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
25056949Polyubiquitinated tristetraprolin protects from TNF-induced, caspase-mediated apoptosis.J Biol Chem2014 Sep 5Resch Udoi: 10.1074/jbc.M114.563312
20157568The mRNA decay factor tristetraprolin (TTP) induces senescence in human papillomavirus-transformed cervical cancer cells by targeting E6-AP ubiquitin ligase.Aging (Albany NY)2009 Sep 10Sanduja S-
23583445Tristetraprolin suppresses AHRR expression through mRNA destabilization.FEBS Lett2013 May 21Lee HHdoi: 10.1016/j.febslet.2013.03.031
23241166Depletion of tristetraprolin in breast cancer cells increases interleukin-16 expression and promotes tumor infiltration with monocytes/macrophages.Carcinogenesis2013 AprMilke Ldoi: 10.1093/carcin/bgs387
22700982Expression of proviral integration site for Moloney murine leukemia virus 1 (Pim-1) is post-transcriptionally regulated by tristetraprolin in cancer cells.J Biol Chem2012 Aug 17Kim HKdoi: 10.1074/jbc.M112.376483
16614304Atherosclerotic plaque macrophage transcriptional regulators are expressed in blood and modulated by tristetraprolin.Circ Res2006 May 26Patino WD-
20335167Stability of the LATS2 tumor suppressor gene is regulated by tristetraprolin.J Biol Chem2010 Jun 4Lee HHdoi: 10.1074/jbc.M109.094235
12751757Tristetraprolin binds to the COX-2 mRNA 3' untranslated region in cancer cells.Adv Exp Med Biol2003Boutaud O-
26497679Tristetraprolin induces cell cycle arrest in breast tumor cells through targeting AP-1/c-Jun and NF-??B pathway.Oncotarget2015 Dec 8Xu Ldoi: 10.18632/oncotarget.6149.
29246442Oncogenic RAS Signaling Promotes Tumor Immunoresistance by Stabilizing PD-L1 mRNA.Immunity2017 Dec 19Coelho MAdoi: 10.1016/j.immuni.2017.11.016
22387927Tristetraprolin: roles in cancer and senescence.Ageing Res Rev2012 SepRoss CRdoi: 10.1016/j.arr.2012.02.005
23401122miR-29a inhibition normalizes HuR over-expression and aberrant AU-rich mRNA stability in invasive cancer.J Pathol2013 MayAl-Ahmadi Wdoi: 10.1002/path.4178
26563146Prognostic value of ZFP36 and SOCS3 expressions in human prostate cancer.Clin Transl Oncol2016 AugZhu JGdoi: 10.1007/s12094-015-1432-6
26486958Tristetraprolin regulation of interleukin-22 production.Sci Rep2015 Oct 21Hrdle Ldoi: 10.1038/srep15112.
26840564Tristetraprolin suppresses the EMT through the down-regulation of Twist1 and Snail1 in cancer cells.Oncotarget2016 Feb 23Yoon NAdoi: 10.18632/oncotarget.7094.
24737323Tristetraprolin represses estrogen receptor α transactivation in breast cancer cells.J Biol Chem2014 May 30Barrios-Garc??a Tdoi: 10.1074/jbc.M114.548552
20498646The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes.Oncogene2010 Jul 22Al-Souhibani Ndoi: 10.1038/onc.2010.168
15067324Gene expression profiling predicts clinical outcome of prostate cancer.J Clin Invest2004 MarGlinsky GV-
21830391Tristetraprolin downregulates the expression of both VEGF and COX-2 in human colon cancer.Hepatogastroenterology2011 May-JunCha HJ-
27074834Tristetraprolin inhibits gastric cancer progression through suppression of IL-33.Sci Rep2016 Apr 14Deng Kdoi: 10.1038/srep24505.
22907529Genetic polymorphisms in RNA binding proteins contribute to breast cancer survival.Int J Cancer2013 Feb 1Upadhyay Rdoi: 10.1002/ijc.27789
19697322Tristetraprolin regulates expression of VEGF and tumorigenesis in human colon cancer.Int J Cancer2010 Apr 15Lee HHdoi: 10.1002/ijc.24847.
23349315Inactivation or loss of TTP promotes invasion in head and neck cancer via transcript stabilization and secretion of MMP9, MMP2, and IL-6.Clin Cancer Res2013 Mar 1Van Tubergen EAdoi: 10.1158/1078-0432.CCR-12-2927
21875902A synonymous polymorphism of the Tristetraprolin (TTP) gene, an AU-rich mRNA-binding protein, affects translation efficiency and response to Herceptin treatment in breast cancer patients.Hum Mol Genet2011 Dec 1Griseri Pdoi: 10.1093/hmg/ddr390
25604244TTP mediates cisplatin-induced apoptosis of head and neck cancer cells by down-regulating the expression of Bcl-2.J Chemother2015 JunPark SBdoi: 10.1179/1973947814Y.0000000234
27825143Tristetraprolin disables prostate cancer maintenance by impairing proliferation and metabolic function.Oncotarget2016 Dec 13Berglund AEdoi: 10.18632/oncotarget.13128.
28410208Tristetraprolin inhibits mitochondrial function through suppression of α-Synuclein expression in cancer cells.Oncotarget2017 Jun 27Vo MTdoi: 10.18632/oncotarget.16706.
29570932PIM2 interacts with tristetraprolin and promotes breast cancer tumorigenesis.Mol Oncol2018 MayRen Cdoi: 10.1002/1878-0261.12192

