Atlas of Genetics and Cytogenetics in Oncology and Haematology


Home   Genes   Leukemias   Solid Tumors   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

RPS6KA6 (Ribosomal Protein S6 Kinase, 90kDa, Polypeptide 6)

Written2013-10Tuoen Liu, Shousong Cao
Department of Internal Medicine, Division of Oncology, Washington University School of Medicine, St Louis, Missouri, United States (TL); Department of Medicine, Roswell Park Cancer Institute, Elm, Carlton Streets, Buffalo, New York 14263, United States (SC)

(Note : for Links provided by Atlas : click)

Identity

Alias_namesribosomal protein S6 kinase
Alias_symbol (synonym)RSK4
Other aliasPP90RSK4
HGNC (Hugo) RPS6KA6
LocusID (NCBI) 27330
Atlas_Id 43481
Location Xq21.1  [Link to chromosome band Xq21]
Location_base_pair Starts at 84058346 and ends at 84187935 bp from pter ( according to hg19-Feb_2009)  [Mapping RPS6KA6.png]
Fusion genes
(updated 2016)
RPS6KA6 (Xq21.1) / HDX (Xq21.1)

DNA/RNA

Description The human RPS6KA6 gene is located at Xq21, and contains 22 exons that span approximately 75 kb of genomic DNA and are located on cosmids E1, H22 and G9 in a telomeric to centromeric orientation (Yntema et al, 1999; Dümmler et al., 2005; Kantojärvi et al., 2011).

Protein

Note Human RPS6KA6 gene codes for the protein RSK4, a serine- threonine kinase with 745 amino acids, also a member of the 90 kDa ribosomal S6 kinase (RSK) family which includes other three members RSK1, RSK2 and RSK3 (Yntema et al., 1999; Dümmler et al., 2005; Anjum and Blenis, 2008; Serra et al., 2013).
 
  The basic structure of the RSK4. The RSK4 protein includes two kinases domains: amino-terminal kinase domain (NTKD) and carboxyl-terminal kinase domain (CTKD), a linker region and amino- and carboxyl-terminal tails. The NTKD is responsible for substrate phosphorylation and CTKD regulates sutophosphorylation of the RSK4. The two kinase domains are connected by a linker region which is about 100 amino acids containing essential regulatory domains including hydrophobic and turn motifs, involved in the activation of NTKD. An ERK-docking motif, known also as the D domain, is located in the carboxyl-terminal tail (Dümmler et al., 2005; Anjum and Blenis, 2008; Romeo et al., 2012).
Description RSK4 is a serine- threonine kinase and there are six phosphorylation sites in RSK4: Ser232, Thr368, Ser372, Ser389, Thr581, and Ser742. Upon activation of the cell surface receptors, ERK first bound to the ERK-docking motif in the carboxyl-terminal and phosphorylates Ser372 in the linker region and Thr581 in the CTKD. Phosphorylation of Thr581 activates CTK which autophosphorylates RSK4 at Ser389 in the linker region. Phosphorylation of Ser389 recruites and activiates PDK1 which phosphorylates Ser232 in NTKD. After dissociation of PDK1 from RSK, the Ser386 phosphorylated motif interacts with NTKD and activates the NTK in synergy with phosphor-Ser232. The phosphorylation of Ser372 increases the activity of NTK. Thr368 is phosphorylated by ERK and Ser742 can be phosphorylated by activated NTK, which leads to the association of RSK and ERK, serving as an inhibitory feedback mechanism to "shut off" the process (Dümmler et al., 2005). The CTKD activity of RSK1, RSK2 and RSK4 can be regulated by the irreversible inhibitor, pyrrolopyrimidine FMK (Z-VAD-FMK, benzyloxycarbonyl-Val-Ala-DL-Asp-fluoromethylketone) (Romeo et al., 2012).
 
