ING1

Last updated
ING1
ING1 .png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases ING1 , p24ING1c, p33, p33p33ING1b, p47, p47ING1a, inhibitor of growth family member 1
External IDs OMIM: 601566 MGI: 1349481 HomoloGene: 40119 GeneCards: ING1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_198219
NM_001267728
NM_005537
NM_198217
NM_198218

Contents

RefSeq (protein)

NP_001254657
NP_005528
NP_937860
NP_937861
NP_937862

Location (UCSC) Chr 13: 110.71 – 110.72 Mb Chr 8: 11.61 – 11.61 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Inhibitor of growth protein 1 is a protein that in humans is encoded by the ING1 gene. [5] [6] [7]

Function

This gene encodes a tumor suppressor protein that can induce cell growth arrest and apoptosis. The encoded protein is a nuclear protein that physically interacts with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. Reduced expression and rearrangement of this gene have been detected in various cancers. Multiple alternatively spliced transcript variants encoding distinct isoforms have been reported. [7]

Location on Chromosome 13

ING1 is located near the following genes on Chromosome 13

Interactions

ING1 has been shown to interact with:

Related Research Articles

p53 Mammalian protein found in Homo sapiens

Tumor protein P53, also known as p53, cellular tumor antigen p53, the Guardian of the Genome, phosphoprotein p53, tumor suppressor p53, antigen NY-CO-13, or transformation-related protein 53 (TRP53), is any isoform of a protein encoded by homologous genes in various organisms, such as TP53 (humans) and Trp53 (mice). This homolog is crucial in multicellular vertebrates, where it prevents cancer formation. As such, p53 has been described as "the guardian of the genome" because of its role in conserving stability by preventing genome mutation. Hence TP53 is classified as a tumor suppressor gene.

Tumor suppressor gene Gene that inhibits expression of the tumorigenic phenotype

A tumor suppressor gene (TSG), or anti-oncogene, is a gene that regulates a cell during cell division and replication. If the cell grows uncontrollably, it will result in cancer. When a tumor suppressor gene is mutated, it results in a loss or reduction in its function. In combination with other genetic mutations, this could allow the cell to grow abnormally. The loss of function for these genes may be even more significant in the development of human cancers, compared to the activation of oncogenes.

p73 Protein-coding gene in the species Homo sapiens

p73 is a protein related to the p53 tumor protein. Because of its structural resemblance to p53, it has also been considered a tumor suppressor. It is involved in cell cycle regulation, and induction of apoptosis. Like p53, p73 is characterized by the presence of different isoforms of the protein. This is explained by splice variants, and an alternative promoter in the DNA sequence.

Promyelocytic leukemia protein

Promyelocytic leukemia protein (PML) is the protein product of the PML gene. PML protein is a tumor suppressor protein required for the assembly of a number of nuclear structures, called PML-nuclear bodies, which form amongst the chromatin of the cell nucleus. These nuclear bodies are present in mammalian nuclei, at about 1 to 30 per cell nucleus. PML-NBs are known to have a number of regulatory cellular functions, including involvement in programmed cell death, genome stability, antiviral effects and controlling cell division. PML mutation or loss, and the subsequent dysregulation of these processes, has been implicated in a variety of cancers.

TP53BP1

Tumor suppressor p53-binding protein 1 also known as p53-binding protein 1 or 53BP1 is a protein that in humans is encoded by the TP53BP1 gene.

RBBP7 Protein-coding gene in the species Homo sapiens

Histone-binding protein RBBP7 is a protein that in humans is encoded by the RBBP7 gene.

DNAJA3

DnaJ homolog subfamily A member 3, mitochondrial, also known as Tumorous imaginal disc 1 (TID1), is a protein that in humans is encoded by the DNAJA3 gene on chromosome 16. This protein belongs to the DNAJ/Hsp40 protein family, which is known for binding and activating Hsp70 chaperone proteins to perform protein folding, degradation, and complex assembly. As a mitochondrial protein, it is involved in maintaining membrane potential and mitochondrial DNA (mtDNA) integrity, as well as cellular processes such as cell movement, growth, and death. Furthermore, it is associated with a broad range of diseases, including neurodegenerative diseases, inflammatory diseases, and cancers.

WWOX Protein-coding gene in the species Homo sapiens

WW domain-containing oxidoreductase is an enzyme that in humans is encoded by the WWOX gene.

SAP30

Sin3A-associated protein, 30kDa, also known as SAP30, is a protein which in humans is encoded by the SAP30 gene.

DLC1

Deleted in Liver Cancer 1 also known as DLC1 and StAR-related lipid transfer protein 12 (STARD12) is a protein which in humans is encoded by the DLC1 gene.

RBM5

RNA-binding protein 5 is a protein that in humans is encoded by the RBM5 gene.

ING2

Inhibitor of growth protein 2 is a protein that in humans is encoded by the ING2 gene.

ING4

Inhibitor of growth protein 4 is a protein that in humans is encoded by the ING4 gene.

SEMA3B

Semaphorin-3B is a protein that in humans is encoded by the SEMA3B gene.