Differential Expression

Expression in 33 cancers

Mutations
CancerChrPosition Mutation TypedbSNPProtein-change Allele FreqRBD
ACCchr1939408609Silentrs752975772P303P0.44
BLCAchr1939406922SilentnovelI12I0.22
BLCAchr1939408056Missense_MutationNAS119L0.08zf-CCCH
BLCAchr19394087193'UTRnovel0.07
BLCAchr1939408694Missense_Mutationrs763230216E332K0.15
BRCAchr1939408253Missense_MutationNAP185S0.1
BRCAchr19394068655'UTRnovel0.22
BRCAchr1939408562Missense_MutationNAD288N0.21
BRCAchr1939408371Missense_MutationnovelS224F0.21
BRCAchr19394087103'UTRnovel0.15
CESCchr1939407766Missense_MutationnovelD22E0.05
CESCchr19394091113'UTRnovel0.12
CESCchr1939407822Missense_MutationNAS41L0.21
CESCchr1939408448Missense_MutationNAD250Y0.1
CESCchr1939408431Frame_Shift_DelNAL246Wfs*1260.4
CESCchr1939406913SilentnovelL9L0.23
CESCchr1939408253Missense_MutationNAP185S0.23
CESCchr1939407797Missense_MutationNAE33Q0.38
CESCchr1939407946Missense_MutationNAF82L0.47
COADchr19394087953'UTRnovel0.6
COADchr1939408679Missense_MutationnovelR327G0.08
COADchr1939408687Frame_Shift_DelnovelV330Ffs*20.35
COADchr1939408431Frame_Shift_DelNAL246Wfs*1260.38
ESCAchr19394090543'UTRnovel0.36
ESCAchr19394091733'UTRnovel0.28
ESCAchr19394087103'UTRnovel0.6
GBMchr1939408448Missense_MutationNAD250Y0.06
GBMchr1939408693SilentNAS331S0.12
HNSCchr1939408293Missense_MutationnovelS198C0.23
HNSCchr1939407946SilentnovelF82F0.41
HNSCchr1939408131Missense_MutationNAR144H0.27
HNSCchr1939407809Missense_MutationnovelG37S0.34
HNSCchr1939408559Missense_MutationnovelP287T0.24
KICHchr1939408431Frame_Shift_DelNAL246Wfs*1260.17
KIRPchr1939407763SilentNAP21P0.35
KIRPchr19394068855'UTRnovel0.35
LAMLchr1939407817SilentnovelG39G0.04
LIHCchr19394087033'UTRnovel0.33
LIHCchr1939407773Missense_Mutationrs752054358V25L0.26
LIHCchr1939408468Nonsense_MutationNAC256*0.38
LIHCchr19394087263'UTRnovel0.33
LUADchr19394068575'UTRnovel0.2
LUADchr1939408390Missense_MutationnovelD230E0.64
LUADchr1939408522Silentrs777948625L274L0.1
LUADchr1939408655Missense_MutationnovelP319S0.18
LUADchr19394068725'UTRrs5770216720.14
LUADchr1939407848Missense_Mutationrs773711012D50Y0.32
LUADchr1939408246SilentnovelG182G0.17
LUADchr1939408694Nonsense_MutationnovelE332*0.08
LUADchr1939408234SilentNAL178L0.17
LUADchr1939408058Missense_MutationnovelE120K0.05zf-CCCH
LUADchr1939408023Missense_MutationnovelS108L0.13
LUADchr1939408229Missense_MutationNAD177Y0.51
LUADchr1939407742Splice_SiteNAX15_splice0.36
LUSCchr19394087103'UTRnovel0.18
LUSCchr19394087083'UTRnovel0.08
LUSCchr19394087513'UTRnovel0.71
LUSCchr1939408004Missense_MutationnovelA102S0.19
LUSCchr1939408299Missense_Mutationrs774467387R200H0.13
MESOchr1939408101Missense_MutationnovelH134R0.12zf-CCCH
OVchr19394087853'UTRnovel0.98
OVchr1939407820SilentNAS40S0.04
OVchr1939408500Missense_MutationnovelV267D0.24
OVchr1939407780Missense_MutationNAS27Y0.47
PAADchr19394068655'UTRnovel0.18
PAADchr19394087433'UTRnovel0.27
PRADchr1939408363Silentrs149138506P221P0.38
READchr1939408658Missense_MutationNAR320G0.9
READchr1939408414Missense_MutationNAF238L0.38
SARCchr1939408507SilentnovelG269G0.08
SARCchr1939407068Intronnovel0.46
SKCMchr19394087273'UTRnovel0.08
SKCMchr19394087413'UTRnovel0.21
SKCMchr1939407890Missense_MutationNAS64T0.46
SKCMchr19394068815'UTRnovel0.43
SKCMchr1939408086Missense_MutationnovelK129R0.41zf-CCCH
STADchr1939408119Missense_MutationnovelR140P0.08
STADchr1939408079Frame_Shift_DelnovelA128Pfs*2440.27zf-CCCH
STADchr1939408309SilentNAS203S0.32
STADchr1939408431Frame_Shift_DelNAL246Wfs*1260.29
THCAchr1939408149Missense_MutationNAT150R0.36
THCAchr1939406891Missense_MutationnovelA2V0.29
THCAchr1939408243Silentrs535257605P181P0.33
THYMchr19394089863'UTRnovel0.07
UCECchr1939408201SilentnovelR167R0.29
UCECchr1939408597SilentnovelG299G0.08
UCECchr1939408565Nonsense_MutationNAE289*0.37
UCECchr1939408592Missense_MutationnovelG298R0.27
UCECchr1939407929Frame_Shift_DelnovelP78Hfs*2940.41
UCECchr19394091793'UTRnovel0.48
UCECchr1939408645Silentrs149251013P315P0.32
UCECchr1939408284Missense_MutationNAG195D0.4
UCECchr1939407935Frame_Shift_DelnovelP80Lfs*2920.49
UCECchr1939406918Missense_MutationNAA11V0.54
UCECchr1939407840Missense_Mutationrs776166452S47N0.14
UCECchr19394090733'UTRnovel0.19
UCECchr1939408285SilentnovelG195G0.32
UCECchr1939407788Nonsense_MutationnovelG30*0.32
UCECchr19394091613'UTRnovel0.31
UCECchr1939408044Missense_MutationnovelC115Y0.38zf-CCCH
UCECchr1939408232Missense_MutationnovelL178M0.46
UCECchr1939408213SilentnovelI171I0.28
UCECchr19394092263'UTRnovel0.3
UCECchr1939408414Missense_MutationNAF238L0.19
UCECchr19394089903'UTRnovel0.38
UCECchr19394090983'UTRnovel0.28

Copy Number Variations (CNVs)
CancerTypeFreq Q-value
KIRPDEL0.04510.054726
OVAMP0.35412.2539e-28
PAADAMP0.20113.1883e-10
READDEL0.05450.23023
UCSDEL0.1250.12448

Survival Analysis
CancerP-value Q-value
STAD0.018

Kaplan-Meier Survival Analysis

SARC0.016

Kaplan-Meier Survival Analysis

ACC0.0023

Kaplan-Meier Survival Analysis

SKCM0.01

Kaplan-Meier Survival Analysis

LUSC0.04

Kaplan-Meier Survival Analysis

BLCA0.0067

Kaplan-Meier Survival Analysis

LAML0.031

Kaplan-Meier Survival Analysis

KICH0.042

Kaplan-Meier Survival Analysis

GBM0.048

Kaplan-Meier Survival Analysis

LGG0.0005

Kaplan-Meier Survival Analysis

CHOL0.037

Kaplan-Meier Survival Analysis

OV0.0042

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
  • Orthologs
  • Gene Ontology
Description
Ensembl ID
ENSG00000128016 (Gene tree)
Gene ID
7538
Gene Symbol
ZFP36
Alias
RNF162A|TIS11|G0S24|TTP|NUP475
Full Name
ZFP36 ring finger protein
Gene Type
protein_coding
Species
Homo_sapiens
Status
confidence
Strand
Plus strand
Length
2,600 bases
Position
chr19:39,406,813-39,409,412
Accession
12862
RBP type
canonical RBP
Summary
(ZFP36 Ring Finger Protein) is a Protein Coding gene. Among its related pathways are Human cytomegalovirus infection and Preimplantation Embryo. Gene Ontology (GO) annotations related to this gene include enzyme binding. An important paralog of this gene is ZFP36L2.
RNA binding domains(RBDs)
Protein IDDomain Pfam IDE-value Domain number Total number
ENSP00000469647zf-CCCHPF00642.241.3e-2012
ENSP00000469647zf-CCCHPF00642.241.3e-2022
ENSP00000471239zf-CCCHPF00642.242.3e-1912
ENSP00000471239zf-CCCHPF00642.242.3e-1922
ENSP00000470200zf-CCCHPF00642.241.9e-1111
RNA binding proteome (RBPome)
PIDTitleMethod TimeAuthorDoi
22658674Insights into RNA biology from an atlas of mammalian mRNA-binding proteinsRIC & Hela2012 May 31Castello ADOI: 10.1016/j.cell.2012.04.031