  The activation of the RSK4 family protein. All RSK family membranes including RSK4 are involved in MAPK pathways and can be activated by various molecules including growth factors, neurotransmitters, hormones, phorbol esters. First, activation of cell surface receptors creates docking site for adaptor molecules like growth factor receptor-bound protein-2 (GRB2). GRB2 links the receptor to the guanine nucleotide-exchange factor son of sevenless (SOS). SOS catalyses GDP release and GTP binding to the small G-protein Ras. The GTP-bound Ras then binds to the Raf protein kinases. Upon the activation of Raf, it activates MAPK kinase (MEK), then downstream extracellular signal-regulated kinase (ERK). All four RSK family members are directly phosphorylated and activated by ERK1/2. RSKs are also phosphorylated by 3'-phosphoinositide-dependent kinase-1 (PDK1) which is a serine-threonine kinase. Activated RSKs can then phosphorylate their substrates via serine and threonine sites (Anjum and Blenis, 2008).
Expression RSK4 expression is low in both mouse and human embryonic and adult tissues compared with other three RSK family members. RSK4 mRNA was detected in the brain, cerebellum, heart, kidney and skeletal muscle, but not in other tissues such as lung, liver, pancreas and adipose. Specifically, RSK4 was found to be ubiquitously expressed at a low level through mouse development, and it is more highly expressed in specific phases of embryogenesis such as egg cylinder, gastrula and organ genesis (Kohn et al., 2003; Lleonart et al., 2006; Romeo et al., 2012).
Localisation RSK is predominantly located in cytosol, and contrary to other RSKs, its expression is relatively low and does not significantly accumulate in the nucleus after mitogenic stimulation (Dümmler et al., 2005; Romeo et al., 2012).
Function Recent studies showed RSK4 can be either oncogenic or tumor suppressive depending on many factors, and Cyclin D1 inhibited RSK4 expression and serum starvation enhanced the inhibition. RSK4 can induce cellular senescence which is mediated by p21. Also, inhibition of RSK4 causes bypass of cellular senescence induced by stress or oncogene, suggesting RSK4 inhibition may be an important factor in facilitating cell transformation. (López-Vicente et al., 2011). shRNA against RPS6KA6 bypassed p53-dependent G1 cell cycle arrest and suppressed mRNA expression of cyclin-dependent kinase inhibitor p21cip1, suggesting RSK4 is needed for growth arrest induced by p53 (Berns et al., 2004). In addition, RSK4 is identified to be an inhibitor of fibroblast growth factor (FGF)-Ras-ERK signal transduction. RSK4 plays an inhibitory role during embryogenesis by suppressing receptor tyrosine kinase signaling (López-Vicente et al., 2009).
Homology The RSK family members share 73-80% amino acids similarity to each other and are mostly different in their amino- and carboxyl-terminal sequences (Romeo et al., 2012). Difference from other RSK members whose activation needs the stimulation by growth factors, RSK4 can be constitutively activated under serum-starved condition without growth factor. The constitutive activation is due to constitutive phosphorylation of Ser232, Ser372 and Ser389 (Dümmler et al., 2005). PDK1 is required for mitogenic stimulation of RSK1-3, however, RSK4 does not appear to require PDK1 to maintain its high basal activity (Romeo et al., 2012). Unlike other three family members, RSK4 expression can disrupt mouse mesoderm formation induced by the FGF-Ras-ERK signaling pathway (Myers et al., 2004).

Implicated in

Note
  
Entity Breast cancer
Note RSK4 is highly expressed and has anti-invasive and anti-metastatic activities in breast cancer. Exogenous expression of RSK4 resulted in decreased breast cancer cell proliferation and increased accumulation of cells in G0-G1 phase of the cell cycle, also with enhanced expression several tumor suppressor genes: retinoblastoma protein, retinoblastoma-associated 46 kDa protein (RbAp46), and p21 protein (Thakur et al., 2007; Thakur et al., 2008). In addition, RSK4 expression enhances breast cancer cell survival upon PI3K/mTOR inhibitors treatment through inhibition of apoptosis and up-regulation of protein translation. Adding MEK- or RSK-specific inhibitors can overcome the RSK4 mediated resistance, thus, combination of RSK and PI3K pathway inhibitors may overcome the resistance mediated by RSK4 in breast cancer (Serra et al., 2013).
  
