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Entry version 188 (02 Dec 2020)
Sequence version 2 (01 Nov 1995)
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Protein

Fructose-2,6-bisphosphatase

Gene

FBP26

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

This is predominantly if not solely a fructose-2,6-bisphosphatase.

Miscellaneous

Present with 1680 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

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 sitei53Fructose 6-phosphateBy similarity1
Binding sitei78Fructose 6-phosphateBy similarity1
<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 sitei104Sequence analysis1
Binding sitei106Fructose 6-phosphateBy similarity1
Binding sitei112Fructose 6-phosphateBy similarity1
Binding sitei169Fructose 6-phosphateBy similarity1
Binding sitei173Fructose 6-phosphateBy similarity1
Binding sitei231Fructose 2,6-bisphosphateBy similarity1
<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>Sitei231Transition state stabilizerBy similarity1
Active sitei232Tele-phosphohistidine intermediateBy similarity1
Binding sitei238Fructose 2,6-bisphosphateBy similarity1
Sitei238Transition state stabilizerBy similarity1
Binding sitei244Fructose 2,6-bisphosphate; via amide nitrogenBy similarity1
Active sitei302Proton donor/acceptorBy similarity1
Binding sitei313Fructose 2,6-bisphosphateBy similarity1
Binding sitei327Fructose 2,6-bisphosphateBy similarity1
Binding sitei331Fructose 2,6-bisphosphateBy similarity1
Binding sitei342Fructose 2,6-bisphosphateBy similarity1
Sitei367Transition state stabilizerBy similarity1
Binding sitei368Fructose 2,6-bisphosphateBy similarity1
Binding sitei372Fructose 2,6-bisphosphateBy similarity1
Binding sitei404ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi20 – 28ATPBy similarity9
Nucleotide bindingi143 – 148ATPBy similarity6
Nucleotide bindingi324 – 327ATPBy similarity4
Nucleotide bindingi368 – 372ATPBy similarity5

<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

  • 6-phosphofructo-2-kinase activity Source: GO_Central
  • ATP binding Source: UniProtKB-KW
  • fructose-2,6-bisphosphate 2-phosphatase 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 functionHydrolase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-9634600, Regulation of glycolysis by fructose 2,6-bisphosphate metabolism

<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:
Fructose-2,6-bisphosphatase (EC:3.1.3.46)
<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:FBP26
Ordered Locus Names:YJL155C
ORF Names:J0575
<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 X

Organism-specific databases

Eukaryotic Pathogen and Host Database Resources

More...
EuPathDBi
FungiDB:YJL155C

Saccharomyces Genome Database

More...
SGDi
S000003691, FBP26

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001799751 – 452Fructose-2,6-bisphosphataseAdd BLAST452

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei435PhosphoserineCombined sources1
Modified residuei446PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32604

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

More...
PaxDbi
P32604

PRoteomics IDEntifications database

More...
PRIDEi
P32604

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32604

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Inhibited by fructose 6-P, activated by glycerol 3-P.

<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 binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33605, 84 interactors

Database of interacting proteins

More...
DIPi
DIP-2593N

Protein interaction database and analysis system

More...
IntActi
P32604, 6 interactors

Molecular INTeraction database

More...
MINTi
P32604

STRING: functional protein association networks

More...
STRINGi
4932.YJL155C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32604, 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
P32604

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 – 2236-phosphofructo-2-kinaseBy similarityAdd BLAST223
Regioni224 – 452Fructose-2,6-bisphosphataseAdd BLAST229

<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 C-terminal section; belongs to the phosphoglycerate mutase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0234, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000182835

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006383_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32604

Identification of Orthologs from Complete Genome Data

More...
OMAi
DMLAWFR

Family and domain databases

Conserved Domains Database

More...
CDDi
cd07067, HP_PGM_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.50.1240, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003094, 6Pfruct_kin
IPR013079, 6Phosfructo_kin
IPR013078, His_Pase_superF_clade-1
IPR029033, His_PPase_superfam
IPR027417, P-loop_NTPase
IPR001345, PG/BPGM_mutase_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10606, PTHR10606, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01591, 6PF2K, 1 hit
PF00300, His_Phos_1, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00991, 6PFRUCTKNASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00855, PGAM, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit
SSF53254, SSF53254, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00175, PG_MUTASE, 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.

