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Search results 201 to 239 out of 239 for Fhit

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0.022s

Type

Details

Score

Publication

15591090 | J:96327

First Author:	Lubet RA
Year:	2005
Journal:	Carcinogenesis
Title:	4-Hydroxybutyl(butyl)nitrosamine-induced urinary bladder cancers in mice: characterization of FHIT and survivin expression and chemopreventive effects of indomethacin.
Volume:	26
Issue:	3
Pages:	571-8

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Publication

9225975 | J:42119

First Author:	Lux A
Year:	1997
Journal:	Hum Genet
Title:	Identification of novel 'expressed sequence tags' within the FHIT gene locus in human chromosome region 3p14.2.
Volume:	100
Issue:	1
Pages:	90-5

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Allele

Fhit<em1Smoc> | MGI:7291982

Name:	fragile histidine triad gene; endonuclease-mediated mutation 1, Shanghai Model Organisms Center
Allele Type:	Endonuclease-mediated
Attribute String:	Null/knockout

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Strain

MGI:6428652 | C57BL/6J-Fhit<em1Smoc>/Smoc

Attribute String:

coisogenic, mutant strain, endonuclease-mediated mutation

•

Publication

10959838 | -

First Author:	Pace HC
Year:	2000
Journal:	Curr Biol
Title:	Crystal structure of the worm NitFhit Rosetta Stone protein reveals a Nit tetramer binding two Fhit dimers.
Volume:	10
Issue:	15
Pages:	907-17

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Publication

9689122 | -

First Author:	Gemmill RM
Year:	1998
Journal:	Proc Natl Acad Sci U S A
Title:	The hereditary renal cell carcinoma 3;8 translocation fuses FHIT to a patched-related gene, TRC8.
Volume:	95
Issue:	16
Pages:	9572-7

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Publication

19395373 | J:149570

First Author:	Zhang H
Year:	2009
Journal:	Int Immunol
Title:	Mammalian nitrilase 1 homologue Nit1 is a negative regulator in T cells.
Volume:	21
Issue:	6
Pages:	691-703

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Publication

15703176 | -

First Author:	Chou TF
Year:	2005
Journal:	J Biol Chem
Title:	31P NMR and genetic analysis establish hinT as the only Escherchia coli purine nucleoside phosphoramidase and as essential for growth under high salt conditions.
Volume:	280
Issue:	15
Pages:	15356-61

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Protein Domain

IPR001310 | Histidine_triad_HIT

Type:

Family

Description:

The Histidine Triad (HIT) motif, His-x-His-x-His-x-x (x, ahydrophobic amino acid) was identified as being highly conserved in a variety of organisms [, ]. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into three branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the FHIT branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases [, ]. In budding yeast Hnt1 has been shown to have adenosine monophosphoramidase activity and function as positive regulators of Cdk7/Kin28 in vivo [, ]. FHIT plays a very important role in the development of tumours. In fact, FHIT deletions are among the earliest and most frequent genetic alterations in the development of tumours [, ]. The third branch of the HIT superfamily, which includes GalT homologues, contains a related His-X-His-X-Gln motif and transfers nucleoside monophosphate moieties to phosphorylated second substrates ratherthan hydrolysing them [].

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Publication

1899836 | -

First Author:	Mozier NM
Year:	1991
Journal:	FEBS Lett
Title:	Characterization of a novel zinc binding site of protein kinase C inhibitor-1.
Volume:	279
Issue:	1
Pages:	14-8

•

Publication

2307677 | -

First Author:	Pearson JD
Year:	1990
Journal:	J Biol Chem
Title:	Amino acid sequence and characterization of a protein inhibitor of protein kinase C.
Volume:	265
Issue:	8
Pages:	4583-91

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Protein Domain

IPR019808 | Histidine_triad_CS

Type:

Conserved_site

Description:

The Histidine Triad (HIT) motif, His-x-His-x-His-x-x (x, ahydrophobic amino acid) was identified as being highly conserved in a variety of organisms []. Crystal structure of rabbit Hint, purified as an adenosine and AMP-binding protein, showed that proteins in the HITsuperfamily are conserved as nucleotide-binding proteins and that Hint homologues, which are found in all forms of life, are structurally related to Fhit homologues and GalT-related enzymes, which have more restricted phylogenetic profiles []. Hint homologues including rabbit Hint and yeastHnt1 hydrolyse adenosine 5' monophosphoramide substrates such as AMP-NH2 andAMP-lysineto AMP plus the amine product and function as positive regulatorsof Cdk7/Kin28 in vivo []. Fhit homologues are diadenosine polyphosphate hydrolases []and function as tumour suppressors in human and mouse []though the tumour suppressing function of Fhit does not depend on ApppA hydrolysis []. The third branch of the HIT superfamily, which includesGalT homologues, contains a related His-X-His-X-Gln motif and transfersnucleoside monophosphate moieties to phosphorylated second substrates ratherthan hydrolysing them [].The bovine protein kinase C inhibitor, PKCI-1, is an inhibitor protein that binds zinc without the use of zinc-finger motifs []. Each protein molecule binds one zinc ion via a novel binding site containing 3 closely-spaced histidine residues []. This region, referred to as the histidine triad (HIT) [], has been identified in various prokaryotic and eukaryotic proteins of uncertain function [].The signature pattern used in this entry contains the region of the histidine triad and includes the three conserved histidine residues which are thought to bind the zinc ion.

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Publication

9164465 | -

First Author:	Brenner C
Year:	1997
Journal:	Nat Struct Biol
Title:	Crystal structures of HINT demonstrate that histidine triad proteins are GalT-related nucleotide-binding proteins.
Volume:	4
Issue:	3
Pages:	231-8

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Publication

11805111 | -

First Author:	Bieganowski P
Year:	2002
Journal:	J Biol Chem
Title:	Adenosine monophosphoramidase activity of Hint and Hnt1 supports function of Kin28, Ccl1, and Tfb3.
Volume:	277
Issue:	13
Pages:	10852-60

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Publication

28373563 | J:242138

First Author:	Peracchi A
Year:	2017
Journal:	Proc Natl Acad Sci U S A
Title:	Nit1 is a metabolite repair enzyme that hydrolyzes deaminated glutathione.
Volume:	114
Issue:	16
Pages:	E3233-E3242

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Publication

14699117 | -

First Author:	Carpio RV
Year:	2004
Journal:	J Biol Chem
Title:	Role of the histidine triad-like motif in nucleotide hydrolysis by the rotavirus RNA-packaging protein NSP2.
Volume:	279
Issue:	11
Pages:	10624-33

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Publication

9261067 | -

First Author:	Lima CD
Year:	1997
Journal:	Structure
Title:	MAD analysis of FHIT, a putative human tumor suppressor from the HIT protein family.
Volume:	5
Issue:	6
Pages:	763-74

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Publication

8812426 | -

First Author:	Brzoska PM
Year:	1996
Journal:	Genomics
Title:	Cloning, mapping, and in vivo localization of a human member of the PKCI-1 protein family (PRKCNH1).
Volume:	36
Issue:	1
Pages:	151-6

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Publication

22674578 | -

First Author:	Chien CH
Year:	2012
Journal:	J Biol Chem
Title:	Structural insights into the catalytic active site and activity of human Nit2/ω-amidase: kinetic assay and molecular dynamics simulation.
Volume:	287
Issue:	31
Pages:	25715-26

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Publication

17488281 | -

First Author:	Lin CH
Year:	2007
Journal:	FEBS J
Title:	Growth inhibitory effect of the human NIT2 gene and its allelic imbalance in cancers.
Volume:	274
Issue:	11
Pages:	2946-56

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Protein Domain

IPR026026 | HIT_Hint

Type:

Family

Description:

HIT (Histidine triad) proteins, named for a motif related to the sequence HxHxH/Qxx (x, a hydrophobic amino acid), are a superfamily of nucleotide hydrolases and transferases that act on the alpha-phosphate of ribonucleotides. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified in the literature into three major branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the Fhit branch, which consists of diadenosine polyphosphate hydrolases, and the GalT branch, consisting of specific nucleoside monophosphate transferases. Further sequence analysis reveals several new, closely related, yet uncharacterised subgroups. This group includes bacterial proteins which are members from the Hint branch of hydrolases. For additional information please see [, , , , , ].

