ING1 (inhibitor of growth family, member 1)

2014-11-01 Audrey Mouche , Katherine Yaacoub , Thierry Guillaudeux , Rémy Pedeux Affiliation

INSERM U917, Microenvironnement et Cancer, Rennes, France, (AM, KY, TG, RP); Universite de Rennes 1, Rennes, France (AM, KY, TG, RP); EFS Bretagne, France (RP); UMS Biosit 3480 CNRS\\\/018 INSERM, Rennes, France (TG)

Identity

HGNC

ING1

LOCATION

13q34

LOCUSID

3621

ALIAS

p24ING1c,p33,p33ING1,p33ING1b,p47,p47ING1a

FUSION GENES

Show Gene Fusions

DNA/RNA

Figure1. Chromosomal localization of the ING1 gene in Homo sapiens.

Figure 2. Structure and transcripts of Human ING1 genes. Coding regions are in dark blue and non-coding regions are represented in light blue. For ING1c v2 and v5: Exons E1d and E1balt (alternative) are represented in yellow. They both code for the same protein: ING1c (Figure 3).

Description

In 1996 Karl Riabowols group identified a new Tumor Suppressor Gene (TSG) by using subtractive hybridization between cDNAs from normal mammary epithelial cells and mammary epithelial cells from tumor (breast cancer cell-lines). This experiment was followed by an in vivo screen for tumourigenesis. Using this method, the authors identified a new candidate TSG they named ING1 for INhibitor of Growth 1 (Garkavtsev et al., 1996).

Transcription

The ING1 gene has been mapped to chromosome 13 at locus 13q34 close to the telomeric region (Figure 1). Human ING1 is made of four exons, exon 1a, 1b, 1c, and 2, resulting in five transcribed variants (ING1a, ING1b, ING1c, and ING1d) (Figure 2).

Pseudogene

INGX is the pseudogene of ING1 (He et al., 2005).

Proteins

Description

The amino acid sequence alignment of human ING proteins revealed several conserved regions in their C-terminal part: a Novel Conserved Region (NCR), a Nuclear Localization Signal (NLS), a Plant Homeo Domain (PHD) and a PolyBasic Region (PBR).
The ING proteins are characterized by the presence of a highly conserved PHD in their C-terminal part. This domain is commonly found in proteins involved in chromatin modification (Bienz, 2006; Mellor, 2006). In the N-terminal part of ING1b isoform, which is the most abundant isoform with ING1a, there is also a PCNA Interacting Protein motif (PIP) and Partial Bromo Domain (PBD) (Figure 3).

Figure 3. Schematic representation of ING1 proteins structure. In the C-terminal part: Novel Conserved Region (NCR), Nuclear Localization Signal (NLS), Plant Homeo Domain (PHD) and PolyBasic Region (PBR). In the N-terminal part of p33ING1b: PCNA Interacting Protein motif (PIP) and Partial Bromo Domain (PBD).

Expression

ING1 is ubiquitously expressed in mammalian tissues (Walzak et al., 2008).

Localisation

The ING1 protein contains an NLS domain, so it is mainly located in the nucleus. Members of the 14-3-3 family are able to interact with ING1 phosphorylated on serine 199 leading to its relocalisation to the cytoplasm (Gong et al., 2006). Recently, it has been found that ING1b translocates also into mitochondria after UV or IR. This translocation is independent of p53 (Bose et al., 2013).