Literatures on RNA binding capacity
PIDTitleArticle TimeAuthorDoi
22542594Cadmium coordination to the zinc binding domains of the non-classical zinc finger protein Tristetraprolin affects RNA binding selectivity.J Inorg Biochem2012 JulMichalek JLdoi: 10.1016/j.jinorgbio.2012.02.023
22242014Genome-wide assessment of AU-rich elements by the AREScore algorithm.PLoS Genet2012 JanSpasic Mdoi: 10.1371/journal.pgen.1002433
20498646The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes.Oncogene2010 Jul 22Al-Souhibani Ndoi: 10.1038/onc.2010.168
20453031Aldosterone and vasopressin affect {alpha}- and {gamma}-ENaC mRNA translation.Nucleic Acids Res2010 SepPerlewitz Adoi: 10.1093/nar/gkq267
24697202Control of pro-angiogenic cytokine mRNA half-life in cancer: the role of AU-rich elements and associated proteins.J Interferon Cytokine Res2014 AprGriseri Pdoi: 10.1089/jir.2013.0140.
28333956Discriminating between HuR and TTP binding sites using the k-spectrum kernel method.PLoS One2017 Mar 23Bhandare Sdoi: 10.1371/journal.pone.0174052
18467502Inhibition of tristetraprolin deadenylation by poly(A) binding protein.Am J Physiol Gastrointest Liver Physiol2008 SepRowlett RMdoi: 10.1152/ajpgi.00508.2007
25246635Rapid proteasomal degradation of posttranscriptional regulators of the TIS11/tristetraprolin family is induced by an intrinsically unstructured region independently of ubiquitination.Mol Cell Biol2014 Dec 1Ngoc LVdoi: 10.1128/MCB.00643-14
11782475Interactions of CCCH zinc finger proteins with mRNA: non-binding tristetraprolin mutants exert an inhibitory effect on degradation of AU-rich element-containing mRNAs.J Biol Chem2002 Mar 15Lai WS-
15535838The tandem CCCH zinc finger protein tristetraprolin and its relevance to cytokine mRNA turnover and arthritis.Arthritis Res Ther2004Carrick DM-
15226444Chorioallantoic fusion defects and embryonic lethality resulting from disruption of Zfp36L1, a gene encoding a CCCH tandem zinc finger protein of the Tristetraprolin family.Mol Cell Biol2004 JulStumpo DJ-
16782553The role of cytokine mRNA stability in the pathogenesis of autoimmune disease.Autoimmun Rev2006 MaySeko Y-
14638848IL-4-Stat6 signaling induces tristetraprolin expression and inhibits TNF-alpha production in mast cells.J Exp Med2003 Dec 1Suzuki K-
24978456hnRNP F complexes with tristetraprolin and stimulates ARE-mRNA decay.PLoS One2014 Jun 30Reznik Bdoi: 10.1371/journal.pone.0100992
30917308GIGYF1/2-Driven Cooperation between ZNF598 and TTP in Posttranscriptional Regulation of Inflammatory Signaling.Cell Rep2019 Mar 26Tollenaere MAXdoi: 10.1016/j.celrep.2019.03.006.
31236273Post-transcriptional control of immune responses and its potential application.Clin Transl Immunology2019 Jun 17Yoshinaga Mdoi: 10.1002/cti2.1063
12705825Selective RNA binding by a single CCCH zinc-binding domain from Nup475 (Tristetraprolin).Biochemistry2003 Apr 29Michel SL-
12324455RNA binding properties of the AU-rich element-binding recombinant Nup475/TIS11/tristetraprolin protein.J Biol Chem2002 Dec 13Worthington MT-
20157568The mRNA decay factor tristetraprolin (TTP) induces senescence in human papillomavirus-transformed cervical cancer cells by targeting E6-AP ubiquitin ligase.Aging (Albany NY)2009 Sep 10Sanduja S-
18678874Suppression of lipopolysaccharide-stimulated tumor necrosis factor-alpha production by adiponectin is mediated by transcriptional and post-transcriptional mechanisms.J Biol Chem2008 Oct 3Park PHdoi: 10.1074/jbc.M802787200
18523301Role of the RNA-binding protein tristetraprolin in glucocorticoid-mediated gene regulation.J Immunol2008 Jun 15Ishmael FT-
22665488The protein Zfand5 binds and stabilizes mRNAs with AU-rich elements in their 3'-untranslated regions.J Biol Chem2012 Jul 20He Gdoi: 10.1074/jbc.M112.362020
22426177HuR post-transcriptionally regulates TNF-α-induced IL-6 expression in human pulmonary microvascular endothelial cells mainly via tristetraprolin.Respir Physiol Neurobiol2012 Apr 30Shi JXdoi: 10.1016/j.resp.2012.02.011
22203679Direct binding of specific AUF1 isoforms to tandem zinc finger domains of tristetraprolin (TTP) family proteins.J Biol Chem2012 Feb 17Kedar VPdoi: 10.1074/jbc.M111.312652
24697206Phylogenetic distribution and evolution of the linked RNA-binding and NOT1-binding domains in the tristetraprolin family of tandem CCCH zinc finger proteins.J Interferon Cytokine Res2014 AprBlackshear PJdoi: 10.1089/jir.2013.0150.
24621334Reduction of TLR4 mRNA stability and protein expressions through inhibiting cytoplasmic translocation of HuR transcription factor by E and/or ERα in LPS-treated H9c2 cardiomyoblast cells.Chin J Physiol2014 Feb 28Fan MJdoi: 10.4077/CJP.2014.BAC197.
24001203MicroRNA-let-7a expression is increased in the mesangial cells of NZB/W mice and increases IL-6 production in vitro.Autoimmunity2013 SepChafin CBdoi: 10.3109/08916934.2013.773976.
27424080Tristetraprolin exerts tumor suppressive functions on the tumorigenesis of glioma by targeting IL-13.Int Immunopharmacol2016 OctZeng Bdoi: 10.1016/j.intimp.2016.07.001
27178967Tristetraprolin binding site atlas in the macrophage transcriptome reveals a switch for inflammationresolution.Mol Syst Biol2016 May 13Sedlyarov Vdoi: 10.15252/msb.20156628.
26644407LARP4 Is Regulated by Tumor Necrosis Factor Alpha in a Tristetraprolin-Dependent Manner.Mol Cell Biol2015 Dec 7Mattijssen Sdoi: 10.1128/MCB.00804-15
28929622Endonuclease Regnase-1/Monocyte chemotactic protein-1-induced protein-1 (MCPIP1) in controlling immune responses and beyond.Wiley Interdiscip Rev RNA2018 JanTakeuchi Odoi: 10.1002/wrna.1449
30226813linc-SCRG1 accelerates liver fibrosis by decreasing RNA-binding protein tristetraprolin.FASEB J2019 FebWu JCdoi: 10.1096/fj.201800098RR
30526691The RNA-binding proteins Zfp36l1 and Zfp36l2 act redundantly in myogenesis.Skelet Muscle2018 Dec 7Bye-A-Jee Hdoi: 10.1186/s13395-018-0183-9.
31046669Tristetraprolin specifically regulates the expression and alternative splicing of immune response genes in HeLa cells.BMC Immunol2019 May 2Tu Ydoi: 10.1186/s12865-019-0292-1.
12789264A novel mechanism of tumor suppression by destabilizing AU-rich growth factor mRNA.Oncogene2003 Jun 5Stoecklin G-
12748283Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease.Mol Cell Biol2003 JunLai WS-
12639954Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.J Biol Chem2003 May 30Blackshear PJ-
16514065Interferons limit inflammatory responses by induction of tristetraprolin.Blood2006 Jun 15Sauer I-
12077361Tristetraprolin and LPS-inducible CXC chemokine are rapidly induced in presumptive satellite cells in response to skeletal muscle injury.J Cell Sci2002 Jul 1Sachidanandan C-
11796723Members of the tristetraprolin family of tandem CCCH zinc finger proteins exhibit CRM1-dependent nucleocytoplasmic shuttling.J Biol Chem2002 Mar 29Phillips RS-
11720287Cellular mutants define a common mRNA degradation pathway targeting cytokine AU-rich elements.RNA2001 NovStoecklin G-
11602610HuA and tristetraprolin are induced following T cell activation and display distinct but overlapping RNA binding specificities.J Biol Chem2001 Dec 21Raghavan A-
