Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

X Y 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 19 20 21 22 NA

HDAC3 (Histone deacetylase 3)

Written2007-08Fabrice Escaffit
Chromatin, Cell Proliferation group, LBCMCP-UMR 5088 CNRS, Université Paul Sabatier, Bät 4R3B1, 118, route de Narbonne, 31062 TOULOUSE Cedex 9, France

(Note : for Links provided by Atlas : click)

Identity

Other namesHDAC3
HD3
RPD3-2
RPD3
SMAP45
HGNC (Hugo) HDAC3
LocusID (NCBI) 8841
Atlas_Id 40804
Location 5q31.3  [Link to chromosome band 5q31]
Location_base_pair Starts at 141000443 and ends at 141016423 bp from pter ( according to hg19-Feb_2009)  [Mapping HDAC3.png]
Local_order 140,980,626 pb to 140,996,596 bp in minus strand orientation
Fusion genes
(updated 2016)
HDAC3 (5q31.3) / NSL1 (1q32.3)HDAC3 (5q31.3) / S100B (21q22.3)MALAT1 (11q13.1) / HDAC3 (5q31.3)

DNA/RNA

 
Description The HDAC3 gene consists of 15 exons and spans 15.97 kb of genomic sequence on chromosome 5 (from position 140,980,626 pb to 140,996,596 bp, in minus strand orientation).
Transcription The mRNA transcribed from this gene is 1,934 nucleotides long. There are actually two described isoforms resulting from an alternative splicing in the 5' region.
Pseudogene No pseudogene have been described.

Protein

Note HDAC3 interacts with other proteins, such as HDAC1, HDAC7, HDAC10, DACH1, YY1, DAXX, PML, RB1, RELA, JUN, SIN3A, BCOR, JMJD2A/JHDM3A, AKAP95, KLF6, DLK1, TR2, NRIP1 and SRY. Also described as a component of the N-CoR/SMRT repressor complexes by interacting with NCOR1/NCOR2.
 
