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TRIB1 (tribbles pseudokinase 1)

Written2015-03Jessica Johnston, Endre Kiss-Toth
Department of Cardiovascular Science, University of Sheffield, Sheffield, Beech Hill Road, Sheffield S10 2RX, United Kingdom

Abstract Review on TRIB1, with data on DNA, on the protein encoded, and where the gene is implicated.

Keywords TRIB1

(Note : for Links provided by Atlas : click)


Alias (NCBI)C8FW
HGNC Alias symbC8FW
HGNC Previous nametribbles homolog 1 (Drosophila)
LocusID (NCBI) 10221
Atlas_Id 43539
Location 8q24.13  [Link to chromosome band 8q24]
Location_base_pair Starts at 125430358 and ends at 125438402 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping TRIB1.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
TRIB1 (8q24.13)::NSMCE2 (8q24.13)TRIB1 (8q24.13)::SLC25A32 (8q22.3)
Note The tribbles family of genes encode a group of highly conserved pseudokinase proteins, which are thought to act as adaptors in several signalling pathways that are intimately involved in the regulation of a number of key cellular processes, including MAPK, and PI3K pathways. Tribbles have also been shown to interact with ubiquitin ligases, thereby promoting degradation of target proteins. Tribbles have been implicated in a number of diseases including leukaemia, metabolic syndromes and cardiovascular disease.
Tribbles proteins were first discovered in Drosophila as a negative regulator of string/cdc25, where when over-expressed directly inhibited mitosis (Grosshans and Wieschaus 2000). Simultaneously, TRIBs were found to promote the degradation of string via the proteasome pathway and showed that overexpression of tribbles in imaginal disc cells blocked the cell cycle at G2 resulting in abnormal wing morphology (Mata, et al 2000). Since then three highly conserved mammalian homologues have been indentified; Trib1, Trib2 and Trib3.


  There are two validated transcripts of TRIB1 (NM_025195 and NM_001282985) coding for isoforms 1 and 2 respectively. Isoform 2 has a shorter 5'UTR (untranslated region) and 5' coding region compared to isoform 1 and initiates translation further downstream. UTRs and exons are represented by the red and grey boxes respectively. Image drawn by FancyGene (Rambaldi and Ciccarelli 2009).
Transcription There are two protein coding transcripts of TRIB1; TRIB1-001 and TRIB1-002.
TRIB1-001 (Isoform 1); Transcript size: 3,635bp; Exon count: 3.
TRIB1-002 (Isoform 2); Transcript size: 1,332 bp; Exon count: 2


