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Search results 101 to 119 out of 119 for Thap4

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0.011s

Type

Details

Score

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

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Publication

- | J:144087

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform

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UniProt Feature

Begin:	1
Description:	Peroxynitrite isomerase THAP4
Type:	chain
End:	569

•

Protein

A0A087WPE8

Organism:	Mus musculus/domesticus
Length:	182
Fragment?:	true

•

Protein

A0A0J9YU08

Organism:	Mus musculus/domesticus
Length:	165
Fragment?:	false

•

Protein

Q6P3Z3

Organism:	Mus musculus/domesticus
Length:	569
Fragment?:	false

•

Protein

Q6P3Z3-2

Organism:	Mus musculus/domesticus
Length:	379
Fragment?:	false

•

Protein

A0A087WQL4

Organism:	Mus musculus/domesticus
Length:	31
Fragment?:	true

•

Publication

17172346 | -

First Author:	Shepard W
Year:	2007
Journal:	J Bacteriol
Title:	The crystal structure of Rv0813c from Mycobacterium tuberculosis reveals a new family of fatty acid-binding protein-like proteins in bacteria.
Volume:	189
Issue:	5
Pages:	1899-904

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Protein Domain

IPR014878 | THAP4-like_heme-bd

Type:

Domain

Description:

Nitrobindins (Nbs), constituting a heme-protein family spanning from bacteria to Homo sapiens, display an all-β-barrel structural organization. Proteins containing this domain are putatively related to fatty acid-binding proteins (FABPs) [].This domain can be found in THAP4 from mammals and At1g79260 from Arabidopsis. THAP4 catalyzes the heme-based conversion of peroxynitrite into nitrate/NO3- in vitro []. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport []. This entry also includes the β-barrel domain of Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology [].

•

Protein Domain

IPR045165 | Nitrobindin

Type:

Family

Description:

Nitrobindins (Nbs) are evolutionary conserved all-β-barrel heme-proteins displaying a highly solvent-exposed heme-Fe(III) atom. Mycobacterium tuberculosis Nb (Mt-Nb(III) and the C terminus of Homo sapiens Nb (Hs-Nb(III)) share this β-barrel structure, suggesting that Nb may act as a sensor possibly modulating the THAP4 transcriptional activity residing in the N-terminal region []. Ferric nitrobindin-like proteins that lack the conserved His residue which binds heme iron are also included in the Nb family.Mt-Nb(III) is a peroxynitrite isomerase that converts peroxynitrite to nitrate. It may be required to scavenge reactive nitrogen and oxygen species produced by the host during the immunity response []. In humans THAP4 catalyses the heme-based conversion of peroxynitrite into nitrate/NO3 in vitro []. At1g79260 is a nitrophorin-like heme-binding protein that may reversibly bind nitric oxide (NO) and be involved in NO transport []. This entry also includes Caenorhabditis elegans protein male abnormal 7 (Mab-7) which plays an important role in determining body shape and sensory ray morphology [].

•

Publication

19938152 | -

First Author:	Bianchetti CM
Year:	2010
Journal:	Proteins
Title:	The structure and NO binding properties of the nitrophorin-like heme-binding protein from Arabidopsis thaliana gene locus At1g79260.1.
Volume:	78
Issue:	4
Pages:	917-31

•

Publication

30524950 | -

First Author:	De Simone G
Year:	2018
Journal:	FEBS Open Bio
Title:	Human nitrobindin: the first example of an all-β-barrel ferric heme-protein that catalyzes peroxynitrite detoxification.
Volume:	8
Issue:	12
Pages:	2002-2010

•

Publication

17959165 | -

First Author:	Tsang SW
Year:	2007
Journal:	Dev Biol
Title:	mab-7 encodes a novel transmembrane protein that orchestrates sensory ray morphogenesis in C. elegans.
Volume:	312
Issue:	1
Pages:	353-66

•

Publication

32295384 | -

First Author:	De Simone G
Year:	2020
Journal:	Antioxid Redox Signal
Title:	Mycobacterial and Human Nitrobindins: Structure and Function.
Volume:	33
Issue:	4
Pages:	229-246

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Protein Domain

IPR022939 | Nb(III)_bact/plant

Type:

Family

Description:

This entry includes the Nitrobindin family members mostly from bacteria and plants. Mycobacterium tuberculosis Nb (Mt-Nb(III) is a peroxynitrite isomerase, which is a heme-binding protein able to scavenge peroxynitrite and to protect free L-tyrosine against peroxynitrite-mediated nitration, by acting as a peroxynitrite isomerase that converts peroxynitrite to nitrate []. This entry also includes ferric nitrobindin-like protein, lacks the conserved His residue that binds heme iron.Nitrobindins (Nbs) are evolutionary conserved all-β-barrel heme-proteins displaying a highly solvent-exposed heme-Fe(III) atom. Mycobacterium tuberculosis Nb (Mt-Nb(III) and the C terminus of Homo sapiens Nb (Hs-Nb(III)) share this β-barrel structure, suggesting that Nb may act as a sensor possibly modulating the THAP4 transcriptional activity residing in the N-terminal region []. Ferric nitrobindin-like proteins that lack the conserved His residue which binds heme iron are also included in the Nb family.

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

•

Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

•

Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

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