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
17109515Comparison of gene expression profiles between primary tumor and metastatic lesions in gastric cancer patients using laser microdissection and cDNA microarray.World J Gastroenterol2006 Nov 21Wang L-
25336120Increased N-glycosylation of Asn in serum pancreatic ribonuclease 1 is a novel diagnostic marker for pancreatic cancer.Sci Rep2014 Oct 22Nakata Ddoi: 10.1038/srep06715.

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
BLCAchr1420801898Missense_MutationNAM57I0.08RnaseA
CESCchr1420801605Missense_MutationNAS155C0.36
CESCchr1420801917Missense_MutationnovelS51F0.41RnaseA
CESCchr14208014873'UTRnovel0.41
COADchr1420801876Nonsense_MutationNAQ65*0.42RnaseA
GBMchr14208015773'UTRnovel0.17
GBMchr1420801853Frame_Shift_DelnovelN72Kfs*90.16RnaseA
LIHCchr1420801940SilentNAS43S0.19
LIHCchr1420801909Missense_MutationNAC54R0.43RnaseA
LIHCchr1420801814SilentnovelV85V0.51
LUADchr14208015803'UTRnovel0.15
LUADchr14208015823'UTRnovel0.17
LUADchr1420801682Silentrs746951001P129P0.3
LUSCchr1420801629Missense_MutationnovelH147R0.1
LUSCchr14208015203'UTRnovel0.86
LUSCchr1420801622SilentNAD149D0.64
OVchr1420801920Frame_Shift_InsnovelS50Kfs*70.04RnaseA
OVchr1420801922In_Frame_InsnovelS49delinsRLPPD0.04RnaseA
OVchr1420802039SilentnovelL10L0.08
OVchr1420801646Missense_MutationNAS141R0.09
READchr1420802004In_Frame_DelnovelW22del0.3RnaseA
SKCMchr1420801932Missense_Mutationrs770257111S46F0.37RnaseA
SKCMchr1420801977Missense_MutationnovelS31F0.45RnaseA
SKCMchr1420801676SilentNAE131E0.34
SKCMchr1420801823SilentNAV82V0.42
SKCMchr1420801834SilentNAL79L0.1
STADchr14208015573'UTRnovel0.48
THCAchr1420801844SilentNAV75V0.07
UCECchr1420802028Missense_MutationNAV14A0.17RnaseA
UCECchr1420801870Missense_MutationnovelR67W0.23RnaseA
UCECchr1420801974In_Frame_InsnovelR32delinsQLMFAW0.07RnaseA
UCECchr14208015633'UTRnovel0.51
UCECchr1420801907Silentrs772113858C54C0.1

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
ACCAMP0.27780.056464
ACCDEL0.14440.19769
CHOLDEL0.36110.00040262
HNSCDEL0.10920.0025503
KIRPDEL0.16320.085174
LUADAMP0.24030.17291
LUSCDEL0.26150.0082553
OVDEL0.24183.8574e-27
PAADDEL0.09240.11332
READDEL0.36970.0043084
SKCMAMP0.08450.00015162
STADAMP0.08390.0078915
TGCTAMP0.27330.019484
THCADEL0.0020.27619