Description The HDAC3 protein is 428 amino acids long (isoelectric point: 4.98) and belongs to the class I histone deacetylase subfamily.
In spite of the presence of a sequence ressembling the canonical NES at the position 29-41, CRM1 binding is observed in the region 180-313 and these residues act as a NES (or as a binding site for a NES-containing protein) that uses CRM1 export pathway. A NLS has been characterised in the C-terminal region (313-428). Another important sequence, required for oligomerisation of HDAC3 with itself and for the cell viability, is present in the N-terminal part (1-122) of the protein.
The HDAC3 protein can be phosphorylated on Ser424 by Caseine Kinase 2 and the same residue is dephosphorylated by protein serine/threonine phosphatase 4 (PP4). HDAC3 can also be symoylated in vitro.
Expression Like the other members of class I HDACs, HDAC3 is widely expressed in organisms, whereas HDACs of other classes are tissue-specific.
Two different isoforms of HDAC3 are expressed depending on an alternative splicing of the mRNA. The resulting proteins differ in their first 15 N-terminal amino acids (MAKTVAYFYDPDVGN -> MIVFKPYQASQHDMCR).
Localisation As opposed to other class I HDACs that have been found predominantly nuclear, HDAC3 is located in both nuclear and cytoplasmic compartments as well as at the plasma membrane.
Function In accordance to the limited homology of HDAC3 with the other HDACs (particularly in the C-terminal part of the protein) and its specific subcellular localisation, HDAC3 plays specific roles in the cell physiology and has substrates in the various cell compartments. Thus, unlike HDAC1/HDAC2, HDAC3 is required for cell growth and is involved in the apoptotic process of almost all cell types via the regulation of pro-apoptotic genes. Moreover, HDAC3 has been suggested to have a role in the cytoplasm, notably in signal transduction since it is a substrate of the membrane associated tyrosine kinase Src. So, in organisms, this protein plays a critical role in development, inflammation and metabolism.
As the other histone deacetylases, HDAC3 acts on the chromatin via the formation of large multiprotein complexes. But unlike HDAC1/2, that are implicated in the formation of Sin3, NuRD and CoREST complexes, HDAC3 is present in specific complexes containing members of the nuclear receptor co-repressor family N-CoR/SMRT (Silencing Mediator of Retinoid acid and Thyroid hormone receptor). HDAC3 is responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4) that correlates with epigenetic repression. This deacetylation is involved in transcriptional regulation of genes important for cell cycle progression and development. Thus, HDAC3 has been implicated to play roles in governing cell proliferation via the inhibition of p15(INK4b) and p21(WAF1/cip1).
Many transcription factors can directly interact with HDAC3 and thus, may target the histone deacetylase to specific promoters. Thus, HDAC3 is able to regulate osteoblast differentiation and bone formation via its association with the osteoblast master protein, Runx2, and the inhibition of the trans-activity of Runx2. Likewise, in hematopoietic stem cells, HDAC3, but not other class I HDACs, directly associates with GATA-2 and suppresses its key transcriptional potential.
The deacetylase activity of HDAC-3 can also target non-histone proteins: for example, HDAC3 is responsible in the inhibition of the myogenesis via its association with the acetyltransferases p300 and p300/CBP-associated factor (PCAF) to reverse autoacetylation and thus, to repress the p300/PCAF/MEF2-dependent transcription.
So, HDAC3 regulates many biological processes in a complex multi-levels manner.
The activity of HDAC3 is regulated by the phosphorylation of the Ser424 residue of the protein (see protein description above) and CK2 and PP4 are responsible for this regulation. Interaction with the other members within multiprotein complexes also regulates the deacetylase activity of HDAC3 (the nuclear receptor corepressor SMRT stimulated this activity towards MEF2 and PCAF). HDAC3 activity can also be indirectly regulated by post-translational modification of its associated proteins (for example, the phosphorylation of SMRT induces the disruption of the complex and the de-repression of the target promoter). The cleavage of the HDAC3 protein is another type of regulation affecting this enzyme: thus, during apoptosis, removal of the C-terminal part of HDAC3 results in accumulation of the cleaved protein in the cytoplasm and so, in its inactivation towards nuclear histones (but a possible role of the cleaved protein in the cytoplasm cannot be excluded).
Homology HDAC3 is very tightly conserved from plants to human. The histone deacetylase domain of HDAC3 (amino acids 3 to 316) is partly homologous to the other class I HDACs (HDAC1, HDAC2 and HDAC8) whereas C-terminal part of the protein is highly divergent. So, the HDAC3 protein is about 50% identical compared with other class I HDACs.

Mutations

Note No mutation is actually known for HDAC3 but Single Nucleotide Polymorphisms have been described in mRNA UTR (TGGGGG/TTCACC), introns (GATCTA/GTATTA; AAGGAA/CACAAT; GAAGGA/GCCCAT; AAACTA/GTAAAA) or in exons where it induces synonymous (TCATGT/CTGGGA (Q/Q)) or non-synonymous (ACCCAA/GTGAGT (N/S); CCAATC/GGATCA (R/P)) coding (non-exhaustive list).

Implicated in

Note
Entity Cancers
Note Phase I/II clinical trials are actually conducted in north America with isoselective inhibitors of class I HDACs for the treatment of the Hodgkin lymphoma (HDACs inhibitors alone), of the acute myeloid leukemia and myelodysplastic syndrome (in association with DNA methylation inhibitors) or of pancreatic cancers (in association with antimetabolites).
Disease Histone Deacetylase 3 and other class I HDACs, that regulate cell maturation and p21 expression, are deregulated in numerous cancers such as colon, ovary, lung, stomach, muscle, bone or skin cancers. The overexpression of HDAC3 is observed in almost tumoral pathologies. The downregulation of HDAC3 in colon cancer cells, in which the enzyme is normally overexpressed, results in cell growth inhibition, differentiation and increased apoptosis.
Prognosis HDAC3 in combination with other antigens may become a useful molecular biomarker with diagnostic or prognostic value for a subset of colon cancer patients.
There is no correlation between HDAC3 polymorphism and the risk of lung cancer .
Oncogenesis HDAC3 was shown to be recruited by the tumor antigen MAGE-A to block the activation of the tumor suppressor p53. In leukaemia, the generation of oncogenic fusion proteins (TEL-AML1, ETO-AML1, MTG16a-AML1, PLZF-RARalpha) causes aberrant recruitment of N-CoR/SMRT-HDAC3 repressor complexes on promoters. Moreover, nuclear HDAC3 plays an anti-apoptotic role that is important for cancer cell growth.
  
