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UniProtKB - P34760 (TSA1_YEAST)

Entry version 189 (10 Feb 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
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Protein

Peroxiredoxin TSA1

Gene

TSA1

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

Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events (PubMed:2895105, PubMed:7961686, PubMed:10681558, PubMed:15210711, PubMed:19106090). Protects the cell against the oxidative stress caused by nascent-protein misfolding and aggregation (PubMed:24424024). Relays hydrogen peroxide as a signal to the transcription factor YAP1 by inducing the formation of intramolecular disulfide bonds in YAP1, which causes its nuclear accumulation and activation (PubMed:15706081, PubMed:19106090). Can act alternatively as peroxidase and molecular chaperone. Oxidative stress and heat shock exposure cause a reversible shift of the protein structure from low MW species to high MW complexes, triggering a peroxidase-to-chaperone functional switch. The chaperone function of the protein enhances resistance to heat shock (PubMed:15163410).8 Publications

Miscellaneous

The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys peroxiredoxin, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.1 Publication
Present with 378000 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=3 µM for H2O21 Publication
  2. KM=4 µM for cumene hydroperoxide1 Publication
  3. KM=10 µM for tert-butyl hydroperoxide1 Publication
  4. KM=2 µM for TRX11 Publication
  5. KM=3 µM for TRX21 Publication
  6. KM=12 µM for H2O21 Publication
  7. KM=17.1 µM for cumene hydroperoxide1 Publication
  8. KM=7.9 µM for tert-butyl hydroperoxide1 Publication
  1. Vmax=4.8 µmol/min/mg enzyme for H2O21 Publication
  2. Vmax=2.2 µmol/min/mg enzyme for cumene hydroperoxide1 Publication
  3. Vmax=2.4 µmol/min/mg enzyme for tert-butyl hydroperoxide1 Publication
  4. Vmax=5.5 µmol/min/mg enzyme for TRX11 Publication
  5. Vmax=5.5 µmol/min/mg enzyme for TRX21 Publication
  6. Vmax=0.66 µM/sec/mg enzyme for H2O21 Publication
  7. Vmax=0.56 µM/sec/mg enzyme for cumene hydroperoxide1 Publication
  8. Vmax=0.61 µM/sec/mg enzyme for tert-butyl hydroperoxide1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei45Important for catalytic activity, helps activating the peroxidatic cysteine through H-bonding1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei48Cysteine sulfenic acid (-SOH) intermediate1 Publication1
<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 sitei124SubstrateCombined sources1 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionAntioxidant, Oxidoreductase, Peroxidase

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-5628897, TP53 Regulates Metabolic Genes
R-SCE-6798695, Neutrophil degranulation

Protein family/group databases

MoonProt database of moonlighting proteins

More...MoonProti		P34760

PeroxiBase, a peroxidase database

More...PeroxiBasei		4465, Sce2CysPrx01

<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:
Peroxiredoxin TSA1Curated (EC:1.11.1.241 Publication)
Short name:
Prx
Alternative name(s):
Cytoplasmic thiol peroxidase 11 Publication
Short name:
cTPx 11 Publication
Protector protein1 Publication
Short name:
PRP
Thiol-specific antioxidant protein 11 Publication
Thioredoxin peroxidase type Ia1 Publication
Short name:
TPx type Ia
Thioredoxin-dependent peroxide reductase1 Publication
Thioredoxin-dependent peroxiredoxin TSA1Curated
<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:TSA11 Publication
Synonyms:TPX1, TSA, ZRG14
Ordered Locus Names:YML028WImported
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000004490, TSA1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YML028W

<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

<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

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>Mutagenesisi48C → S: Exists mainly as monomer. Has no peroxiredoxin activity. Fails to protect glutamine synthetase against damage by DTT oxidation. 2 Publications1
Mutagenesisi171C → S: Exists mainly as monomer. Has no peroxiredoxin activity. 2 Publications1

<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 <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemoved1 Publication
<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_00001350952 – 196Peroxiredoxin TSA1Add BLAST195

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki14Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi48Interchain (with C-171); in linked form1 Publication
Disulfide bondi48Interchain (with C-84 in SRX1); transient1 Publication
Cross-linki89Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Cross-linki132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
Disulfide bondi171Interchain (with C-48); in linked form1 Publication
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei174PhosphothreonineCombined sources1

<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

The enzyme can be inactivated by further oxidation of the cysteine sulfenic acid (C(P)-SOH) to sulphinic acid (C(P)-SO2H) instead of its condensation to a disulfide bond. It can be reactivated by forming a transient disulfide bond with sulfiredoxin SRX1, which reduces the cysteine sulfinic acid in an ATP- and Mg-dependent manner.1 Publication

Keywords - PTMi

Disulfide bond, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P34760

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

More...PaxDbi		P34760

PRoteomics IDEntifications database

More...PRIDEi		P34760

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P34760

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P34760

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P34760

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P34760

<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; disulfide-linked, upon oxidation (PubMed:8041739).