Function

ING1 has been identified as a tumor suppressor gene with Gatekeepers and Caretakers functions.
Initially ING1 has been characterized as gatekeeper genes which are known to regulate the growth of tumors through senescence, apoptosis and cell cycle regulation. Indeed, ING1 is involved in the regulation of the cell cycle arrest, apoptosis and senescence.
Firtsly, ING1b has been described to physically interact with the tumor suppressor protein p53 and being necessary for its transcriptional activity (Garkavtsev et al., 1998). ING1 is also involved in the regulation of p53 activity. Under stress, ING1b interact with PI5P in order to activate the p300 acetylase which acetylates p53 on lysine 382. This acetylation promotes the transcription of factors involved in cell cycle arrest, senescence and apoptosis (p21, Bax) (Garkavtsev et al., 1998; Kataoka et al., 2003). ING1b is also able to interact with SIRT1, a histone deacetylase known for the p53 deacetylation. SIRT1 interaction with ING1b competitively inhibits its interaction with p53 leading to the maintenance of p53 activity (Kataoka et al., 2003). Moreover, ING1b is known to stabilize p53 by disrupting the regulation of p53 by MDM2 (Leung et al., 2002).
ING1 functions can also be independent of p53 signaling pathways. ING1 has been described to interact with the Sin3/HDAC1/HDAC2/SAP30 complex through a direct interaction with SAP30 (Kuzmichev et al., 2002). ING1b has also been reported to increase the expression of Heat Shock Protein 70 (HSP70). This induction of HSP70 required the amino terminus of ING1b but not the PHD, PBR and NLS region (Feng et al., 2006). HSP70 is known to inhibit the NF-kB pathways (Ran et al., 2004; Shi et al., 2006). More recently, it has been shown that the C-terminal PHD of ING1 interacts with histone H3 trimethylated at Lys4 (H3K4me3). This interaction is involved in DNA repair and apoptotic activities of ING1 (Peña et al., 2008). Under stress, ING1 interaction with H3K4me4 leads to the recruitment of the Sin3/HDAC1-2/SAP30 transcriptional repressor complex. Under UV stress, ING1b targets the nucleolus and stabilizes Cellular Senescence-Inhibited Gene (CSIG) through its Nucleolar Targeting Signal (NTS). This interaction is required for ING1b dependent apoptosis after UV stress (Li et al., 2012).
More recently, ING1 has been characterized as a caretaker gene which controls the integrity of the genome.
Indeed, ING1b is involved in DNA repair in response to UV. ING1b overexpression has been described to enhance repair of UV-damaged DNA in a p53 dependent manner. Furthermore, binding between ING1b and Growth Arrest and DNA Damage 45 (GADD45) has been reported. These findings suggest that ING1b cooperates with GADD45 and p53 in Nucleotide Excision Repair (NER) (Cheung Jr. et al., 2001). Interestingly, ING1b is also required for PCNA monoubiquitination in response to UV. More precisely, ING1b is necessary for the loading of the E3 ubiquitin ligase Rad18 at stalled replication forks through histone H4 acetylation (Wong et al., 2011).

Figure 4. Schematic representation of ING1 functions. Modified from Guérillon et al., 2013.

Homology

The C-terminal part of ING proteins is highly-conserved through human to plant, especially the PHD-finger motif. There are five human ING genes (ING1, ING2, ING3, ING4, and ING5) which encode multiple isoforms via splicing.

Implicated in

Entity name

Various cancers

Note

For review: Ythier et al., 2008; Guérillon et al., 2014.
Many genetics and epigenetics alterations of tumor suppressor genes (TSGs) or oncogenes contribute to cancerogenesis. Thus, the expression of tumor suppressor gene ING1 has been analysed in many tumor types.

Entity name

Adenocarcinoma of the esophagogastric junction

Note

Among 19 adenocarcinoma of the esophagogastric junction (AdEGJs), two tumors presented ING1b alterations (11%). One missense mutation at codon 147 had a G to T transition resulting in serine to isoleucine substitution. The second silent mutation at codon 173 had a G to A transition with no amino acid change. In addition, p33ING1b mRNA expression was reduced in 63% of AdEGJs samples compared to normal esophageal tissues. Moreover, ING1b protein expression was frequently decreased or not detected in tumor samples, while all normal gastric mucosa had ING1b protein expression (Hara et al., 2003).

Entity name

Ameloblastoma

Note

In the case of Ameloblastoma, a high frequency of loss of heterozygosity (33% - 72%) is found in the loci of each ING gene family member. In the case of ING1, 51% of 35 patients showed an allelic loss in the ING1 coding region. Different mechanisms, such as deletions, gene conversion or mitotic combination might be implicated to enhance INGs gene alterations and promote ameloblastoma tumorigenesis (Borkosky et al., 2010).