Entity Neurodegenerative and neuromuscular diseases
Note Clinical trials are conducted with class I HDACs isoselective inhibitors for the treatment of Spinal Muscular Atrophy.
HDAC inhibitors are also tested to enhance neuronal survival in both in vitro and in vivo models of neurodegenerative diseases such as polyglutamine-related diseases and amyotrophic lateral sclerosis.
  

Bibliography

Epigenetics of lung cancer.
Bowman RV, Yang IA, Semmler AB, Fong KM
Respirology (Carlton, Vic.). 2006 ; 11 (4) : 355-365.
PMID 16771905
 
Characterization of a human RPD3 ortholog, HDAC3.
Emiliani S, Fischle W, Van Lint C, Al-Abed Y, Verdin E
Proceedings of the National Academy of Sciences of the United States of America. 1998 ; 95 (6) : 2795-2800.
PMID 9501169
 
Cleavage and cytoplasmic relocalization of histone deacetylase 3 are important for apoptosis progression.
Escaffit F, Vaute O, Chevillard-Briet M, Segui B, Takami Y, Nakayama T, Trouche D
Molecular and cellular biology. 2007 ; 27 (2) : 554-567.
PMID 17101790
 
Histone deacetylase 3 interacts with and deacetylates myocyte enhancer factor 2.
Grégoire S, Xiao L, Nie J, Zhang X, Xu M, Li J, Wong J, Seto E, Yang XJ
Molecular and cellular biology. 2007 ; 27 (4) : 1280-1295.
PMID 17158926
 
The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3.
Guenther MG, Barak O, Lazar MA
Molecular and cellular biology. 2001 ; 21 (18) : 6091-6101.
PMID 11509652
 
Histone deacetylase 3 represses p15(INK4b) and p21(WAF1/cip1) transcription by interacting with Sp1.
Huang W, Tan D, Wang X, Han S, Tan J, Zhao Y, Lu J, Huang B
Biochemical and biophysical research communications. 2006 ; 339 (1) : 165-171.
PMID 16298343
 
HDAC3: taking the SMRT-N-CoRrect road to repression.
Karagianni P, Wong J
Oncogene. 2007 ; 26 (37) : 5439-5449.
PMID 17694085
 
Histone deacetylase 3 localizes to the plasma membrane and is a substrate of Src.
Longworth MS, Laimins LA
Oncogene. 2006 ; 25 (32) : 4495-4500.
PMID 16532030
 
Histone deacetylase 3 associates with and represses the transcription factor GATA-2.
Ozawa Y, Towatari M, Tsuzuki S, Hayakawa F, Maeda T, Miyata Y, Tanimoto M, Saito H
Blood. 2001 ; 98 (7) : 2116-2123.
PMID 11567998
 
Histone deacetylase 3 interacts with runx2 to repress the osteocalcin promoter and regulate osteoblast differentiation.
Schroeder TM, Kahler RA, Li X, Westendorf JJ
The Journal of biological chemistry. 2004 ; 279 (40) : 41998-42007.
PMID 15292260
 
