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ING4 (inhibitor of growth family, member 4)

Written2010-12Angela Greco, Claudia Miranda
Dept Experimental Oncology, Molecular Mechanisms Unit, Istituto Nazionale Tumori IRCCS Foundation - via Venezian 1 - 20133 Milan Italy

(Note : for Links provided by Atlas : click)


Alias (NCBI)MGC12557
HGNC (Hugo) ING4
HGNC Alias symbp29ING4
LocusID (NCBI) 51147
Atlas_Id 40978
Location 12p13.31  [Link to chromosome band 12p13]
Location_base_pair Starts at 6650301 and ends at 6663119 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping ING4.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)
DNALI1 (1p34.3)::ING4 (12p13.31)ING4 (12p13.31)::ATP2B4 (1q32.1)ING4 (12p13.31)::C17orf50 (17q12)
ING4 (12p13.31)::CD163L1 (12p13.31)


  Figure adapted from Atlas of Genetics and Cytogenetics in Oncology and Haematology.
Description ING4 belongs to family of highly homologous five members containing PHD domain and has been identified through a computational sequence homology search for expressed tag clones with a PHD finger motif (Shiseki et al., 2003). ING4 gene is located on chromosome 12p13.31 and consists of eight exons encoding a 29-kDa protein expressed in multiple human tissues.
Transcription Multiple alternatively spliced transcript variants have been observed using different splice sites in the coding region; transcript variants span from 1461 bp to 1313 bp.
Wobble splicing events have been described at exon 4 and 5 boundary. Different splicing variants have been identified (among them -v1, -v2, -v3 and -v4/Δ4AA) involving 12 bp (379-390) and resulting in in frame deletions of one to four aminoacids in NLS (Tsai and Lin, 2006).
Several splicing variants have been described lacking exon 2, 3 and 6 (entirely or in part), and named ING4-ΔEx2, -ΔEx3, -ΔEx6A and -ΔEx6B, respectively (Raho et al., 2007).
Splicing variants have been detected in all tissues analysed, indicating that are not tissue specific (Tsai and Lin, 2006; Raho et al., 2007).
More recently five novel spliced variants of ING4-v1 and -v2 were identified, causing codon frame shift and eventually deletion of NLS or PHD domains. Increased expression of these variants was found in gastric adenocarcinomas compared to normal tissue (Li M et al., 2009).