Survival Analysis
CancerP-value Q-value
THYM0.032

Kaplan-Meier Survival Analysis

KIRC0.0025

Kaplan-Meier Survival Analysis

STAD0.0022

Kaplan-Meier Survival Analysis

SARC0.025

Kaplan-Meier Survival Analysis

BRCA0.028

Kaplan-Meier Survival Analysis

COAD0.022

Kaplan-Meier Survival Analysis

PCPG0.014

Kaplan-Meier Survival Analysis

LIHC0.02

Kaplan-Meier Survival Analysis

THCA0.021

Kaplan-Meier Survival Analysis

LUAD0.00028

Kaplan-Meier Survival Analysis

Drugs

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Eesembl ID



Cell lines and drugs in GSE70138 or GSE92742

  • Description
  • RBDs
  • Literatures
  • Expression
  • Transcripts
  • Gene Model
  • Phenotypes
  • PPI
  • Paralogs
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000129538 (Gene tree)
Gene ID
6035
Gene Symbol
RNASE1
Alias
RAC1|RNS1
Full Name
ribonuclease A family member 1, pancreatic
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Minus strand
Length
2,051 bases
Position
chr14:20,801,228-20,803,278
Accession
10044
RBP type
canonical RBP
Summary
This gene encodes a member of the pancreatic-type of secretory ribonucleases, a subset of the ribonuclease A superfamily. The encoded endonuclease cleaves internal phosphodiester RNA bonds on the 3'-side of pyrimidine bases. It prefers poly(C) as a substrate and hydrolyzes 2',3'-cyclic nucleotides, with a pH optimum near 8.0. The encoded protein is monomeric and more commonly acts to degrade ds-RNA over ss-RNA. Alternative splicing occurs at this locus and four transcript variants encoding the same protein have been identified. [provided by RefSeq, Jul 2008]
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000344193RnaseAPF00074.207.9e-4411
ENSP00000381057RnaseAPF00074.207.9e-4411
ENSP00000381060RnaseAPF00074.207.9e-4411
ENSP00000399493RnaseAPF00074.207.9e-4411
ENSP00000451058RnaseAPF00074.201.5e-3911

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
3790497Effects of bovine pancreatic ribonuclease A, S protein, and S peptide on activation of purified rat hepatic glucocorticoid-receptor complexes.Biochemistry1986 Oct 7Schmidt TJ-
16730994The binding of 3'-N-piperidine-4-carboxyl-3'-deoxy-ara-uridine to ribonuclease A in the crystal.Bioorg Med Chem2006 Sep 1Leonidas DD-
3316356Isolating and sequencing the infrequent 3'-ends of a specific mRNA.J Biochem Biophys Methods1987 JulCannistraro VJ-
8985594The autoantigen La/SSB is a calmodulin-binding protein.Cell Calcium1996 DecCastro A-
19120453Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent.FEBS J2009 FebGentz PMdoi: 10.1111/j.1742-4658.2008.06817.x
23194006Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.Biochemistry2012 Dec 21Burdisso Pdoi: 10.1021/bi301247r
12785787Aminoglycoside complexation with a DNA.RNA hybrid duplex: the thermodynamics of recognition and inhibition of RNA processing enzymes.J Am Chem Soc2003 May 28Barbieri CM-
25890199Complexities due to single-stranded RNA during antibody detection of genomic rna:dna hybrids.BMC Res Notes2015 Apr 8Zhang ZZdoi: 10.1186/s13104-015-1092-1.
1700132RNA dependence of the bacteriophage phi 29 DNA packaging ATPase.J Mol Biol1990 Oct 20Grimes S-
8643340Double-stranded RNA: the variables controlling its degradation by RNases.Nucleic Acids Symp Ser1995Yakovlev GI-