  
Entity Colon, kidney cancer and melanoma
Note RSK4 is down-regulated in colon carcinomas, renal cell carcinomas and colon adenomas. Overexpression of RSK4 induced cell arrest and senescence features in normal fibroblasts and malignant colon carcinoma cell lines. In addition, RSK4 is up-regulated in both replicative and stress-induced senescence and RSK4 inhibition induces senescence resistance in colon carcinoma cells, suggesting RSK4 may be a tumor suppressor gene by regulating senescence induction and inviting cell proliferation in colon carcinogenesis and renal cell carcinomas (Myers et al., 2004). RSK4 expression causes Sunitinib resistance in kidney carcinoma and melanoma cells, thus, RSK4 may be a potential resistance marker in Sunitinib therapy and a potential target for new drug development to overcome Sunitinib resistance (Llenaont et al., 2006; Bender and Ullrich, 2012).
  
  
Entity Endometrial cancer
Note RSK4 is frequently hypermethylated in endometrial cancer and RSK4 methylation is significantly associated with tumor grade, with higher grade tumors having lower levels of methylation. Thus, RSK4 appears to be epigenetically silenced in endometrial cancer as evidenced by hypermethylation (Dewdney et al., 2011).
  
  
Entity X-linked mental retardation
Note RPS6KA6 gene is commonly deleted in complex X-linked mental retardation patients (Yntema et al., 1999).
  
  
Entity Autism spectrum disorder
Note RPS6KA6 plays a role in brain development and could be associated with mental retardation. RSP6KA6 is located in the chromosomal region, which is commonly deleted in males with mental retardation. Its mutation may be associated with autism spectrum disorders (Kantojärvi et al., 2011).
  
  
Entity AIDS
Note SNP rs5968255, located at human Xq21.1 in a conserved sequence element near the RPS6KA6 and CYLC1 genes, was identified as a significant genetic determinant of AIDS progression in HIV infected women. However, whether RPS6KA6 gene is functionally involved in the observed phenotype is not clear (Siddiqui et al., 2009).
  

Bibliography

The RSK family of kinases: emerging roles in cellular signalling.
Anjum R, Blenis J.
Nat Rev Mol Cell Biol. 2008 Oct;9(10):747-58. doi: 10.1038/nrm2509. (REVIEW)
PMID 18813292
 
PRKX, TTBK2 and RSK4 expression causes Sunitinib resistance in kidney carcinoma- and melanoma-cell lines.
Bender C, Ullrich A.
Int J Cancer. 2012 Jul 15;131(2):E45-55. doi: 10.1002/ijc.26486. Epub 2012 Feb 28.
PMID 22020623
 
A large-scale RNAi screen in human cells identifies new components of the p53 pathway.
Berns K, Hijmans EM, Mullenders J, Brummelkamp TR, Velds A, Heimerikx M, Kerkhoven RM, Madiredjo M, Nijkamp W, Weigelt B, Agami R, Ge W, Cavet G, Linsley PS, Beijersbergen RL, Bernards R.
Nature. 2004 Mar 25;428(6981):431-7.
PMID 15042092
 
Aberrant methylation of the X-linked ribosomal S6 kinase RPS6KA6 (RSK4) in endometrial cancers.
Dewdney SB, Rimel BJ, Thaker PH, Thompson DM Jr, Schmidt A, Huettner P, Mutch DG, Gao F, Goodfellow PJ.
Clin Cancer Res. 2011 Apr 15;17(8):2120-9. doi: 10.1158/1078-0432.CCR-10-2668. Epub 2011 Mar 3.
PMID 21372219
 
Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types.
Dummler BA, Hauge C, Silber J, Yntema HG, Kruse LS, Kofoed B, Hemmings BA, Alessi DR, Frodin M.
J Biol Chem. 2005 Apr 8;280(14):13304-14. Epub 2005 Jan 4.
PMID 15632195
 
Fine mapping of Xq11.1-q21.33 and mutation screening of RPS6KA6, ZNF711, ACSL4, DLG3, and IL1RAPL2 for autism spectrum disorders (ASD).
Kantojarvi K, Kotala I, Rehnstrom K, Ylisaukko-Oja T, Vanhala R, von Wendt TN, von Wendt L, Jarvela I.
Autism Res. 2011 Jun;4(3):228-33. doi: 10.1002/aur.187. Epub 2011 Feb 22.
PMID 21384559
 
