prognosis in urothelial bladder cancer.BMC Urol2013 Apr 8Boman Kdoi: 10.1186/1471-2490-13-17.
21955582High RBM3 expression in prostate cancer independently predicts a reduced risk of biochemical recurrence and disease progression.Diagn Pathol2011 Sep 28Jonsson Ldoi: 10.1186/1746-1596-6-91.
20727170Expression of the RNA-binding protein RBM3 is associated with a favourable prognosis and cisplatin sensitivity in epithelial ovarian cancer.J Transl Med2010 Aug 20Ehl??n Adoi: 10.1186/1479-5876-8-78.
16552754Positive correlation between the expression of X-chromosome RBM genes (RBMX, RBM3, RBM10) and the proapoptotic Bax gene in human breast cancer.J Cell Biochem2006 Apr 15Mart??nez-Arribas F-
28373441Expression of RNA-binding Motif Protein 3 (RBM3) and Cold-inducible RNA-binding protein (CIRP) Is Associated with Improved Clinical Outcome in Patients with Colon Cancer.Anticancer Res2017 AprJang HH-
28800641High RBM3 expression is associated with an improved survival and oxaliplatin response in patients with metastatic colorectal cancer.PLoS One2017 Aug 11Siesing Cdoi: 10.1371/journal.pone.0182512
29263314High RNA-Binding Motif Protein 3 (RBM3) Expression is Independently Associated with Prolonged Overall Survival in Intestinal-Type Gastric Cancer.Med Sci Monit2017 Dec 21Ye F-
30419865Reduced RBM3 expression is associated with aggressive tumor features in esophageal cancer but not significantly linked to patient outcome.BMC Cancer2018 Nov 12Grupp Kdoi: 10.1186/s12885-018-5032-z.

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
ACCchrX485751805'UTRrs7822908030.97
ACCchrX485751805'UTRrs7822908030.46
BRCAchrX48575642Missense_MutationNAV62D0.39RRM_1
CESCchrX48575682IntronNA0.23
CESCchrX48575219SilentnovelL13L0.18
CESCchrX48575207SilentnovelF9F0.38
CESCchrX48575387IntronNA0.13
CESCchrX48577046Missense_Mutationrs111680576R145H0.36
CESCchrX48576372Missense_MutationnovelR90T0.17
CESCchrX48576390Missense_MutationNAA96V0.15
COADchrX485750355'UTRnovel0.39
COADchrX48576398Missense_Mutationrs782287047R99C0.48
ESCAchrX48575268Missense_MutationnovelG30R0.09RRM_1
GBMchrX48575566Missense_MutationnovelV37I0.2RRM_1
KICHchrX48576414Missense_MutationnovelS104F0.07
LAMLchrX485751795'UTRrs7826635130.32
LAMLchrX48575192Missense_MutationnovelE4D0.09
LAMLchrX48575268Missense_MutationnovelG30R0.19RRM_1
LIHCchrX48575239Missense_MutationNAQ20L0.43RRM_1
LUADchrX48577080Missense_MutationnovelD156E0.05
LUSCchrX48576320Missense_MutationnovelD73Y0.31RRM_1
SARCchrX48576582Missense_MutationnovelR131C0.2
SKCMchrX48575223Missense_MutationNAF15L0.47RRM_1
SKCMchrX48575565SilentNAV36V0.34
STADchrX48575208Missense_MutationNAV10M0.18RRM_1
STADchrX48576398Missense_Mutationrs782287047R99C0.22
UCECchrX48575222Missense_MutationnovelN14K0.33RRM_1
UCECchrX485751585'UTRnovel0.35
UCECchrX48575204Silentrs782613569L8L0.4
UCECchrX48575270SilentnovelG30G0.56
UCECchrX48575570Missense_MutationNAV38G0.34RRM_1
UCECchrX48576408Missense_MutationnovelS102I0.06
UCECchrX48575988Intronnovel0.11
UCECchrX485745525'Flanknovel0.15
UCECchrX48575910Intronnovel0.34
UCECchrX485744805'Flanknovel0.1
UCECchrX485749555'UTRnovel0.46
UCECchrX48576014Intronnovel0.38
UCECchrX48575268Missense_MutationnovelG30R0.38RRM_1
UCECchrX48575631Missense_MutationnovelE58D0.36RRM_1
UCECchrX485745255'Flankrs7824195900.16
UCECchrX485750815'UTRnovel0.4
UCECchrX48575836Intronnovel0.14
UCECchrX48576583Missense_MutationnovelR131H0.64
UCECchrX485745155'Flanknovel0.25
UCECchrX485751065'UTRrs7823747600.25
UCECchrX485744915'Flanknovel0.44
UCECchrX48576387Missense_MutationNAG95E0.27
UCECchrX485771023'UTRnovel0.44
UCECchrX485751805'UTRNA0.27
UCECchrX48575592SilentNAR45R0.41
UCECchrX485745165'Flanknovel0.41
UCECchrX485751275'UTRnovel0.35
UCECchrX48575285Splice_SitenovelX35_splice0.44
UCECchrX485745005'Flanknovel0.48
UCECchrX48575891Intronnovel0.34

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
SARCAMP0.2840.19108
THCADEL0.0020.21991