Antibody response to a non-conserved C-terminal part of human histone deacetylase 3 in colon cancer patients.
Shebzukhov YV, Koroleva EP, Khlgatian SV, Belousov PV, Kuz'mina KE, Radko BV, Longpre F, Lagarkova MA, Kadachigova TS, Gurova OV, Meshcheryakov AA, Lichinitser MR, Knuth A, Jager E, Kuprash DV, Nedospasov SA
International journal of cancer. Journal international du cancer. 2005 ; 117 (5) : 800-806.
PMID 15981215
 
Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer.
Wilson AJ, Byun DS, Popova N, Murray LB, L'Italien K, Sowa Y, Arango D, Velcich A, Augenlicht LH, Mariadason JM
The Journal of biological chemistry. 2006 ; 281 (19) : 13548-13558.
PMID 16533812
 
Functional domains of histone deacetylase-3.
Yang WM, Tsai SC, Wen YD, Fejer G, Seto E
The Journal of biological chemistry. 2002 ; 277 (11) : 9447-9454.
PMID 11779848
 
Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4.
Zhang X, Ozawa Y, Lee H, Wen YD, Tan TH, Wadzinski BE, Seto E
Genes & development. 2005 ; 19 (7) : 827-839.
PMID 15805470
 

Citation

This paper should be referenced as such :
Escaffit, F
HDAC3 (histone deacetylase 3)
Atlas Genet Cytogenet Oncol Haematol. 2008;12(2):104-107.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/HDAC3ID40804ch5q31.html


Other Leukemias implicated (Data extracted from papers in the Atlas) [ 3 ]
  t(9;13)(p12;q21) PAX5/DACH1
t(9;17)(p13;p12) PAX5/NCOR1
t(X;9)(q21;p13) PAX5/DACH2