Expression pattern of the Rsk2, Rsk4 and Pdk1 genes during murine embryogenesis.
Kohn M, Hameister H, Vogel M, Kehrer-Sawatzki H.
Gene Expr Patterns. 2003 May;3(2):173-7.
PMID 12711546
 
New p53 related genes in human tumors: significant downregulation in colon and lung carcinomas.
LLeonart ME, Vidal F, Gallardo D, Diaz-Fuertes M, Rojo F, Cuatrecasas M, Lopez-Vicente L, Kondoh H, Blanco C, Carnero A, Ramon y Cajal S.
Oncol Rep. 2006 Sep;16(3):603-8.
PMID 16865262
 
RSK4 inhibition results in bypass of stress-induced and oncogene-induced senescence.
Lopez-Vicente L, Pons B, Coch L, Teixido C, Hernandez-Losa J, Armengol G, Ramon Y Cajal S.
Carcinogenesis. 2011 Apr;32(4):470-6. doi: 10.1093/carcin/bgr003. Epub 2011 Jan 14.
PMID 21239520
 
Characterization of mouse Rsk4 as an inhibitor of fibroblast growth factor-RAS-extracellular signal-regulated kinase signaling.
Myers AP, Corson LB, Rossant J, Baker JC.
Mol Cell Biol. 2004 May;24(10):4255-66.
PMID 15121846
 
Regulation and function of the RSK family of protein kinases.
Romeo Y, Zhang X, Roux PP.
Biochem J. 2012 Jan 15;441(2):553-69. doi: 10.1042/BJ20110289. (REVIEW)
PMID 22187936
 
RSK3/4 mediate resistance to PI3K pathway inhibitors in breast cancer.
Serra V, Eichhorn PJ, Garcia-Garcia C, Ibrahim YH, Prudkin L, Sanchez G, Rodriguez O, Anton P, Parra JL, Marlow S, Scaltriti M, Perez-Garcia J, Prat A, Arribas J, Hahn WC, Kim SY, Baselga J.
J Clin Invest. 2013 Jun 3;123(6):2551-63. doi: 10.1172/JCI66343. Epub 2013 May 1.
PMID 23635776
 
X chromosomal variation is associated with slow progression to AIDS in HIV-1-infected women.
Siddiqui RA, Sauermann U, Altmuller J, Fritzer E, Nothnagel M, Dalibor N, Fellay J, Kaup FJ, Stahl-Hennig C, Nurnberg P, Krawczak M, Platzer M.
Am J Hum Genet. 2009 Aug;85(2):228-39. doi: 10.1016/j.ajhg.2009.07.013.
PMID 19679225
 
Aberrant expression of X-linked genes RbAp46, Rsk4, and Cldn2 in breast cancer.
Thakur A, Rahman KW, Wu J, Bollig A, Biliran H, Lin X, Nassar H, Grignon DJ, Sarkar FH, Liao JD.
Mol Cancer Res. 2007 Feb;5(2):171-81.
PMID 17314274
 
Anti-invasive and antimetastatic activities of ribosomal protein S6 kinase 4 in breast cancer cells.
Thakur A, Sun Y, Bollig A, Wu J, Biliran H, Banerjee S, Sarkar FH, Liao DJ.
Clin Cancer Res. 2008 Jul 15;14(14):4427-36. doi: 10.1158/1078-0432.CCR-08-0458.
PMID 18628456
 
A novel ribosomal S6-kinase (RSK4; RPS6KA6) is commonly deleted in patients with complex X-linked mental retardation.
Yntema HG, van den Helm B, Kissing J, van Duijnhoven G, Poppelaars F, Chelly J, Moraine C, Fryns JP, Hamel BC, Heilbronner H, Pander HJ, Brunner HG, Ropers HH, Cremers FP, van Bokhoven H.
Genomics. 1999 Dec 15;62(3):332-43.
PMID 10644430
 