Survival Analysis
CancerP-value Q-value
THYM0.048

Kaplan-Meier Survival Analysis

KIRC0.0012

Kaplan-Meier Survival Analysis

PRAD0.042

Kaplan-Meier Survival Analysis

BRCA0.0071

Kaplan-Meier Survival Analysis

KIRP0.017

Kaplan-Meier Survival Analysis

COAD0.0001

Kaplan-Meier Survival Analysis

PCPG0.025

Kaplan-Meier Survival Analysis

CESC0.014

Kaplan-Meier Survival Analysis

UCEC0.00054

Kaplan-Meier Survival Analysis

LIHC0.038

Kaplan-Meier Survival Analysis

UVM0.032

Kaplan-Meier Survival Analysis

OV0.032

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
  • GWAS
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000102317 (Gene tree)
Gene ID
5935
Gene Symbol
RBM3
Alias
IS1-RNPL
Full Name
RNA binding motif protein 3
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Plus strand
Length
6,813 bases
Position
chrX:48,574,353-48,581,165
Accession
9900
RBP type
canonical RBP
Summary
This gene is a member of the glycine-rich RNA-binding protein family and encodes a protein with one RNA recognition motif (RRM) domain. Expression of this gene is induced by cold shock and low oxygen tension. A pseudogene exists on chromosome 1. Multiple alternatively spliced transcript variants that are predicted to encode different isoforms have been characterized although some of these variants fit nonsense-mediated decay (NMD) criteria. [provided by RefSeq, Jul 2008]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000365946RRM_1PF00076.221.1e-2311
ENSP00000365950RRM_1PF00076.221.1e-2311
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 RNANascentRICK & Hela2018 Feb 12Bao XDOI: 10.1038/nmeth.4595
29431736Capturing the interactome of newly transcribed RNAPolyT-RICK & 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
15075239Oxygen-regulated expression of the RNA-binding proteins RBM3 and CIRP by a HIF-1-independent mechanism.J Cell Sci2004 Apr 1Wellmann S-
27147467Cold-inducible proteins CIRP and RBM3, a unique couple with activities far beyond the cold.Cell Mol Life Sci2016 OctZhu Xdoi: 10.1007/s00018-016-2253-7
28536481TRPV4-dependent induction of a novel mammalian cold-inducible protein SRSF5 as well as CIRP and RBM3.Sci Rep2017 May 23Fujita Tdoi: 10.1038/s41598-017-02473-x.
29175331Involvement of TRPV3 and TRPM8 ion channel proteins in induction of mammalian cold-inducible proteins.Biochem Biophys Res Commun2018 Jan 1Fujita Tdoi: 10.1016/j.bbrc.2017.11.136
28373441Expression of RNA-binding Motif Protein 3 (RBM3) and Cold-inducible RNA-binding protein (CIRP) Is Associated with Improved Clinical Outcome in Patients with Colon Cancer.Anticancer Res2017 AprJang HH-
10793079Decreased expression of mouse Rbm3, a cold-shock protein, in Sertoli cells of cryptorchid testis.Am J Pathol2000 MayDanno S-
23415676Effects of moderate and deep hypothermia on RNA-binding proteins RBM3 and CIRP expressions in murine hippocampal brain slices.Brain Res2013 Apr 4Tong Gdoi: 10.1016/j.brainres.2013.01.041
19277990Down-regulating cold shock protein genes impairs cancer cell survival and enhances chemosensitivity.J Cell Biochem2009 May 1Zeng Ydoi: 10.1002/jcb.22114.
27556928Cold Shock Proteins Are Expressed in the Retina Following Exposure to Low Temperatures.PLoS One2016 Aug 24Larrayoz IMdoi: 10.1371/journal.pone.0161458
29743635Morphoregulatory functions of the RNA-binding motif protein 3 in cell spreading, polarity and migration.Sci Rep2018 May 9Pilotte Jdoi: 10.1038/s41598-018-25668-2.
19770690The RNA-binding protein RBM3 is required for cell proliferation and protects against serum deprivation-induced cell death.Pediatr Res2010 JanWellmann Sdoi: 10.1203/PDR.0b013e3181c13326.
21527344The RNA-binding protein RBM3 is involved in hypothermia induced neuroprotection.Neurobiol Dis2011 AugChip Sdoi: 10.1016/j.nbd.2011.04.010
25482277Comparative efficacies of six different media for cryopreservation of immature buffalo (Bubalus bubalis) calf testis.Reprod Fertil Dev2016 JunDevi Ldoi: 10.1071/RD14171.
27364162Cellular Functions of RNA-Binding Motif Protein 3 (RBM3): Clues in Hypothermia, Cancer Biology and Apoptosis.Protein Pept Lett2016Al-Astal HI-
30051360Cold shock protein RBM3 attenuates atrophy and induces hypertrophy in skeletal muscle.J Muscle Res Cell Motil2018 AprVan Pelt DWdoi: 10.1007/s10974-018-9496-x
12824175The internal ribosome entry site (IRES) contained within the RNA-binding motif protein 3 (Rbm3) mRNA is composed of functionally distinct elements.J Biol Chem2003 Sep 5Chappell SA-
12475980Analysis of the cytosolic proteome in a cell culture model of familial amyotrophic lateral sclerosis reveals alterations to the proteasome, antioxidant defenses, and nitric oxide synthetic pathways.J Biol Chem2003 Feb 21Allen S-
12217956Modulation of polyglutamine-induced cell death by genes identified by expression profiling.Hum Mol Genet2002 Sep 15Kita H-
15821108Gene regulation by NMDA receptor activation in the SDN-POA neurons of male rats during sexual development.J Mol Endocrinol2005 AprHsu HK-
15684048Cold stress-induced protein Rbm3 binds 60S ribosomal subunits, alters microRNA levels, and enhances global protein synthesis.Proc Natl Acad Sci U S A2005 Feb 8Dresios J-
19150436Developmentally regulated expression of the cold-inducible RNA-binding motif protein 3 in euthermic rat brain.Brain Res2009 Mar 3Pilotte Jdoi: 10.1016/j.brainres.2008.12.050
18753264Identification of cold-shock protein RBM3 as a possible regulator of skeletal muscle size through expression profiling.Am J Physiol Regul Integr Comp Physiol2008 OctDupont-Versteegden EEdoi: 10.1152/ajpregu.90455.2008
