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Entry version 183 (07 Apr 2021)
Sequence version 1 (01 Jun 1994)
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Protein

Oxysterol-binding protein homolog 4

Gene

KES1

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

Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1 phosphatase in the endoplasmic reticulum (PubMed:16136145, PubMed:22162133). Displays a similar affinity for PI4P and sterols (PubMed:22162133). Binds sterol and PI4P in a mutually exclusive manner (Probable).Curated2 Publications

Miscellaneous

Present with 32200 molecules/cell in log phase SD medium.1 Publication

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 sitei96SterolCombined sources2 Publications1
Binding sitei336Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei340Phosphatidylinositol 4-phosphateCombined sources1 Publication1
Binding sitei344Phosphatidylinositol 4-phosphateCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

Biological processLipid transport, Transport
LigandLipid-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1482801, Acyl chain remodelling of PS
R-SCE-192105, Synthesis of bile acids and bile salts

<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:
Oxysterol-binding protein homolog 4
Alternative name(s):
Protein KES1
<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:KES1Imported
Synonyms:OSH4
Ordered Locus Names:YPL145C
ORF Names:LPI3C, P2614
<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 XVI

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000006066, KES1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YPL145C

<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

Keywords - Cellular componenti

Golgi apparatus, 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi97Y → F: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi109K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1
Mutagenesisi111L → D: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi112N → E: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication1
Mutagenesisi117E → A: Abolishes both cholesterol binding and biological function. 1 Publication1
Mutagenesisi143 – 144HH → AA: Reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 3 Publications2
Mutagenesisi168K → A: Slight reduction in cholesterol transport. 1 Publication1
Mutagenesisi168K → A: Strong reduction in cholesterol transport. 1 Publication1
Mutagenesisi202 – 204HIE → AIA: Strong reduction in cholesterol binding without affecting phosphatidylinositol 4-phosphate binding. 1 Publication3
Mutagenesisi336K → A: Strong reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1
Mutagenesisi340E → A: Abolishes binding to phosphatidylinositol 4-phosphate. 1 Publication1
Mutagenesisi344R → A: Slight reduction in cholesterol transport. Abolishes binding to phosphatidylinositol 4-phosphate. 2 Publications1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the '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_00001003861 – 434Oxysterol-binding protein homolog 4Add BLAST434

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 residuei370PhosphothreonineCombined sources1
Modified residuei389PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P35844

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

More...
PaxDbi
P35844

PRoteomics IDEntifications database

More...
PRIDEi
P35844

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P35844

<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
36038, 296 interactors

Database of interacting proteins

More...
DIPi
DIP-2867N

Protein interaction database and analysis system

More...
IntActi
P35844, 13 interactors

Molecular INTeraction database

More...
MINTi
P35844

STRING: functional protein association networks

More...
STRINGi
4932.YPL145C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P35844, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1434
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P35844

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P35844

<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>Regioni24 – 29Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication6
Regioni109 – 112Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication4
Regioni143 – 144Phosphatidylinositol 4-phosphate bindingCombined sources1 Publication2

<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

Consists of a beta-barrel forming a sterol-binding pocket. When empty, the N-terminal lid (29 residues) is unfolded and leaves the pocket open. Upon sterol binding, this segment forms a lid that blocks the sterol molecule in the pocket (PubMed:16136145). Phosphatidylinositol 4-phosphate (PI4P) binding sites are roughly the same as for sterol. First, the sterol-binding pocket accommodates the PI4P acyl chains. Second, a shallow pocket at the entrance of the tunnel, which contains critical residues such as Lys-336, His-143 and His-144, selects the polar head of PI4P with high specificity. This interaction is probably essential for compensating loose binding of the PI4P acyl chains. Third, the N-terminal lid secures the bound PI4P molecule by wrapping its glycerol moiety (PubMed:22162133).2 Publications

<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 OSBP family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2210, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176691

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_012334_0_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P35844

Identification of Orthologs from Complete Genome Data

More...
OMAi
QGYNQVK

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR037239, OSBP_sf
IPR000648, Oxysterol-bd
IPR018494, Oxysterol-bd_CS

The PANTHER Classification System

More...
PANTHERi
PTHR10972, PTHR10972, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01237, Oxysterol_BP, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF144000, SSF144000, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01013, OSBP, 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.