Citation

This paper should be referenced as such :
Liu, T ; Cao, S
RPS6KA6 (Ribosomal Protein S6 Kinase, 90kDa, Polypeptide 6)
Atlas Genet Cytogenet Oncol Haematol. 2014;18(5):330-333.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/RPS6KA6ID43481chXq21.html


External links

Nomenclature
HGNC (Hugo)RPS6KA6   10435
Cards
AtlasRPS6KA6ID43481chXq21
Entrez_Gene (NCBI)RPS6KA6  27330  ribosomal protein S6 kinase A6
AliasesPP90RSK4; RSK-4; RSK4; S6K-alpha-6; 
p90RSK6
GeneCards (Weizmann)RPS6KA6
Ensembl hg19 (Hinxton)ENSG00000072133 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000072133 [Gene_View]  chrX:84058346-84187935 [Contig_View]  RPS6KA6 [Vega]
ICGC DataPortalENSG00000072133
TCGA cBioPortalRPS6KA6
AceView (NCBI)RPS6KA6
Genatlas (Paris)RPS6KA6
WikiGenes27330
SOURCE (Princeton)RPS6KA6
Genetics Home Reference (NIH)RPS6KA6
Genomic and cartography
GoldenPath hg38 (UCSC)RPS6KA6  -     chrX:84058346-84187935 -  Xq21.1   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)RPS6KA6  -     Xq21.1   [Description]    (hg19-Feb_2009)
EnsemblRPS6KA6 - Xq21.1 [CytoView hg19]  RPS6KA6 - Xq21.1 [CytoView hg38]
Mapping of homologs : NCBIRPS6KA6 [Mapview hg19]  RPS6KA6 [Mapview hg38]
OMIM300303   
Gene and transcription
Genbank (Entrez)AF184965 AK023104 AK026301 AK310346 AK313240
RefSeq transcript (Entrez)NM_001330512 NM_014496
RefSeq genomic (Entrez)
Consensus coding sequences : CCDS (NCBI)RPS6KA6
Cluster EST : UnigeneHs.234478 [ NCBI ]
CGAP (NCI)Hs.234478
Alternative Splicing GalleryENSG00000072133
Gene ExpressionRPS6KA6 [ NCBI-GEO ]   RPS6KA6 [ EBI - ARRAY_EXPRESS ]   RPS6KA6 [ SEEK ]   RPS6KA6 [ MEM ]
Gene Expression Viewer (FireBrowse)RPS6KA6 [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)27330
GTEX Portal (Tissue expression)RPS6KA6
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UK32   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UK32  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UK32
Splice isoforms : SwissVarQ9UK32
Catalytic activity : Enzyme2.7.11.1 [ Enzyme-Expasy ]   2.7.11.12.7.11.1 [ IntEnz-EBI ]   2.7.11.1 [ BRENDA ]   2.7.11.1 [ KEGG ]   
PhosPhoSitePlusQ9UK32
Domaine pattern : Prosite (Expaxy)AGC_KINASE_CTER (PS51285)    PROTEIN_KINASE_ATP (PS00107)    PROTEIN_KINASE_DOM (PS50011)    PROTEIN_KINASE_ST (PS00108)   
Domains : Interpro (EBI)AGC-kinase_C    Kinase-like_dom    Pkinase_C    Prot_kinase_dom    Protein_kinase_ATP_BS    Ribosomal_S6_kinase_II    Ser/Thr_kinase_AS   
Domain families : Pfam (Sanger)Pkinase (PF00069)    Pkinase_C (PF00433)   
Domain families : Pfam (NCBI)pfam00069    pfam00433   
Domain families : Smart (EMBL)S_TK_X (SM00133)  S_TKc (SM00220)  
Conserved Domain (NCBI)RPS6KA6
DMDM Disease mutations27330
Blocks (Seattle)RPS6KA6
SuperfamilyQ9UK32
Human Protein AtlasENSG00000072133
Peptide AtlasQ9UK32
HPRD02250
IPIIPI00007123   IPI01011266   
Protein Interaction databases
DIP (DOE-UCLA)Q9UK32
IntAct (EBI)Q9UK32
FunCoupENSG00000072133
BioGRIDRPS6KA6
STRING (EMBL)RPS6KA6
ZODIACRPS6KA6
Ontologies - Pathways
QuickGOQ9UK32
Ontology : AmiGOmagnesium ion binding  fibrillar center  protein kinase activity  protein serine/threonine kinase activity  ATP binding  nucleus  nucleus  nucleoplasm  nucleolus  cytoplasm  mitochondrion  cytosol  protein phosphorylation  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  signal transduction  central nervous system development  kinase activity  negative regulation of embryonic development  negative regulation of ERK1 and ERK2 cascade  negative regulation of mesoderm development  