17403028Two isoforms of the cold-inducible mRNA-binding protein RBM3 localize to dendrites and promote translation.J Neurochem2007 JunSmart F-
22805320High MCM3 expression is an independent biomarker of poor prognosis and correlates with reduced RBM3 expression in a prospective cohort of malignant melanoma.Diagn Pathol2012 Jul 17Nodin Bdoi: 10.1186/1746-1596-7-82.
22145045Widespread regulation of miRNA biogenesis at the Dicer step by the cold-inducible RNA-binding protein, RBM3.PLoS One2011Pilotte Jdoi: 10.1371/journal.pone.0028446
21804916RBM3-regulated genes promote DNA integrity and affect clinical outcome in epithelial ovarian cancer.Transl Oncol2011 AugEhlen A-
21684257Generation of mice deficient in RNA-binding motif protein 3 (RBM3) and characterization of its role in innate immune responses and cell growth.Biochem Biophys Res Commun2011 Jul 22Matsuda Adoi: 10.1016/j.bbrc.2011.06.038
21593448Enhanced survival of skeletal muscle myoblasts in response to overexpression of cold shock protein RBM3.Am J Physiol Cell Physiol2011 AugFerry ALdoi: 10.1152/ajpcell.00098.2011
21080034Proteomic analysis of cisplatin resistance in human ovarian cancer using 2-DE method.Mol Cell Biochem2011 FebGong Fdoi: 10.1007/s11010-010-0648-6
25561795Tricistronic hepatitis C virus subgenomic replicon expressing double transgenes.World J Gastroenterol2014 Dec 28Cheng Xdoi: 10.3748/wjg.v20.i48.18284.
25544695Molecular characterization of RNA binding motif protein 3 (RBM3) gene from Pashmina goat.Res Vet Sci2015 FebZargar Rdoi: 10.1016/j.rvsc.2014.11.016
24963396High expression of RNA-binding motif protein 3 in esophageal and gastric adenocarcinoma correlates with intestinal metaplasia-associated tumours and independently predicts a reduced risk of recurrence and death.Biomark Res2014 Jun 17Jonsson Ldoi: 10.1186/2050-7771-2-11
24668366Spatiotemporal profile and essential role of RBM3 expression after spinal cord injury in adult rats.J Mol Neurosci2014Cui Zdoi: 10.1007/s12031-014-0282-y
24570111Spatiotemporal pattern of RNA-binding motif protein 3 expression after spinal cord injury in rats.Cell Mol Neurobiol2014 MayZhao Wdoi: 10.1007/s10571-014-0033-1
24380696High RNA-binding motif protein 3 expression is an independent prognostic marker in operated prostate cancer and tightly linked to ERG activation and PTEN deletions.Eur J Cancer2014 MarGrupp Kdoi: 10.1016/j.ejca.2013.12.003
23667174Stress-response protein RBM3 attenuates the stem-like properties of prostate cancer cells by interfering with CD44 variant splicing.Cancer Res2013 Jul 1Zeng Ydoi: 10.1158/0008-5472.CAN-12-1343
23673116Differential expression of the RNA-binding motif protein 3 in human astrocytoma.Chin Med J (Engl)2013Zhang HT-
23565664Decreased expression of RNA-binding motif protein 3 correlates with tumour progression and poor prognosis in urothelial bladder cancer.BMC Urol2013 Apr 8Boman Kdoi: 10.1186/1471-2490-13-17.
28118608RNA binding motif protein 3: a potential biomarker in cancer and therapeutic target in neuroprotection.Oncotarget2017 Mar 28Zhou RBdoi: 10.18632/oncotarget.14755.
27930406Stress Response Protein RBM3 Promotes the Development of Colitis-associated Cancer.Inflamm Bowel Dis2017 JanSakurai Tdoi: 10.1097/MIB.0000000000000968.
28002126-----
28293425Podocalyxin-like and RNA-binding motif protein 3 are prognostic biomarkers in urothelial bladder cancer: a validatory study.Biomark Res2017 Mar 14Boman Kdoi: 10.1186/s40364-017-0090-y
26825461RBM3 regulates temperature sensitive miR-142-5p and miR-143 (thermomiRs), which target immune genes and control fever.Nucleic Acids Res2016 Apr 7Wong JJdoi: 10.1093/nar/gkw041
26577765Evaluation of RNA-binding motif protein 3 expression in urothelial carcinoma of the bladder: an immunohistochemical study.World J Surg Oncol2015 Nov 14Florianova Ldoi: 10.1186/s12957-015-0730-3.
26472337Cold-inducible RBM3 inhibits PERK phosphorylation through cooperation with NF90 to protect cells from endoplasmic reticulum stress.FASEB J2016 FebZhu Xdoi: 10.1096/fj.15-274639
25912293Preliminary Transcriptome Analysis in Lymphoblasts from Cluster Headache and Bipolar Disorder Patients Implicates Dysregulation of Circadian and Serotonergic Genes.J Mol Neurosci2015 JulCosta Mdoi: 10.1007/s12031-015-0567-9
25922889Loss of RNA-binding motif protein 3 expression is associated with right-sided localization and poor prognosis in colorectal cancer.Histopathology2016 JanMelling Ndoi: 10.1111/his.12726
25872349[The research progress of RNA binding motif protein 3 biological function].Sheng Li Ke Xue Jin Zhan2014 DecLi YL-
25811459Low RBM3 protein expression correlates with clinical stage, prognostic classification and increased risk of treatment failure in testicular non-seminomatous germ cell cancer.PLoS One2015 Mar 26Olofsson SEdoi: 10.1371/journal.pone.0121300
28580361Neuroprotection via RNA-binding protein RBM3 expression is regulated by hypothermia but not by hypoxia in human SK-N-SH neurons.Hypoxia (Auckl)2017 May 23Rosenthal LMdoi: 10.2147/HP.S132462
28616776Evidence towards RNA Binding Motif (RNP1, RRM) Protein 3 (RBM3) as a Potential Biomarker of Lithium Response in Bipolar Disorder Patients.J Mol Neurosci2017 AugPapadima EMdoi: 10.1007/s12031-017-0938-5
28761115Hypothermia Prevents Retinal Damage Generated by Optic Nerve Trauma in the Rat.Sci Rep2017 Jul 31Rey-Funes Mdoi: 10.1038/s41598-017-07294-6.
28800641High RBM3 expression is associated with an improved survival and oxaliplatin response in patients with metastatic colorectal cancer.PLoS One2017 Aug 11Siesing Cdoi: 10.1371/journal.pone.0182512