Note 249 aminoacids, 29 kDa protein.
  LZL: leucine zipper-like; NLS1: nuclear localization signal 1; PHD: plant homology domain; NLS2: nuclear localization signal 2.
Description ING4 protein contains several conserved regions: i) a leucine zipper-like (LZL) domain, probably involved in protein interactions, located at the N-terminus; ii) a functional bipartite nuclear localization signal (NLS1); iii) a C-terminal plant homeo-domain (PHD), a Cys4-His-Cys3 zinc finger motif spanning 50-80 residues, found in many nuclear proteins, such as transcription factors and proteins regulating chromatin structure; iv) a non functional NLS located at the C-terminal end.
Expression Ubiquitous.
Localisation p29ING4 is a nuclear protein. It possess a bipartite nuclear localization signal. ING4 splicing variants have been described involving the NLS1 domain; most/all of them retain nuclear localization. Furthermore ING4-v1 is translocated to the nucleolus and such subcellular localization is modulated by two wobble-splicing events at the exon 4-5 boundary, causing displacement from the nucleolus to the nucleus.
Function ING4 was also isolated through a screening for genes able to suppress loss of contact inhibition, thus suggesting its tumor suppressor role.
ING4 is a nuclear protein participating to a variety of cellular functions, such as apoptosis, cell-cycle regulation, chromatin remodeling, and regulation of gene expression. Several ING4 partners have been described. Similarly to the other ING members, ING4 was described to interact with p53 and to modulate p53 transcriptional activity (Shiseki et al., 2003). The interaction of ING4 with p53 is mediated by the bipartite ING4 nuclear localization signal (NLS) (Zhang et al., 2005) and drives an increase of p53 acetylation at lysine 382 (Shiseki et al., 2003). ING4 is a critical regulator of chromatin acetylation required for gene expression. In particular, ING4 associates with the HAT complex HBO1 and it is required for the majority of histone 4 acetylation and for normal progression through S phase (Doyon et al., 2006; Shi et al., 2006). Recently a critical role for specific recognition of histone H3 trimethylated at lysine 4 (H3K4me3) by the ING4 PHD finger in mediating ING4 gene expression and tumor suppressor functions has been shown (Hung et al., 2009).
ING4 can also function as repressor of factors mediating angiogenesis. It was demonstrated that ING4 plays an inhibitory role on NF-kappaB activity by interaction with p65NF-kappaB and that the lack of inhibition of the NF-kappaB pathway by ING4 results in increased angiogenesis in glioblastomas (Garkavtsev et al., 2004). More recently, it has been described that physiologic levels of ING4 govern innate immunity in mice by regulating the levels of IkappaB and NF-kappaB proteins and the activation of select cytokine promoters (Coles et al., 2010).
ING4 was also described to repress the ability of hypoxia inducible factor (HIF)-1 to activate transcription of its downstream target genes by interacting with the HPH-2 prolyl hydroxylase. Under hypoxic conditions, ING4 may act as an adapter protein recruiting transcriptional repressors to mediate HIF activity (Ozer et al., 2005).
Involvement of ING4 in regulation of apoptosis has been demonstrated in several cellular systems. Its overexpression can induce apoptosis through the downregulation of Bcl-2 and the upregulation of p21 and Bax expression (Shiseki et al., 2003; Yu et al., 2007; Li X et al., 2009b; Cai et al., 2009).
Homology ING4 protein shares homology with other ING family members with respect to the following regions: i) a leucine zipper-like (LZL) domain, probably involved in interaction with proteins, located at the N-terminus of all the ING proteins except for ING1; ii) a nuclear localization signal (NLS); iii) a C-terminal plant homeo-domain (PHD) involved in chromatin.


Note The following ING4 point mutations have been found in lung adenocarcinoma and small cell lung carcinoma (H23 and H28, respectively) human cancer cell lines.
N214D: it alters ING4 capability of inhibition of proliferation, anchorage independent cell migration reducing protein stability by proteasome mediated degradation.
Y121N: it does not alter ING4 functions (Moreno et al., 2010).