P32604-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MGYSTISNDN DIKVCVIMVG LPARGKSFIS QKIIRYLSWL SIKAKCFNVG
60 70 80 90 100
NYRRDVSGNV PMDAEFFNFE NTDNFKLREL AAQNAIKDIV NFFTKEDGSV
110 120 130 140 150
AVFDATNSTR KRRKWLKDIC EKNNIQPMFL ESWSNDHELI INNAKDIGST
160 170 180 190 200
SPDYENSEPH VAEADFLERI RQYERFYEPL DPQKDKDMTF IKLVNIIEEV
210 220 230 240 250
VINKIRTYLE SRIVFYVMNI RPKPKYIWLS RHGESIYNVE KKIGGDSSLS
260 270 280 290 300
ERGFQYAKKL EQLVKESAGE INLTVWTSTL KRTQQTANYL PYKKLQWKAL
310 320 330 340 350
DELDAGVCDG MTYEEIEKEY PEDFKARDND KYEYRYRGGE SYRDVVIRLE
360 370 380 390 400
PVIMELERQE NVLIITHQAV LRCIYAYFMN VPQEESPWMS IPLHTLIKLE
410 420 430 440 450
PRAYGTKVTK IKANIPAVST YKEKGTSQVG ELSQSSTKLH QLLNDSPLED

KF
Length:452
Mass (Da):52,595
Last modified:November 1, 1995 - v2
<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:i228766A302F32F82
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti199E → Q in AAB22823 (PubMed:1322693).Curated1
Sequence conflicti362V → E in AAB22823 (PubMed:1322693).Curated1
Sequence conflicti448 – 449LE → FQ in AAB22823 (PubMed:1322693).Curated2

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
S42124 Genomic DNA Translation: AAB22823.1
Z49430 Genomic DNA Translation: CAA89450.1
BK006943 Genomic DNA Translation: DAA08648.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S56938

NCBI Reference Sequences

More...
RefSeqi
NP_012380.1, NM_001181588.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YJL155C_mRNA; YJL155C; YJL155C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853286

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YJL155C

<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
S42124 Genomic DNA Translation: AAB22823.1
Z49430 Genomic DNA Translation: CAA89450.1
BK006943 Genomic DNA Translation: DAA08648.1
PIRiS56938
RefSeqiNP_012380.1, NM_001181588.1

3D structure databases

SMRiP32604
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33605, 84 interactors
DIPiDIP-2593N
IntActiP32604, 6 interactors
MINTiP32604
STRINGi4932.YJL155C

PTM databases

iPTMnetiP32604

Proteomic databases

MaxQBiP32604
PaxDbiP32604
PRIDEiP32604

Genome annotation databases

EnsemblFungiiYJL155C_mRNA; YJL155C; YJL155C
GeneIDi853286
KEGGisce:YJL155C

Organism-specific databases

EuPathDBiFungiDB:YJL155C
SGDiS000003691, FBP26

Phylogenomic databases

eggNOGiKOG0234, Eukaryota
GeneTreeiENSGT00950000182835
HOGENOMiCLU_006383_1_0_1
InParanoidiP32604
OMAiDMLAWFR

Enzyme and pathway databases

ReactomeiR-SCE-9634600, Regulation of glycolysis by fructose 2,6-bisphosphate metabolism

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32604
RNActiP32604, protein

Family and domain databases

CDDicd07067, HP_PGM_like, 1 hit
Gene3Di3.40.50.1240, 1 hit
InterProiView protein in InterPro
IPR003094, 6Pfruct_kin
IPR013079, 6Phosfructo_kin
IPR013078, His_Pase_superF_clade-1
IPR029033, His_PPase_superfam
IPR027417, P-loop_NTPase
IPR001345, PG/BPGM_mutase_AS
PANTHERiPTHR10606, PTHR10606, 1 hit
PfamiView protein in Pfam
PF01591, 6PF2K, 1 hit
PF00300, His_Phos_1, 1 hit
PRINTSiPR00991, 6PFRUCTKNASE
SMARTiView protein in SMART
SM00855, PGAM, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
SSF53254, SSF53254, 1 hit
PROSITEiView protein in PROSITE
PS00175, PG_MUTASE, 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 nameiF26_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: P32604
Secondary accession number(s): D6VW32
<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: October 1, 1993
Last sequence update: November 1, 1995
Last modified: December 2, 2020
This is version 188 of the entry and version 2 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 X
    Yeast (Saccharomyces cerevisiae) chromosome X: entries and gene names
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