10763822Similar but distinct effects of the tristetraprolin/TIS11 immediate-early proteins on cell survival.Oncogene2000 Mar 23Johnson BA-
15778452Tristetraprolin regulates the expression of the human inducible nitric-oxide synthase gene.Mol Pharmacol2005 JunFechir M-
15687258Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1.Genes Dev2005 Feb 1Lykke-Andersen J-
15117938RNA sequence elements required for high affinity binding by the zinc finger domain of tristetraprolin: conformational changes coupled to the bipartite nature of Au-rich MRNA-destabilizing motifs.J Biol Chem2004 Jul 2Brewer BY-
16759646Differential regulation of ARE-mediated TNFalpha and IL-1beta mRNA stability by lipopolysaccharide in RAW264.7 cells.Biochem Biophys Res Commun2006 Jul 21Chen YL-
16702957Tristetraprolin regulates Cyclin D1 and c-Myc mRNA stability in response to rapamycin in an Akt-dependent manner via p38 MAPK signaling.Oncogene2006 Oct 12Marderosian M-
20042592IL-17 regulates CXCL1 mRNA stability via an AUUUA/tristetraprolin-independent sequence.J Immunol2010 Feb 1Datta Sdoi: 10.4049/jimmunol.0902423
19995385Anthrax lethal toxin promotes dephosphorylation of TTP and formation of processing bodies.Cell Microbiol2010 Apr 1Chow EMdoi: 10.1111/j.1462-5822.2009.01418.x
19945750The RNA binding protein tristetraprolin influences the activation state of murine dendritic cells.Mol Immunol2010 FebBros Mdoi: 10.1016/j.molimm.2009.11.002
19801654Von Hippel-Lindau gene product modulates TIS11B expression in renal cell carcinoma: impact on vascular endothelial growth factor expression in hypoxia.J Biol Chem2009 Nov 20Sinha Sdoi: 10.1074/jbc.M109.058065
23042536MicroRNA-466l inhibits antiviral innate immune response by targeting interferon-alpha.Cell Mol Immunol2012 NovLi Ydoi: 10.1038/cmi.2012.35
19327732HuR and TTP: two RNA binding proteins that deliver message from the 3' end.Gastroenterology2009 MayAnant Sdoi: 10.1053/j.gastro.2009.03.024
19208339The mRNA binding proteins HuR and tristetraprolin regulate cyclooxygenase 2 expression during colon carcinogenesis.Gastroenterology2009 MayYoung LEdoi: 10.1053/j.gastro.2009.01.010
22995314Role of RNA-binding protein tristetraprolin in tumor necrosis factor-α mediated gene expression.Biochem Biophys Res Commun2012 Nov 23Chen Xdoi: 10.1016/j.bbrc.2012.09.033
18682699Targeting mRNA stability arrests inflammatory bone loss.Mol Ther2008 OctPatil CSdoi: 10.1038/mt.2008.163
22960231AU-rich elements in the 3'-UTR regulate the stability of the 141 amino acid isoform of parathyroid hormone-related protein mRNA.Mol Cell Endocrinol2012 Nov 25Luchin AIdoi: 10.1016/j.mce.2012.08.015
22968342Multiple functions of tristetraprolin/TIS11 RNA-binding proteins in the regulation of mRNA biogenesis and degradation.Cell Mol Life Sci2013 JunCiais Ddoi: 10.1007/s00018-012-1150-y
22968621Mammary differentiation induces expression of Tristetraprolin, a tumor suppressor AU-rich mRNA-binding protein.Breast Cancer Res Treat2012 OctGoddio MVdoi: 10.1007/s10549-012-2216-0
18481987Control of mRNA decay by phosphorylation of tristetraprolin.Biochem Soc Trans2008 JunSandler Hdoi: 10.1042/BST0360491.
18504409HMG-CoA reductase inhibitor simvastatin inhibits proinflammatory cytokine production from murine mast cells.Int Arch Allergy Immunol2008Kagami Sdoi: 10.1159/000126063
18256032Genome-wide analysis identifies interleukin-10 mRNA as target of tristetraprolin.J Biol Chem2008 Apr 25Stoecklin Gdoi: 10.1074/jbc.M709657200
18245466Tristetraprolin down-regulates interleukin-8 and vascular endothelial growth factor in malignant glioma cells.Cancer Res2008 Feb 1Suswam Edoi: 10.1158/0008-5472.CAN-07-2751.
18032482MNK kinases regulate multiple TLR pathways and innate proinflammatory cytokines in macrophages.Am J Physiol Gastrointest Liver Physiol2008 FebRowlett RM-
18047469Post-transcriptional regulation of CLMP mRNA is controlled by tristetraprolin in response to TNFalpha via c-Jun N-terminal kinase signalling.Biochem J2008 Mar 15Sze KL-
22907529Genetic polymorphisms in RNA binding proteins contribute to breast cancer survival.Int J Cancer2013 Feb 1Upadhyay Rdoi: 10.1002/ijc.27789
22865915Cutting edge: IL-10-mediated tristetraprolin induction is part of a feedback loop that controls macrophage STAT3 activation and cytokine production.J Immunol2012 Sep 1Gaba Adoi: 10.4049/jimmunol.1201126
17606626Ligand-independent regulation of transforming growth factor beta1 expression and cell cycle progression by the aryl hydrocarbon receptor.Mol Cell Biol2007 SepChang X-
17322004Post-transcriptional regulation of human inducible nitric-oxide synthase expression by the Jun N-terminal kinase.Mol Pharmacol2007 MayKorhonen R-
17288565Regulation of tristetraprolin during differentiation of 3T3-L1 preadipocytes.FEBS J2007 FebLin NY-
17087518Functional characterization of iron-substituted tristetraprolin-2D (TTP-2D, NUP475-2D): RNA binding affinity and selectivity.Biochemistry2006 Nov 14diTargiani RC-
17105199Substrate dependence of conformational changes in the RNA-binding domain of tristetraprolin assessed by fluorescence spectroscopy of tryptophan mutants.Biochemistry2006 Nov 21Brewer BY-
16950790The polypyrimidine tract-binding protein (PTB) is involved in the post-transcriptional regulation of human inducible nitric oxide synthase expression.J Biol Chem2006 Oct 27Pautz A-
22544323ZFP36 expression impairs glioblastoma cell lines viability and invasiveness by targeting multiple signal transduction pathways.Cell Cycle2012 May 15Selmi Tdoi: 10.4161/cc.20309
23339930Altered gene expression profiles associated with enhanced skin inflammation induced by 12-O-tetradecanoylphorbol-13-acetate in streptozotocin-diabetic mice.Int Immunopharmacol2013 MarIba Ydoi: 10.1016/j.intimp.2013.01.007
23342169Comparative functional analysis of ZFP36 genes during Xenopus development.PLoS One2013Treguer Kdoi: 10.1371/journal.pone.0054550
22428029Downregulation of the AU-rich RNA-binding protein ZFP36 in chronic HBV patients: implications for anti-inflammatory therapy.PLoS One2012Jin WJdoi: 10.1371/journal.pone.0033356
22315682MAPK usage in periodontal disease progression.J Signal Transduct2012Li Qdoi: 10.1155/2012/308943
22268119MK2 posttranscriptionally regulates TNF-α-induced expression of ICAM-1 and IL-8 via tristetraprolin in human pulmonary microvascular endothelial cells.Am J Physiol Lung Cell Mol Physiol2012 Apr 15Shi JXdoi: 10.1152/ajplung.00339.2011
22232680Phytochrome regulates translation of mRNA in the cytosol.Proc Natl Acad Sci U S A2012 Jan 24Paik Idoi: 10.1073/pnas.1109683109
22201737The role of tristetraprolin in cancer and inflammation.Front Biosci (Landmark Ed)2012 Jan 1Sanduja S-
22093924Nicotinic stimulation induces Tristetraprolin over-production and attenuates inflammation in muscle.Biochim Biophys Acta2012 FebGeyer BCdoi: 10.1016/j.bbamcr.2011.11.001
21982546RNA-binding proteins and gene regulation in myogenesis.Trends Pharmacol Sci2011 NovApponi LHdoi: 10.1016/j.tips.2011.06.004
21964062Protor-2 interacts with tristetraprolin to regulate mRNA stability during stress.Cell Signal2012 JanHolmes Bdoi: 10.1016/j.cellsig.2011.09.015
