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Entry version 137 (13 Nov 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Protein UPS1, mitochondrial

Gene

UPS1

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

Required for maintenance of normal mitochondrial morphology (PubMed:16754953, PubMed:26071601). Required for PCP1-dependent processing of MGM1 (PubMed:16754953). The UPS1:MDM35 complex mediates the transfer of phosphatidic acid (PA) between liposomes and probably functions as a PA transporter across the mitochondrion intermembrane space (PubMed:26071602, PubMed:26071601, PubMed:26235513). Phosphatidic acid release requires dissociation of the UPS1:MDM35 complex (PubMed:26235513). Phosphatidic acid import is required for cardiolipin (CL) synthesis in the mitochondrial inner membrane (PubMed:26071602). With UPS2, controls the level of cardiolipin in mitochondria (PubMed:19506038). Cardiolipin is a unique phospholipid with four fatty acid chains and is present mainly in the mitochondrial inner membrane where it stabilizes the electron transport chain supercomplex between complexes III and IV through direct interaction of their subunits.6 Publications

Miscellaneous

Present with 704 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_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei26Phosphatidic acid1 Publication1
Binding sitei58Phosphatidic acid1 Publication1
Binding sitei148Phosphatidic acid1 Publication1
Binding sitei152Phosphatidic acid2 Publications1

<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

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32315-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-6803204 TP53 Regulates Transcription of Genes Involved in Cytochrome C Release

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Protein UPS1, mitochondrial
Alternative name(s):
Unprocessed MGM1 protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:UPS1
Ordered Locus Names:YLR193C
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
FungiDB:YLR193C

Saccharomyces Genome Database

More...
SGDi
S000004183 UPS1

<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

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner 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

Cells show slow growth, fragmented mitochondria and have a 50-fold reduced level of s-MGM1. These defects can be complemented by human PRELI or bypassed by growth on a nonfermentable carbon source.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi23F → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi25R → E: Nearly abolishes phosphatidic acid transfer activity. 1 Publication1
Mutagenesisi25R → K: No effect on phosphatidic acid transfer activity. 1 Publication1
Mutagenesisi33H → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-58; E-61; E-148 and E-155. 1 Publication1
Mutagenesisi42R → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi50L → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi54R → E: Decreases phosphatidic acid transfer activity and impairs cardiolipin biosynthesis. 1 Publication1
Mutagenesisi58K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-61; E-148 and E-155. 1 Publication1
Mutagenesisi61K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-148 and E-155. 1 Publication1
Mutagenesisi61K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-155. 1 Publication1
Mutagenesisi62L → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-65. 1 Publication1
Mutagenesisi65W → A: Decreases phosphatidic acid binding and impairs cardiolipin biosynthesis; when associated with A-62. 1 Publication1
Mutagenesisi77W → D: Impairs interaction with MDM35. Reduces ability to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi78I → D: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi84V → E: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi96R → D: Strongly impairs interaction with MDM35. Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi97N → A: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi104M → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-144. 1 Publication1
Mutagenesisi106V → E: Failure to complement the mitochondrial defects of UPS1-deficient cells. 1 Publication1
Mutagenesisi144W → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-104. 1 Publication1
Mutagenesisi148K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-155. 1 Publication1
Mutagenesisi155K → E: Failure to complement the mitochondrial defects of UPS1-deficient cells; when associated with E-33; E-58; E-61 and E-148. 1 Publication1
Mutagenesisi155K → E: Nearly abolishes phosphatidic acid transfer activity; when associated with E-61. 1 Publication1

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002712691 – 175Protein UPS1, mitochondrialAdd BLAST175

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q05776

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

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PaxDbi
Q05776

PRoteomics IDEntifications database

More...
PRIDEi
Q05776

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with MDM35 (PubMed:20622808, PubMed:20657548, PubMed:26071602, PubMed:26071601, PubMed:26235513). Found associated with a 170 kDa complex.