Implicated in

Entity Breast cancer
Cytogenetics Analysis of CGH data revealed that 10-20% of primary breast tumors present deletions in 12p13. The deletions appear to affect only one copy of the gene; no genomic mutations were found in the remaining allele of ING4 (Kim et al., 2004).
Entity Head and neck squamous cell carcinoma (HNSCC)
Cytogenetics LOH of 12p13.
Oncogenesis Loss of heterozygosity at 12p12-13 region was found in 66% (33/50) of head and neck squamous cell carcinomas by using six highly polymorphic microsatellite markers. No mutations of the ING4 gene were found.
Quantitative real-time RT-PCR analysis demonstrated decreased expression of ING4 mRNA in 76% of primary tumors compared to matched normal samples (Gunduz et al., 2005).
Entity Glioma
Oncogenesis Expression of ING4 is significantly reduced in gliomas as compared with normal human brain tissue, and the extent of reduction correlates with the progression from lower to higher grades of tumours. ING4 regulates brain tumour angiogenesis through transcriptional repression of NF-kB-responsive genes (Garkavtsev et al., 2004).
Entity Astrocytoma
Prognosis A potential of role of ING4 as a biomarker for the prediction of the grade of astrocytic neoplasms has been suggested (Klironomos et al., 2010).
Oncogenesis Significantly reduced levels of ING4 were observed in human astrocytomas compared to normal brain tissue, suggesting that down-regulation of this protein might be involved in the pathogenesis of human astrocytic tumors. Decreased ING4 expression correlated significantly with tumor progression, with lower expression levels of ING4 observed in cases of high-grade neoplasms. A statistical significant negative correlation between expression of ING4 and expression of nuclear p65 was noticed (Klironomos et al., 2010).
Entity Hepatocellular carcinoma (HCC)
Prognosis Survival and metastasis analysis indicated that HCC patients with lower ING4 expression had poorer overall and disease-free survival than those with high expression. Multivariable Cox regression analysis revealed that the ING4 expression level was an independent factor for prognosis (Fang et al., 2009).
Oncogenesis The ING4 mRNA and protein levels were significantly lower in HCC than paracarcinomatous liver tissue. ING4 expression level correlates with prognosis and metastatic potential, suggesting that ING4 as a candidate prognostic marker of HCC (Fang et al., 2009).
Entity Multiple myeloma (MM)
Prognosis MM patients with high IL-8 production and microvascular density (MVD) have significantly lower ING4 levels compared with those with low IL-8 and MVD.
Oncogenesis ING4 suppression in MM cells up-regulated IL-8 and OPN under hypoxic conditions, increasing the hypoxia inducible factor-1alpha (HIF-1alpha) activity and its target gene NIP-3 expression. ING4 suppression in MM cells significantly increased vessel formation in vitro, blunted by blocking IL-8 or OPN (Colla et al., 2007).
Entity Lung cancer
Oncogenesis Reduced ING4 nuclear and cytoplasmic expression were both revealed in lung cancer and associated with tumour grade. ING4 expression in the cytoplasm was found higher than in the nucleus in a high percentage of tumors. Nuclear ING4 inhibition correlated with the tumour stage and lymph node metastasis, thus suggesting that ING4 is involved in the initiation and progression of lung cancers (Wang et al., 2010).
Entity Gastric cancer
Oncogenesis ING4 RNA and protein were drastically reduced in stomach adenocarcinoma cell lines and tissues, significantly less in female than male patients. Novel spliced forms of ING4-v1 and -v2 were identified in both normal and tumor tissue; increased expression of the novel spliced variants was observed in tumors; however no correlation with clinical parameters was observed (Li M et al., 2009).