Entity name

Brain tumor

Note

In human brain tumors, ING1b mislocalization is observed in all of the analyzed glioma samples and in some glioma cell lines. However, mutations of ING1 seem to be infrequent. A single point mutation was detected in 29 brain tumor specimens (3.5%) manifested by an arginine to histidine substitution. This amino acid change is caused by a G-to-A transition. Furthermore, this mutation does not affect the expression of ING1b mRNA, but it leads to a cytoplasmic shift of p33ING1b, according to taking place in a sequence of ING1 reported to target p33ING1b to the nucleus (Vieyra et al., 2003).

Entity name

Breast cancer

Note

In breast cancer, expression of ING1 mRNA is decreased in 17 of 24 breast cancer tissues (71%), compared to normal tissues (Tokunaga et al., 2000). Furthermore, a downregulation of ING1 gene has been established in breast cancer cell lines. Mutations of ING1 are rare (1/377) in breast carcinomas (Toyama et al., 1999). In addition, 7 of 86 invasive breast carcinoma cases showed an increase of p33ING1b expression in the cytoplasm, while the 79 cases had a low p33ING1b cytoplasmic expression, with 33 of them lacking absolutely cytoplasmic expression of p33ING1b (Nouman et al., 2003).

Entity name

Childhood acute lymphoblastic leukemia

Note

In childhood Acute Lymphoblastic Leukeamia (ALL), 78% of cases showed a decrease in the expression of nuclear p37ING1b which undergoes a shift to the cytoplasm. This translocation may attenuate the function of p37ING1b protein and plays an important role in pathogenesis of ALL (Nouman et al., 2002b).

Entity name

Colorectal carcinoma

Note

In colorectal carcinomas, no loss of alleles has been detected in ING1 gene. Neither Loss Of Heterozygosity (LOH) nor mutations have been observed in 29 sporadic colorectal carcinomas samples. It suggests that another mechanism might be implicated in the loss of gene. For example, hypermethylation of the promoter might be responsible for the inactivation of tumour suppressor genes (Sarela et al., 1999). In addition, the ratios of p33ING1b and p47ING1a mRNA expression were significantly lower in human sporadic colorectal tissus than those in normal tissues (Chen et al., 2005). Moreover, 32 % of patients with DukesA colorectal cancer display a low expression of p33ING1b protein (Ahmed et al., 2008).

Entity name

Esophageal squamous cell cancer

Note

In the case of Esophageal squamous cell cancer (ESCC), 59 % of 31 informative cases showed allelic loss at chromosome 13q33-34 where ING1 is mapped. Four somatic missense mutations are located between codons 214 and 270, and two somatic silent mutations are located between codons 219 and 223. All of the missense mutations found in ESCC were localised within the highly conserved PHD finger-like domain which is implicated in transcriptional regulation. Loss of ING1 protein expression has been observed in all ESCC samples, this absence of ING1 may contribute to ESCC carcinogenesis (Chen et al., 2001).

Entity name

Gastric cancer

Note

It has been demonstrated that 75% of tumor samples tested showed a significant decrease in p33ING1 expression associated with gastric carcinogenesis. Moreover, a silent mutation is detected in 2/12 gastric cancer cells with no amino acid change in codon 188, and only one cell line(1/12) had a missense mutation in codon 172 resulting in glutamine to lysine amino acid substitution. However, these findings suggest that p33ING1 acts as a tumor suppressor gene even if it is preserved in the majority of gastric cancer (Oki et al., 1999).

Entity name

Haematological malignancies

Note

49 patients with heamatological malignancies and 5 normal patients showed a predominant expression of p33ING1b transcript, while p24/ING1 and p47/ING1 transcripts are very weakly expressed. In addition, no p33ING1b sequence variation has been observed in all of the 49 patients with heamatological malignancies, suggesting that neither p33ING1b mutation, nor dysregulation of alternative splicing of ING1 gene are significantly responsible of heamatological malignancies progression (Bromidge et al., 2002).