8816469Upstream binding factor stabilizes Rib 1, the TATA-binding-protein-containing Xenopus laevis RNA polymerase I transcription factor, by multiple protein interactions in a DNA-independent manner.Mol Cell Biol1996 OctBodeker M-
23772376Crystal structure of human angiogenin with an engineered loop exhibits conformational flexibility at the functional regions of the molecule.FEBS Open Bio2012 Dec 26Thiyagarajan Ndoi: 10.1016/j.fob.2012.12.003
28575276Structural determinants of APOBEC3B non-catalytic domain for molecular assembly and catalytic regulation.Nucleic Acids Res2017 Jul 7Xiao Xdoi: 10.1093/nar/gkx362.
7038676 double helix in a RNA-protein contact site.Proc Natl Acad Sci U S A1981 DecPeattie DA-
4340162Polyadenylic acid at the 3'-terminus of poliovirus RNA.Proc Natl Acad Sci U S A1972 JulYogo Y-
3901927Synthesis of messenger-like RNA in avian erythrocyte nuclei.Arch Biochem Biophys1985 OctWiersma PA-
3681967Analysis of RNase-A-resistant regions of adenovirus 2 major late precursor-mRNA in splicing extracts reveals an ordered interaction of nuclear components with the substrate RNA.J Mol Biol1987 Aug 5Kramer A-
2442753Cytoplasmic Z-RNA.Proc Natl Acad Sci U S A1987 SepZarling DA-
9358156Binding of Hoechst 33258 to the TAR RNA of HIV-1. Recognition of a pyrimidine bulge-dependent structure.Nucleic Acids Res1997 Nov 15Dassonneville L-
9029158The Xenopus RNA polymerase I transcription factor, UBF, has a role in transcriptional enhancement distinct from that at the promoter.EMBO J1997 Jan 15McStay B-
8603681Interaction of intermediate filaments with ribosomes in vitro.Eur J Cell Biol1995 NovBauer C-
12939146Degradation of double-stranded RNA by human pancreatic ribonuclease: crucial role of noncatalytic basic amino acid residues.Biochemistry2003 Sep 2Sorrentino S-
12663761Homo-oligomerization of the porcine reproductive and respiratory syndrome virus nucleocapsid protein and the role of disulfide linkages.J Virol2003 AprWootton SK-
12270158Inhibition of the U1A-RNA complex by an aminoacridine derivative.Bioorg Med Chem Lett2002 Oct 21Gayle AY-
11131140Binding patterns and kinetics of RNase a interaction with RNA.J Protein Chem2000 JulSafarian S-
10715103Aminoglycoside-arginine conjugates that bind TAR RNA: synthesis, characterization, and antiviral activity.Biochemistry2000 Mar 21Litovchick A-
15064727Binding of RNA to p53 regulates its oligomerization and DNA-binding activity.Oncogene2004 May 27Yoshida Y-
23643491The retrovirus MA and PreTM proteins follow immature MLV cores.Virus Res2013 AugAndersen KBdoi: 10.1016/j.virusres.2013.04.014
29946031Arthropod EVs mediate dengue virus transmission through interaction with a tetraspanin domain containing glycoprotein Tsp29Fb.Proc Natl Acad Sci U S A2018 Jul 10Vora Adoi: 10.1073/pnas.1720125115
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000397967RNASE1-2021348-ENSP00000381057156 (aa)-P07998
ENST00000412779RNASE1-204896-ENSP00000399493156 (aa)-P07998
ENST00000397970RNASE1-203769-ENSP00000381060156 (aa)-P07998
ENST00000555698RNASE1-205655-ENSP00000451058116 (aa)-G3V357
ENST00000340900RNASE1-201878-ENSP00000344193156 (aa)-P07998
Gene Model
Click here to download ENSG00000129538's gene model file
Phenotypes
ensgIDTraitpValuePubmed ID
ENSG00000129538Platelet Function Tests3.2837100E-005-
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000129538's network

