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Entry version 172 (25 May 2022)
Sequence version 2 (01 Oct 1996)
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Protein

Delta(24(24(1)))-sterol reductase ERG4

Gene

ERG4

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

C-24(28) sterol reductase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:8125337, PubMed:10722850, PubMed:12882006).

ERG4 Catalyzes the last step of ergosterol biosynthesis by converting ergosta-5,7,22,24(28)-tetraen-3beta-ol into ergosterol (PubMed:10722850, PubMed:12882006).

The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase ERG9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, the squalene epoxidase ERG1 catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, which is considered to be a rate-limiting enzyme in steroid biosynthesis. Then, the lanosterol synthase ERG7 catalyzes the cyclization of (S)-2,3 oxidosqualene to lanosterol, a reaction that forms the sterol core. In the next steps, lanosterol is transformed to zymosterol through a complex process involving various demethylation, reduction and desaturation reactions. The lanosterol 14-alpha-demethylase ERG11 (also known as CYP51) catalyzes C14-demethylation of lanosterol to produce 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol, which is critical for ergosterol biosynthesis. The C-14 reductase ERG24 reduces the C14=C15 double bond of 4,4-dimethyl-cholesta-8,14,24-trienol to produce 4,4-dimethyl-cholesta-8,24-dienol. 4,4-dimethyl-cholesta-8,24-dienol is substrate of the C-4 demethylation complex ERG25-ERG26-ERG27 in which ERG25 catalyzes the three-step monooxygenation required for the demethylation of 4,4-dimethyl and 4alpha-methylsterols, ERG26 catalyzes the oxidative decarboxylation that results in a reduction of the 3-beta-hydroxy group at the C-3 carbon to an oxo group, and ERG27 is responsible for the reduction of the keto group on the C-3. ERG28 has a role as a scaffold to help anchor ERG25, ERG26 and ERG27 to the endoplasmic reticulum and ERG29 regulates the activity of the iron-containing C4-methylsterol oxidase ERG25. Then, the sterol 24-C-methyltransferase ERG6 catalyzes the methyl transfer from S-adenosyl-methionine to the C-24 of zymosterol to form fecosterol. The C-8 sterol isomerase ERG2 catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase ERG3 then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The C-22 sterol desaturase ERG5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductase ERG4 to produce ergosterol (PubMed:32679672).

1 Publication3 Publications

Miscellaneous

Present with 1640 molecules/cell in log phase SD medium.1 Publication

Caution

Was originally thought to be a transport protein.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 <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 5 of the subpathway that synthesizes ergosterol from zymosterol.1 Publication 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.

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 sitei353NADPBy similarity1
Binding sitei357NADPBy similarity1
Binding sitei393NADP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei445NADPBy similarity1
Binding sitei460NADPBy 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 bindingi405 – 406NADPBy similarity2
Nucleotide bindingi449 – 453NADPBy 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

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
LigandNADP

Enzyme and pathway databases

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

More...
UniPathwayi
UPA00768;UER00764

<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(24(24(1)))-sterol reductase ERG41 Publication (EC:1.3.1.711 Publication)
Alternative name(s):
C-24(28) sterol reductase ERG41 Publication
Ergosterol biosynthetic protein 41 Publication
Sterol Delta(24(28))-reductase ERG41 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ERG41 Publication
Ordered Locus Names:YGL012W
ORF Names:YGL022
<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 VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002980, ERG4

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YGL012W

<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

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 – 39LumenalSequence analysisAdd BLAST39
<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>Transmembranei40 – 64HelicalSequence analysisAdd BLAST25
Topological domaini65 – 101CytoplasmicSequence analysisAdd BLAST37
Transmembranei102 – 123HelicalSequence analysisAdd BLAST22
Topological domaini124 – 138LumenalSequence analysisAdd BLAST15
Transmembranei139 – 157HelicalSequence analysisAdd BLAST19
Topological domaini158 – 174CytoplasmicSequence analysisAdd BLAST17
Transmembranei175 – 197HelicalSequence analysisAdd BLAST23
Topological domaini198 – 232LumenalSequence analysisAdd BLAST35
Transmembranei233 – 249HelicalSequence analysisAdd BLAST17
Topological domaini250 – 326CytoplasmicSequence analysisAdd BLAST77
Transmembranei327 – 346HelicalSequence analysisAdd BLAST20
Topological domaini347 – 414LumenalSequence analysisAdd BLAST68
Transmembranei415 – 439HelicalSequence analysisAdd BLAST25
Topological domaini440 – 473CytoplasmicSequence analysisAdd BLAST34

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

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

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

Leads to pleiotropic defects such as hypersensitivity to divalent cations and a number of drugs such as cycloheximide, miconazole, 4-nitroquinoline, fluconazole, and sodium dodecyl sulfate (PubMed:10722850). Leads also to sensitivity to the Golgi-destabilizing drug brefeldin A (PubMed:10722850).1 Publication

<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_00002074911 – 473Delta(24(24(1)))-sterol reductase ERG4Add BLAST473