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Protein Domain

IPR045254 | Nit1/2_C-N_Hydrolase

Type:

Domain

Description:

Proteins containing this domain include mammalian Nit1 and Nit2, the Nit1-like domain of the invertebrate NitFhit, yeast Nit3 and various uncharacterized bacterial and archaeal Nit-like proteins. In general, they are amidases involved in various metabolic processes. Nit1 is a deaminated glutathione amidase [], while Nit2 is an omega-amidase []. They are candidate tumour suppressor proteins []. In NitFhit, the Nit1-like domain is encoded as a fusion protein with the non-homologous tumour suppressor, fragile histidine triad (Fhit) []. Mammalian Nit1 and Fhit may affect distinct signal pathways, and both may participate in DNA damage-induced apoptosis []. Nit1 is a negative regulator in T cells []. Overexpression of Nit2 in HeLa cells leads to a suppression of cell growth through cell cycle arrest in G2 [].

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Protein Domain

IPR039384 | HINT

Type:

Family

Description:

HINT (histidine triad nucleotide-binding protein) are related to the HIT family members that carry a motif HxHxH/Qxx (x, is a hydrophobic amino acid) []. On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into three branches: the Hint branch, which consists of adenosine 5' -monophosphoramide hydrolases, the FHIT branch, that consists of diadenosine polyphosphate hydrolases, and the GalT branch consisting of specific nucloside monophosphate transferases []. HINT family includes members from all three forms of cellular life. In budding yeast Hnt1 has been shown to have adenosine monophosphoramidase activity []. It is involved in secretion, peroxisome formation and gene expression [, ]. The bacterial and archaeal members of this family are mostly uncharacterised.

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Protein

Q9D0S9

Organism:	Mus musculus/domesticus
Length:	163
Fragment?:	false

•

Protein

P70349

Organism:	Mus musculus/domesticus
Length:	126
Fragment?:	false

•

Protein

Q5M9J2

Organism:	Mus musculus/domesticus
Length:	163
Fragment?:	false

•

Publication

11979549 | J:76101

First Author:	Krummel KA
Year:	2002
Journal:	Genes Chromosomes Cancer
Title:	The common fragile site FRA16D and its associated gene WWOX are highly conserved in the mouse at Fra8E1.
Volume:	34
Issue:	2
Pages:	154-67

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Publication

11423973 | J:70638

First Author:	Powell DJ Jr
Year:	2001
Journal:	Oncogene
Title:	Altered gene expression in immunogenic poorly differentiated thyroid carcinomas from RET/PTC3p53-/- mice.
Volume:	20
Issue:	25
Pages:	3235-46

•

Publication

18167129 | J:142485

First Author:	Yutori H
Year:	2008
Journal:	Cancer Sci
Title:	Restoration of fragile histidine triad expression restores Chk2 activity in response to ionizing radiation in oral squamous cell carcinoma cells.
Volume:	99
Issue:	3
Pages:	524-30

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Publication

1860879 | -

First Author:	Fröhlich KU
Year:	1991
Journal:	J Cell Biol
Title:	Yeast cell cycle protein CDC48p shows full-length homology to the mammalian protein VCP and is a member of a protein family involved in secretion, peroxisome formation, and gene expression.
Volume:	114
Issue:	3
Pages:	443-53

•

Publication

9770345 | J:50522

First Author:	Klein MG
Year:	1998
Journal:	Exp Cell Res
Title:	Characterization of PKCI and comparative studies with FHIT, related members of the HIT protein family.
Volume:	244
Issue:	1
Pages:	26-32

•

Publication

18155953 | J:138915

First Author:	De Flora S
Year:	2008
Journal:	Mutat Res
Title:	High susceptibility of neonatal mice to molecular, biochemical and cytogenetic alterations induced by environmental cigarette smoke and light.
Volume:	659
Issue:	1-2
Pages:	137-46

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Protein

Q9DAR7

Organism:	Mus musculus/domesticus
Length:	338
Fragment?:	false

•

Protein

B0R1E3

Organism:	Mus musculus/domesticus
Length:	119
Fragment?:	false

•

Protein

Q9JHW2

Organism:	Mus musculus/domesticus
Length:	276
Fragment?:	false

•

Protein

Q8VDK1

Organism:	Mus musculus/domesticus
Length:	323
Fragment?:	false

•

Protein

A0A338P6G0

Organism:	Mus musculus/domesticus
Length:	196
Fragment?:	false

•

Protein

Q7TQC5

Organism:	Mus musculus/domesticus
Length:	342
Fragment?:	false

•

Protein

Q6IR21

Organism:	Mus musculus/domesticus
Length:	352
Fragment?:	true

•

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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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