28117799Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay.J Vis Exp2017 Jan 16Zhu Xdoi: 10.3791/55218.
29263314High RNA-Binding Motif Protein 3 (RBM3) Expression is Independently Associated with Prolonged Overall Survival in Intestinal-Type Gastric Cancer.Med Sci Monit2017 Dec 21Ye F-
29421306Prenatal cold stress: Effect on maternal hippocampus and offspring behavior in rats.Behav Brain Res2018 Jul 2Lian Sdoi: 10.1016/j.bbr.2018.02.002
29464064Translational study reveals a two-faced role of RBM3 in pancreatic cancer and suggests its potential value as a biomarker for improved patient stratification.Oncotarget2017 Dec 15Karnevi Edoi: 10.18632/oncotarget.23486
29505791Hypothermia-induced RNA-binding motif protein 3 (RBM3) stimulates osteoblast differentiation via the ERK signaling pathway.Biochem Biophys Res Commun2018 Apr 6Kim DYdoi: 10.1016/j.bbrc.2018.02.209
29931857[Effect of RNA binding motif protein 3 overexpression on Caspase 3 expression in swine testiclar cell under cold exposure].Zhongguo Ying Yong Sheng Li Xue Za Zhi2016 Feb 8Li YLdoi: 10.13459/j.cnki.cjap.2016.02.002.
30275857High RNA-binding Motif Protein 3 Expression Is Associated with Improved Clinical Outcomes in Invasive Breast Cancer.J Breast Cancer2018 SepKang SHdoi: 10.4048/jbc.2018.21.e34
30399610Infants Uniquely Express High Levels of RBM3 and Other Cold-Adaptive Neuroprotectant Proteins in the Human Brain.Dev Neurosci2018Jackson TCdoi: 10.1159/000493637
30758670Prevalence and clinical significance of RBM3 immunostaining in non-small cell lung cancers.J Cancer Res Clin Oncol2019 AprMelling Ndoi: 10.1007/s00432-019-02850-1
27451143Contextual fear conditioning induces differential alternative splicing.Neurobiol Learn Mem2016 OctPoplawski SGdoi: 10.1016/j.nlm.2016.07.018
31235426The RNA-binding protein RBM3 promotes cell proliferation in hepatocellular carcinoma by regulating circular RNA SCD-circRNA 2 production.EBioMedicine2019 JulDong Wdoi: 10.1016/j.ebiom.2019.06.030
30037926Cold-induced protein RBM3 orchestrates neurogenesis via modulating Yap mRNA stability in cold stress.J Cell Biol2018 Oct 1Xia Wdoi: 10.1083/jcb.201801143
9245737Increased transcript level of RBM3, a member of the glycine-rich RNA-binding protein family, in human cells in response to cold stress.Biochem Biophys Res Commun1997 Jul 30Danno S-
8634703RBM3, a novel human gene in Xp11.23 with a putative RNA-binding domain.Hum Mol Genet1995 DecDerry JM-
16249311Seasonally hibernating phenotype assessed through transcript screening.Physiol Genomics2005 Dec 14Williams DR-
14662769Identification of RNA-binding proteins in RAW 264.7 cells that recognize a lipopolysaccharide-responsive element in the 3-untranslated region of the murine cyclooxygenase-2 mRNA.J Biol Chem2004 Feb 27Cok SJ-
19900510A new generation of proto-oncogenes: cold-inducible RNA binding proteins.Biochim Biophys Acta2010 JanLleonart MEdoi: 10.1016/j.bbcan.2009.11.001
19734850Nuclear expression of the RNA-binding protein RBM3 is associated with an improved clinical outcome in breast cancer.Mod Pathol2009 DecJogi Adoi: 10.1038/modpathol.2009.124
19240299Elevated expression of protein biosynthesis genes in liver and muscle of hibernating black bears (Ursus americanus).Physiol Genomics2009 Apr 10Fedorov VBdoi: 10.1152/physiolgenomics.90398.2008
21955582High RBM3 expression in prostate cancer independently predicts a reduced risk of biochemical recurrence and disease progression.Diagn Pathol2011 Sep 28Jonsson Ldoi: 10.1186/1746-1596-6-91.
21777469Low RBM3 protein expression correlates with tumour progression and poor prognosis in malignant melanoma: an analysis of 215 cases from the Malm Diet and Cancer Study.J Transl Med2011 Jul 21Jonsson Ldoi: 10.1186/1479-5876-9-114.
21737612mRNA expression of the putative antimetastatic gene BRMS1 and of apoptosis-related genes in breast cancer.Cancer Genomics Proteomics2011 Jul-AugSchneider J-
21453527Modulation of gene expression in heart and liver of hibernating black bears (Ursus americanus).BMC Genomics2011 Mar 31Fedorov VBdoi: 10.1186/1471-2164-12-171.
20926767Late-gestational systemic hypoxia leads to a similar early gene response in mouse placenta and developing brain.Am J Physiol Regul Integr Comp Physiol2010 DecTrollmann Rdoi: 10.1152/ajpregu.00697.2009
20727170Expression of the RNA-binding protein RBM3 is associated with a favourable prognosis and cisplatin sensitivity in epithelial ovarian cancer.J Transl Med2010 Aug 20Ehlen Adoi: 10.1186/1479-5876-8-78.
25607368RBM3 mediates structural plasticity and protective effects of cooling in neurodegeneration.Nature2015 Feb 12Peretti Ddoi: 10.1038/nature14142
24622240Microarray meta-analysis of RNA-binding protein functions in alternative polyadenylation.PLoS One2014 Mar 12Hu Wdoi: 10.1371/journal.pone.0090774
28134320RNA-binding protein RBM3 prevents NO-induced apoptosis in human neuroblastoma cells by modulating p38 signaling and miR-143.Sci Rep2017 Jan 30Yang HJdoi: 10.1038/srep41738.
23792593Cold-induced RNA-binding proteins regulate circadian gene expression by controlling alternative polyadenylation.Sci Rep2013Liu Ydoi: 10.1038/srep02054.
26331352RNA binding protein RBM3 increases β-catenin signaling to increase stem cell characteristics in colorectal cancer cells.Mol Carcinog2016 NovVenugopal Adoi: 10.1002/mc.22404
26528939In Vitro and In Vivo Modulation of Alternative Splicing by the Biguanide Metformin.Mol Ther Nucleic Acids2015 Nov 3Laustriat Ddoi: 10.1038/mtna.2015.35.
26816005Homologous Transcription Factors DUX4 and DUX4c Associate with Cytoplasmic Proteins during Muscle Differentiation.PLoS One2016 Jan 27Ansseau Edoi: 10.1371/journal.pone.0146893