21875902A synonymous polymorphism of the Tristetraprolin (TTP) gene, an AU-rich mRNA-binding protein, affects translation efficiency and response to Herceptin treatment in breast cancer patients.Hum Mol Genet2011 Dec 1Griseri Pdoi: 10.1093/hmg/ddr390
23266986Involvement of XZFP36L1, an RNA-binding protein, in Xenopus neural development.Dongwuxue Yanjiu2012 DecXia YJdoi: 10.3724/SP.J.1141.2012.E05-06E82.
23269677Post-transcriptional regulation of meprin α by the RNA-binding proteins Hu antigen R (HuR) and tristetraprolin (TTP).J Biol Chem2013 Feb 15Roff ANdoi: 10.1074/jbc.M112.444208
23241166Depletion of tristetraprolin in breast cancer cells increases interleukin-16 expression and promotes tumor infiltration with monocytes/macrophages.Carcinogenesis2013 AprMilke Ldoi: 10.1093/carcin/bgs387
21457063Tristetraprolin regulates interleukin-6 expression through p38 MAPK-dependent affinity changes with mRNA 3' untranslated region.J Interferon Cytokine Res2011 AugZhao Wdoi: 10.1089/jir.2010.0154
21278420Not1 mediates recruitment of the deadenylase Caf1 to mRNAs targeted for degradation by tristetraprolin.Nucleic Acids Res2011 MaySandler Hdoi: 10.1093/nar/gkr011
21278925The roles of TTP and BRF proteins in regulated mRNA decay.Wiley Interdiscip Rev RNA2011 Jan-FebSanduja Sdoi: 10.1002/wrna.28.
21118139Molecular mechanisms of phosphorylation-regulated TTP (tristetraprolin) action and screening for further TTP-interacting proteins.Biochem Soc Trans2010 DecTiedje Cdoi: 10.1042/BST0381632.
21078877Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment.Mol Cell Biol2011 JanClement SLdoi: 10.1128/MCB.00717-10
23185455MCPIP1 down-regulates IL-2 expression through an ARE-independent pathway.PLoS One2012Li Mdoi: 10.1371/journal.pone.0049841
20639458A combination of hypoxia and lipopolysaccharide activates tristetraprolin to destabilize proinflammatory mRNAs such as tumor necrosis factor-alpha.Am J Pathol2010 SepWerno Cdoi: 10.2353/ajpath.2010.091212
20410487MicroRNA-466l upregulates IL-10 expression in TLR-triggered macrophages by antagonizing RNA-binding protein tristetraprolin-mediated IL-10 mRNA degradation.J Immunol2010 Jun 1Ma Fdoi: 10.4049/jimmunol.0902308
20418095Structure and function of nematode RNA-binding proteins.Curr Opin Struct Biol2010 JunKaymak Edoi: 10.1016/j.sbi.2010.03.010
20430641Diversity in post-transcriptional control of neutrophil chemoattractant cytokine gene expression.Cytokine2010 Oct-NovHamilton Tdoi: 10.1016/j.cyto.2010.04.003
20435889MicroRNAs distinguish translational from transcriptional silencing during endotoxin tolerance.J Biol Chem2010 Jul 2El Gazzar Mdoi: 10.1074/jbc.M110.115063
20438856Regulation of the expression of inducible nitric oxide synthase.Nitric Oxide2010 Sep 15Pautz Adoi: 10.1016/j.niox.2010.04.007
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25541715CREB targets define the gene expression signature of malignancies having reduced levels of the tumor suppressor tristetraprolin.PLoS One2014 Dec 26Fallahi Mdoi: 10.1371/journal.pone.0115517
25429052Tristetraprolin and its role in regulation of airway inflammation.Mol Pharmacol2015 AprPrabhala Pdoi: 10.1124/mol.114.095984
25301952RNase L attenuates mitogen-stimulated gene expression via transcriptional and post-transcriptional mechanisms to limit the proliferative response.J Biol Chem2014 Nov 28Brennan-Laun SEdoi: 10.1074/jbc.M114.589556
25261697Translational control of the oogenic program by components of OMA ribonucleoprotein particles in Caenorhabditis elegans.Genetics2014 DecSpike CAdoi: 10.1534/genetics.114.168823
25189382microRNA and human inducible nitric oxide synthase.Vitam Horm2014Guo Zdoi: 10.1016/B978-0-12-800254-4.00002-7.
25111853Tristetraprolin is involved in the glucocorticoid-mediated interleukin 8 repression.Int Immunopharmacol2014 OctShi JXdoi: 10.1016/j.intimp.2014.07.031
25038453CNOT7/hCAF1 is involved in ICAM-1 and IL-8 regulation by tristetraprolin.Cell Signal2014 NovShi JXdoi: 10.1016/j.cellsig.2014.07.020
24692066Posttranscriptional control of the chemokine receptor CXCR4 expression in cancer cells.Carcinogenesis2014 SepAl-Souhibani Ndoi: 10.1093/carcin/bgu080
24401661Global target mRNA specification and regulation by the RNA-binding protein ZFP36.Genome Biol2014 Jan 8Mukherjee Ndoi: 10.1186/gb-2014-15-1-r12.
24085785Characterization of squamous cell carcinoma in an organotypic culture via subsurface non-linear optical molecular imaging.Exp Biol Med (Maywood)2013 Nov 1Scanlon CSdoi: 10.1177/1535370213502628
24103357Tristetraprolin expression and microRNA-mediated regulation during simian immunodeficiency virus infection of the central nervous system.Mol Brain2013 Sep 2Liu Jdoi: 10.1186/1756-6606-6-40.
27458159Tristetraprolin functions in cytoskeletal organization during mouse oocyte maturation.Oncotarget2016 Aug 16Liu Xdoi: 10.18632/oncotarget.10755.
23880304Trichostatin-A modulates claudin-1 mRNA stability through the modulation of Hu antigen R and tristetraprolin in colon cancer cells.Carcinogenesis2013 NovSharma Adoi: 10.1093/carcin/bgt207
23644599Structural basis for the recruitment of the human CCR4-NOT deadenylase complex by tristetraprolin.Nat Struct Mol Biol2013 JunFabian MRdoi: 10.1038/nsmb.2572
27220464The RNA-binding protein TTP is a global post-transcriptional regulator of feedback control in inflammation.Nucleic Acids Res2016 Sep 6Tiedje Cdoi: 10.1093/nar/gkw474
25985190Basal protein phosphatase 2A activity restrains cytokine expression: role for MAPKs and tristetraprolin.Sci Rep2015 May 18Rahman MMdoi: 10.1038/srep10063.
27732963RNA binding protein, tristetraprolin in a murine model of recurrent pregnancy loss.Oncotarget2016 Nov 8Khalaj Kdoi: 10.18632/oncotarget.12539.
26546680Negative Feed-forward Control of Tumor Necrosis Factor (TNF) by Tristetraprolin (ZFP36) Is Limited by the Mitogen-activated Protein Kinase Phosphatase, Dual-specificity Phosphatase 1 (DUSP1): IMPLICATIONS FOR REGULATION BY GLUCOCORTICOIDS.J Biol Chem2016 Jan 1Shah Sdoi: 10.1074/jbc.M115.697599
281242573'UTR AU-Rich Elements (AREs) and the RNA-Binding Protein Tristetraprolin (TTP) Are Not Required for the LPS-Mediated Destabilization of Phospholipase-Cβ-2 mRNA in Murine Macrophages.Inflammation2017 AprShukla Sdoi: 10.1007/s10753-017-0511-y.
27825143Tristetraprolin disables prostate cancer maintenance by impairing proliferation and metabolic function.Oncotarget2016 Dec 13Berglund AEdoi: 10.18632/oncotarget.13128.
28302726The RNA-binding protein Tristetraprolin (TTP) is a critical negative regulator of the NLRP3 inflammasome.J Biol Chem2017 Apr 28Haneklaus Mdoi: 10.1074/jbc.M116.772947
27503556Tristetraprolin as a Therapeutic Target in Inflammatory Disease.Trends Pharmacol Sci2016 OctPatial Sdoi: 10.1016/j.tips.2016.07.002
27487322Structural Basis of the Disorder in the Tandem Zinc Finger Domain of the RNA-Binding Protein Tristetraprolin.J Chem Theory Comput2016 Oct 11Tavella D-
27197193Systematic Analysis of AU-Rich Element Expression in Cancer Reveals Common Functional Clusters Regulated by Key RNA-Binding Proteins.Cancer Res2016 Jul 15Hitti Edoi: 10.1158/0008-5472.CAN-15-3110
