Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 157 (17 Jun 2020)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Arsenical-resistance protein ARR1

Gene

ARR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Transcription activator required for resistance to arsenic compounds and for a regulated expression of ACR2, ACR3 and YCF1.6 Publications

Miscellaneous

One of 8 closely related fungi-specific YAP proteins (YAP1 to YAP8), which all seem to be transcription activators of the environmental stress response and metabolism control pathways and to have similar but not identical DNA binding specificities.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Transcriptional activity is controled by regulated degradation by the ubiquitin-proteasome pathway in absence of arsenic (PubMed:17200139). Arsenic-exposure results in stabilization and increased transcriptional activity (PubMed:15147884, PubMed:17200139).2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei132Arsenic (covalent)1 Publication1
Binding sitei137Arsenic (covalent)1 Publication1
Binding sitei274Arsenic (covalent)1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding
Biological processArsenical resistance, Transcription, Transcription regulation

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-34319-MONOMER

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Arsenical-resistance protein ARR11 Publication
Alternative name(s):
AP-1-like transcription factor YAP81 Publication
Arsenic compound resistance protein 11 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ARR11 Publication
Synonyms:ACR11 Publication, YAP81 Publication
Ordered Locus Names:YPR199C
ORF Names:P9677.15
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XVI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YPR199C

Saccharomyces Genome Database

More...
SGDi
S000006403 ARR1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Leads to hypersensitivity to arsenic (PubMed:9234670). Impairs the arsenic-dependent induction of arsenate reductase ARR2, arsenite transporter ARR3 and vacuolar transporter YCF1 (PubMed:11527213, PubMed:15147884).3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi14S → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-16, A-138, A-141, A-145, A-282 and A-292. 1 Publication1
Mutagenesisi16T → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-138, A-141, A-145, A-282 and A-292. 1 Publication1
Mutagenesisi92C → A: Retains about 60% of activity; when assocoated with A-93. 1 Publication1
Mutagenesisi93C → A: Retains about 60% of activity; when assocoated with A-92. 1 Publication1
Mutagenesisi121C → A: Retains about 60% of activity. 1 Publication1
Mutagenesisi132C → A: Impairs nuclear relocalization in response to arsenic and transcriptional activity, and leads to arsenic hypersensitivity. Loses most of the arsenic-binding capacity; when assciated with A-274. 3 Publications1
Mutagenesisi137C → A: Impairs nuclear relocalization in response to arsenic and transcriptional activity, and leads to arsenic hypersensitivity. 2 Publications1
Mutagenesisi138T → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-16, A-141, A-145, A-282 and A-292. 1 Publication1
Mutagenesisi141S → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-16, A-138, A-145, A-282 and A-292. 1 Publication1
Mutagenesisi145S → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-16, A-138, A-141, A-282 and A-292. 1 Publication1
Mutagenesisi274C → A: Impairs nuclear relocalization in response to arsenic and transcriptional activity, and leads to arsenic hypersensitivity. Loses most of the arsenic-binding capacity; when assciated with A-274. 3 Publications1
Mutagenesisi282S → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-16, A-138, A-141, A-145 and A-292. 1 Publication1
Mutagenesisi292S → A: Impairs largely arsenic-induced phosphorylation, shows strong sensitivity to arsenic treatment and a strong, although not complete, reduction in arsenite-induced expression of ARR2 and ARR3; when associated with A-14, A-16, A-138, A-141, A-145 and A-282. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000765281 – 294Arsenical-resistance protein ARR1Add BLAST294

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by HOG1 promotes nuclear localization in the presence of arsenic.1 Publication

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q06596

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
36369, 73 interactors

Database of interacting proteins

More...
DIPi
DIP-4388N

STRING: functional protein association networks

More...
STRINGi
4932.YPR199C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q06596 protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
Q06596

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini22 – 72bZIP1 PublicationAdd BLAST51

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni22 – 45Basic motif1 PublicationAdd BLAST24
Regioni44 – 72Leucine-zipper1 PublicationAdd BLAST29

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the bZIP family. YAP subfamily.Curated

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q06596

KEGG Orthology (KO)

More...
KOi
K09043

Identification of Orthologs from Complete Genome Data

More...
OMAi
YRERRIN

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.238.100, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR023167 Yap1_redox_dom_sf

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF111430 SSF111430, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q06596-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKPRGRKGG RKPSLTPPKN KRAAQLRASQ NAFRKRKLER LEELEKKEAQ
60 70 80 90 100
LTVTNDQIHI LKKENELLHF MLRSLLTERN MPSDERNISK ACCEEKPPTC
110 120 130 140 150
NTLDGSVVLS STYNSLEIQQ CYVFFKQLLS VCVGKNCTVP SPLNSFDRSF
160 170 180 190 200
YPIGCTNLSN DIPGYSFLND AMSEIHTFGD FNGELDSTFL EFSGTEIKEP
210 220 230 240 250
NNFITENTNA IETAAASMVI RQGFHPRQYY TVDAFGGDVL LSAMDIWSFM
260 270 280 290
KVHPKVNTFD LEILGTELKK SATCSNFDIL ISLKHFIKVF SSKL
Length:294
Mass (Da):33,227
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iBDED49B5C0BF8CD3
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U25841 Genomic DNA Translation: AAB64627.1
AY558064 Genomic DNA Translation: AAS56390.1
BK006949 Genomic DNA Translation: DAA11613.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S58828

NCBI Reference Sequences

More...
RefSeqi
NP_015525.1, NM_001184296.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPR199C_mRNA; YPR199C; YPR199C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856329

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPR199C

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U25841 Genomic DNA Translation: AAB64627.1
AY558064 Genomic DNA Translation: AAS56390.1
BK006949 Genomic DNA Translation: DAA11613.1
PIRiS58828
RefSeqiNP_015525.1, NM_001184296.1

3D structure databases

SMRiQ06596
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi36369, 73 interactors
DIPiDIP-4388N
STRINGi4932.YPR199C

Proteomic databases

PaxDbiQ06596

Genome annotation databases

EnsemblFungiiYPR199C_mRNA; YPR199C; YPR199C
GeneIDi856329
KEGGisce:YPR199C

Organism-specific databases

EuPathDBiFungiDB:YPR199C
SGDiS000006403 ARR1

Phylogenomic databases

InParanoidiQ06596
KOiK09043
OMAiYRERRIN

Enzyme and pathway databases

BioCyciYEAST:G3O-34319-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q06596
RNActiQ06596 protein

Family and domain databases

Gene3Di1.10.238.100, 1 hit
InterProiView protein in InterPro
IPR023167 Yap1_redox_dom_sf
SUPFAMiSSF111430 SSF111430, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiARR1_YEAST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q06596
Secondary accession number(s): D6W4J7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: June 17, 2020
This is version 157 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again