26265550Cold stress protein RBM3 responds to temperature change in an ultra-sensitive manner in young neurons.Neuroscience2015 Oct 1Jackson TCdoi: 10.1016/j.neuroscience.2015.08.012
28831692Cold-Inducible Protein RBM3 Protects UV Irradiation-Induced Apoptosis in Neuroblastoma Cells by Affecting p38 and JNK Pathways and Bcl2 Family Proteins.J Mol Neurosci2017 OctZhuang RJdoi: 10.1007/s12031-017-0964-3
29388696RBM3 expression is upregulated by NF-kB p65 activity, protecting cells from apoptosis, during mild hypothermia.J Cell Biochem2018 JulUshio Adoi: 10.1002/jcb.26757
30106430Impact of RNAbinding motif 3 expression on the whole transcriptome of prostate cancer cells: An RNA sequencing study.Oncol Rep2018 OctDong Qdoi: 10.3892/or.2018.6618
30662656RNA binding motif protein 3 (RBM3) drives radioresistance in nasopharyngeal carcinoma by reducing apoptosis via the PI3K/AKT/Bcl-2 signaling pathway.Am J Transl Res2018 Dec 15Ma R-
30720048RBM3 upregulates ARPC2 by binding the 3'UTR and contributes to breast cancer progression.Int J Oncol2019 AprChen Pdoi: 10.3892/ijo.2019.4698
30821572Regulating glycolysis, the TLR4 signal pathway and expression of RBM3 in mouse liver in response to acute cold exposure.Stress2019 MayShi Hdoi: 10.1080/10253890.2019.1568987
30973305A Prospective Clinical Trial Measuring the Effects of Cardiopulmonary Bypass Under Mild Hypothermia on the Inflammatory Response and Regulation of Cold-Shock Protein RNA-Binding Motif 3.Ther Hypothermia Temp Manag2019 Apr 11Rosenthal LMdoi: 10.1089/ther.2018.0038
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000485213RBM3-206947--- (aa)--
ENST00000489344RBM3-208724--- (aa)--
ENST00000491236RBM3-210729--- (aa)--
ENST00000490127RBM3-209567--- (aa)--
ENST00000472897RBM3-205501--- (aa)--
ENST00000376759RBM3-2032162-ENSP00000365950157 (aa)-P98179
ENST00000376755RBM3-2021130-ENSP00000365946157 (aa)-P98179
ENST00000354480RBM3-2011884XM_024452413ENSP00000346473155 (aa)XP_024308181Q9H5V0
ENST00000488216RBM3-207835--- (aa)--
ENST00000466764RBM3-2041375--- (aa)--
ENST00000491240RBM3-211951--- (aa)--
Gene Model
Click here to download ENSG00000102317's gene model file
GWAS
ensgIDSNPChromosomePositionSNP-risk TraitPubmedID95% CIOr or BEAT EFO ID
ENSG00000102317rs3200611X48578038?Hepatitis A28928442[0.16-0.44] unit increase0.2987EFO_0008415
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000102317's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000102317RBM35255.556ENSG00000213516RBMXL15254.878
ENSG00000102317RBM35840.789ENSG00000254535PABPC4L8240.789
ENSG00000102317RBM310057.059ENSG00000099622CIRBP10073.750
ENSG00000102317RBM35940.000ENSG00000101104PABPC1L6740.789
ENSG00000102317RBM35254.321ENSG00000234414RBMY1A18155.224
ENSG00000102317RBM38032.812ENSG00000114503NCBP25436.486
ENSG00000102317RBM35254.321ENSG00000244395RBMY1D8155.224
ENSG00000102317RBM35337.349ENSG00000151923TIAL15541.096
ENSG00000102317RBM35541.071ENSG00000135486HNRNPA15443.662
ENSG00000102317RBM35230.864ENSG00000265241RBM8A7130.667
ENSG00000102317RBM35254.321ENSG00000242389RBMY1E8155.224
ENSG00000102317RBM38034.109ENSG00000138668HNRNPD6834.667
ENSG00000102317RBM38942.857ENSG00000153944MSI27542.667
ENSG00000102317RBM35254.321ENSG00000242875RBMY1B8155.224
ENSG00000102317RBM35436.905ENSG00000116001TIA16941.333
ENSG00000102317RBM35530.233ENSG00000115875SRSF75431.579
ENSG00000102317RBM35538.824ENSG00000140488CELF65340.000
ENSG00000102317RBM36241.935ENSG00000070756PABPC18935.821
ENSG00000102317RBM35254.878ENSG00000147274RBMX8356.923
ENSG00000102317RBM36236.111ENSG00000090621PABPC46337.500
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000102317RBM310056.962ENSAMEG00000003278CIRBP5154.375Ailuropoda_melanoleuca
ENSG00000102317RBM310095.541ENSAMEG00000012653RBM39795.541Ailuropoda_melanoleuca
ENSG00000102317RBM310063.522ENSACAG00000023931-10067.925Anolis_carolinensis
ENSG00000102317RBM35970.833ENSACAG00000000441CIRBP9758.824Anolis_carolinensis
ENSG00000102317RBM310081.132ENSACAG00000013718-10076.101Anolis_carolinensis
ENSG00000102317RBM310088.050ENSANAG00000028569-10088.050Aotus_nancymaae
ENSG00000102317RBM38061.240ENSANAG00000027805-5874.000Aotus_nancymaae
ENSG00000102317RBM310053.571ENSANAG00000036495-9757.831Aotus_nancymaae
ENSG00000102317RBM310097.484ENSANAG00000028883-9597.484Aotus_nancymaae
ENSG00000102317RBM310088.820ENSBTAG00000025848RBM310088.820Bos_taurus
ENSG00000102317RBM310057.396ENSBTAG00000007480CIRBP7759.394Bos_taurus
ENSG00000102317RBM310056.471ENSCJAG00000005504CIRBP9956.024Callithrix_jacchus
ENSG00000102317RBM310097.484ENSCJAG00000047341-10097.484Callithrix_jacchus
ENSG00000102317RBM38186.614ENSCJAG00000047359-8988.525Callithrix_jacchus
ENSG00000102317RBM310056.471ENSCAFG00000019506CIRBP9058.434Canis_familiaris
ENSG00000102317RBM310091.411ENSCAFG00000015485RBM310092.025Canis_familiaris
ENSG00000102317RBM310084.076ENSCAFG00000016002-10084.076Canis_familiaris
ENSG00000102317RBM37591.453ENSCAFG00020017705-9891.453Canis_lupus_dingo
ENSG00000102317RBM35088.750ENSCAFG00020021344-9087.654Canis_lupus_dingo
ENSG00000102317RBM35386.747ENSCAFG00020020106-7986.747Canis_lupus_dingo
ENSG00000102317RBM310056.471ENSCAFG00020017138CIRBP9058.434Canis_lupus_dingo
ENSG00000102317RBM310088.820ENSCHIG00000009007RBM310088.820Capra_hircus
ENSG00000102317RBM310057.396ENSCHIG00000021288CIRBP9659.394Capra_hircus
ENSG00000102317RBM310078.981ENSTSYG00000035938-10075.796Carlito_syrichta
ENSG00000102317RBM38383.333ENSTSYG00000035220-6487.640Carlito_syrichta
ENSG00000102317RBM38381.679ENSTSYG00000031540-6485.393Carlito_syrichta
