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Entry version 164 (16 Oct 2019)
Sequence version 1 (01 Nov 1995)
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Protein

Thiamine biosynthetic bifunctional enzyme

Gene

THI6

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>
-Protein inferred from homologyi <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

Essential for thiamine biosynthesis. The kinase activity is involved in the salvage synthesis of TH-P from the thiazole.
Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole monophosphate (THZ-P) and 2-methyl-4-amino-5-hydroxymethyl pyrimidine pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP).By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarityNote: Binds 1 Mg2+ ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole.
Proteins known to be involved in this subpathway in this organism are:
  1. Thiamine biosynthetic bifunctional enzyme (THI6)
This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 4-methyl-5-(2-phosphoethyl)-thiazole from 5-(2-hydroxyethyl)-4-methylthiazole, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole.
Proteins known to be involved in this subpathway in this organism are:
  1. Thiamine biosynthetic bifunctional enzyme (THI6)
This subpathway is part of the pathway thiamine diphosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes thiamine phosphate from 4-amino-2-methyl-5-diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)-thiazole, the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei75HMP-PPBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi76MagnesiumBy similarity1
Metal bindingi95MagnesiumBy similarity1
Binding sitei114HMP-PPBy similarity1
Binding sitei146HMP-PPBy similarity1
Binding sitei181THZ-P; via amide nitrogenBy similarity1
Binding sitei2904-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogenBy similarity1
Binding sitei365ATPBy similarity1
Binding sitei415ATPBy similarity1
Binding sitei4624-methyl-5-(2-hydroxyethyl)thiazole; via amide nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei465Proton acceptor; for hydroxyethylthiazole kinase activityBy similarity1

<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

  • ATP binding Source: UniProtKB-KW
  • hydroxyethylthiazole kinase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
  • thiamine-phosphate diphosphorylase activity Source: SGD

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 functionKinase, Multifunctional enzyme, Transferase
Biological processThiamine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YPL214C-MONOMER
YEAST:YPL214C-MONOMER

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00060;UER00139
UPA00060;UER00141

<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_and_taxonomy_section">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:
Thiamine biosynthetic bifunctional enzyme
Including the following 2 domains:
Thiamine-phosphate synthase (EC:2.5.1.3)
Short name:
TP synthase
Short name:
TPS
Alternative name(s):
Thiamine-phosphate pyrophosphorylase
Short name:
TMP pyrophosphorylase
Short name:
TMP-PPase
Hydroxyethylthiazole kinase (EC:2.7.1.50)
Alternative name(s):
4-methyl-5-beta-hydroxyethylthiazole kinase
Short name:
TH kinase
Short name:
THZ kinase
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:THI6
Ordered Locus Names:YPL214C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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:YPL214C

Saccharomyces Genome Database

More...
SGDi
S000006135 THI6

<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

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001570901 – 540Thiamine biosynthetic bifunctional enzymeAdd BLAST540

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P41835

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

More...
PaxDbi
P41835

PRoteomics IDEntifications database

More...
PRIDEi
P41835

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homooctamer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
35971, 113 interactors

Database of interacting proteins

More...
DIPi
DIP-1666N

Protein interaction database and analysis system

More...
IntActi
P41835, 1 interactor

Molecular INTeraction database

More...
MINTi
P41835

STRING: functional protein association networks

More...
STRINGi
4932.YPL214C

<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
P41835

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

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>Regioni1 – 238Thiamine-phosphate synthaseAdd BLAST238
Regioni43 – 47HMP-PP bindingBy similarity5
Regioni143 – 145THZ-P bindingBy similarity3
Regioni209 – 210THZ-P bindingBy similarity2
Regioni239 – 540Hydroxyethylthiazole kinaseAdd BLAST302

<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

In the N-terminal section; belongs to the thiamine-phosphate synthase family.Curated
In the C-terminal section; belongs to the Thz kinase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000214306

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P41835

KEGG Orthology (KO)

More...
KOi
K14154

Identification of Orthologs from Complete Genome Data

More...
OMAi
PIMANYA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01170 THZ_kinase, 1 hit
cd00564 TMP_TenI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.20.70, 1 hit
3.40.1190.20, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00097 TMP_synthase, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR013785 Aldolase_TIM
IPR000417 Hyethyz_kinase
IPR029056 Ribokinase-like
IPR036206 ThiamineP_synth_sf
IPR022998 ThiamineP_synth_TenI
IPR034291 TMP_synthase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02110 HK, 1 hit
PF02581 TMP-TENI, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01099 HYETHTZKNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51391 SSF51391, 1 hit
SSF53613 SSF53613, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00693 thiE, 1 hit
TIGR00694 thiM, 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_length">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_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