Inhibitor of growth 4 is involved in melanomagenesis and induces growth suppression and apoptosis in melanoma cell line M14.
Cai L, Li X, Zheng S, Wang Y, Wang Y, Li H, Yang J, Sun J.
Melanoma Res. 2009 Feb;19(1):1-7.
PMID 19430401
Inhibitor of growth-4 promotes IkappaB promoter activation to suppress NF-kappaB signaling and innate immunity.
Coles AH, Gannon H, Cerny A, Kurt-Jones E, Jones SN.
Proc Natl Acad Sci U S A. 2010 Jun 22;107(25):11423-8. Epub 2010 Jun 7.
PMID 20534538
The new tumor-suppressor gene inhibitor of growth family member 4 (ING4) regulates the production of proangiogenic molecules by myeloma cells and suppresses hypoxia-inducible factor-1 alpha (HIF-1alpha) activity: involvement in myeloma-induced angiogenesis.
Colla S, Tagliaferri S, Morandi F, Lunghi P, Donofrio G, Martorana D, Mancini C, Lazzaretti M, Mazzera L, Ravanetti L, Bonomini S, Ferrari L, Miranda C, Ladetto M, Neri TM, Neri A, Greco A, Mangoni M, Bonati A, Rizzoli V, Giuliani N.
Blood. 2007 Dec 15;110(13):4464-75. Epub 2007 Sep 11.
PMID 17848618
ING tumor suppressor proteins are critical regulators of chromatin acetylation required for genome expression and perpetuation.
Doyon Y, Cayrou C, Ullah M, Landry AJ, Cote V, Selleck W, Lane WS, Tan S, Yang XJ, Cote J.
Mol Cell. 2006 Jan 6;21(1):51-64.
PMID 16387653
Decreased expression of inhibitor of growth 4 correlated with poor prognosis of hepatocellular carcinoma.
Fang F, Luo LB, Tao YM, Wu F, Yang LY.
Cancer Epidemiol Biomarkers Prev. 2009 Feb;18(2):409-16.
PMID 19208663
The candidate tumour suppressor protein ING4 regulates brain tumour growth and angiogenesis.
Garkavtsev I, Kozin SV, Chernova O, Xu L, Winkler F, Brown E, Barnett GH, Jain RK.
Nature. 2004 Mar 18;428(6980):328-32.
PMID 15029197
Frequent deletion and down-regulation of ING4, a candidate tumor suppressor gene at 12p13, in head and neck squamous cell carcinomas.
Gunduz M, Nagatsuka H, Demircan K, Gunduz E, Cengiz B, Ouchida M, Tsujigiwa H, Yamachika E, Fukushima K, Beder L, Hirohata S, Ninomiya Y, Nishizaki K, Shimizu K, Nagai N.
Gene. 2005 Aug 15;356:109-17.
PMID 15935570
ING4 mediates crosstalk between histone H3 K4 trimethylation and H3 acetylation to attenuate cellular transformation.
Hung T, Binda O, Champagne KS, Kuo AJ, Johnson K, Chang HY, Simon MD, Kutateladze TG, Gozani O.
Mol Cell. 2009 Jan 30;33(2):248-56.
PMID 19187765
A screen for genes that suppress loss of contact inhibition: identification of ING4 as a candidate tumor suppressor gene in human cancer.
Kim S, Chin K, Gray JW, Bishop JM.
Proc Natl Acad Sci U S A. 2004 Nov 16;101(46):16251-6. Epub 2004 Nov 4.
PMID 15528276
A dominant mutant allele of the ING4 tumor suppressor found in human cancer cells exacerbates MYC-initiated mouse mammary tumorigenesis.
Kim S, Welm AL, Bishop JM.
Cancer Res. 2010 Jun 15;70(12):5155-62. Epub 2010 May 25.
PMID 20501848
Loss of inhibitor of growth (ING-4) is implicated in the pathogenesis and progression of human astrocytomas.
Klironomos G, Bravou V, Papachristou DJ, Gatzounis G, Varakis J, Parassi E, Repanti M, Papadaki H.
Brain Pathol. 2010 Mar;20(2):490-7. Epub 2009 Aug 6.
PMID 19775294
Reduced expression and novel splice variants of ING4 in human gastric adenocarcinoma.
Li M, Jin Y, Sun WJ, Yu Y, Bai J, Tong DD, Qi JP, Du JR, Geng JS, Huang Q, Huang XY, Huang Y, Han FF, Meng XN, Rosales JL, Lee KY, Fu SB.
J Pathol. 2009 Sep;219(1):87-95.
PMID 19479822
Inhibitor of growth 4 induces growth suppression and apoptosis in glioma U87MG.
Li X, Cai L, Chen H, Zhang Q, Zhang S, Wang Y, Dong Y, Cheng H, Qi J.
Pathobiology. 2009a;76(4):181-92. Epub 2009 Jun 29.
PMID 19571607
Inhibitor of growth 4 induces apoptosis in human lung adenocarcinoma cell line A549 via Bcl-2 family proteins and mitochondria apoptosis pathway.