P35844-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSQYASSSSW TSFLKSIASF NGDLSSLSAP PFILSPISLT EFSQYWAEHP
60 70 80 90 100
ELFLEPSFIN DDNYKEHCLI DPEVESPELA RMLAVTKWFI STLKSQYCSR
110 120 130 140 150
NESLGSEKKP LNPFLGELFV GKWENKEHPE FGETVLLSEQ VSHHPPVTAF
160 170 180 190 200
SIFNDKNKVK LQGYNQIKAS FTKSLMLTVK QFGHTMLDIK DESYLVTPPP
210 220 230 240 250
LHIEGILVAS PFVELEGKSY IQSSTGLLCV IEFSGRGYFS GKKNSFKARI
260 270 280 290 300
YKDSKDSKDK EKALYTISGQ WSGSSKIIKA NKKEESRLFY DAARIPAEHL
310 320 330 340 350
NVKPLEEQHP LESRKAWYDV AGAIKLGDFN LIAKTKTELE ETQRELRKEE
360 370 380 390 400
EAKGISWQRR WFKDFDYSVT PEEGALVPEK DDTFLKLASA LNLSTKNAPS
410 420 430
GTLVGDKEDR KEDLSSIHWR FQRELWDEEK EIVL
Length:434
Mass (Da):49,492
Last modified:June 1, 1994 - 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:i360E4A46ABE2D87B
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 conflicti355I → T in AAS56373 (PubMed:17322287).Curated1

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
U03913 Unassigned DNA Translation: AAA17736.1
U43703 Genomic DNA Translation: AAB68217.1
X96770 Genomic DNA Translation: CAA65548.1
Z73501 Genomic DNA Translation: CAA97849.1
AY558047 Genomic DNA Translation: AAS56373.1
BK006949 Genomic DNA Translation: DAA11290.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S42676

NCBI Reference Sequences

More...
RefSeqi
NP_015180.1, NM_001183959.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YPL145C_mRNA; YPL145C; YPL145C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855958

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YPL145C

<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
U03913 Unassigned DNA Translation: AAA17736.1
U43703 Genomic DNA Translation: AAB68217.1
X96770 Genomic DNA Translation: CAA65548.1
Z73501 Genomic DNA Translation: CAA97849.1
AY558047 Genomic DNA Translation: AAS56373.1
BK006949 Genomic DNA Translation: DAA11290.1
PIRiS42676
RefSeqiNP_015180.1, NM_001183959.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZHTX-ray1.90A2-434[»]
1ZHWX-ray1.70A2-434[»]
1ZHXX-ray1.50A2-434[»]
1ZHYX-ray1.60A2-434[»]
1ZHZX-ray1.90A2-434[»]
1ZI7X-ray2.50A/B/C30-434[»]
3SPWX-ray2.60A/B1-434[»]
4F4BX-ray1.87A/B2-434[»]
4FESX-ray2.00A/B2-434[»]
4JCHX-ray1.70A/B2-434[»]
SMRiP35844
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi36038, 296 interactors
DIPiDIP-2867N
IntActiP35844, 13 interactors
MINTiP35844
STRINGi4932.YPL145C

PTM databases

iPTMnetiP35844

Proteomic databases

MaxQBiP35844
PaxDbiP35844
PRIDEiP35844

Genome annotation databases

EnsemblFungiiYPL145C_mRNA; YPL145C; YPL145C
GeneIDi855958
KEGGisce:YPL145C

Organism-specific databases

SGDiS000006066, KES1
VEuPathDBiFungiDB:YPL145C

Phylogenomic databases

eggNOGiKOG2210, Eukaryota
GeneTreeiENSGT00940000176691
HOGENOMiCLU_012334_0_0_1
InParanoidiP35844
OMAiQGYNQVK

Enzyme and pathway databases

ReactomeiR-SCE-1482801, Acyl chain remodelling of PS
R-SCE-192105, Synthesis of bile acids and bile salts

Miscellaneous databases

EvolutionaryTraceiP35844

Protein Ontology

More...
PROi
PR:P35844
RNActiP35844, protein

Family and domain databases

InterProiView protein in InterPro
IPR037239, OSBP_sf
IPR000648, Oxysterol-bd
IPR018494, Oxysterol-bd_CS
PANTHERiPTHR10972, PTHR10972, 1 hit
PfamiView protein in Pfam
PF01237, Oxysterol_BP, 1 hit
SUPFAMiSSF144000, SSF144000, 1 hit
PROSITEiView protein in PROSITE
PS01013, OSBP, 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 nameiKES1_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: P35844
Secondary accession number(s): D6W3M4, E9P8U8
<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: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 7, 2021
This is version 183 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

3D-structure, Reference proteome

Documents

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