P41835-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVFTKEEVDY SLYLVTDSTM LPPGTTLCSQ VEAGLKNGVT LVQIREKDIE
60 70 80 90 100
TKNFVAEALE VQKICKKYNV PLIINDRIDV AMAIDADGVH VGQDDMPIPM
110 120 130 140 150
VRKLLGPSKI LGWSVGKPSE VETLAKWGPD MVDYIGVGTL FPTSTKKNPK
160 170 180 190 200
KSPMGPQGAI AILDALEEFK ATWCRTVGIG GLHPDNIQRV LCQCVASNGK
210 220 230 240 250
RSLDGISLVS DIMAAPDACA ATKRLRGLLD ATRYQFVECE LNNTFPTTTS
260 270 280 290 300
IQNVISQVSN NRPLVQHITN KVHQNFGANV TLALGSSPIM SEIESEVSEL
310 320 330 340 350
ARIPNASLLL NTGSVAPIEM LKAAINAYNE VNRPITFDPV GYSATETRLC
360 370 380 390 400
LNNTLLTYGQ FACIKGNCSE ILSLAKLNNH KMKGVDSSSG KTNIDTLVRA
410 420 430 440 450
TQIVAFQYRT VAVCTGEFDC VADGTFGGEY KLSSGTEGIT AEDLPCVIIE
460 470 480 490 500
DGPIPIMGDI TASGCSLGST IASFIGGLDS TGKLFDAVVG AVLLYKSAGK
510 520 530 540
LASTRCQGSG SFHVELIDAL YQLFHENKPE KWSASLKKFK
Length:540
Mass (Da):58,059
Last modified:November 1, 1995 - 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:iF34FA1E0B76E3930
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural varianti370E → K in THI6-3; possesses TMP-PPASE activity only. 1
Natural varianti476G → D in THI6-2; both enzyme activities greatly decreased. 1
Natural varianti510G → D in THI6-1; both enzyme activities greatly decreased. 1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D31908 Genomic DNA Translation: BAA06703.1
Z73570 Genomic DNA Translation: CAA97929.1
BK006949 Genomic DNA Translation: DAA11222.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A55145

NCBI Reference Sequences

More...
RefSeqi
NP_015110.1, NM_001184028.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL214C_mRNA; YPL214C; YPL214C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855887

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL214C

<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
D31908 Genomic DNA Translation: BAA06703.1
Z73570 Genomic DNA Translation: CAA97929.1
BK006949 Genomic DNA Translation: DAA11222.1
PIRiA55145
RefSeqiNP_015110.1, NM_001184028.1

3D structure databases

SMRiP41835
ModBaseiSearch...

Protein-protein interaction databases

BioGridi35971, 113 interactors
DIPiDIP-1666N
IntActiP41835, 1 interactor
MINTiP41835
STRINGi4932.YPL214C

Proteomic databases

MaxQBiP41835
PaxDbiP41835
PRIDEiP41835

Genome annotation databases

EnsemblFungiiYPL214C_mRNA; YPL214C; YPL214C
GeneIDi855887
KEGGisce:YPL214C

Organism-specific databases

EuPathDBiFungiDB:YPL214C
SGDiS000006135 THI6

Phylogenomic databases

HOGENOMiHOG000214306
InParanoidiP41835
KOiK14154
OMAiPIMANYA

Enzyme and pathway databases

UniPathwayiUPA00060;UER00139
UPA00060;UER00141
BioCyciMetaCyc:YPL214C-MONOMER
YEAST:YPL214C-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P41835

Family and domain databases

CDDicd01170 THZ_kinase, 1 hit
cd00564 TMP_TenI, 1 hit
Gene3Di3.20.20.70, 1 hit
3.40.1190.20, 1 hit
HAMAPiMF_00097 TMP_synthase, 1 hit
InterProiView protein in InterPro
IPR013785 Aldolase_TIM
IPR000417 Hyethyz_kinase
IPR029056 Ribokinase-like
IPR036206 ThiamineP_synth_sf
IPR022998 ThiamineP_synth_TenI
IPR034291 TMP_synthase
PfamiView protein in Pfam
PF02110 HK, 1 hit
PF02581 TMP-TENI, 1 hit
PRINTSiPR01099 HYETHTZKNASE
SUPFAMiSSF51391 SSF51391, 1 hit
SSF53613 SSF53613, 1 hit
TIGRFAMsiTIGR00693 thiE, 1 hit
TIGR00694 thiM, 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 nameiTHI6_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: P41835
Secondary accession number(s): D6W3F6
<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_and_isoforms">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, 1995
Last sequence update: November 1, 1995
Last modified: October 16, 2019
This is version 164 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome XVI
    Yeast (Saccharomyces cerevisiae) chromosome XVI: entries and gene names
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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