Summary
- Splice variants
- Transcript comparison
- Gene alleles
Sequence
- Secondary Structure
Gene families
Literature
Plant Compara
Pan-taxonomic Compara
- Gene Tree
- Orthologues
Ontologies
- GO: Anatomical entity
Phenotypes
Genetic Variation
- Variant table
- Variant image
- Structural variants
Gene expression
Pathway
Molecular interactions
External references
Supporting evidence
ID History
- Gene history

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Ensembl Plants is produced in collaboration with Gramene

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Gene: AT2G33255

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Description

Haloacid dehalogenase-like hydrolase (HAD) superfamily protein [Source:NCBI gene (formerly Entrezgene);Acc:817888]

Location

Chromosome 2: 14,098,778-14,100,623 forward strand.

About this gene

This gene has 1 transcript (splice variant), 138 orthologues and 5 paralogues.

Transcripts

Show transcript tableHide transcript table

Name	Transcript ID	bp	Protein	Biotype	UniProt	RefSeq	Flags
AT2G33255-201	AT2G33255.1	1020	245aa	Gene/transcipt that contains an open reading frame (ORF).Protein coding	Q8RYE9	-	A single transcript chosen for a gene which is the most conserved, most highly expressed, has the longest coding sequence and is represented in other key resources, such as NCBI and UniProt. This is defined in detail on http://www.ensembl.org/info/genome/genebuild/canonical.htmlEnsembl Canonical,

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Literature

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Showing the top 3 hits from Europe PubMed Central

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PubMed ID	Title	Authors	Journal
23179445	HAD hydrolase function unveiled by substrate screening: enzymatic characterization of Arabidopsis thaliana subclass I phosphosugar phosphatase AtSgpp.	Caparrós-Martín JA, McCarthy-Suárez I, Culiáñez-Macià FA.	Planta 237 (4) 2013
28981840	The siRNA suppressor RTL1 is redox-regulated through glutathionylation of a conserved cysteine in the double-stranded-RNA-binding domain.	Charbonnel C, Niazi AK, Elvira-Matelot E, Nowak E, Zytnicki M, de Bures A, Jobet E, Opsomer A, Shamandi N, Nowotny M, Carapito C, Reichheld JP, Vaucheret H, Sáez-Vásquez J.	Nucleic Acids Res 45 (20) 2017
22002057	An FMN hydrolase of the haloacid dehalogenase superfamily is active in plant chloroplasts.	Rawat R, Sandoval FJ, Wei Z, Winkler R, Roje S.	J Biol Chem 286 (49) 2011

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