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Entry version 179 (17 Jun 2020)
Sequence version 1 (01 Oct 1993)
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Protein

Delta(7)-sterol 5(6)-desaturase

Gene

ERG3

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

Catalyzes the introduction of a C-5 double bond in the B ring of ergosterol. May contribute to the regulation of ergosterol biosynthesis.1 Publication

Miscellaneous

Present with 36200 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 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

Fe cationBy similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: ergosterol biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes ergosterol from zymosterol.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Sterol 24-C-methyltransferase (ERG6)
  2. C-8 sterol isomerase (ERG2)
  3. Delta(7)-sterol 5(6)-desaturase (ERG3)
  4. Cytochrome P450 61 (ERG5)
  5. Delta(24(24(1)))-sterol reductase (ERG4)
This subpathway is part of the pathway ergosterol biosynthesis, which is itself part of Steroid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes ergosterol from zymosterol, the pathway ergosterol biosynthesis and in Steroid metabolism.

<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

  • C-5 sterol desaturase activity Source: SGD
  • iron ion binding Source: InterPro
  • oxidoreductase activity Source: GO_Central

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 functionOxidoreductase
Biological processLipid biosynthesis, Lipid metabolism, Steroid biosynthesis, Steroid metabolism, Sterol biosynthesis, Sterol metabolism
LigandIron

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YLR056W-MONOMER
YEAST:YLR056W-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-6807047 Cholesterol biosynthesis via desmosterol
R-SCE-6807062 Cholesterol biosynthesis via lathosterol

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
P32353

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

More...
UniPathwayi
UPA00768;UER00762

<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:
Delta(7)-sterol 5(6)-desaturase (EC:1.14.19.201 Publication)
Alternative name(s):
C-5 sterol desaturase
Ergosterol Delta(5,6) desaturase
Sterol-C5-desaturase
<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:ERG31 Publication
Synonyms:PSO6, SYR1
Ordered Locus Names:YLR056W
ORF Names:L2150
<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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YLR056W

Saccharomyces Genome Database

More...
SGDi
S000004046 ERG3

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 92CytoplasmicSequence analysisAdd BLAST92
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei93 – 113HelicalSequence analysisAdd BLAST21
Topological domaini114 – 140LumenalSequence analysisAdd BLAST27
Transmembranei141 – 161HelicalSequence analysisAdd BLAST21
Topological domaini162 – 242CytoplasmicSequence analysisAdd BLAST81
Transmembranei243 – 263HelicalSequence analysisAdd BLAST21
Topological domaini264 – 365LumenalSequence analysisAdd BLAST102

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<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_00001170271 – 365Delta(7)-sterol 5(6)-desaturaseAdd BLAST365

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-linki324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki344Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P32353

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

More...
PaxDbi
P32353

PRoteomics IDEntifications database

More...
PRIDEi
P32353

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P32353

<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

Interacts with ERG28.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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
31331, 1131 interactors

Database of interacting proteins

More...
DIPi
DIP-4136N

Protein interaction database and analysis system

More...
IntActi
P32353, 12 interactors

Molecular INTeraction database

More...
MINTi
P32353

STRING: functional protein association networks

More...
STRINGi
4932.YLR056W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P32353 protein

<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>Domaini187 – 311Fatty acid hydroxylaseSequence analysisAdd BLAST125

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi200 – 204Histidine box-15
Motifi213 – 217Histidine box-25
Motifi288 – 292Histidine box-35

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The histidine box domains may contain the active site and/or be involved in metal ion binding.

<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 sterol desaturase family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000075101

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_047036_3_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P32353

KEGG Orthology (KO)

More...
KOi
K00227

Identification of Orthologs from Complete Genome Data

More...
OMAi
FLHHKLI

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006694 Fatty_acid_hydroxylase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04116 FA_hydroxylase, 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.

P32353-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLVLEVADH YVLDDLYAKV LPASLAANIP VKWQKLLGLN SGFSNSTILQ
60 70 80 90 100
ETLNSKNAVK ECRRFYGQVP FLFDMSTTSF ASLLPRSSIL REFLSLWVIV
110 120 130 140 150
TIFGLLLYLF TASLSYVFVF DKSIFNHPRY LKNQMAMEIK LAVSAIPWMS
160 170 180 190 200
MLTVPWFVME LNGHSKLYMK IDYENHGVRK LIIEYFTFIF FTDCGVYLAH
210 220 230 240 250
RWLHWPRVYR ALHKPHHKWL VCTPFASHSF HPVDGFLQSI SYHIYPLILP
260 270 280 290 300
LHKVSYLILF TFVNFWTVMI HDGQYLSNNP AVNGTACHTV HHLYFNYNYG
310 320 330 340 350
QFTTLWDRLG GSYRRPDDSL FDPKLRDAKE TWDAQVKEVE HFIKEVEGDD
360
NDRIYENDPN TKKNN
Length:365
Mass (Da):42,730
Last modified:October 1, 1993 - 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:i7F441DA6927A711C
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
M62623 Genomic DNA Translation: AAA34594.1
S46162 Genomic DNA Translation: AAB39844.1
M64989 Genomic DNA Translation: AAA34595.1
D14299 Genomic DNA Translation: BAA20292.1
X94607 Genomic DNA Translation: CAA64303.1
Z73228 Genomic DNA Translation: CAA97586.1
AY692996 Genomic DNA Translation: AAT93015.1
BK006945 Genomic DNA Translation: DAA09374.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JQ1146

NCBI Reference Sequences

More...
RefSeqi
NP_013157.1, NM_001181943.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR056W_mRNA; YLR056W; YLR056W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850745

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR056W

<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
M62623 Genomic DNA Translation: AAA34594.1
S46162 Genomic DNA Translation: AAB39844.1
M64989 Genomic DNA Translation: AAA34595.1
D14299 Genomic DNA Translation: BAA20292.1
X94607 Genomic DNA Translation: CAA64303.1
Z73228 Genomic DNA Translation: CAA97586.1
AY692996 Genomic DNA Translation: AAT93015.1
BK006945 Genomic DNA Translation: DAA09374.1
PIRiJQ1146
RefSeqiNP_013157.1, NM_001181943.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi31331, 1131 interactors
DIPiDIP-4136N
IntActiP32353, 12 interactors
MINTiP32353
STRINGi4932.YLR056W

PTM databases

iPTMnetiP32353

Proteomic databases

MaxQBiP32353
PaxDbiP32353
PRIDEiP32353

Genome annotation databases

EnsemblFungiiYLR056W_mRNA; YLR056W; YLR056W
GeneIDi850745
KEGGisce:YLR056W

Organism-specific databases

EuPathDBiFungiDB:YLR056W
SGDiS000004046 ERG3

Phylogenomic databases

GeneTreeiENSGT00550000075101
HOGENOMiCLU_047036_3_0_1
InParanoidiP32353
KOiK00227
OMAiFLHHKLI

Enzyme and pathway databases

UniPathwayiUPA00768;UER00762
BioCyciMetaCyc:YLR056W-MONOMER
YEAST:YLR056W-MONOMER
ReactomeiR-SCE-6807047 Cholesterol biosynthesis via desmosterol
R-SCE-6807062 Cholesterol biosynthesis via lathosterol
SABIO-RKiP32353

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P32353
RNActiP32353 protein

Family and domain databases

InterProiView protein in InterPro
IPR006694 Fatty_acid_hydroxylase
PfamiView protein in Pfam
PF04116 FA_hydroxylase, 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 nameiERG3_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: P32353
Secondary accession number(s): D6VY58
<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: October 1, 1993
Last modified: June 17, 2020
This is version 179 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
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