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P25340

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

More...
PaxDbi
P25340

PRoteomics IDEntifications database

More...
PRIDEi
P25340

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P25340

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33234, 273 interactors

Database of interacting proteins

More...
DIPi
DIP-7177N

Protein interaction database and analysis system

More...
IntActi
P25340, 13 interactors

Molecular INTeraction database

More...
MINTi
P25340

STRING: functional protein association networks

More...
STRINGi
4932.YGL012W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P25340, 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

AlphaFold Protein Structure Database

More...
AlphaFoldDBi
P25340

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

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SMRi
P25340

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 – 20DisorderedSequence analysisAdd BLAST20

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1 – 15Basic and acidic residuesSequence analysisAdd BLAST15

<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 ERG4/ERG24 family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1435, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000000417

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_015631_3_1_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P25340

Identification of Orthologs from Complete Genome Data

More...
OMAi
KQLPYFC

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001171, Ergosterol_biosynth_ERG4_ERG24
IPR018083, Sterol_reductase_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01222, ERG4_ERG24, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01017, STEROL_REDUCT_1, 1 hit
PS01018, STEROL_REDUCT_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.

P25340-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAKDNSEKLQ VQGEEKKSKQ PVNFLPQGKW LKPNEIEYEF GGTTGVIGML
60 70 80 90 100
IGFPLLMYYM WICAEFYHGK VALPKAGESW MHFIKHLYQL VLENGIPEKY
110 120 130 140 150
DWTIFLTFWV FQIIFYYTLP GIWTKGQPLS HLKGKQLPYF CNAMWTLYVT
160 170 180 190 200
TTLVLVLHFT NLFRLYVIID RFGRIMTCAI ISGFAFSIIL YLWTLFISHD
210 220 230 240 250
YHRMTGNHLY DFFMGAPLNP RWGILDLKMF FEVRLPWFTL YFITLGACLK
260 270 280 290 300
QWETYGYVTP QLGVVMLAHW LYANACAKGE ELIVPTWDMA YEKFGFMLIF
310 320 330 340 350
WNIAGVPYTY CHCTLYLYYH DPSEYHWSTL YNVSLYVVLL CAYYFFDTAN
360 370 380 390 400
AQKNAFRKQM SGDKTGRKTF PFLPYQILKN PKYMVTSNGS YLLIDGWYTL
410 420 430 440 450
ARKIHYTADW TQSLVWALSC GFNSVFPWFF PVFFLVVLIH RAFRDQAKCK
460 470
RKYGKDWDEY CKHCPYVFIP YVF
Length:473
Mass (Da):56,040
Last modified:October 1, 1996 - 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:iB4BFF14559272DD6
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 conflicti33P → L in AAT93224 (PubMed:17322287).Curated1
Sequence conflicti366G → V (PubMed:1882555).Curated1
Sequence conflicti366G → V (PubMed:1882553).Curated1

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
S58126 Genomic DNA Translation: AAD13895.1
S57891 Genomic DNA Translation: AAB19615.1
Z72534 Genomic DNA Translation: CAA96712.1
AY693205 Genomic DNA Translation: AAT93224.1
BK006941 Genomic DNA Translation: DAA08086.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64014

NCBI Reference Sequences

More...
RefSeqi
NP_011503.1, NM_001180877.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL012W_mRNA; YGL012W; YGL012W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852872

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL012W

<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
S58126 Genomic DNA Translation: AAD13895.1
S57891 Genomic DNA Translation: AAB19615.1
Z72534 Genomic DNA Translation: CAA96712.1
AY693205 Genomic DNA Translation: AAT93224.1
BK006941 Genomic DNA Translation: DAA08086.1
PIRiS64014
RefSeqiNP_011503.1, NM_001180877.1

3D structure databases

AlphaFoldDBiP25340
SMRiP25340
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi33234, 273 interactors
DIPiDIP-7177N
IntActiP25340, 13 interactors
MINTiP25340
STRINGi4932.YGL012W

PTM databases

iPTMnetiP25340

Proteomic databases

MaxQBiP25340
PaxDbiP25340
PRIDEiP25340

Genome annotation databases

EnsemblFungiiYGL012W_mRNA; YGL012W; YGL012W
GeneIDi852872
KEGGisce:YGL012W

Organism-specific databases

SGDiS000002980, ERG4
VEuPathDBiFungiDB:YGL012W

Phylogenomic databases

eggNOGiKOG1435, Eukaryota
GeneTreeiENSGT00390000000417
HOGENOMiCLU_015631_3_1_1
InParanoidiP25340
OMAiKQLPYFC

Enzyme and pathway databases

UniPathwayiUPA00768;UER00764

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25340
RNActiP25340, protein

Family and domain databases

InterProiView protein in InterPro
IPR001171, Ergosterol_biosynth_ERG4_ERG24
IPR018083, Sterol_reductase_CS
PfamiView protein in Pfam
PF01222, ERG4_ERG24, 1 hit
PROSITEiView protein in PROSITE
PS01017, STEROL_REDUCT_1, 1 hit
PS01018, STEROL_REDUCT_2, 1 hit

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 nameiERG4_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: P25340
Secondary accession number(s): D6VUC5, E9P929
<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: May 1, 1992
Last sequence update: October 1, 1996
Last modified: May 25, 2022
This is version 172 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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