External links

Nomenclature
HGNC (Hugo)HDAC3   4854
Cards
AtlasHDAC3ID40804ch5q31
Entrez_Gene (NCBI)HDAC3  8841  histone deacetylase 3
AliasesHD3; RPD3; RPD3-2
GeneCards (Weizmann)HDAC3
Ensembl hg19 (Hinxton)ENSG00000171720 [Gene_View]  chr5:141000443-141016423 [Contig_View]  HDAC3 [Vega]
Ensembl hg38 (Hinxton)ENSG00000171720 [Gene_View]  chr5:141000443-141016423 [Contig_View]  HDAC3 [Vega]
ICGC DataPortalENSG00000171720
TCGA cBioPortalHDAC3
AceView (NCBI)HDAC3
Genatlas (Paris)HDAC3
WikiGenes8841
SOURCE (Princeton)HDAC3
Genomic and cartography
GoldenPath hg19 (UCSC)HDAC3  -     chr5:141000443-141016423 -  5q31.1-q31.2   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)HDAC3  -     5q31.1-q31.2   [Description]    (hg38-Dec_2013)
EnsemblHDAC3 - 5q31.1-q31.2 [CytoView hg19]  HDAC3 - 5q31.1-q31.2 [CytoView hg38]
Mapping of homologs : NCBIHDAC3 [Mapview hg19]  HDAC3 [Mapview hg38]
OMIM605166   
Gene and transcription
Genbank (Entrez)AF005482 AF039703 AY429537 AY429538 BC000614
RefSeq transcript (Entrez)NM_003883
RefSeq genomic (Entrez)NC_000005 NC_018916 NG_029678 NT_029289 NW_004929324
Consensus coding sequences : CCDS (NCBI)HDAC3
Cluster EST : UnigeneHs.519632 [ NCBI ]
CGAP (NCI)Hs.519632
Alternative Splicing GalleryENSG00000171720
Gene ExpressionHDAC3 [ NCBI-GEO ]   HDAC3 [ EBI - ARRAY_EXPRESS ]   HDAC3 [ SEEK ]   HDAC3 [ MEM ]
Gene Expression Viewer (FireBrowse)HDAC3 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)8841
GTEX Portal (Tissue expression)HDAC3
Protein : pattern, domain, 3D structure
UniProt/SwissProtO15379 (Uniprot)
NextProtO15379  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProO15379
Splice isoforms : SwissVarO15379 (Swissvar)
Catalytic activity : Enzyme3.5.1.98 [ Enzyme-Expasy ]   3.5.1.983.5.1.98 [ IntEnz-EBI ]   3.5.1.98 [ BRENDA ]   3.5.1.98 [ KEGG ]   
PhosPhoSitePlusO15379
Domains : Interpro (EBI)His_deacetylse    His_deacetylse_1    His_deacetylse_dom   
Domain families : Pfam (Sanger)Hist_deacetyl (PF00850)   
Domain families : Pfam (NCBI)pfam00850   
DMDM Disease mutations8841
Blocks (Seattle)HDAC3
PDB (SRS)4A69   
PDB (PDBSum)4A69   
PDB (IMB)4A69   
PDB (RSDB)4A69   
Structural Biology KnowledgeBase4A69   
SCOP (Structural Classification of Proteins)4A69   
CATH (Classification of proteins structures)4A69   
SuperfamilyO15379
Human Protein AtlasENSG00000171720
Peptide AtlasO15379
HPRD08950
IPIIPI00006187   IPI00217965   IPI00930193   IPI00976829   IPI00978185   
Protein Interaction databases
DIP (DOE-UCLA)O15379
IntAct (EBI)O15379
FunCoupENSG00000171720
BioGRIDHDAC3
STRING (EMBL)HDAC3
ZODIACHDAC3
Ontologies - Pathways
QuickGOO15379
Ontology : AmiGOhistone deacetylase complex  negative regulation of transcription from RNA polymerase II promoter  negative regulation of transcription from RNA polymerase II promoter  positive regulation of protein phosphorylation  chromatin binding  transcription corepressor activity  transcription corepressor activity  transcription corepressor activity  histone deacetylase activity  histone deacetylase activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytoplasm  Golgi apparatus  cytosol  spindle microtubule  plasma membrane  transcription, DNA-templated  protein deacetylation  circadian rhythm  transcription factor binding  transcription factor binding  negative regulation of myotube differentiation  chromatin modification  transcriptional repressor complex  enzyme binding  cyclin binding  regulation of protein stability  positive regulation of TOR signaling  NAD-dependent histone deacetylase activity (H3-K14 specific)  protein deacetylase activity  histone deacetylase binding  positive regulation of transcription factor import into nucleus  negative regulation of apoptotic process  cellular lipid metabolic process  negative regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  negative regulation of JNK cascade  NF-kappaB binding  spindle assembly  histone H3 deacetylation  cellular response to fluid shear stress  negative regulation of nucleic acid-templated transcription  