Entity name

Head and neck squamous cell carcinoma

Note

In Head and Neck Squamous Cell Carcinomas (HNSCC), a deletion is found on chromosome 13q33-34, where ING1 gene is mapped. A loss of heterozigosity has been detected in 68 % of HNSCC cases. Six mutations were identified in the 23 tumors with allelic loss, 13% showed missense mutations with amino acid change and the other 3 samples showed an alteration at codon 173 of p33ING1b without an amino acid change. All these mutations are found in the PHD finger or NLS domain of ING1 (Gunduz et al., 2000). Another study showed that there is no somatic mutation in any of 20 primary tumors showing 13q LOH and in 5 head and neck cancer cell lines, suggesting an alternative factor implicated in this type of tumor (Sanchez-Cespedes et al., 2000).

Entity name

Hepatocellular carcinoma

Note

In hepatocellular carcinoma (HCC), p33ING1 gene is not frequently altered (7%). This mutation resulted in G to C transversion, in the codon 215, with an amino change (cysteine to serine) in ING1b gene. However, 42 % of HCC tissus had an up-regulation of p33ING1b, whereas 58% showed a downregulation of p33ING1b protein. Although the rate of mutation in ING1 is low, loss or inactivation of p33ING1b may be an important mechanism for malignant transformation of HCC (Zhu et al., 2005). Another study suggests that ING1 protein was expressed in either hepatocarcinoma cells or hepatocytes, and localized in the nuclei of hepatocarcinoma cells. In advanced stage group, the general expression level of ING1 was increased in the tumor tissue. Besides, transcriptional levels showed that ING1b is up-regulated in HCC tissus, whereas ING1a expression level remains unchanged (Chen et al., 2009).

Entity name

Lung cancer

Note

In lung cancer, 6/31 of primary lung cancer tumors and 1/30 human lung cancer cell lines showed a G to A transition that occurred in codon 173 located in the NLS domain of ING1. This substitution does not result in amino acid change. There is no point mutation detected in ING1b gene. An up-regulation of ING1b mRNA expression is detected in 7 of 8 lung cancer cell lines having a p53 mutation (Okano et al., 2006). In the case of non-small cell lung cancer (NSCLC), another study demonstrated that only 2 % had point mutations in the coding regions of ING1b, but there was no missense mutation detected in ING1b coding region. In addition, 42 % showed a reduction of ING1b gene expression associated with p53 mutations (Kameyama et al., 2003).

Entity name

Lymphoid malignancies

Note

In lymphoid malignancies, many deletions and chromosomal translocations were observed in q33-34 region of chromosome 13 where ING1 gene is mapped. A decrease in the expression of ING1 gene is found in 4/5 T-cell lines derived from acute lymphocytic leukemia. A decrease of ING1 expression was also found in 5/11 B- cell lines including 2 myeloma and 2 Burkitt lymphoma cell lines. Moreover, no point mutation or deletion was detected in the 9 cell lines having reduced ING1 expression. These findings suggest that transcriptional or post-transcriptional mechanisms are responsible of ING1 decreased expression which contributes to the development of lymphoid malignancies (Ohmori et al., 1999).

Entity name

Mantle cell lymphoma

Note

The genetic alteration of mantle cell lymphoma (MCL) is a translocation t(11;14)(q13;q32), detected in all MCL cases. Additional aberrations are implicated in lymphoma malignancies, such as the inactivation of tumor suppressor genes. For example, the expression of ING1 is decreased in all the cell lines. No evidence of promoter methylation of ING1 gene has been found in MCL cell lines (Ripperger et al., 2007).

Entity name

Melanoma

Note

The p33ING1b protein expression level is significantly increased in 14 melanoma cell lines studied. An overexpression of p33ING1b mRNA was also found in all 6 melanoma cell lines examined, but it was absent in normal melanocytes. There is a low mutation rate (14 %) in melanoma cell lines. Two silent nucleotide changes have been detected in exon 1a in Sk-mel-110, whereas, in Sk-mel-24, 8 nucleotide alterations in exon 2 were found. Seven alterations were silent and 1 missense alteration at codon 260 results in an aspargine to serine amino acid subsitution. No mutation has been detected in 25 samples of healthy volunteers suggesting that these nucleotide alterations in the 2 melanoma cell lines are not due to a polymorphism. Thus, ING1 gene is not frequently mutated in melanoma cells. These findings demonstrated that other mechanisms, such as DNA hypomethylation, may contribute to the overexpression of ING1 (Campos et al., 2002).
Another study showed a loss of nuclear p33ING1b expression associated with a strong or intermediate cytoplasmic p33ING1b expression in 35 % of the invasive malignant melanomas. Also, 47 % showed a complete loss of nuclear p33ING1b expression. The translocation or the shift to the cytoplasm may result in a loss of p33ING1b function (Nouman et al., 2002a).