Note TRIB1-001: 372 amino acids; TRIB1-002: 206 amino acids
  Protein structure of Tribbles 1: TRIB1 has a N terminal, pseudokinase and C terminal domains. It contains four protein motifs; a putative PEST sequence, a kinase dead catalytic loop, a MEK1 binding and COP1 binding motif. The characteristic amino acid sequence for each motif is shown along with location.
Description TRIB1 contain a N terminal (NT) domain of 60-80 residues and a C-terminal domain of 35-40 residues and a characteristic single central Ser/Thr kinase-like (pseudokinase) domain. TRIB1 contains features consistent with its emerging role as a protein adaptor in signalling pathways.
N-Terminal Domain The NT fragment of TRIB1 is proline and serine rich, mostly in the sequence adjacent to the kinase-like domain. The abundance of these amino acids are a characteristic of PEST proteins that are involved in controlling the half life of proteins by altering their susceptibility to degradation. Other functions of these types of proteins include the anchoring of SH3 or WW domains of other proteins or acting as a substrate for proline dependent phosphorylation. TRIB1 contains possible phosphorylation sites for proline-dependent kinases (Hegedus, et al 2007).
TRIB1 also contains two evolutionary conserved motifs. The first consists of a putative nuclear localisation signal, [K/R]2X2[D/E]X[D/E]. The second motif contains a G-S-P consensus pattern found close to the kinase-like domain. The G-S-P motif is present in human SNIP1 (Smad nuclear interacting protein) which functionally associates with BGR1, which interacts with the Drosophila homologue of Slbo, C/EBP transcription factors (Beausoleil, et al 2004, Kadam, et al 2000). C/EBP transcription factors have been shown to functionally and physically interact with TRIB1 promoting their degradation (Yoshida, et al 2013).
Kinase-like domain TRIB1 contains a Ser/Thr kinase-like domain that is composed of some of the motifs present in catalytically active kinases such as a Lysine crucial for ATP binding whilst others are missing. Despite this evidence would suggest TRIB1 no to possess kinase activity. However this domain is highly conserved during evolution suggesting it is important for the role of TRIB1(Hegedus, et al 2007).
C-Terminal Domain The CT domain is around 35-45 amino acids long and is rich in charged amino acids important for protein interactions. Two important motifs have been identified in the CT domain; a hexapeptide motif [D/E]QXVP[D/E] as a COP1 (E3 ubiqutin ligase) binding site, essential for proteasome mediated degradation of C/EBPα family members and a MEK 1 binding site (ILLHPWF) (Hegedus, et al 2007).
Post translational modifications Several post translational modifications of TRIB1 have been reported and validated by mass spectrometry and listed in the PhosphoSitePlus database (Hornbeck, et al 2012).
Expression TRIB1 expression is ubiquitious with highest expression in the thyroid and myeloid cells (Figure?). TRIB1 is thought to expressed in a cell-type specific manner (Sung, et al 2006).
  The tissue specific expression of human TRIB1 mRNA is shown. Data and figure taken from BioGPS. Additional microarray expression data from the Human Gene Expression Atlas from the Genomics Institute of the Novartis Research Foundation (GNF) can be found on the UCSC browser ( (Su, et al 2004, Wu, et al 2009).
Localisation Numerous over-expression experiments have shown TRIB1 to be located in the nucleus. It contains a putative nuclear localisation signal (Yokoyama, et al 2010).
Function TRIB1 has been shown to interact with a number of proteins as detailed herein (Table1):
MEK-1 and MKK4 Co-immunoprecipitation experiments have shown specific interactions with MEK1 (an ERK activator MAPKK) and MKK4 (a JNK activator MAPKK). Interactions with Tribbles control the extent and specificity of MAPK activation and are dependent on levels of TRIB expression (Kiss-Toth, et al 2004, Sung, et al 2007).
MEK1 phosphorylates ERK which in turn promotes cell proliferation and suppression of apoptosis. The interaction between TRIB1 (via ILLHPWF motif) and MEK1
enhances ERK phosphorylation as mutants lacking the motif were unable to do so (Yokoyama, et al 2010) .
TRIB1 also interacts with MKK4, a JNK activator and implicated in the migration and proliferation of smooth muscle and involved in the pathogenesis of atherosclerosis. The nuclear localisation of TRIB1-MKK4 complex is dependent on the NT domain of TRIB1, however the central kinase-like domain of TRIB1 is sufficient for its interaction with MKK4 but the interaction is no longer preferentially nuclear (Sung, et al 2007).
COP1 AND C/EBPalpha TRIB1 contains a COP1 binding site at the carboxy terminus. COP1 is an E3 ubiquitin ligase that promotes the transfer of ubiquitin to target substrates for degradation via the proteasome. One of the prinicipal targets of COP1 are the family of transcription proteins CCAT/enhancer binding proteins (C/EBPs). It is thought TRIB1 acts to negatively regulate C/EBP proteins by acting as adaptors to recruit COP1 to C/EBP family members thereby promoting ubiquitination and degradation. Studies have shown that COP1 requires TRIB1 for its action of α (Yoshida, et al 2013).
Homology TRIB1 homologues have been indentified in different species including mouse, frog and zebrafish. Table 2 illustrates some of the TRIB1 homologues.
  Table 2: % protein and DNA identity of human TRIB1 vs other species. Data taken from Homologene and NCBI.