ENSG00000102317RBM310072.611ENSTSYG00000034265-10071.975Carlito_syrichta
ENSG00000102317RBM310095.541ENSTSYG00000008670-10095.541Carlito_syrichta
ENSG00000102317RBM39964.375ENSTSYG00000027687-10071.875Carlito_syrichta
ENSG00000102317RBM310073.885ENSTSYG00000033076-10080.892Carlito_syrichta
ENSG00000102317RBM310092.500ENSCAPG00000005923RBM310092.500Cavia_aperea
ENSG00000102317RBM35570.930ENSCPOG00000019403CIRBP9755.090Cavia_porcellus
ENSG00000102317RBM310093.125ENSCPOG00000003553RBM310093.125Cavia_porcellus
ENSG00000102317RBM310079.618ENSCCAG00000035552-10079.618Cebus_capucinus
ENSG00000102317RBM35970.833ENSCCAG00000034994CIRBP9756.024Cebus_capucinus
ENSG00000102317RBM310097.484ENSCCAG00000038019-10097.484Cebus_capucinus
ENSG00000102317RBM310098.726ENSCATG00000029986-10098.726Cercocebus_atys
ENSG00000102317RBM310097.452ENSCATG00000038524-10097.452Cercocebus_atys
ENSG00000102317RBM310056.471ENSCATG00000042253CIRBP9956.627Cercocebus_atys
ENSG00000102317RBM310056.471ENSCLAG00000016087CIRBP9956.024Chinchilla_lanigera
ENSG00000102317RBM310096.835ENSCLAG00000002908RBM310096.835Chinchilla_lanigera
ENSG00000102317RBM310057.059ENSCSAG00000012245CIRBP9756.627Chlorocebus_sabaeus
ENSG00000102317RBM3100100.000ENSCSAG00000013242RBM3100100.000Chlorocebus_sabaeus
ENSG00000102317RBM310091.720ENSCHOG00000007642RBM310091.720Choloepus_hoffmanni
ENSG00000102317RBM310062.893ENSCPBG00000021863-10067.296Chrysemys_picta_bellii
ENSG00000102317RBM310057.895ENSCPBG00000022930CIRBP9960.465Chrysemys_picta_bellii
ENSG00000102317RBM310071.698ENSCPBG00000021859RBM310080.503Chrysemys_picta_bellii
ENSG00000102317RBM310057.059ENSCANG00000037000CIRBP9956.627Colobus_angolensis_palliatus
ENSG00000102317RBM310098.726ENSCANG00000014668-10098.726Colobus_angolensis_palliatus
ENSG00000102317RBM3100100.000ENSCANG00000037907-100100.000Colobus_angolensis_palliatus
ENSG00000102317RBM310068.153ENSCANG00000031890-10066.879Colobus_angolensis_palliatus
ENSG00000102317RBM310096.178ENSCGRG00001018909Rbm310096.178Cricetulus_griseus_chok1gshd
ENSG00000102317RBM310056.471ENSCGRG00000013689Cirbp9956.627Cricetulus_griseus_crigri
ENSG00000102317RBM310096.178ENSCGRG00000014636Rbm310096.178Cricetulus_griseus_crigri
ENSG00000102317RBM39992.308ENSDNOG00000040748-7392.308Dasypus_novemcinctus
ENSG00000102317RBM310075.159ENSDNOG00000040058-9775.159Dasypus_novemcinctus
ENSG00000102317RBM39989.103ENSDNOG00000035132-8889.103Dasypus_novemcinctus
ENSG00000102317RBM39072.535ENSDNOG00000037833-9472.535Dasypus_novemcinctus
ENSG00000102317RBM39990.385ENSDNOG00000042033-7290.385Dasypus_novemcinctus
ENSG00000102317RBM310095.541ENSDNOG00000010420-7395.541Dasypus_novemcinctus
ENSG00000102317RBM310092.994ENSDNOG00000032565-10092.994Dasypus_novemcinctus
ENSG00000102317RBM310094.904ENSDNOG00000048200-7494.904Dasypus_novemcinctus
ENSG00000102317RBM39992.308ENSDNOG00000041625-7292.308Dasypus_novemcinctus
ENSG00000102317RBM39964.516ENSDNOG00000043650-9563.871Dasypus_novemcinctus
ENSG00000102317RBM39478.378ENSDNOG00000040147-8278.378Dasypus_novemcinctus
ENSG00000102317RBM310076.101ENSDNOG00000033435-9674.214Dasypus_novemcinctus
ENSG00000102317RBM39993.590ENSDNOG00000049801-9693.590Dasypus_novemcinctus
ENSG00000102317RBM310056.471ENSDORG00000023540Cirbp9958.434Dipodomys_ordii
ENSG00000102317RBM310096.203ENSDORG00000000182Rbm310096.203Dipodomys_ordii
ENSG00000102317RBM37570.085ENSEASG00005023389-9870.085Equus_asinus_asinus
ENSG00000102317RBM310087.273ENSEASG00005008251RBM310087.273Equus_asinus_asinus
ENSG00000102317RBM310056.471ENSEASG00005021677CIRBP7359.036Equus_asinus_asinus
ENSG00000102317RBM37962.903ENSECAG00000038298-9763.433Equus_caballus
ENSG00000102317RBM310096.815ENSECAG00000024257RBM310096.815Equus_caballus
ENSG00000102317RBM35465.882ENSECAG00000002141-9469.136Equus_caballus
ENSG00000102317RBM35158.750ENSELUG00000004652-6058.537Esox_lucius
ENSG00000102317RBM35276.829ENSELUG00000019617-5175.581Esox_lucius
ENSG00000102317RBM310092.547ENSFCAG00000002245RBM310093.168Felis_catus
ENSG00000102317RBM37580.342ENSFCAG00000021952-9675.294Felis_catus
ENSG00000102317RBM310055.882ENSFCAG00000013724CIRBP9957.831Felis_catus
ENSG00000102317RBM310059.748ENSFALG00000014000CIRBP9663.522Ficedula_albicollis
ENSG00000102317RBM310096.835ENSFDAG00000007909RBM310096.835Fukomys_damarensis
ENSG00000102317RBM310056.471ENSFDAG00000002848CIRBP9756.024Fukomys_damarensis
ENSG00000102317RBM310057.988ENSGALG00000030918CIRBP9659.394Gallus_gallus
ENSG00000102317RBM310072.785ENSGAGG00000016475RBM310081.646Gopherus_agassizii
ENSG00000102317RBM310062.893ENSGAGG00000016473-10067.296Gopherus_agassizii
ENSG00000102317RBM3100100.000ENSGGOG00000005864RBM3100100.000Gorilla_gorilla
ENSG00000102317RBM310057.059ENSGGOG00000002338CIRBP9756.627Gorilla_gorilla
ENSG00000102317RBM37476.271ENSGGOG00000025080-7278.824Gorilla_gorilla
ENSG00000102317RBM310056.471ENSHGLG00000005839CIRBP9956.627Heterocephalus_glaber_female
ENSG00000102317RBM310096.835ENSHGLG00000006552RBM310096.835Heterocephalus_glaber_female
ENSG00000102317RBM310082.278ENSHGLG00000013635-10081.646Heterocephalus_glaber_female
ENSG00000102317RBM310081.013ENSHGLG00000010919-10079.747Heterocephalus_glaber_female
ENSG00000102317RBM310096.835ENSHGLG00100017487-10096.835Heterocephalus_glaber_male
ENSG00000102317RBM310082.278ENSHGLG00100015330-10081.646Heterocephalus_glaber_male
ENSG00000102317RBM310081.013ENSHGLG00100014556-10079.747Heterocephalus_glaber_male
ENSG00000102317RBM310056.471ENSHGLG00100004955CIRBP9956.627Heterocephalus_glaber_male
ENSG00000102317RBM35947.917ENSHGLG00100005516-9643.396Heterocephalus_glaber_male