Li X, Zhang Q, Cai L, Wang Y, Wang Q, Huang X, Fu S, Bai J, Liu J, Zhang G, Qi J.
J Cancer Res Clin Oncol. 2009b Jun;135(6):829-35. Epub 2008 Nov 26.
PMID 19034511
Functional impact of cancer-associated mutations in the tumor suppressor protein ING4.
Moreno A, Palacios A, Orgaz JL, Jimenez B, Blanco FJ, Palmero I.
Carcinogenesis. 2010 Nov;31(11):1932-8. Epub 2010 Aug 12.
PMID 20705953
The ING4 tumor suppressor attenuates NF-kappaB activity at the promoters of target genes.
Nozell S, Laver T, Moseley D, Nowoslawski L, De Vos M, Atkinson GP, Harrison K, Nabors LB, Benveniste EN.
Mol Cell Biol. 2008 Nov;28(21):6632-45. Epub 2008 Sep 8.
PMID 18779315
Regulation of HIF by prolyl hydroxylases: recruitment of the candidate tumor suppressor protein ING4.
Ozer A, Bruick RK.
Cell Cycle. 2005 Sep;4(9):1153-6. Epub 2005 Sep 19. (REVIEW)
PMID 16096374
The candidate tumor suppressor ING4 represses activation of the hypoxia inducible factor (HIF).
Ozer A, Wu LC, Bruick RK.
Proc Natl Acad Sci U S A. 2005 May 24;102(21):7481-6. Epub 2005 May 16.
PMID 15897452
The dimeric structure and the bivalent recognition of H3K4me3 by the tumor suppressor ING4 suggests a mechanism for enhanced targeting of the HBO1 complex to chromatin.
Palacios A, Moreno A, Oliveira BL, Rivera T, Prieto J, Garcia P, Fernandez-Fernandez MR, Bernado P, Palmero I, Blanco FJ.
J Mol Biol. 2010 Mar 5;396(4):1117-27. Epub 2010 Jan 4.
PMID 20053357
Detection of novel mRNA splice variants of human ING4 tumor suppressor gene.
Raho G, Miranda C, Tamborini E, Pierotti MA, Greco A.
Oncogene. 2007 Aug 9;26(36):5247-57. Epub 2007 Feb 26.
PMID 17325660
ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression.
Shi X, Hong T, Walter KL, Ewalt M, Michishita E, Hung T, Carney D, Pena P, Lan F, Kaadige MR, Lacoste N, Cayrou C, Davrazou F, Saha A, Cairns BR, Ayer DE, Kutateladze TG, Shi Y, Cote J, Chua KF, Gozani O.
Nature. 2006 Jul 6;442(7098):96-9. Epub 2006 May 21.
PMID 16728974
p29ING4 and p28ING5 bind to p53 and p300, and enhance p53 activity.
Shiseki M, Nagashima M, Pedeux RM, Kitahama-Shiseki M, Miura K, Okamura S, Onogi H, Higashimoto Y, Appella E, Yokota J, Harris CC.
Cancer Res. 2003 May 15;63(10):2373-8.
PMID 12750254
Quantitative analysis of wobble splicing indicates that it is not tissue specific.
Tsai KW, Lin WC.
Genomics. 2006 Dec;88(6):855-64. Epub 2006 Aug 22.
PMID 16920330
Two wobble-splicing events affect ING4 protein subnuclear localization and degradation.
Tsai KW, Tseng HC, Lin WC.
Exp Cell Res. 2008 Oct 15;314(17):3130-41. Epub 2008 Aug 15.
PMID 18775696
Down-regulation of the inhibitor of growth family member 4 (ING4) in different forms of pulmonary fibrosis.
Tzouvelekis A, Aidinis V, Harokopos V, Karameris A, Zacharis G, Mikroulis D, Konstantinou F, Steiropoulos P, Sotiriou I, Froudarakis M, Pneumatikos I, Tringidou R, Bouros D.
Respir Res. 2009 Feb 27;10:14.
PMID 19250543
Novel splice variants of ING4 and their possible roles in the regulation of cell growth and motility.
Unoki M, Shen JC, Zheng ZM, Harris CC.
J Biol Chem. 2006 Nov 10;281(45):34677-86. Epub 2006 Sep 13.
PMID 16973615
Down-regulation of ING4 is associated with initiation and progression of lung cancer.
Wang QS, Li M, Zhang LY, Jin Y, Tong DD, Yu Y, Bai J, Huang Q, Liu FL, Liu A, Lee KY, Fu SB.
Histopathology. 2010 Aug;57(2):271-81.
PMID 20716169
Ad-ING4 inhibits K562 cell growth.
Yu X, Zhang HF, Wang JZ, Xie YF, Yang JC, Miao JC.
Zhonghua Xue Ye Xue Za Zhi. 2007 Jun;28(6):396-400.
PMID 17939406
Nuclear localization signal of ING4 plays a key role in its binding to p53.
Zhang X, Wang KS, Wang ZQ, Xu LS, Wang QW, Chen F, Wei DZ, Han ZG.
Biochem Biophys Res Commun. 2005 Jun 17;331(4):1032-8.
PMID 15882981