Ontology : EGO-EBIhistone deacetylase complex  negative regulation of transcription from RNA polymerase II promoter  negative regulation of transcription from RNA polymerase II promoter  positive regulation of protein phosphorylation  chromatin binding  transcription corepressor activity  transcription corepressor activity  transcription corepressor activity  histone deacetylase activity  histone deacetylase activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytoplasm  cytoplasm  Golgi apparatus  cytosol  spindle microtubule  plasma membrane  transcription, DNA-templated  protein deacetylation  circadian rhythm  transcription factor binding  transcription factor binding  negative regulation of myotube differentiation  chromatin modification  transcriptional repressor complex  enzyme binding  cyclin binding  regulation of protein stability  positive regulation of TOR signaling  NAD-dependent histone deacetylase activity (H3-K14 specific)  protein deacetylase activity  histone deacetylase binding  positive regulation of transcription factor import into nucleus  negative regulation of apoptotic process  cellular lipid metabolic process  negative regulation of transcription, DNA-templated  positive regulation of transcription from RNA polymerase II promoter  negative regulation of JNK cascade  NF-kappaB binding  spindle assembly  histone H3 deacetylation  cellular response to fluid shear stress  negative regulation of nucleic acid-templated transcription  
Pathways : BIOCARTACARM1 and Regulation of the Estrogen Receptor [Genes]   
Pathways : KEGGThyroid hormone signaling pathway    Alcoholism    Viral carcinogenesis   
REACTOMEO15379 [protein]
REACTOME PathwaysR-HSA-1368108 BMAL1:CLOCK,NPAS2 activates circadian gene expression [pathway]
REACTOME PathwaysR-HSA-1989781 PPARA activates gene expression [pathway]
REACTOME PathwaysR-HSA-193670 p75NTR negatively regulates cell cycle via SC1 [pathway]
REACTOME PathwaysR-HSA-3214815 HDACs deacetylate histones [pathway]
REACTOME PathwaysR-HSA-400253 Circadian Clock [pathway]
REACTOME PathwaysR-HSA-1368071 NR1D1 (REV-ERBA) represses gene expression [pathway]
REACTOME PathwaysR-HSA-2122947 NOTCH1 Intracellular Domain Regulates Transcription [pathway]
REACTOME PathwaysR-HSA-1368082 RORA activates gene expression [pathway]
REACTOME PathwaysR-HSA-381340 Transcriptional regulation of white adipocyte differentiation [pathway]
REACTOME PathwaysR-HSA-400206 Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha) [pathway]
REACTOME PathwaysR-HSA-2151201 Transcriptional activation of mitochondrial biogenesis [pathway]
REACTOME PathwaysR-HSA-2894862 Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants [pathway]
REACTOME PathwaysR-HSA-2644606 Constitutive Signaling by NOTCH1 PEST Domain Mutants [pathway]
NDEx Network
Atlas of Cancer Signalling NetworkHDAC3
Wikipedia pathwaysHDAC3
Orthology - Evolution
OrthoDB8841
GeneTree (enSembl)ENSG00000171720
Phylogenetic Trees/Animal Genes : TreeFamHDAC3
Homologs : HomoloGeneHDAC3
Homology/Alignments : Family Browser (UCSC)HDAC3
Gene fusions - Rearrangements
Polymorphisms : SNP, variants
NCBI Variation ViewerHDAC3 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)HDAC3
dbVarHDAC3
ClinVarHDAC3
1000_GenomesHDAC3 
Exome Variant ServerHDAC3
ExAC (Exome Aggregation Consortium)HDAC3 (select the gene name)
Genetic variants : HAPMAP8841
Genomic Variants (DGV)HDAC3 [DGVbeta]
Mutations
ICGC Data PortalHDAC3 
TCGA Data PortalHDAC3 
Broad Tumor PortalHDAC3
OASIS PortalHDAC3 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICHDAC3 
intOGen PortalHDAC3
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD - Leiden Open Variation Database
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch HDAC3
DgiDB (Drug Gene Interaction Database)HDAC3
DoCM (Curated mutations)HDAC3 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)HDAC3 (select a term)
intoGenHDAC3
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] 
Diseases
DECIPHER (Syndromes)5:141000443-141016423  ENSG00000171720
CONAN: Copy Number AnalysisHDAC3 
Mutations and Diseases : HGMDHDAC3
OMIM605166   
MedgenHDAC3
Genetic Testing Registry HDAC3
NextProtO15379 [Medical]
TSGene8841
GENETestsHDAC3
Huge Navigator HDAC3 [HugePedia]
snp3D : Map Gene to Disease8841
BioCentury BCIQHDAC3
ClinGenHDAC3
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD8841
Chemical/Pharm GKB GenePA29228
Clinical trialHDAC3
Miscellaneous
canSAR (ICR)HDAC3 (select the gene name)
Probes
Litterature
PubMed338 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineHDAC3
EVEXHDAC3
GoPubMedHDAC3
iHOPHDAC3
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

Search in all EBI   NCBI

© Atlas of Genetics and Cytogenetics in Oncology and Haematology
indexed on : Wed Aug 10 18:47:40 CEST 2016

Home   Genes   Leukemias   Solid Tumours   Cancer-Prone   Deep Insight   Case Reports   Journals  Portal   Teaching   

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.