ENSG00000102317RBM35265.854ENSIPUG00000007089RBM35163.953Ictalurus_punctatus
ENSG00000102317RBM310096.178ENSSTOG00000027493-10096.178Ictidomys_tridecemlineatus
ENSG00000102317RBM310055.882ENSSTOG00000027646CIRBP9756.627Ictidomys_tridecemlineatus
ENSG00000102317RBM310096.178ENSJJAG00000012962-10096.178Jaculus_jaculus
ENSG00000102317RBM310068.153ENSJJAG00000022888-10064.968Jaculus_jaculus
ENSG00000102317RBM310055.294ENSJJAG00000013649Cirbp9755.422Jaculus_jaculus
ENSG00000102317RBM38550.314ENSLACG00000014490-5068.675Latimeria_chalumnae
ENSG00000102317RBM35274.390ENSLOCG00000000112-7173.256Lepisosteus_oculatus
ENSG00000102317RBM35475.581ENSLOCG00000005031-5975.581Lepisosteus_oculatus
ENSG00000102317RBM39976.101ENSLAFG00000029211-9971.069Loxodonta_africana
ENSG00000102317RBM310056.471ENSLAFG00000032156-9755.422Loxodonta_africana
ENSG00000102317RBM310094.268ENSLAFG00000007003-10094.268Loxodonta_africana
ENSG00000102317RBM310057.310ENSMFAG00000034048CIRBP9956.627Macaca_fascicularis
ENSG00000102317RBM3100100.000ENSMFAG00000003694RBM3100100.000Macaca_fascicularis
ENSG00000102317RBM38097.600ENSMFAG00000003836-9397.600Macaca_fascicularis
ENSG00000102317RBM39998.077ENSMMUG00000037648-9998.077Macaca_mulatta
ENSG00000102317RBM310057.059ENSMMUG00000022101CIRBP10065.625Macaca_mulatta
ENSG00000102317RBM3100100.000ENSMNEG00000042115-100100.000Macaca_nemestrina
ENSG00000102317RBM310057.310ENSMNEG00000033116CIRBP9956.627Macaca_nemestrina
ENSG00000102317RBM39998.718ENSMNEG00000000984-9998.718Macaca_nemestrina
ENSG00000102317RBM310056.471ENSMLEG00000038347CIRBP9956.627Mandrillus_leucophaeus
ENSG00000102317RBM39996.154ENSMLEG00000027951-9996.154Mandrillus_leucophaeus
ENSG00000102317RBM3100100.000ENSMLEG00000041745-100100.000Mandrillus_leucophaeus
ENSG00000102317RBM310057.988ENSMGAG00000010253CIRBP9752.406Meleagris_gallopavo
ENSG00000102317RBM310057.059ENSMAUG00000002162CIRP9956.627Mesocricetus_auratus
ENSG00000102317RBM310075.159ENSMAUG00000008646-10076.433Mesocricetus_auratus
ENSG00000102317RBM310096.178ENSMAUG00000016488-10096.178Mesocricetus_auratus
ENSG00000102317RBM310094.969ENSMICG00000047440-10094.969Microcebus_murinus
ENSG00000102317RBM310063.057ENSMICG00000045835-10056.688Microcebus_murinus
ENSG00000102317RBM310056.471ENSMICG00000038000CIRBP9756.627Microcebus_murinus
ENSG00000102317RBM310085.093ENSMICG00000028982-10083.851Microcebus_murinus
ENSG00000102317RBM310057.059ENSMOCG00000012643Cirbp9956.627Microtus_ochrogaster
ENSG00000102317RBM310096.178ENSMOCG00000001511Rbm310096.178Microtus_ochrogaster
ENSG00000102317RBM310052.381ENSMODG00000005290CIRBP7258.434Monodelphis_domestica
ENSG00000102317RBM35797.753MGP_CAROLIEiJ_G0032914-9090.123Mus_caroli
ENSG00000102317RBM310056.471MGP_CAROLIEiJ_G0015568Cirbp9956.627Mus_caroli
ENSG00000102317RBM310056.471ENSMUSG00000045193Cirbp9956.627Mus_musculus
ENSG00000102317RBM310093.631ENSMUSG00000031167Rbm310092.357Mus_musculus
ENSG00000102317RBM310093.631MGP_PahariEiJ_G0031463Rbm310092.357Mus_pahari
ENSG00000102317RBM310055.882MGP_PahariEiJ_G0030981Cirbp9956.024Mus_pahari
ENSG00000102317RBM310056.471MGP_SPRETEiJ_G0016386Cirbp9956.627Mus_spretus
ENSG00000102317RBM310093.631MGP_SPRETEiJ_G0034063Rbm310092.357Mus_spretus
ENSG00000102317RBM310096.178ENSMPUG00000013632RBM310096.178Mustela_putorius_furo
ENSG00000102317RBM37853.676ENSMPUG00000008455-7856.061Mustela_putorius_furo
ENSG00000102317RBM310057.059ENSMLUG00000015007CIRBP9758.434Myotis_lucifugus
ENSG00000102317RBM310096.178ENSMLUG00000003996RBM39696.178Myotis_lucifugus
ENSG00000102317RBM35971.875ENSNGAG00000001192Cirbp9958.434Nannospalax_galili
ENSG00000102317RBM310096.815ENSNGAG00000012951Rbm310096.815Nannospalax_galili
ENSG00000102317RBM35970.833ENSNLEG00000028393-6073.256Nomascus_leucogenys
ENSG00000102317RBM310075.796ENSNLEG00000031601-10074.522Nomascus_leucogenys
ENSG00000102317RBM310099.363ENSNLEG00000028027-10099.363Nomascus_leucogenys
ENSG00000102317RBM310097.452ENSNLEG00000019350-10097.452Nomascus_leucogenys
ENSG00000102317RBM310060.510ENSODEG00000009372-6796.970Octodon_degus
ENSG00000102317RBM310096.203ENSODEG00000020479-10096.203Octodon_degus
ENSG00000102317RBM310048.408ENSODEG00000000843-5863.953Octodon_degus
ENSG00000102317RBM310092.405ENSODEG00000019234-10092.405Octodon_degus
ENSG00000102317RBM310087.342ENSODEG00000019976-10086.076Octodon_degus
ENSG00000102317RBM310055.294ENSODEG00000012711-9955.422Octodon_degus
ENSG00000102317RBM310074.684ENSODEG00000003178-9374.051Octodon_degus
ENSG00000102317RBM310087.975ENSODEG00000019283-10087.342Octodon_degus
ENSG00000102317RBM310079.747ENSODEG00000003511-10079.114Octodon_degus
ENSG00000102317RBM37862.903ENSOANG00000012483RBM39571.200Ornithorhynchus_anatinus
ENSG00000102317RBM310052.381ENSOANG00000012230CIRBP9758.434Ornithorhynchus_anatinus
ENSG00000102317RBM39994.872ENSOCUG00000002271RBM39694.872Oryctolagus_cuniculus
ENSG00000102317RBM39968.387ENSOCUG00000027309-9968.387Oryctolagus_cuniculus
ENSG00000102317RBM310091.139ENSOGAG00000026654RBM310088.535Otolemur_garnettii
ENSG00000102317RBM310060.234ENSOGAG00000029550CIRBP9758.683Otolemur_garnettii
ENSG00000102317RBM39988.750ENSOARG00000012250RBM39688.750Ovis_aries
ENSG00000102317RBM310057.396ENSOARG00000011412CIRBP8559.394Ovis_aries
ENSG00000102317RBM3100100.000ENSPPAG00000034179RBM3100100.000Pan_paniscus
ENSG00000102317RBM310057.059ENSPPAG00000033562CIRBP9956.627Pan_paniscus
ENSG00000102317RBM37576.068ENSPPAG00000036405-7378.571Pan_paniscus
ENSG00000102317RBM310092.547ENSPPRG00000013315RBM310093.168Panthera_pardus
ENSG00000102317RBM35975.269ENSPPRG00000011438-6884.810Panthera_pardus