This paper should be referenced as such :
Greco, A ; Miranda, C
ING4 (inhibitor of growth family, member 4)
Atlas Genet Cytogenet Oncol Haematol. 2011;15(8):620-624.
Free journal version : [ pdf ]   [ DOI ]

Other Leukemias implicated (Data extracted from papers in the Atlas) [ 1 ]
  t(12;17)(p13;q12) ING4::C17orf50

External links


HGNC (Hugo)ING4   19423
Entrez_Gene (NCBI)ING4    inhibitor of growth family member 4
Aliasesmy036; p29ING4
GeneCards (Weizmann)ING4
Ensembl hg19 (Hinxton)ENSG00000111653 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000111653 [Gene_View]  ENSG00000111653 [Sequence]  chr12:6650301-6663119 [Contig_View]  ING4 [Vega]
ICGC DataPortalENSG00000111653
TCGA cBioPortalING4
AceView (NCBI)ING4
Genatlas (Paris)ING4
SOURCE (Princeton)ING4
Genetics Home Reference (NIH)ING4
Genomic and cartography
GoldenPath hg38 (UCSC)ING4  -     chr12:6650301-6663119 -  12p13.31   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)ING4  -     12p13.31   [Description]    (hg19-Feb_2009)
GoldenPathING4 - 12p13.31 [CytoView hg19]  ING4 - 12p13.31 [CytoView hg38]
Genome Data Viewer NCBIING4 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB197695 AB197696 AB197697 AF063594 AF110645
RefSeq transcript (Entrez)NM_001127582 NM_001127583 NM_001127584 NM_001127585 NM_001127586 NM_016162 NM_198287
Consensus coding sequences : CCDS (NCBI)ING4
Gene ExpressionING4 [ NCBI-GEO ]   ING4 [ EBI - ARRAY_EXPRESS ]   ING4 [ SEEK ]   ING4 [ MEM ]
Gene Expression Viewer (FireBrowse)ING4 [ Firebrowse - Broad ]
GenevisibleExpression of ING4 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)51147
GTEX Portal (Tissue expression)ING4
Human Protein AtlasENSG00000111653-ING4 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtQ9UNL4   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtQ9UNL4  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProQ9UNL4
Domaine pattern : Prosite (Expaxy)ZF_PHD_1 (PS01359)    ZF_PHD_2 (PS50016)   
Domains : Interpro (EBI)ING4/ING5    ING_fam    ING_N_histone-binding    Zinc_finger_PHD-type_CS    Znf_FYVE_PHD    Znf_PHD    Znf_PHD-finger    Znf_RING/FYVE/PHD   
Domain families : Pfam (Sanger)ING (PF12998)   
Domain families : Pfam (NCBI)pfam12998   
Domain families : Smart (EMBL)ING (SM01408)  PHD (SM00249)  
Conserved Domain (NCBI)ING4
PDB (RSDB)2K1J    2M1R    2PNX    2VNF    4AFL   
PDB Europe2K1J    2M1R    2PNX    2VNF    4AFL   
PDB (PDBSum)2K1J    2M1R    2PNX    2VNF    4AFL   
PDB (IMB)2K1J    2M1R    2PNX    2VNF    4AFL   
Structural Biology KnowledgeBase2K1J    2M1R    2PNX    2VNF    4AFL   
SCOP (Structural Classification of Proteins)2K1J    2M1R    2PNX    2VNF    4AFL   
CATH (Classification of proteins structures)2K1J    2M1R    2PNX    2VNF    4AFL   
AlphaFold pdb e-kbQ9UNL4   
Human Protein Atlas [tissue]ENSG00000111653-ING4 [tissue]
Protein Interaction databases
IntAct (EBI)Q9UNL4
Complex Portal (EBI)Q9UNL4 CPX-718 HBO1-4.1 histone acetyltransferase complex
Q9UNL4 CPX-719 HBO1-4.2 histone acetyltransferase complex
Q9UNL4 CPX-720 HBO1-4.3 histone acetyltransferase complex
Ontologies - Pathways