Entity name

Oral squamous cell carcinoma

Note

Few studies about p33ING1b role and expression in oral squamous cell carcinoma (OSCC) have been published. In normal squamous cells, p33ING1b showed only a nuclear expression, whereas 24 % of OSCC showed a shift of p33ING1b protein from the nucleus to the cytoplasm with a weak nuclear staining, and 76 % of OSCC had a negative expression of p33ING1b. Furthemore, p33ING1b shift to the cytoplasm may result in an unfonctional protein that enhances oncogenesis of OSCC. Besides, it is demonstrated that the tumors with p33ING1b cytoplasmic expression are more aggressive, however the reason is still unknown (Zhang et al., 2008).

Entity name

Ovarian cancer

Note

Among the 111 cases of ovarian carcinoma analysed, 25 % are observed with a low or absent p33ING1b protein expression. Besides, a total of 32 cases showed a significant reduction of p33ING1b mRNA expression, with a decrease or absence of p33ING1b protein in 53 % of them. No mutation of p33ING1b has been detected in these samples. An allelic loss at the p33ING1b locus was detected in 25 % of the cases with a correlation between mRNA expression and p33ING1b protein decrease. Twenty four percent of 88 patients had p33ING1b promoter methylation. In addition, p33ING1b promoter methylation has been observed in two ovarian cancer cell lines, OVCA3 and SKOV3 (2/2). The absence of mutation suggests that other inactivation mechanisms can occur, such as histone deacetylation, and might contribute to p33ING1b silencing and tumorigenesis of ovarian cancer (Shen et al., 2005).

Entity name

Pancreatic carcinoma

Note

Only 15 % of pancreatic carcinoma specimens showed a reduction of p33ING1b protein expression. This low percentage demonstrates that there is no correlation between p33ING1b expression and clinicopathological factors. In addition, a single germline missense mutation located at codon 215 has been identified in 1/40 pancreatic carcinoma cases. This mutation is manifested by a cysteine to serine substitution at codon 215 localised in the PHD domain of ING1. However, p33ING1b protein expression is still normal in this sample. 60 % of tumor cases showed a loss of heterozygosity (LOH) with no mutation detected. In addition, 2 of these samples have an absence of p33ING1b protein expression. These findings suggested that mutations are not the only reason for the loss of function of p33ING1b in pancreatic carcinomas (Yu et al., 2004).