Note A somatic point mutation of TRIB1 has been reported in Down syndrome (DS)- related acute megakaryocytic leukaemia (AMKL) (Yokoyama, et al 2012). A G:T point mutation was found in the pseudokinase domain resulting in an amino acid change from arginine to leucine (R107L). When the mutation was expressed in mouse bone marrow cells and transferred into lethally irradiated recipient mice there was a more rapid development of AML and enhancement of ERK phosporylation suggesting a gain of function mutation. Yokoyama, et al (2012) suggests that the mutation of TRIB1 is an early event in leukaemogenesis.
A wide range of allelic variants of TRIB1 have been reported. There are several genetic and protein variations of TRIB1 listed on Ensembl.
Table (3) shows the types of genetic variation of TRIB1. Data taken from:;g=ENSG00000173334;r=8:126442563-126450647
Protein variants of TRIB1: Table 4 shows the protein variants of TRIB1. Each variant is listed in order according to residue number. The table also lists SIFT and Poly-Phen scores for the variations. SIFT predicts whether an amino acid substitution is likely to affect protein function based on the sequence homology and the physico-chemical similarity between the alternate amino acids. Each variant is accompanied with a score and predictive consequence that is based on the probability that the amino acid change is tolerable. A score closer to 0 is more likely to be deleterious. A score of <0.05 are deleterious and all others are tolerated'. PolyPhen predicts the effect of an amino acid substitution on the structure and function of a protein using sequence homology. A PolyPhen score represent the probability that a substitution is damaging, scores nearer to 1 are more confidently to be predicted to be deleterious (opposite to SIFT score). Each score is colour coded according to damage (SIFT; Red= deleterious, Green= tolerated. PolyPhen; Red= probably damaging, Orange= possibly damaging, Green= benign) (Adzhubei, et al 2010, Gonzalez-Perez and Lopez-Bigas 2011, Kumar, et al 2009). Data taken from:;g=ENSG00000173334;r=8:126442563-126450647;t=ENST00000311922
  Table 3: Genetic variations of TRIB1
Somatic [Table 4: Protein variants of TRIB1]