Ontology : AmiGOhistone acetyltransferase complex  transcription coactivator activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytosol  DNA replication  protein acetylation  apoptotic process  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  cell cycle  negative regulation of cell population proliferation  methylated histone binding  methylated histone binding  positive regulation of apoptotic process  positive regulation of apoptotic process  histone H3 acetylation  histone H4-K5 acetylation  histone H4-K8 acetylation  histone H4-K12 acetylation  histone H4-K16 acetylation  intermediate filament cytoskeleton  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  negative regulation of growth  metal ion binding  regulation of cell cycle  MOZ/MORF histone acetyltransferase complex  
Ontology : EGO-EBIhistone acetyltransferase complex  transcription coactivator activity  protein binding  nucleus  nucleus  nucleoplasm  nucleoplasm  cytosol  DNA replication  protein acetylation  apoptotic process  DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator  cell cycle  negative regulation of cell population proliferation  methylated histone binding  methylated histone binding  positive regulation of apoptotic process  positive regulation of apoptotic process  histone H3 acetylation  histone H4-K5 acetylation  histone H4-K8 acetylation  histone H4-K12 acetylation  histone H4-K16 acetylation  intermediate filament cytoskeleton  negative regulation of transcription, DNA-templated  positive regulation of transcription, DNA-templated  negative regulation of growth  metal ion binding  regulation of cell cycle  MOZ/MORF histone acetyltransferase complex  
REACTOMEQ9UNL4 [protein]
REACTOME PathwaysR-HSA-3214847 [pathway]   
NDEx NetworkING4
Atlas of Cancer Signalling NetworkING4
Wikipedia pathwaysING4
Orthology - Evolution
GeneTree (enSembl)ENSG00000111653
Phylogenetic Trees/Animal Genes : TreeFamING4
Homologs : HomoloGeneING4
Homology/Alignments : Family Browser (UCSC)ING4
Gene fusions - Rearrangements
Fusion : QuiverING4
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerING4 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)ING4
Exome Variant ServerING4
GNOMAD BrowserENSG00000111653
Varsome BrowserING4
ACMGING4 variants
Genomic Variants (DGV)ING4 [DGVbeta]
DECIPHERING4 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisING4 
ICGC Data PortalING4 
TCGA Data PortalING4 
Broad Tumor PortalING4
OASIS PortalING4 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICING4  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DING4
Mutations and Diseases : HGMDING4
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)ING4
DoCM (Curated mutations)ING4
CIViC (Clinical Interpretations of Variants in Cancer)ING4
NCG (London)ING4
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Genetic Testing Registry ING4
NextProtQ9UNL4 [Medical]
Target ValidationING4
Huge Navigator ING4 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDING4
Pharm GKB GenePA134976283
Clinical trialING4
DataMed IndexING4
PubMed120 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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