* RBP PPI network refers to all genes directly bind to RBP
Paralogs
Ensembl IDGene SymbolCoverageIdentiy ParalogGene SymbolCoverageIdentiy
ENSG00000129538RNASE18531.532ENSG00000169397RNASE36931.532
ENSG00000129538RNASE18637.963ENSG00000165799RNASE77436.066
ENSG00000129538RNASE18941.228ENSG00000173431RNASE86841.818
ENSG00000129538RNASE18933.621ENSG00000169385RNASE27733.077
ENSG00000129538RNASE19436.522ENSG00000214274ANG8635.507
ENSG00000129538RNASE17733.333ENSG00000258436RNASE126234.066
ENSG00000129538RNASE18938.182ENSG00000169413RNASE68334.351
ENSG00000129538RNASE19646.000ENSG00000258818RNASE410046.000
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000129538RNASE19773.026ENSAMEG00000020058RNASE110072.368Ailuropoda_melanoleuca
ENSG00000129538RNASE19768.750ENSBTAG00000004950BRB7870.769Bos_taurus
ENSG00000129538RNASE19770.536ENSBTAG00000008793RNASE18771.538Bos_taurus
ENSG00000129538RNASE19772.321ENSBTAG00000025663RNASE18773.846Bos_taurus
ENSG00000129538RNASE110091.379ENSCJAG00000009640RNASE110089.103Callithrix_jacchus
ENSG00000129538RNASE19667.333ENSCAFG00000005431RNASE19765.789Canis_familiaris
ENSG00000129538RNASE19267.593ENSCAFG00020014411RNASE18767.460Canis_lupus_dingo
ENSG00000129538RNASE19772.321ENSCHIG00000013517-8973.846Capra_hircus
ENSG00000129538RNASE18663.000ENSCHIG00000021682-10064.516Capra_hircus
ENSG00000129538RNASE19769.643ENSCHIG00000012401-7871.756Capra_hircus
ENSG00000129538RNASE19766.964ENSCAPG00000005648-8868.939Cavia_aperea
ENSG00000129538RNASE110072.414ENSCAPG00000006876-8874.265Cavia_aperea
ENSG00000129538RNASE110071.552ENSCAPG00000006524-8969.630Cavia_aperea
ENSG00000129538RNASE110071.552ENSCPOG00000027335-8969.630Cavia_porcellus
ENSG00000129538RNASE110072.414ENSCPOG00000026584-8874.265Cavia_porcellus
ENSG00000129538RNASE19775.658ENSCLAG00000001527-10075.658Chinchilla_lanigera
ENSG00000129538RNASE110073.276ENSCLAG00000000721-8368.382Chinchilla_lanigera
ENSG00000129538RNASE110093.103ENSCSAG00000000345RNASE110087.179Chlorocebus_sabaeus
ENSG00000129538RNASE110075.000ENSCHOG00000004379RNASE110075.000Choloepus_hoffmanni
ENSG00000129538RNASE19771.429ENSCGRG00001015062Rnase18972.727Cricetulus_griseus_chok1gshd
ENSG00000129538RNASE19771.429ENSCGRG00000006090Rnase18972.727Cricetulus_griseus_crigri
ENSG00000129538RNASE110076.724ENSDORG00000025686Rnase110075.385Dipodomys_ordii
ENSG00000129538RNASE110068.590ENSETEG00000011243RNASE110068.590Echinops_telfairi
ENSG00000129538RNASE110081.897ENSEASG00005002959RNASE17579.487Equus_asinus_asinus
ENSG00000129538RNASE110081.897ENSECAG00000011930-7679.487Equus_caballus
ENSG00000129538RNASE110059.119ENSFDAG00000013709-10059.119Fukomys_damarensis
ENSG00000129538RNASE110075.862ENSFDAG00000019850-9377.778Fukomys_damarensis
ENSG00000129538RNASE110098.276ENSGGOG00000002779RNASE110097.436Gorilla_gorilla
ENSG00000129538RNASE18666.000ENSHGLG00000002268-6267.347Heterocephalus_glaber_female
ENSG00000129538RNASE110076.724ENSHGLG00000002223-10076.282Heterocephalus_glaber_female
ENSG00000129538RNASE110074.359ENSHGLG00100019990-10074.359Heterocephalus_glaber_male
ENSG00000129538RNASE18666.000ENSHGLG00100000274-5967.347Heterocephalus_glaber_male
ENSG00000129538RNASE18666.000ENSHGLG00100000307-6067.347Heterocephalus_glaber_male
ENSG00000129538RNASE19976.522ENSSTOG00000007439RNASE19975.484Ictidomys_tridecemlineatus
ENSG00000129538RNASE110075.641ENSLAFG00000001701RNASE110075.641Loxodonta_africana
ENSG00000129538RNASE110092.241ENSMMUG00000017666RNASE110086.538Macaca_mulatta
ENSG00000129538RNASE19770.536ENSMAUG00000016055Rnase18971.970Mesocricetus_auratus
ENSG00000129538RNASE19773.214ENSMOCG00000006631Rnase110071.053Microtus_ochrogaster
ENSG00000129538RNASE19442.727ENSMODG00000006908-8743.846Monodelphis_domestica
ENSG00000129538RNASE19939.610ENSMODG00000024490-8540.625Monodelphis_domestica
ENSG00000129538RNASE19759.821ENSMODG00000006948-8761.069Monodelphis_domestica
ENSG00000129538RNASE19770.536MGP_CAROLIEiJ_G0019220Rnase18972.727Mus_caroli
ENSG00000129538RNASE19769.643ENSMUSG00000035896Rnase18971.970Mus_musculus