Bibliography

Pubmed ID	Last Year	Title	Authors
17949449	2008	The predictive value of p53 and p33(ING1b) in patients with Dukes'C colorectal cancer.	Ahmed IA et al
16297627	2006	The PHD finger, a nuclear protein-interaction domain.	Bienz M et al
20681410	2010	Allelic loss of the ING gene family loci is a frequent event in ameloblastoma.	Borkosky SS et al
24008732	2013	ING1 induces apoptosis through direct effects at the mitochondria.	Bose P et al
12008079	2002	Relative levels of alternative transcripts of the ING1 gene and lack of mutations of p33/ING1 in haematological malignancies.	Bromidge T et al
11966686	2002	The novel tumour suppressor gene ING1 is overexpressed in human melanoma cell lines.	Campos EI et al
11389058	2001	Genetic alterations of candidate tumor suppressor ING1 in human esophageal squamous cell cancer.	Chen L et al
16273637	2005	Genetic alterations and expression of inhibitor of growth 1 in human sporadic colorectal cancer.	Chen LS et al
18450387	2009	ING1a and ING1b different expressed in sporadic hepatocellular carcinoma.	Chen X et al
11431327	2001	The tumor suppressor candidate p33(ING1) mediates repair of UV-damaged DNA.	Cheung KJ Jr et al
17030616	2006	HSP70 induction by ING proteins sensitizes cells to tumor necrosis factor alpha receptor-mediated apoptosis.	Feng X et al
9440695	1998	The candidate tumour suppressor p33ING1 cooperates with p53 in cell growth control.	Garkavtsev I et al
16581770	2006	Subcellular targeting of p33ING1b by phosphorylation-dependent 14-3-3 binding regulates p21WAF1 expression.	Gong W et al
24333729	2014	The ING tumor suppressor genes: status in human tumors.	Guérillon C et al
10866301	2000	Genomic structure of the human ING1 gene and tumor-specific mutations detected in head and neck squamous cell carcinomas.	Gunduz M et al
12637159	2003	ING1 and p53 tumor suppressor gene alterations in adenocarcinomas of the esophagogastric junction.	Hara Y et al
15356280	2005	Phylogenetic analysis of the ING family of PHD finger proteins.	He GH et al
25324173	2015	Loss of heterozygosity of chromosome 13q33-34 region and molecular analysis of ING1 and p53 genes in bladder carcinoma.	Igci M et al
14581367	2003	Reduced ING1b gene expression plays an important role in carcinogenesis of non-small cell lung cancer patients.	Kameyama K et al
14522900	2003	ING1 represses transcription by direct DNA binding and through effects on p53.	Kataoka H et al
11784859	2002	Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1).	Kuzmichev A et al
12208736	2002	The candidate tumor suppressor ING1b can stabilize p53 by disrupting the regulation of p53 by MDM2.	Leung KM et al
22419112	2012	Nucleolar protein CSIG is required for p33ING1 function in UV-induced apoptosis.	Li N et al
16839870	2006	It takes a PHD to read the histone code.	Mellor J et al
12835295	2003	Downregulation of nuclear expression of the p33(ING1b) inhibitor of growth protein in invasive carcinoma of the breast.	Nouman GS et al
10577281	1999	Decreased expression of p33ING1 mRNA in lymphoid malignancies.	Ohmori M et al
16465410	2006	Alterations in novel candidate tumor suppressor genes, ING1 and ING2 in human lung cancer.	Okano T et al
10660101	1999	Reduced expression of p33(ING1) and the relationship with p53 expression in human gastric cancer.	Oki E et al
18533182	2008	Histone H3K4me3 binding is required for the DNA repair and apoptotic activities of ING1 tumor suppressor.	Peña PV et al
15198984	2004	Hsp70 promotes TNF-mediated apoptosis by binding IKK gamma and impairing NF-kappa B survival signaling.	Ran R et al
17488656	2007	Promoter methylation of PARG1, a novel candidate tumor suppressor gene in mantle-cell lymphomas.	Ripperger T et al
10679922	2000	Molecular analysis of the candidate tumor suppressor gene ING1 in human head and neck tumors with 13q deletions.	Sanchez-Cespedes M et al
10615239	1999	The candidate tumour suppressor gene, ING1, is retained in colorectal carcinomas.	Sarela AI et al
15677627	2005	Epigenetic and genetic alterations of p33ING1b in ovarian cancer.	Shen DH et al
16912653	2006	The inhibition of LPS-induced production of inflammatory cytokines by HSP70 involves inactivation of the NF-kappaB pathway but not the MAPK pathways.	Shi Y et al
10754201	2000	Diminished expression of ING1 mRNA and the correlation with p53 expression in breast cancers.	Tokunaga E et al
10498868	1999	Suppression of ING1 expression in sporadic breast cancer.	Toyama T et al
14676120	2003	Altered subcellular localization and low frequency of mutations of ING1 in human brain tumors.	Vieyra D et al
17720155	2008	Expression profiles of mRNA transcript variants encoding the human inhibitor of growth tumor suppressor gene family in normal and neoplastic tissues.	Walzak AA et al
21227930	2011	Tumour suppressor ING1b maintains genomic stability upon replication stress.	Wong RP et al
18636562	2008	The new tumor suppressor genes ING: genomic structure and status in cancer.	Ythier D et al
15534913	2004	Genetic alterations and reduced expression of tumor suppressor p33(ING1b) in human exocrine pancreatic carcinoma.	Yu GZ et al
17805569	2008	Nuclear to cytoplasmic shift of p33(ING1b) protein from normal oral mucosa to oral squamous cell carcinoma in relation to clinicopathological variables.	Zhang JT et al
15800978	2005	Inhibitory effect of tumor suppressor p33(ING1b) and its synergy with p53 gene in hepatocellular carcinoma.	Zhu Z et al