Implicated in

Entity Smooth muscle cells
Note TRIB1 is selectively over-expressed in chronically inflamed human atherosclerotic arteries and regulates vascular smooth muscle cell (VSMC) chemotaxis and proliferation, a characteristic feature of atherosclerosis via the JNK pathway (Sung, et al 2007).
Entity Macrophages
Note Trib1 is expressed in plaque resident macrophages in murine experimental atherosclerosis. The expression of Trib1 could be upregulated by IL-1, a major contributor to plaque development as the percentage of Trib1 expressing macrophages significantly decreases in ApoE -/- IL1R-/- double knockout mice compared to ApoE-/- controls. Overexpression of Trib1 in macrophages in vitro also leads to a significant attenuation (~70%) of IL-6 production and suppressed IL-12 expression induced with a pro-inflammatory stimulus (Sung, et al 2012).
It has also been shown that TRIB1 is involved in macrophage migration through interactions with C/EBP β and TNF- α. Knockdown of TRIB1 in RAW246.7 cells resulted in an increase in TNF- α production and C/EBPβ expression suggesting TRIB1 may modulate TNF- α through C/EBP β (Liu, et al 2013).
Trib1 has been shown to also be involved with adipose tissue maintenance and suppression of metabolic disorders by controlling the differentiation of tissue M2-like macrophages. Trib1 deficiency results in a significant reduction of M2-like macrophages. Mice lacking Trib1 in haematopoietic cells show a reduced adipocyte tissue mass and have evidence of increased lipolysis even on a normal diet. Supplementation of M2-like macrophages causes rescue suggesting the lack of these M2-like macrophages are responsible for lipolysis. When mice are fed a high fat diet, mice lacking Trib1 in haematopoietic cells develop hypertriglyceridaemia and insulin resistance and a pro-inflammatory cytokine induction (Satoh, et al 2013).
Entity Cancer
Note TRIB1 has been associated with the development of cancer and is considered as a leukaemia disease gene. It was identified as a collaborator of Hoxa9 and Meis1 in myeloid leukaemogenesis (Jin, et al 2007). Cooperative genes for Hoxa9/Meis1 were identified as common targets for retroviral integration, where TRIB1 was identified as the most frequent common site for integration in AML (Nakamura 2005). Table 5 shows the common integration sites and candidate cooperative genes in TRIB1-induced AML (Yokoyama and Nakamura 2011). TRIB1 alone is a transforming gene for myeloid cells and also significantly accelerates the development of Hoxa9/Meis1 AML.
Table 5: Common integration sites and candidate cooperative genes in TRIB1-induced AML.
Oncogenesis Phosphorylation of ERK is enhanced in TRIB1 transfected HeLa and Baf3 cells and leukaemia cells derived from TRIB1-induced AML upon cytokine stimulation (Jin, et al 2007).
MEK1 and enhancement of MEK/ERK phosporylation is required for reactivity. Mutant lacking MEK1 binding site is unable to enhance phosphorylation of ERK or extend self renewal in bone marrow cells or induce AML/accelerate Hoxa9/Meis1 induced AML (Yokoyama, et al 2010).
TRB1 has been implicated in human AML. TRIB1 is found on chromosome 8q24, 1.5Mb away from c-MYC, the target of AML amplification. TRIB1 is over-expressed even in some cases of AML when c-MYC amplification is not detected (Roethlisberger, et al 2007, Storlazzi, et al 2006)
Entity Cardiovascular Disease and Atherosclerosis
Note Emerging evidence from several genome-wide association studies (GWAS) has implicated TRIB1 in the risk of cardiovascular disease and events specifically due to the levels of circulating lipids (Kathiresan, et al 2008, Willer, et al 2008).
Two SNPs (rs2954029 and rs17321515) near the TRIB1 gene have been implicated with triglyceride, LDL and HDL levels. A minor G allele at rs17321515 was associated with lower triglyceride and LDL cholesterol and higher HDL cholesterol levels. A TT -> TA -> AA genotypes at rs2954029 were associated with step wise increases in the levels of triglyceride, remnant cholesterol and apo-lipoprotein B, the primary apolipoproteins present on LDLs. Likewise HDL cholesterol levels decreased step-wise through the genotypes. Additionally the genotypes were found to be significantly associated with increased risk of ischemic heart disease (IHD) and increased risk of MI
Further bivariate analysis showed TRIB1 expression to be significantly associated with triglyceride/ elevated blood pressure and triglyceride/HDL-cholesterol suggesting TRIB1 may be involved in a specific feature of lipid homeostasis (Kraja, et al 2011).
These genetic studies were further validated in in vivo models. Specific hepatic over-expression of Trib1 using an adenovirus vector reduced lipid plasma levels in a dose-dependent manner due to reduced VLDL production. Equally the opposite was seen in Trib1- knockout mice due to increased VLDL production. Interestingly when hepatic expression was reconstituted in knockout mice, VLDL-triglyceride production decreased to levels found in control mice (Burkhardt, et al 2010). The precise mechanisms of Trib1 involvement in lipid metabolism however are unknown.
Burkhardt, et al (2010) further investigated by examining the mRNA levels of genes associated with lipid metabolism in the livers of Trib1 over-expressing and Trib1- deficient mice. A significant decrease was found for genes involved in fatty acid oxidation such as Cpt1a (carnitine palmitoyltransferase 1A), Cpt2, and Acox1 (acyl-Coenzyme A oxidase 1) in Trib1 -/- mice. A significant up-regulation of key lipogeneic genes was also found such as Acc1 (acetyl-Coenzyme A carboxylase), fatty acid synthesis (Fasn) and stearoyl-Coenzyme A desaturase 1(Scd1). Significant downregulation of these genes were found in Trib1-over expressing mice. These genes have been noted to have effects on VLDL secretion and plasma triglyceride and cholesterol levels.
TRIB1 may also have a further role in lipogenesis. TRIB1 over-expression resulted in a significant decrease in 35S-methionine labelled apoB secretion in HepG2 cells (human liver carcinoma cell line). The authors speculate that TRIB1-mediated regulation of hepatic lipid availability might alter the secretion of apoB particles via a mechanism involving ER-associated degradation (ERAD) as previous data has shown a reduced availability or synthesis of lipid for apoB lipidation leads to co-translational targeting of apoB for ERAD (Ginsberg, et al 2009).
Entity Type 2 Diabetes
Note Trib1 has been hypothesised to have a regulatory role in inflammation in adipoctyes that may contribute towards obesity related type 2 diabetes. Trib1 is specifically up-regulated during acute and chronic inflammation in white adipose tissue in mice. Trib1 knockout mice show it to be a key regulator of inflammatory cytokines such as TNF-a and are protected from high fat diet induced obesity (Ostertag, et al 2010). It is proposed that Trib1 is pro-inflammatory in the adipose by acting as a co-activator for NF-kB inducing the expression of proinflammatory cytokines.