6 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
O602005EBI-30337,EBI-2080774

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31463, 571 interactors

Database of interacting proteins

More...
DIPi
DIP-4798N

Protein interaction database and analysis system

More...
IntActi
Q05776, 1 interactor

Molecular INTeraction database

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MINTi
Q05776

STRING: functional protein association networks

More...
STRINGi
4932.YLR193C

<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

1175
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

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SMRi
Q05776

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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>Domaini2 – 172PRELI/MSF1PROSITE-ProRule annotationAdd BLAST171

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 – 80Required for mitochondrial targeting1 PublicationAdd BLAST80

<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 slowmo family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000185150

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q05776

Identification of Orthologs from Complete Genome Data

More...
OMAi
YSNHVLT

Family and domain databases

Database of protein disorder

More...
DisProti
DP02326

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR006797 PRELI/MSF1_dom
IPR037365 Slowmo/Ups

The PANTHER Classification System

More...
PANTHERi
PTHR11158 PTHR11158, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04707 PRELI, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50904 PRELI_MSF1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q05776-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLLHKSTHI FPTDFASVSR AFFNRYPNPY SPHVLSIDTI SRNVDQEGNL
60 70 80 90 100
RTTRLLKKSG KLPTWVKPFL RGITETWIIE VSVVNPANST MKTYTRNLDH
110 120 130 140 150
TGIMKVEEYT TYQFDSATSS TIADSRVKFS SGFNMGIKSK VEDWSRTKFD
160 170
ENVKKSRMGM AFVIQKLEEA RNPQF
Length:175
Mass (Da):20,108
Last modified:November 1, 1996 - 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:i5B9003B6A2323109
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U14913 Genomic DNA Translation: AAB67434.1
BK006945 Genomic DNA Translation: DAA09512.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48546

NCBI Reference Sequences

More...
RefSeqi
NP_013294.1, NM_001182080.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR193C_mRNA; YLR193C; YLR193C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850890

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR193C

<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
U14913 Genomic DNA Translation: AAB67434.1
BK006945 Genomic DNA Translation: DAA09512.1
PIRiS48546
RefSeqiNP_013294.1, NM_001182080.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XHRX-ray2.55A/B1-175[»]
4XIZX-ray2.00A/B1-170[»]
4YTWX-ray1.40B/D1-170[»]
4YTXX-ray3.20B/D/F/H/J/L/N/P1-170[»]
5JQLX-ray2.90A/C/E/G/I/K1-175[»]
5JQMX-ray1.50A/B/C1-175[»]
6KYLX-ray3.55B/D1-175[»]
SMRiQ05776
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi31463, 571 interactors
DIPiDIP-4798N
IntActiQ05776, 1 interactor
MINTiQ05776
STRINGi4932.YLR193C

Proteomic databases

MaxQBiQ05776
PaxDbiQ05776
PRIDEiQ05776

Genome annotation databases

EnsemblFungiiYLR193C_mRNA; YLR193C; YLR193C
GeneIDi850890
KEGGisce:YLR193C

Organism-specific databases

EuPathDBiFungiDB:YLR193C
SGDiS000004183 UPS1

Phylogenomic databases

HOGENOMiHOG000185150
InParanoidiQ05776
OMAiYSNHVLT

Enzyme and pathway databases

BioCyciYEAST:G3O-32315-MONOMER
ReactomeiR-SCE-6803204 TP53 Regulates Transcription of Genes Involved in Cytochrome C Release

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q05776

Family and domain databases

DisProtiDP02326
InterProiView protein in InterPro
IPR006797 PRELI/MSF1_dom
IPR037365 Slowmo/Ups
PANTHERiPTHR11158 PTHR11158, 1 hit
PfamiView protein in Pfam
PF04707 PRELI, 1 hit
PROSITEiView protein in PROSITE
PS50904 PRELI_MSF1, 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 nameiUPS1_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: Q05776
Secondary accession number(s): D6VYJ6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: November 1, 1996
Last modified: November 13, 2019
This is version 137 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, Complete proteome, Reference proteome

Documents

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