ENSG00000129538RNASE19767.857MGP_PahariEiJ_G0030245Rnase18969.697Mus_pahari
ENSG00000129538RNASE19769.643MGP_SPRETEiJ_G0020113Rnase18971.970Mus_spretus
ENSG00000129538RNASE19768.750ENSMPUG00000018382-10068.421Mustela_putorius_furo
ENSG00000129538RNASE19762.500ENSMPUG00000019871-10062.500Mustela_putorius_furo
ENSG00000129538RNASE19758.261ENSMPUG00000019285-8760.741Mustela_putorius_furo
ENSG00000129538RNASE19657.895ENSMPUG00000010701-9659.016Mustela_putorius_furo
ENSG00000129538RNASE19779.464ENSMLUG00000027439-10079.688Myotis_lucifugus
ENSG00000129538RNASE19677.333ENSMLUG00000023955-10076.667Myotis_lucifugus
ENSG00000129538RNASE110079.487ENSMLUG00000024436-10078.205Myotis_lucifugus
ENSG00000129538RNASE110070.513ENSMLUG00000030554-10069.231Myotis_lucifugus
ENSG00000129538RNASE110072.436ENSMLUG00000029157-10071.154Myotis_lucifugus
ENSG00000129538RNASE19678.667ENSMLUG00000024781-10077.333Myotis_lucifugus
ENSG00000129538RNASE19772.549ENSNGAG00000011713Rnase110072.549Nannospalax_galili
ENSG00000129538RNASE110098.276ENSNLEG00000007524RAC110096.154Nomascus_leucogenys
ENSG00000129538RNASE110070.690ENSODEG00000002038-10069.531Octodon_degus
ENSG00000129538RNASE110071.552ENSODEG00000001688-9870.866Octodon_degus
ENSG00000129538RNASE19772.368ENSODEG00000018720-9972.368Octodon_degus
ENSG00000129538RNASE19068.269ENSOCUG00000007495RNASE18863.910Oryctolagus_cuniculus
ENSG00000129538RNASE110080.342ENSOGAG00000010961RNASE110079.618Otolemur_garnettii
ENSG00000129538RNASE19770.536ENSOARG00000019721-6872.519Ovis_aries
ENSG00000129538RNASE19772.321ENSOARG00000012671-8973.846Ovis_aries
ENSG00000129538RNASE110099.138ENSPPAG00000008180RNASE110098.077Pan_paniscus
ENSG00000129538RNASE110099.138ENSPTRG00000006105RNASE110098.077Pan_troglodytes
ENSG00000129538RNASE19769.737ENSPEMG00000014451Rnase18971.970Peromyscus_maniculatus_bairdii
ENSG00000129538RNASE19640.541ENSPCIG00000028758-9241.026Phascolarctos_cinereus
ENSG00000129538RNASE19752.679ENSPCIG00000028757-8455.303Phascolarctos_cinereus
ENSG00000129538RNASE19443.636ENSPCIG00000028752-8645.385Phascolarctos_cinereus
ENSG00000129538RNASE110096.552ENSPPYG00000005578RNASE19996.078Pongo_abelii
ENSG00000129538RNASE110081.897ENSPVAG00000013558RNASE110076.282Pteropus_vampyrus
ENSG00000129538RNASE19760.714ENSRNOG00000054433Rnase1l210061.935Rattus_norvegicus
ENSG00000129538RNASE19765.179ENSRNOG00000053633LOC10369035410065.161Rattus_norvegicus
ENSG00000129538RNASE19760.177ENSRNOG00000025615Rnase1l110059.477Rattus_norvegicus
ENSG00000129538RNASE19760.714ENSRNOG00000057064LOC10369485310061.935Rattus_norvegicus
ENSG00000129538RNASE19765.179ENSRNOG00000057266Rnase18966.667Rattus_norvegicus
ENSG00000129538RNASE19143.810ENSSHAG00000005129-8441.860Sarcophilus_harrisii
ENSG00000129538RNASE19965.584ENSSARG00000004138RNASE19965.584Sorex_araneus
ENSG00000129538RNASE19775.893ENSSSCG00000031649RNASE18778.788Sus_scrofa
ENSG00000129538RNASE110079.487ENSTBEG00000001674RNASE110079.487Tupaia_belangeri
ENSG00000129538RNASE19772.321ENSTTRG00000010672RNASE18675.000Tursiops_truncatus
ENSG00000129538RNASE19769.643ENSUAMG00000011269RNASE18671.970Ursus_americanus
ENSG00000129538RNASE19769.643ENSUMAG00000003444RNASE18771.970Ursus_maritimus
ENSG00000129538RNASE19662.162ENSVPAG00000011245-9064.615Vicugna_pacos
ENSG00000129538RNASE17266.071ENSVPAG00000011243-9065.714Vicugna_pacos
ENSG00000129538RNASE19665.766ENSVVUG00000009069-9168.317Vulpes_vulpes
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0003676nucleic acid binding-IEAFunction
GO:0004522ribonuclease A activity-IEAFunction
GO:0004540ribonuclease activity21873635.IBAFunction
GO:0004540ribonuclease activity9826755.IDAFunction
GO:0005515protein binding17350650.29997244.IPIFunction
GO:0051607defense response to virus9826755.IDAProcess
GO:0070062extracellular exosome23533145.HDAComponent
GO:0090501RNA phosphodiester bond hydrolysis9826755.IDAProcess
GO:0090502RNA phosphodiester bond hydrolysis, endonucleolytic-IEAProcess
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