Interacts with YAP1 via transient disulfide linkages (PubMed:19106090).

2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35141, 595 interactors

Database of interacting proteins

More...DIPi		DIP-1667N

Protein interaction database and analysis system

More...IntActi		P34760, 38 interactors

Molecular INTeraction database

More...MINTi		P34760

STRING: functional protein association networks

More...STRINGi		4932.YML028W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P34760, 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

Secondary structure

1196
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P34760

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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>Domaini3 – 161ThioredoxinPROSITE-ProRule annotationAdd BLAST159

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>Regioni45 – 47Substrate bindingCombined sources1 Publication3

<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 peroxiredoxin family. AhpC/Prx1 subfamily.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG0852, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153430

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_042529_21_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P34760

Identification of Orthologs from Complete Genome Data

More...OMAi		FWYPKDF

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.40.30.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR000866, AhpC/TSA
IPR024706, Peroxiredoxin_AhpC-typ
IPR019479, Peroxiredoxin_C
IPR036249, Thioredoxin-like_sf
IPR013766, Thioredoxin_domain

Pfam protein domain database

More...Pfami		View protein in Pfam
PF10417, 1-cysPrx_C, 1 hit
PF00578, AhpC-TSA, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000239, AHPC, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52833, SSF52833, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51352, THIOREDOXIN_2, 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P34760-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVAQVQKQAP TFKKTAVVDG VFDEVSLDKY KGKYVVLAFI PLAFTFVCPT 
        60         70         80         90        100
EIIAFSEAAK KFEEQGAQVL FASTDSEYSL LAWTNIPRKE GGLGPINIPL 
       110        120        130        140        150
LADTNHSLSR DYGVLIEEEG VALRGLFIID PKGVIRHITI NDLPVGRNVD 
       160        170        180        190 
EALRLVEAFQ WTDKNGTVLP CNWTPGAATI KPTVEDSKEY FEAANK
Length:196
Mass (Da):21,590
Last modified:January 23, 2007 - v3
<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:i9ACF40E410F2C04A
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
L14640 Unassigned DNA Translation: AAA16374.1
Z46659 Genomic DNA Translation: CAA86627.1
BK006946 Genomic DNA Translation: DAA09870.1

Protein sequence database of the Protein Information Resource

More...PIRi		A47362

NCBI Reference Sequences

More...RefSeqi		NP_013684.1, NM_001182386.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YML028W_mRNA; YML028W; YML028W

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854980

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YML028W

<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
L14640 Unassigned DNA Translation: AAA16374.1
Z46659 Genomic DNA Translation: CAA86627.1
BK006946 Genomic DNA Translation: DAA09870.1
PIRiA47362
RefSeqiNP_013684.1, NM_001182386.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3SBCX-ray2.80A/B/C/D/E/F/G/H/I/J1-196[»]
SMRiP34760
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35141, 595 interactors
DIPiDIP-1667N
IntActiP34760, 38 interactors
MINTiP34760
STRINGi4932.YML028W

Protein family/group databases

MoonProtiP34760
PeroxiBasei4465, Sce2CysPrx01

PTM databases

CarbonylDBiP34760
iPTMnetiP34760

2D gel databases

SWISS-2DPAGEiP34760

Proteomic databases

MaxQBiP34760
PaxDbiP34760
PRIDEiP34760
TopDownProteomicsiP34760

Genome annotation databases

EnsemblFungiiYML028W_mRNA; YML028W; YML028W
GeneIDi854980
KEGGisce:YML028W

Organism-specific databases

SGDiS000004490, TSA1
VEuPathDBiFungiDB:YML028W

Phylogenomic databases

eggNOGiKOG0852, Eukaryota
GeneTreeiENSGT00940000153430
HOGENOMiCLU_042529_21_1_1
InParanoidiP34760
OMAiFWYPKDF

Enzyme and pathway databases

ReactomeiR-SCE-5628897, TP53 Regulates Metabolic Genes
R-SCE-6798695, Neutrophil degranulation

Miscellaneous databases

Protein Ontology

More...PROi		PR:P34760
RNActiP34760, protein

Family and domain databases

Gene3Di3.40.30.10, 1 hit
InterProiView protein in InterPro
IPR000866, AhpC/TSA
IPR024706, Peroxiredoxin_AhpC-typ
IPR019479, Peroxiredoxin_C
IPR036249, Thioredoxin-like_sf
IPR013766, Thioredoxin_domain
PfamiView protein in Pfam
PF10417, 1-cysPrx_C, 1 hit
PF00578, AhpC-TSA, 1 hit
PIRSFiPIRSF000239, AHPC, 1 hit
SUPFAMiSSF52833, SSF52833, 1 hit
PROSITEiView protein in PROSITE
PS51352, THIOREDOXIN_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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<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 nameiTSA1_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: P34760
Secondary accession number(s): D6VZE6
<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: February 1, 1994
Last sequence update: January 23, 2007
Last modified: February 10, 2021
This is version 189 of the entry and version 3 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

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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