27193233Destabilization of the ornithine decarboxylase mRNA transcript by the RNA-binding protein tristetraprolin.Amino Acids2016 OctNowotarski SLdoi: 10.1007/s00726-016-2261-9
26497679Tristetraprolin induces cell cycle arrest in breast tumor cells through targeting AP-1/c-Jun and NF-kB pathway.Oncotarget2015 Dec 8Xu Ldoi: 10.18632/oncotarget.6149.
26517838The Expression of Tristetraprolin and Its Relationship with Urinary Proteins in Patients with Diabetic Nephropathy.PLoS One2015 Oct 30Liu Fdoi: 10.1371/journal.pone.0141471
26343742Histone Deacetylase Inhibitors Activate Tristetraprolin Expression through Induction of Early Growth Response Protein 1 (EGR1) in Colorectal Cancer Cells.Biomolecules2015 Aug 28Sobolewski Cdoi: 10.3390/biom5032035.
26183929Tristetraprolin Limits Inflammatory Cytokine Production in Tumor-Associated Macrophages in an mRNA Decay-Independent Manner.Cancer Res2015 Aug 1Kratochvill Fdoi: 10.1158/0008-5472.CAN-15-0205
26144867A post-transcriptional mechanism pacing expression of neural genes with precursor cell differentiation status.Nat Commun2015 Jul 6Dai Wdoi: 10.1038/ncomms8576.
25815583Post-transcriptional regulation of satellite cell quiescence by TTP-mediated mRNA decay.Elife2015 Mar 27Hausburg MAdoi: 10.7554/eLife.03390.
28504646The RNA-binding protein tristetraprolin schedules apoptosis of pathogen-engaged neutrophils during bacterial infection.J Clin Invest2017 Jun 1Ebner Fdoi: 10.1172/JCI80631
28570274Tristetraprolin expression by keratinocytes controls local and systemic inflammation.JCI Insight2017 Jun 2Andrianne Mdoi: 10.1172/jci.insight.92979
28724967A balancing act: RNA binding protein HuR/TTP axis in endometriosis patients.Sci Rep2017 Jul 19Khalaj Kdoi: 10.1038/s41598-017-06081-7.
29021521Tristetraprolin inhibits macrophage IL-27-induced activation of antitumour cytotoxic T cell responses.Nat Commun2017 Oct 11Wang Qdoi: 10.1038/s41467-017-00892-y.
29124478The role of RNA-binding protein tristetraprolin in cancer and immunity.Med Oncol2017 Nov 9Guo Jdoi: 10.1007/s12032-017-1055-6.
29203639A Knock-In Tristetraprolin (TTP) Zinc Finger Point Mutation in Mice: Comparison with Complete TTP Deficiency.Mol Cell Biol2018 Jan 29Lai WSdoi: 10.1128/MCB.00488-17
29514008Tristetraprolin Is Required for Alveolar Bone Homeostasis.J Dent Res2018 JulSteinkamp HMdoi: 10.1177/0022034518756889
29577897The RNA binding protein tristetraprolin down-regulates autophagy in lung adenocarcinoma cells.Exp Cell Res2018 Jun 1Dong Fdoi: 10.1016/j.yexcr.2018.03.028
29723192The ARE-binding protein Tristetraprolin (TTP) is a novel target and mediator of calcineurin tumor suppressing function in the skin.PLoS Genet2018 May 3Wu Xdoi: 10.1371/journal.pgen.1007366
29848443ZFP36 RNA-binding proteins restrain T cell activation and anti-viral immunity.Elife2018 May 31Moore MJdoi: 10.7554/eLife.33057.
29936792Tristetraprolin Overexpression in Gastric Cancer Cells Suppresses PD-L1 Expression and Inhibits Tumor Progression by Enhancing Antitumor Immunity.Mol Cells2018 Jul 31Guo Jdoi: 10.14348/molcells.2018.0040
29997282Hepatic tristetraprolin promotes insulin resistance through RNA destabilization of FGF21.JCI Insight2018 Jul 12Sawicki KTdoi: 10.1172/jci.insight.95948.
30171775IL-33 regulates cytokine production and neutrophil recruitment via the p38 MAPK-activated kinases MK2/3.Immunol Cell Biol2019 JanMcCarthy PCdoi: 10.1111/imcb.12200
30524947Critical role of tristetraprolin and AU-rich element RNA-binding protein 1 in the suppression of cancer cell growth by globular adiponectin.FEBS Open Bio2018 Nov 12Tilija Pun Ndoi: 10.1002/2211-5463.12541
30664390Bi-phased regulation of the post-transcriptional inflammatory response by Tristetraprolin levels.RNA Biol2019 MarMahmoud Ldoi: 10.1080/15476286.2019.1572437
30864256The tandem zinc finger RNA binding domain of members of the tristetraprolin protein family.Wiley Interdiscip Rev RNA2019 JulLai WSdoi: 10.1002/wrna.1531
30926667Hepatic posttranscriptional network comprised of CCR4-NOT deadenylase and FGF21 maintains systemic metabolic homeostasis.Proc Natl Acad Sci U S A2019 Apr 16Morita Mdoi: 10.1073/pnas.1816023116
30938272Recent advances in the role of RNA-binding protein, tristetraprolin, in arthritis.Immunol Med2018 SepYamasaki Sdoi: 10.1080/25785826.2018.1531187
31068309[Tristetraprolin inhibits autophagy in cultured lung cancer cells via the nuclear factor-kB pathway].Nan Fang Yi Ke Da Xue Xue Bao2019 Mar 30Deng Xdoi: 10.12122/j.issn.1673-4254.2019.03.09.
31149039Myeloid cell-derived LL-37 promotes lung cancer growth by activating Wnt/β-catenin signaling.Theranostics2019 Apr 12Ji Pdoi: 10.7150/thno.30726
16061475Influence of nonameric AU-rich tristetraprolin-binding sites on mRNA deadenylation and turnover.J Biol Chem2005 Oct 7Lai WS-
18262561Clonidine-induced enhancement of iNOS expression involves NF-kappaB.J Surg Res2008 SepSu NYdoi: 10.1016/j.jss.2007.11.725
30195796Elevated Tristetraprolin Impairs Trophoblast Invasion in Women with Recurrent Miscarriage by Destabilization of HOTAIR.Mol Ther Nucleic Acids2018 Sep 7Tian FJdoi: 10.1016/j.omtn.2018.07.001
17599736Effects of infliximab therapy on gene expression levels of tumor necrosis factor alpha, tristetraprolin, T cell intracellular antigen 1, and Hu antigen R in patients with rheumatoid arthritis.Arthritis Rheum2007 JulSugihara M-
16935542Tristetraprolin inhibits HIV-1 production by binding to genomic RNA.Microbes Infect2006 SepMaeda M-
15766526Involvement of microRNA in AU-rich element-mediated mRNA instability.Cell2005 Mar 11Jing Q-
17971298Modulation of immediate early gene expression by tristetraprolin in the differentiation of 3T3-L1 cells.Biochem Biophys Res Commun2008 Jan 4Lin NY-
17170118Tristetraprolin (TTP)-14-3-3 complex formation protects TTP from dephosphorylation by protein phosphatase 2a and stabilizes tumor necrosis factor-alpha mRNA.J Biol Chem2007 Feb 9Sun L-
20221403Phosphorylation of human tristetraprolin in response to its interaction with the Cbl interacting protein CIN85.PLoS One2010 Mar 8Kedar VPdoi: 10.1371/journal.pone.0009588.
25010646Identification of a major phosphopeptide in human tristetraprolin by phosphopeptide mapping and mass spectrometry.PLoS One2014 Jul 10Cao Hdoi: 10.1371/journal.pone.0100977
24253039Mutational and structural analysis of the tandem zinc finger domain of tristetraprolin.J Biol Chem2014 Jan 3Lai WSdoi: 10.1074/jbc.M113.466326
26555753Sodium butyrate down-regulates tristetraprolin-mediated cyclin B1 expression independent of the formation of processing bodies.Int J Biochem Cell Biol2015 DecZheng XTdoi: 10.1016/j.biocel.2015.11.002
Expression
Transcripts
Transcript IDNameLengthRefSeq ID Protein IDLengthRefSeq IDUniportKB ID
ENST00000594045ZFP36-201690-ENSP0000047232971 (aa)-M0R252
ENST00000597629ZFP36-2031786-ENSP00000469647332 (aa)-M0QY76
ENST00000594442ZFP36-2021699-ENSP00000471239343 (aa)-M0R0H3
ENST00000600033ZFP36-204444-ENSP00000470200148 (aa)-M0QZ04
Gene Model
Click here to download ENSG00000128016's gene model file
Pathways
Pathway IDPathway NameSource
hsa05166Human T-cell leukemia virus 1 infectionKEGG
hsa05167Kaposi sarcoma-associated herpesvirus infectionKEGG
Protein-Protein Interaction (PPI)