Ontology : EGO-EBImagnesium ion binding  fibrillar center  protein kinase activity  protein serine/threonine kinase activity  ATP binding  nucleus  nucleus  nucleoplasm  nucleolus  cytoplasm  mitochondrion  cytosol  protein phosphorylation  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  signal transduction  central nervous system development  kinase activity  negative regulation of embryonic development  negative regulation of ERK1 and ERK2 cascade  negative regulation of mesoderm development  
Pathways : KEGGMAPK signaling pathway    Oocyte meiosis    mTOR signaling pathway    Long-term potentiation    Neurotrophin signaling pathway    Progesterone-mediated oocyte maturation   
REACTOMEQ9UK32 [protein]
REACTOME PathwaysR-HSA-444257 [pathway]   
NDEx NetworkRPS6KA6
Atlas of Cancer Signalling NetworkRPS6KA6
Wikipedia pathwaysRPS6KA6
Orthology - Evolution
OrthoDB27330
GeneTree (enSembl)ENSG00000072133
Phylogenetic Trees/Animal Genes : TreeFamRPS6KA6
HOVERGENQ9UK32
HOGENOMQ9UK32
Homologs : HomoloGeneRPS6KA6
Homology/Alignments : Family Browser (UCSC)RPS6KA6
Gene fusions - Rearrangements
Fusion : MitelmanRPS6KA6/HDX [Xq21.1/Xq21.1]  
Fusion: TCGARPS6KA6 Xq21.1 HDX Xq21.1 BRCA
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerRPS6KA6 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)RPS6KA6
dbVarRPS6KA6
ClinVarRPS6KA6
1000_GenomesRPS6KA6 
Exome Variant ServerRPS6KA6
ExAC (Exome Aggregation Consortium)RPS6KA6 (select the gene name)
Genetic variants : HAPMAP27330
Genomic Variants (DGV)RPS6KA6 [DGVbeta]
DECIPHERRPS6KA6 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisRPS6KA6 
Mutations
ICGC Data PortalRPS6KA6 
TCGA Data PortalRPS6KA6 
Broad Tumor PortalRPS6KA6
OASIS PortalRPS6KA6 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICRPS6KA6  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDRPS6KA6
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
LOVD (Leiden Open Variation Database)X-chromosome gene database
BioMutasearch RPS6KA6
DgiDB (Drug Gene Interaction Database)RPS6KA6
DoCM (Curated mutations)RPS6KA6 (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)RPS6KA6 (select a term)
intoGenRPS6KA6
NCG5 (London)RPS6KA6
Cancer3DRPS6KA6(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM300303   
Orphanet
MedgenRPS6KA6
Genetic Testing Registry RPS6KA6
NextProtQ9UK32 [Medical]
TSGene27330
GENETestsRPS6KA6
Target ValidationRPS6KA6
Huge Navigator RPS6KA6 [HugePedia]
snp3D : Map Gene to Disease27330
BioCentury BCIQRPS6KA6
ClinGenRPS6KA6
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD27330
Chemical/Pharm GKB GenePA34850
Clinical trialRPS6KA6
Miscellaneous
canSAR (ICR)RPS6KA6 (select the gene name)
Probes
Litterature
PubMed34 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMineRPS6KA6
EVEXRPS6KA6
GoPubMedRPS6KA6
iHOPRPS6KA6
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 : Fri Jun 30 11:17:22 CEST 2017

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

For comments and suggestions or contributions, please contact us

jlhuret@AtlasGeneticsOncology.org.