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This paper should be referenced as such :
Jessica Johnston, Endre Kiss-Toth
TRIB1 (tribbles pseudokinase 1)
Atlas Genet Cytogenet Oncol Haematol. 2016;20(3):106-114.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]

External links


HGNC (Hugo)TRIB1   16891
Entrez_Gene (NCBI)TRIB1    tribbles pseudokinase 1
AliasesC8FW; GIG-2; GIG2; SKIP1; 
GeneCards (Weizmann)TRIB1
Ensembl hg19 (Hinxton)ENSG00000173334 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000173334 [Gene_View]  ENSG00000173334 [Sequence]  chr8:125430358-125438402 [Contig_View]  TRIB1 [Vega]
ICGC DataPortalENSG00000173334
TCGA cBioPortalTRIB1
Genatlas (Paris)TRIB1
SOURCE (Princeton)TRIB1
Genetics Home Reference (NIH)TRIB1
Genomic and cartography
GoldenPath hg38 (UCSC)TRIB1  -     chr8:125430358-125438402 +  8q24.13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)TRIB1  -     8q24.13   [Description]    (hg19-Feb_2009)
GoldenPathTRIB1 - 8q24.13 [CytoView hg19]  TRIB1 - 8q24.13 [CytoView hg38]
Genome Data Viewer NCBITRIB1 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AF205437 AF250310 AJ000480 AK001319 AK022787
RefSeq transcript (Entrez)NM_001282985 NM_025195
Consensus coding sequences : CCDS (NCBI)TRIB1
Gene ExpressionTRIB1 [ NCBI-GEO ]   TRIB1 [ EBI - ARRAY_EXPRESS ]   TRIB1 [ SEEK ]   TRIB1 [ MEM ]
Gene Expression Viewer (FireBrowse)TRIB1 [ Firebrowse - Broad ]
GenevisibleExpression of TRIB1 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)10221
GTEX Portal (Tissue expression)TRIB1
Human Protein AtlasENSG00000173334-TRIB1 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ96RU8   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ96RU8  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ96RU8
Domaine pattern : Prosite (Expaxy)PROTEIN_KINASE_DOM (PS50011)   
Domains : Interpro (EBI)Kinase-like_dom_sf    Prot_kinase_dom    TRB1    Tribbles/Ser_Thr_kinase_40   
Domain families : Pfam (Sanger)Pkinase (PF00069)   
Domain families : Pfam (NCBI)pfam00069   
Domain families : Smart (EMBL)S_TKc (SM00220)  
Conserved Domain (NCBI)TRIB1
PDB (RSDB)5CEK    5CEM    5IGO    5IGQ    6DC0   
PDB Europe5CEK    5CEM    5IGO    5IGQ    6DC0   
PDB (PDBSum)5CEK    5CEM    5IGO    5IGQ    6DC0   
PDB (IMB)5CEK    5CEM    5IGO    5IGQ    6DC0   
Structural Biology KnowledgeBase5CEK    5CEM    5IGO    5IGQ    6DC0   
SCOP (Structural Classification of Proteins)5CEK    5CEM    5IGO    5IGQ    6DC0   
CATH (Classification of proteins structures)5CEK    5CEM    5IGO    5IGQ    6DC0   
AlphaFold pdb e-kbQ96RU8   
Human Protein Atlas [tissue]ENSG00000173334-TRIB1 [tissue]
Protein Interaction databases
IntAct (EBI)Q96RU8
Ontologies - Pathways
Ontology : AmiGOprotein kinase activity  protein kinase inhibitor activity  protein binding  ATP binding  nucleus  nucleus  cytoplasm  cytosol  protein phosphorylation  negative regulation of protein kinase activity  JNK cascade  transcription factor binding  negative regulation of smooth muscle cell migration  mitogen-activated protein kinase kinase binding  mitogen-activated protein kinase kinase binding  ubiquitin protein ligase binding  negative regulation of lipopolysaccharide-mediated signaling pathway  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  