Clik here to download ENSG00000128016's network

* RBP PPI network refers to all genes directly bind to RBP
Orthologs
Ensembl IDGene SymbolCoverageIdentiy OrthologGene SymbolCoverageIdentiy Species
ENSG00000128016ZFP369887.768ENSAMEG00000008499ZFP3610088.991Ailuropoda_melanoleuca
ENSG00000128016ZFP3610093.994ENSANAG00000034306ZFP3610093.393Aotus_nancymaae
ENSG00000128016ZFP369885.321ENSBTAG00000008573ZFP3610086.239Bos_taurus
ENSG00000128016ZFP3610093.994ENSCJAG00000014156ZFP3610093.393Callithrix_jacchus
ENSG00000128016ZFP369883.180ENSCAFG00000005530ZFP3610084.404Canis_familiaris
ENSG00000128016ZFP369984.290ENSCAFG00020015861ZFP369985.498Canis_lupus_dingo
ENSG00000128016ZFP369885.321ENSCHIG00000023209ZFP3610085.933Capra_hircus
ENSG00000128016ZFP369884.098ENSCPOG00000038352ZFP3610082.569Cavia_porcellus
ENSG00000128016ZFP3610093.393ENSCCAG00000034094ZFP3610092.793Cebus_capucinus
ENSG00000128016ZFP3610097.892ENSCATG00000039148ZFP3610097.892Cercocebus_atys
ENSG00000128016ZFP369878.963ENSCLAG00000014820ZFP3610079.878Chinchilla_lanigera
ENSG00000128016ZFP3610097.892ENSCSAG00000003862ZFP3610097.892Chlorocebus_sabaeus
ENSG00000128016ZFP3610097.289ENSCANG00000010605ZFP3610097.289Colobus_angolensis_palliatus
ENSG00000128016ZFP369883.636ENSCGRG00001007290Zfp3610081.818Cricetulus_griseus_chok1gshd
ENSG00000128016ZFP369284.516ENSCGRG00000019003Zfp369883.548Cricetulus_griseus_crigri
ENSG00000128016ZFP369081.955ENSDNOG00000033326ZFP369282.418Dasypus_novemcinctus
ENSG00000128016ZFP369881.040ENSDORG00000013487Zfp3610079.141Dipodomys_ordii
ENSG00000128016ZFP369888.073ENSEASG00005012802ZFP3610089.297Equus_asinus_asinus
ENSG00000128016ZFP369687.500ENSECAG00000033926ZFP3610086.850Equus_caballus
ENSG00000128016ZFP3610087.087ENSFCAG00000045634ZFP3610088.288Felis_catus
ENSG00000128016ZFP369882.317ENSFDAG00000008740ZFP3610080.183Fukomys_damarensis
ENSG00000128016ZFP366852.846ENSGAGG00000021476ZFP367848.443Gopherus_agassizii
ENSG00000128016ZFP3610099.699ENSGGOG00000014399ZFP3610099.699Gorilla_gorilla
ENSG00000128016ZFP369884.146ENSHGLG00000007955ZFP3610082.012Heterocephalus_glaber_female
ENSG00000128016ZFP369878.963ENSHGLG00100017184ZFP3610076.829Heterocephalus_glaber_male
ENSG00000128016ZFP3610087.349ENSSTOG00000019840ZFP3610088.554Ictidomys_tridecemlineatus
ENSG00000128016ZFP369879.091ENSJJAG00000010452-10082.121Jaculus_jaculus
ENSG00000128016ZFP369876.667ENSJJAG00000011735-10078.485Jaculus_jaculus
ENSG00000128016ZFP3610098.193ENSMFAG00000000900ZFP3610098.193Macaca_fascicularis
ENSG00000128016ZFP3610097.892ENSMMUG00000038702ZFP3610097.892Macaca_mulatta
ENSG00000128016ZFP3610097.590ENSMNEG00000039734ZFP3610097.590Macaca_nemestrina
ENSG00000128016ZFP3610097.590ENSMLEG00000041066ZFP3610097.590Mandrillus_leucophaeus
ENSG00000128016ZFP369879.755ENSMAUG00000021250Zfp3610080.675Mesocricetus_auratus
ENSG00000128016ZFP3610082.985ENSMICG00000026814ZFP3610085.373Microcebus_murinus
ENSG00000128016ZFP369885.276ENSMOCG00000014548Zfp3610085.276Microtus_ochrogaster
ENSG00000128016ZFP369856.583ENSMODG00000013494ZFP369954.121Monodelphis_domestica
ENSG00000128016ZFP369884.098MGP_CAROLIEiJ_G0029444Zfp3610083.841Mus_caroli
ENSG00000128016ZFP369883.792ENSMUSG00000044786Zfp3610083.537Mus_musculus
ENSG00000128016ZFP369883.792MGP_PahariEiJ_G0012680Zfp3610083.537Mus_pahari
ENSG00000128016ZFP369884.098MGP_SPRETEiJ_G0030542Zfp3610083.841Mus_spretus
ENSG00000128016ZFP369883.891ENSMPUG00000017726ZFP3610086.018Mustela_putorius_furo
ENSG00000128016ZFP369881.957ENSMLUG00000002942ZFP3610083.792Myotis_lucifugus
ENSG00000128016ZFP3610082.883ENSNGAG00000019033Zfp3610082.583Nannospalax_galili
ENSG00000128016ZFP3610094.880ENSNLEG00000014418ZFP3610094.880Nomascus_leucogenys
ENSG00000128016ZFP368962.121ENSMEUG00000010317ZFP3610058.434Notamacropus_eugenii
ENSG00000128016ZFP369884.098ENSODEG00000016693ZFP3610083.792Octodon_degus
ENSG00000128016ZFP369685.266ENSOCUG00000003400ZFP369884.953Oryctolagus_cuniculus
ENSG00000128016ZFP369889.571ENSOGAG00000034231ZFP3610089.571Otolemur_garnettii
ENSG00000128016ZFP369883.180ENSOARG00000006068ZFP3610082.569Ovis_aries
ENSG00000128016ZFP3610099.699ENSPPAG00000032232ZFP3610099.699Pan_paniscus
ENSG00000128016ZFP3610086.787ENSPPRG00000013318ZFP3610087.988Panthera_pardus
ENSG00000128016ZFP3610086.787ENSPTIG00000010660ZFP3610087.988Panthera_tigris_altaica
ENSG00000128016ZFP3610099.699ENSPTRG00000010968ZFP3610099.699Pan_troglodytes
ENSG00000128016ZFP3610097.892ENSPANG00000007276ZFP3610097.892Papio_anubis
ENSG00000128016ZFP369884.663ENSPEMG00000007506Zfp3610084.663Peromyscus_maniculatus_bairdii
ENSG00000128016ZFP368357.742ENSPCIG00000010489ZFP369159.091Phascolarctos_cinereus
ENSG00000128016ZFP3690100.000ENSPPYG00000010577-10098.611Pongo_abelii
ENSG00000128016ZFP3610086.826ENSPCOG00000016898ZFP3610087.725Propithecus_coquereli
ENSG00000128016ZFP369885.015ENSPVAG00000011124ZFP3610085.933Pteropus_vampyrus
ENSG00000128016ZFP3610084.084ENSRNOG00000058388Zfp3610084.084Rattus_norvegicus
ENSG00000128016ZFP3610096.687ENSRBIG00000038385ZFP3610096.687Rhinopithecus_bieti
ENSG00000128016ZFP3610096.687ENSRROG00000042031ZFP3610096.687Rhinopithecus_roxellana
ENSG00000128016ZFP3610093.393ENSSBOG00000033740ZFP3610092.793Saimiri_boliviensis_boliviensis
ENSG00000128016ZFP367855.052ENSSHAG00000009151-8760.800Sarcophilus_harrisii
ENSG00000128016ZFP369844.772ENSSPUG00000011402ZFP365949.327Sphenodon_punctatus