Other Information

Locus ID:

NCBI: 3621
MIM: 601566
HGNC: 6062
Ensembl: ENSG00000153487

Variants:

dbSNP: 3621
ClinVar: 3621
TCGA: ENSG00000153487
COSMIC: ING1

RNA/Proteins

Gene ID	Transcript ID	Uniprot
ENSG00000153487	ENST00000333219	Q9UK53
ENSG00000153487	ENST00000338450	Q9UK53
ENSG00000153487	ENST00000375774	A0A0C4DFW2
ENSG00000153487	ENST00000375775	Q9UK53
ENSG00000153487	ENST00000464141	A0A087WXF7

Expression (GTEx)

Adipose - Subcutaneous

Adipose - Visceral

Adrenal Gland

Artery - Aorta

Artery - Tibial

Bladder

Brain - Amygdala

Brain - Anterior cingulate cortex

Brain - Caudate

Brain - Cerebellar Hemisphere

Brain - Cerebellum

Brain - Cortex

Brain - Frontal Cortex

Brain - Hippocampus

Brain - Hypothalamus

Brain - Nucleus accumbens

Brain - Putamen

Brain - Spinal cord

Brain - Substantia nigra

Breast - Mammary Tissue

Cells - Cultured fibroblasts

Cells - EBV - transformed lymphocytes

Cervix - Ectocervix

Cervix - Endocervix

Colon - Sigmoid

Colon - Transverse

Esophagus - Gastroesophageal Junction

Esophagus - Mucosa

Esophagus - Muscularis

Fallopian Tube

Heart - Atrial Appendage

Heart - Left Ventricle

Kidney - Cortex

Kidney - Medulla

Liver

Lung

Minor Salivary Gland

Muscle - Skeletal

Nerve - Tibial

Ovary

Pancreas

Pituitary

Prostate

Skin - Not Sun Exposed

Skin - Sun Exposed

Small Intestine - Terminal Ileum

Spleen

Stomach

Testis

Thyroid

Uterus

Vagina

Whole Blood

Protein levels (Protein atlas)

Not detected

Low

Medium

High

References

Pubmed ID	Year	Title	Citations
18836436	2008	Tethering by lamin A stabilizes and targets the ING1 tumour suppressor.	39
15526165	2004	Biological functions of the ING family tumor suppressors.	38
12015309	2002	Human ING1 proteins differentially regulate histone acetylation.	32
18388957	2008	NAD(P)H quinone oxidoreductase 1 inhibits the proteasomal degradation of the tumour suppressor p33(ING1b).	28
18691180	2008	ING1a expression increases during replicative senescence and induces a senescent phenotype.	23
21528065	2011	Down-regulation of miR-622 in gastric cancer promotes cellular invasion and tumor metastasis by targeting ING1 gene.	22
16581770	2006	Subcellular targeting of p33ING1b by phosphorylation-dependent 14-3-3 binding regulates p21WAF1 expression.	21
19680556	2009	Genetic variation in healthy oldest-old.	20
25411783	2014	MiR-371-5p facilitates pancreatic cancer cell proliferation and decreases patient survival.	19
23388825	2013	Ing1 functions in DNA demethylation by directing Gadd45a to H3K4me3.	17

Citation

Audrey Mouche ; Katherine Yaacoub ; Thierry Guillaudeux ; Rémy Pedeux

ING1 (inhibitor of growth family, member 1)

Atlas Genet Cytogenet Oncol Haematol. 2014-11-01

Online version: http://atlasgeneticsoncology.org/gene/40974/ing1