A metastasis suppressor is a protein that acts to slow or prevent metastases from spreading in the body of an organism with cancer. Metastasis is one of the most lethal cancer processes. This process is responsible for about ninety percent of human cancer deaths. Proteins that act to slow or prevent metastases are different from those that act to suppress tumor growth. Genes for about a dozen such proteins are known in humans and other animals.

ING3

Inhibitor of growth protein 3 is a protein that in humans is encoded by the ING3 gene.

JADE1

JADE1 is a protein that in humans is encoded by the JADE1 gene.

ING5

Inhibitor of growth protein 5 is a protein that in humans is encoded by the ING5 gene.

YPEL3 Proteine

Yippee-like 3 (Drosophila) is a protein that in humans is encoded by the YPEL3 gene. YPEL3 has growth inhibitory effects in normal and tumor cell lines. One of five family members (YPEL1-5), YPEL3 was named in reference to its Drosophila melanogaster orthologue. Initially discovered in a gene expression profiling assay of p53 activated MCF7 cells, induction of YPEL3 has been shown to trigger permanent growth arrest or cellular senescence in certain human normal and tumor cell types. DNA methylation of a CpG island near the YPEL3 promoter as well as histone acetylation may represent possible epigenetic mechanisms leading to decreased gene expression in human tumors.

Anticancer genes are genes that, when ectopically overexpressed, specifically destroy tumour cells without harming normal, untransformed cells. This cellular destruction can be due to a variety of mechanisms, such as apoptosis, mitotic catastrophe followed by apoptosis or necrosis, and autophagy. Anticancer genes emerged from studies on cancer cells in the late 1990s. Currently, there have been 291 anticancer genes discovered in the human genome. In order to be classified as an anticancer gene, the gene must have base substitutions leading to missense amino-acid changes, deletions, or insertions leading to frameshifts that alter the protein the gene codes for, increases and decreases in copy-number increases, or gene rearrangements leading to their deregulation.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000153487 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000045969 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Garkavtsev I, Kazarov A, Gudkov A, Riabowol K (Dec 1996). "Suppression of the novel growth inhibitor p33ING1 promotes neoplastic transformation". Nature Genetics. 14 (4): 415–20. doi:10.1038/ng1296-415. PMID   8944021. S2CID   10173092.
  6. Garkavtsev I, Demetrick D, Riabowol K (Jul 1997). "Cellular localization and chromosome mapping of a novel candidate tumor suppressor gene (ING1)". Cytogenetics and Cell Genetics. 76 (3–4): 176–8. doi:10.1159/000134539. PMID   9186514.
  7. 1 2 "Entrez Gene: ING1 inhibitor of growth family, member 1".
  8. 1 2 Vieyra D, Loewith R, Scott M, Bonnefin P, Boisvert FM, Cheema P, Pastyryeva S, Meijer M, Johnston RN, Bazett-Jones DP, McMahon S, Cole MD, Young D, Riabowol K (Aug 2002). "Human ING1 proteins differentially regulate histone acetylation". The Journal of Biological Chemistry. 277 (33): 29832–9. doi: 10.1074/jbc.M200197200 . PMID   12015309.
  9. Xin H, Yoon HG, Singh PB, Wong J, Qin J (Mar 2004). "Components of a pathway maintaining histone modification and heterochromatin protein 1 binding at the pericentric heterochromatin in Mammalian cells". The Journal of Biological Chemistry. 279 (10): 9539–46. doi: 10.1074/jbc.M311587200 . PMID   14665632.
  10. 1 2 3 4 5 Kuzmichev A, Zhang Y, Erdjument-Bromage H, Tempst P, Reinberg D (Feb 2002). "Role of the Sin3-histone deacetylase complex in growth regulation by the candidate tumor suppressor p33(ING1)". Molecular and Cellular Biology. 22 (3): 835–48. doi:10.1128/mcb.22.3.835-848.2002. PMC   133546 . PMID   11784859.
  11. Leung KM, Po LS, Tsang FC, Siu WY, Lau A, Ho HT, Poon RY (Sep 2002). "The candidate tumor suppressor ING1b can stabilize p53 by disrupting the regulation of p53 by MDM2". Cancer Research. 62 (17): 4890–3. PMID   12208736.
  12. Garkavtsev I, Grigorian IA, Ossovskaya VS, Chernov MV, Chumakov PM, Gudkov AV (Jan 1998). "The candidate tumour suppressor p33ING1 cooperates with p53 in cell growth control". Nature. 391 (6664): 295–8. Bibcode:1998Natur.391..295G. doi:10.1038/34675. PMID   9440695. S2CID   4429461.
  13. Scott M, Bonnefin P, Vieyra D, Boisvert FM, Young D, Bazett-Jones DP, Riabowol K (Oct 2001). "UV-induced binding of ING1 to PCNA regulates the induction of apoptosis". Journal of Cell Science. 114 (Pt 19): 3455–62. doi:10.1242/jcs.114.19.3455. PMID   11682605.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.