ENSG00000128016ZFP369887.156ENSSSCG00000028056ZFP3610088.379Sus_scrofa
ENSG00000128016ZFP369290.164ENSTBEG00000005948ZFP3610089.342Tupaia_belangeri
ENSG00000128016ZFP369884.709ENSTTRG00000003564ZFP3610085.627Tursiops_truncatus
ENSG00000128016ZFP369887.462ENSUAMG00000009986ZFP3610088.685Ursus_americanus
ENSG00000128016ZFP369387.055ENSUMAG00000019533ZFP3610086.850Ursus_maritimus
ENSG00000128016ZFP369984.290ENSVVUG00000006271ZFP369985.498Vulpes_vulpes
ENSG00000128016ZFP366750.661ENSXETG00000002899zfp367947.810Xenopus_tropicalis
Gene Ontology
Go IDGo_termPubmedIDEvidenceCategory
GO:0000122negative regulation of transcription by RNA polymerase II21784977.IMPProcess
GO:0000165MAPK cascade15187101.IMPProcess
GO:0000165MAPK cascade-ISSProcess
GO:0000178exosome (RNase complex)11719186.IDAComponent
GO:0000288nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay23644599.IDAProcess
GO:0000289nuclear-transcribed mRNA poly(A) tail shortening23644599.IMPProcess
GO:0000932P-body17369404.21964062.IDAComponent
GO:0003677DNA binding-IEAFunction
GO:0003723RNA binding22658674.HDAFunction
GO:0003727single-stranded RNA binding9703499.TASFunction
GO:0003729mRNA binding11782475.15687258.IDAFunction
GO:0003730mRNA 3'-UTR binding21873635.IBAFunction
GO:0005515protein binding14679154.14766228.15687258.15766526.16126846.16364915.20221403.21784977.21964062.23644599.25106868.IPIFunction
GO:0005634nucleus10330172.12198173.14679154.IDAComponent
GO:0005737cytoplasm10330172.12198173.14679154.14766228.15634918.20221403.21784977.25038453.IDAComponent
GO:0005829cytosol21873635.IBAComponent
GO:0005829cytosol10751406.IDAComponent
GO:0005829cytosol-TASComponent
GO:0006402mRNA catabolic process10330172.10751406.11782475.20221403.IDAProcess
GO:0009611response to wounding27182009.IDAProcess
GO:0009611response to wounding-ISSProcess
GO:0010494cytoplasmic stress granule15014438.21964062.IDAComponent
GO:0010837regulation of keratinocyte proliferation27182009.IMPProcess
GO:0017091AU-rich element binding10330172.15014438.20221403.IDAFunction
GO:0017091AU-rich element binding21784977.IMPFunction
GO:0019899enzyme binding25038453.IPIFunction
GO:0019901protein kinase binding15014438.IPIFunction
GO:0019957C-C chemokine binding21784977.IPIFunction
GO:0030014CCR4-NOT complex-ISSComponent
GO:0031072heat shock protein binding20221403.IDAFunction
GO:0031086nuclear-transcribed mRNA catabolic process, deadenylation-independent decay11279239.IDAProcess
GO:0032680regulation of tumor necrosis factor production15014438.IDAProcess
GO:0032897negative regulation of viral transcription14679154.IMPProcess
GO:0035278miRNA mediated inhibition of translation-ISSProcess
GO:0035925mRNA 3'-UTR AU-rich region binding9703499.12748283.15187101.15634918.15766526.20702587.25038453.IDAFunction
GO:0038066p38MAPK cascade-ISSProcess
GO:0042594response to starvation15014438.IDAProcess
GO:0043488regulation of mRNA stability9703499.11719186.15687258.20702587.IDAProcess
GO:0043488regulation of mRNA stability15187101.15634918.IMPProcess
GO:0043488regulation of mRNA stability-TASProcess
GO:0044344cellular response to fibroblast growth factor stimulus20166898.IDAProcess
GO:0045085negative regulation of interleukin-2 biosynthetic process-ISSProcess
GO:0045600positive regulation of fat cell differentiation-ISSProcess
GO:0045616regulation of keratinocyte differentiation27182009.IMPProcess
GO:0045647negative regulation of erythrocyte differentiation20702587.IDAProcess
GO:0046872metal ion binding-IEAFunction
GO:0051028mRNA transport17369404.IMPProcess
GO:0060213positive regulation of nuclear-transcribed mRNA poly(A) tail shortening10330172.IDAProcess
GO:00611583'-UTR-mediated mRNA destabilization21873635.IBAProcess
GO:00611583'-UTR-mediated mRNA destabilization9703499.11719186.15687258.20221403.27193233.IDAProcess
GO:00611583'-UTR-mediated mRNA destabilization14679154.15187101.15634918.15766526.IMPProcess
GO:0070063RNA polymerase binding-ISSFunction
GO:0070578RISC-loading complex15766526.IDAComponent
GO:00709353'-UTR-mediated mRNA stabilization15014438.IDAProcess
GO:0071222cellular response to lipopolysaccharide14766228.IDAProcess
GO:0071222cellular response to lipopolysaccharide14679154.15187101.IMPProcess
GO:0071356cellular response to tumor necrosis factor20166898.IDAProcess
GO:0071364cellular response to epidermal growth factor stimulus20166898.IDAProcess
GO:0071385cellular response to glucocorticoid stimulus20166898.IDAProcess
GO:007188914-3-3 protein binding15014438.IDAFunction
GO:0097011cellular response to granulocyte macrophage colony-stimulating factor stimulus20166898.IDAProcess
GO:0098745Dcp1-Dcp2 complex16364915.IDAComponent
GO:1900153positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay12748283.IDAProcess
GO:1900153positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay-ISSProcess
GO:1901835positive regulation of deadenylation-independent decapping of nuclear-transcribed mRNA16364915.IDAProcess
GO:1902172regulation of keratinocyte apoptotic process27182009.IMPProcess
GO:1904246negative regulation of polynucleotide adenylyltransferase activity-ISSProcess
GO:1904582positive regulation of intracellular mRNA localization17369404.IMPProcess
GO:1990904ribonucleoprotein complex10330172.15687258.20702587.IDAComponent
GO:2000637positive regulation of gene silencing by miRNA15766526.IMPProcess
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