ING1 Protein

ING1 Protein Overview

ING1 reagents

Garkavtsev et al. (1996) described a new strategy for the isolation of tumor suppressor genes. This strategy was based on subtractive hybridization followed by selection of transforming genetic suppressor elements. It was used to isolate a novel gene called ING1, which encodes a 33-kD, 294-amino acid protein that displays the characteristics of a tumor suppressor gene. An erratum to Garkavtsev et al. (1996) reported that the initial sequence for ING1 was incorrect. The error appeared to have been the result of a compression introducing a frameshift and of the ING1 gene encoding several differentially spliced isoforms that contained a common 3-prime exon. The correct sequence is available at GenBank AF181849. By SEREX (serologic analysis of recombinant tumor cDNA expression libraries) of a breast cancer cell cDNA library and a testis cDNA library using autologous and allogenic breast cancer sera, Jager et al. (1999) cloned ING1. They identified 4 splice variants that differ in their 5-prime regions. The predicted proteins encoded by variants A (279 amino acids), C (235 amino acids), and D (294 amino acids) share a common 233-amino acid C terminus but differ in their N termini. Variant B encodes an N-terminally truncated protein of 210 amino acids. Jager et al. (1999) evaluated the expression of variants A, B, and C by RT-PCR using variant-specific primers. Variant A was expressed in all normal tissues and cells examined, as well as in all breast cancer and melanoma cell lines examined. Variant B was expressed in testis, liver, and kidney, weakly expressed in colon and brain, and not expressed in breast and cultured melanocytes. Weak expression of variant B was detected in 4 of 6 breast cancer cell lines. Variant C was highly expressed in testis and weakly expressed in brain, but not expressed in breast, colon, kidney, or melanocytes. It was not expressed in breast cancer or melanoma cell lines. Saito et al. (2000) analyzed the complete transcripts, primary structures, and expression of p33/ING1. They found 2 novel, related alternatively spliced transcripts encoding p24/ING1-ALT1 and p47/ING1-ALT2. These transcripts share C-terminal residues with the candidate tumor suppressors p33/ING1. The candidate tumor suppressors p33/ING1 and p24/ING1-ALT1 were coexpressed in a variety of fetal and adult human tissues, but p47/ING1-ALT2 was minimally expressed.

ING1 protein family

Belongs to the ING family.

ING1 protein name

Recommended name
Inhibitor of growth protein 1
Aliases
growth inhibitor ING1, growth inhibitory protein ING1, inhibitor of growth 1, p24ING1c, p33, p33ING1, p33ING1b, p47, p47ING1a, tumor suppressor ING1

ING1 Gene family protein

PHD finger proteins
Approved symbol Common name
ING4 ING4 protein, recombinant
ING5 ING5 protein, recombinant

ING1 Protein Sequence

Species Human ING1 protein
Length 422
Mass (Da) 46738
Sequence Human ING1 protein sequence
Species Mouse ING1 protein
Length 279
Mass (Da) 32109
Sequence Mouse ING1 protein sequence
Species
Length
Mass (Da)
Sequence

ING1 Protein Molecular Weight & PI

Inhibitor of growth protein 1 Homo sapiens (Human).

The parameters have been computed for the following feature

FT CHAIN 1-422 Inhibitor of growth protein 1.

Molecular weight (Da)

46737.81

Theoretical pI

9.28

ING1 Protein Structure

Crystal Structure of the ING1 PHD Finger in complex with a Histone H3K4ME3 peptide
Deposited
2007-07-03   Released:  2008-05-13
Deposition Author(s)
Pena, P.V., Champagne, K., Zhao, R., Kutateladze, T.G.
Organism(s)
Homo sapiens
Expression System
Escherichia coli
Experimental Data Snapshot
Method
X-RAY DIFFRACTION
Resolution
2.1000 Å
R-Value Free
0.264
R-Value Work
0.240
2QIC From PDB

Human ING1 protein Secondary structure

ING1 Protein Interaction

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