response to lipopolysaccharide  response to lipopolysaccharide  regulation of MAP kinase activity  regulation of MAP kinase activity  negative regulation of DNA-binding transcription factor activity  negative regulation of DNA-binding transcription factor activity  positive regulation of eosinophil differentiation  positive regulation of macrophage differentiation  negative regulation of neutrophil differentiation  negative regulation of smooth muscle cell proliferation  ubiquitin-protein transferase regulator activity  
Ontology : EGO-EBIprotein kinase activity  protein kinase inhibitor activity  protein binding  ATP binding  nucleus  nucleus  cytoplasm  cytosol  protein phosphorylation  negative regulation of protein kinase activity  JNK cascade  transcription factor binding  negative regulation of smooth muscle cell migration  mitogen-activated protein kinase kinase binding  mitogen-activated protein kinase kinase binding  ubiquitin protein ligase binding  negative regulation of lipopolysaccharide-mediated signaling pathway  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  positive regulation of proteasomal ubiquitin-dependent protein catabolic process  response to lipopolysaccharide  response to lipopolysaccharide  regulation of MAP kinase activity  regulation of MAP kinase activity  negative regulation of DNA-binding transcription factor activity  negative regulation of DNA-binding transcription factor activity  positive regulation of eosinophil differentiation  positive regulation of macrophage differentiation  negative regulation of neutrophil differentiation  negative regulation of smooth muscle cell proliferation  ubiquitin-protein transferase regulator activity  
NDEx NetworkTRIB1
Atlas of Cancer Signalling NetworkTRIB1
Wikipedia pathwaysTRIB1
Orthology - Evolution
GeneTree (enSembl)ENSG00000173334
Phylogenetic Trees/Animal Genes : TreeFamTRIB1
Homologs : HomoloGeneTRIB1
Homology/Alignments : Family Browser (UCSC)TRIB1
Gene fusions - Rearrangements
Fusion : MitelmanTRIB1::NSMCE2 [8q24.13/8q24.13]  
Fusion : MitelmanTRIB1::SLC25A32 [8q24.13/8q22.3]  
Fusion : QuiverTRIB1
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerTRIB1 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)TRIB1
Exome Variant ServerTRIB1
GNOMAD BrowserENSG00000173334
Varsome BrowserTRIB1
ACMGTRIB1 variants
Genomic Variants (DGV)TRIB1 [DGVbeta]
DECIPHERTRIB1 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisTRIB1 
ICGC Data PortalTRIB1 
TCGA Data PortalTRIB1 
Broad Tumor PortalTRIB1
OASIS PortalTRIB1 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICTRIB1  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DTRIB1
Mutations and Diseases : HGMDTRIB1
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)TRIB1
DoCM (Curated mutations)TRIB1
CIViC (Clinical Interpretations of Variants in Cancer)TRIB1
NCG (London)TRIB1
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry TRIB1
NextProtQ96RU8 [Medical]
Target ValidationTRIB1
Huge Navigator TRIB1 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDTRIB1
Pharm GKB GenePA134963922
Clinical trialTRIB1
DataMed IndexTRIB1
PubMed111 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:30:05 CEST 2021

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