ENSG00000102317RBM310056.471ENSPPRG00000008838CIRBP9958.434Panthera_pardus
ENSG00000102317RBM35087.500ENSPPRG00000013361-9086.420Panthera_pardus
ENSG00000102317RBM37580.342ENSPTIG00000003747-6479.048Panthera_tigris_altaica
ENSG00000102317RBM310092.547ENSPTIG00000017702RBM310093.168Panthera_tigris_altaica
ENSG00000102317RBM310056.471ENSPTIG00000012111CIRBP9958.434Panthera_tigris_altaica
ENSG00000102317RBM3100100.000ENSPTRG00000021864RBM3100100.000Pan_troglodytes
ENSG00000102317RBM310057.059ENSPTRG00000010192CIRBP9956.627Pan_troglodytes
ENSG00000102317RBM37576.068ENSPTRG00000044048-7378.571Pan_troglodytes
ENSG00000102317RBM310057.310ENSPANG00000032449CIRBP9956.627Papio_anubis
ENSG00000102317RBM3100100.000ENSPANG00000034727-100100.000Papio_anubis
ENSG00000102317RBM38497.727ENSPANG00000005561-9297.727Papio_anubis
ENSG00000102317RBM310092.357ENSPANG00000010520-10090.446Papio_anubis
ENSG00000102317RBM35466.667ENSPKIG00000024430CIRBP6467.073Paramormyrops_kingsleyae
ENSG00000102317RBM310056.471ENSPSIG00000002812CIRBP9759.064Pelodiscus_sinensis
ENSG00000102317RBM310072.327ENSPSIG00000007145RBM39681.132Pelodiscus_sinensis
ENSG00000102317RBM310056.471ENSPEMG00000022859Cirbp9956.627Peromyscus_maniculatus_bairdii
ENSG00000102317RBM310095.541ENSPEMG00000012411Rbm310095.541Peromyscus_maniculatus_bairdii
ENSG00000102317RBM310054.438ENSPCIG00000011223-7158.788Phascolarctos_cinereus
ENSG00000102317RBM35579.070ENSPPYG00000000510-8879.070Pongo_abelii
ENSG00000102317RBM3100100.000ENSPPYG00000020314RBM3100100.000Pongo_abelii
ENSG00000102317RBM35889.011ENSPCOG00000017170-9097.403Propithecus_coquereli
ENSG00000102317RBM310084.076ENSPCOG00000013194-10083.439Propithecus_coquereli
ENSG00000102317RBM310093.082ENSPCOG00000014346-10093.711Propithecus_coquereli
ENSG00000102317RBM310056.471ENSPCOG00000028262CIRBP9956.627Propithecus_coquereli
ENSG00000102317RBM310056.471ENSPVAG00000005629CIRBP9758.434Pteropus_vampyrus
ENSG00000102317RBM310096.815ENSPVAG00000015630RBM310096.815Pteropus_vampyrus
ENSG00000102317RBM310096.815ENSRNOG00000005387Rbm310096.815Rattus_norvegicus
ENSG00000102317RBM310056.471ENSRNOG00000015999Cirbp9756.627Rattus_norvegicus
ENSG00000102317RBM310060.116ENSRBIG00000031290CIRBP9756.627Rhinopithecus_bieti
ENSG00000102317RBM3100100.000ENSRBIG00000040498RBM3100100.000Rhinopithecus_bieti
ENSG00000102317RBM39969.231ENSRROG00000035651-9768.387Rhinopithecus_roxellana
ENSG00000102317RBM310060.116ENSRROG00000022862CIRBP9756.627Rhinopithecus_roxellana
ENSG00000102317RBM3100100.000ENSRROG00000034767RBM3100100.000Rhinopithecus_roxellana
ENSG00000102317RBM35195.000ENSSBOG00000020829-9595.000Saimiri_boliviensis_boliviensis
ENSG00000102317RBM310056.471ENSSBOG00000021043CIRBP9956.024Saimiri_boliviensis_boliviensis
ENSG00000102317RBM37991.935ENSSBOG00000035691-9391.803Saimiri_boliviensis_boliviensis
ENSG00000102317RBM37998.387ENSSBOG00000005354-8898.361Saimiri_boliviensis_boliviensis
ENSG00000102317RBM310052.381ENSSHAG00000006035CIRBP9758.434Sarcophilus_harrisii
ENSG00000102317RBM310069.811ENSSPUG00000000444RBM310078.981Sphenodon_punctatus
ENSG00000102317RBM310054.070ENSSPUG00000006459CIRBP9757.485Sphenodon_punctatus
ENSG00000102317RBM310079.245ENSSSCG00000005430-10076.101Sus_scrofa
ENSG00000102317RBM310074.843ENSSSCG00000030003-10079.874Sus_scrofa
ENSG00000102317RBM310081.761ENSSSCG00000021591-10088.679Sus_scrofa
ENSG00000102317RBM310054.118ENSSSCG00000013427CIRBP9758.434Sus_scrofa
ENSG00000102317RBM310055.621ENSTGUG00000000884CIRBP9959.394Taeniopygia_guttata
ENSG00000102317RBM310095.541ENSTTRG00000008587RBM310095.541Tursiops_truncatus
ENSG00000102317RBM310055.294ENSTTRG00000011049CIRBP9757.831Tursiops_truncatus
ENSG00000102317RBM310096.815ENSUAMG00000013289RBM310096.815Ursus_americanus
ENSG00000102317RBM310057.059ENSUAMG00000014659CIRBP9058.434Ursus_americanus
ENSG00000102317RBM310056.471ENSUMAG00000005794CIRBP7558.434Ursus_maritimus
ENSG00000102317RBM310096.815ENSUMAG00000007785RBM310096.815Ursus_maritimus
ENSG00000102317RBM310095.597ENSVVUG00000017670RBM310095.597Vulpes_vulpes
ENSG00000102317RBM310057.059ENSVVUG00000022844-7558.434Vulpes_vulpes
ENSG00000102317RBM310057.055ENSXETG00000003281cirbp9757.143Xenopus_tropicalis
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0003723RNA binding22658674.22681889.HDAFunction
GO:0003723RNA binding21873635.IBAFunction
GO:0003730mRNA 3'-UTR binding21873635.IBAFunction
GO:0005515protein binding15518812.25416956.IPIFunction
GO:0005634nucleus21873635.IBAComponent
GO:0005634nucleus-ISSComponent
GO:0005654nucleoplasm-IDAComponent
GO:0005681spliceosomal complex21873635.IBAComponent
GO:0005730nucleolus-IDAComponent
GO:0005737cytoplasm21873635.IBAComponent
GO:0005737cytoplasm-ISSComponent
GO:0006396RNA processing8634703.TASProcess
GO:0006417regulation of translation21873635.IBAProcess
GO:0006417regulation of translation-ISSProcess
GO:0008266poly(U) RNA binding21873635.IBAFunction
GO:0009409response to cold21873635.IBAProcess
GO:0015934large ribosomal subunit21873635.IBAComponent
GO:0015934large ribosomal subunit-ISSComponent
GO:0017148negative regulation of translation-IEAProcess
GO:0030371translation repressor activity21873635.IBAFunction
GO:0030425dendrite-ISSComponent
GO:0043023ribosomal large subunit binding21873635.IBAFunction
GO:0045727positive regulation of translation21873635.IBAProcess
GO:0045727positive regulation of translation-ISSProcess
GO:0048026positive regulation of mRNA splicing, via spliceosome21873635.IBAProcess
GO:0070181small ribosomal subunit rRNA binding21873635.IBAFunction
GO:1990904ribonucleoprotein complex21873635.IBAComponent
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