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Entry version 188 (07 Oct 2020)
Sequence version 2 (01 Feb 1995)
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Protein

mRNA-capping enzyme subunit alpha

Gene

CEG1

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

Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.

Miscellaneous

Present with 279 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

a divalent metal cationNote: Divalent metal ions.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei70N6-GMP-lysine intermediate1 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

  • GTP binding Source: UniProtKB-KW
  • mRNA guanylyltransferase activity Source: SGD

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionNucleotidyltransferase, Transferase
Biological processmRNA capping, mRNA processing
LigandGTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G3O-30626-MONOMER

<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:
mRNA-capping enzyme subunit alpha
Alternative name(s):
GTP--RNA guanylyltransferase
Short name:
GTase
mRNA guanylyltransferase (EC:2.7.7.50)
<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:CEG1
Ordered Locus Names:YGL130W
ORF Names:G2853
<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

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGL130W

Saccharomyces Genome Database

More...
SGDi
S000003098, CEG1

<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

Nucleus

<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>Mutagenesisi57E → A: No effect. 1 Publication1
Mutagenesisi58E → A: No effect. 1 Publication1
Mutagenesisi59K → A, T, S or R: No effect. 1 Publication1
Mutagenesisi66Y → A: Temperature-sensitive. 1 Publication1
Mutagenesisi70K → A, R, M, I or T: Lethal. 1 Publication1
Mutagenesisi71T → A: No effect. 1 Publication1
Mutagenesisi72D → A: No effect. 1 Publication1
Mutagenesisi73G → A: Lethal. 1 Publication1
Mutagenesisi95D → A: Temperature-sensitive. 1 Publication1
Mutagenesisi96R → A: Temperature-sensitive. 1 Publication1
Mutagenesisi97E → A: Temperature-sensitive. 1 Publication1
Mutagenesisi107 – 109RFP → AAA: Reduced growth at 25 degrees and lethal at 37 degrees. 1 Publication3
Mutagenesisi114K → A: No effect. 1 Publication1
Mutagenesisi115K → A: No effect. 1 Publication1
Mutagenesisi116K → A: No effect. 1 Publication1
Mutagenesisi117E → A: No effect. 1 Publication1
Mutagenesisi118E → A: No effect. 1 Publication1
Mutagenesisi129L → A: No effect. 1 Publication1
Mutagenesisi130D → A: Lethal. 1 Publication1
Mutagenesisi131G → A: Temperature-sensitive. 1 Publication1
Mutagenesisi132E → A: Lethal. 1 Publication1
Mutagenesisi134V → A: No effect. 1 Publication1
Mutagenesisi218D → A: No effect. 1 Publication1
Mutagenesisi219K → A: No effect. 1 Publication1
Mutagenesisi225D → A: Lethal. 1 Publication1
Mutagenesisi226G → A: Lethal. 1 Publication1
Mutagenesisi241K → A: No effect. 1 Publication1
Mutagenesisi242D → A: No effect. 1 Publication1
Mutagenesisi249K → A: Lethal. 1 Publication1
Mutagenesisi253E → A: No effect. 1 Publication1
Mutagenesisi254N → A: No effect. 1 Publication1
Mutagenesisi255T → A: Temperature-sensitive. 1 Publication1
Mutagenesisi257D → A: Lethal. 1 Publication1
Mutagenesisi274K → A: No effect. 1 Publication1
Mutagenesisi275D → A: No effect. 1 Publication1
Mutagenesisi276D → A: No effect. 1 Publication1
Mutagenesisi395E → A: No effect. 1 Publication1
Mutagenesisi396D → A: No effect. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002101061 – 459mRNA-capping enzyme subunit alphaAdd BLAST459

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q01159

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

More...
PaxDbi
Q01159

PRoteomics IDEntifications database

More...
PRIDEi
Q01159

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q01159

<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

The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33121, 592 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-580, mRNA cap methyltransferase complex

Database of interacting proteins

More...
DIPi
DIP-2298N

Protein interaction database and analysis system

More...
IntActi
Q01159, 27 interactors

Molecular INTeraction database

More...
MINTi
Q01159

STRING: functional protein association networks

More...
STRINGi
4932.YGL130W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q01159, 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

1459
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
Q01159

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
Q01159

<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

<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 eukaryotic GTase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2386, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000156953

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021710_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q01159

KEGG Orthology (KO)

More...
KOi
K00987

Identification of Orthologs from Complete Genome Data

More...
OMAi
DPHILKW

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR001339, mRNA_cap_enzyme
IPR017075, mRNA_cap_enzyme_alpha
IPR013846, mRNA_cap_enzyme_C
IPR012340, NA-bd_OB-fold

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03919, mRNA_cap_C, 1 hit
PF01331, mRNA_cap_enzyme, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF036959, mRNA_cap_alpha, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF50249, SSF50249, 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.

Q01159-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS
60 70 80 90 100
FQHSDVEEKL LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY
110 120 130 140 150
YLVNGFRFPR LPQKKKEELL ETLQDGTLLD GELVIQTNPM TKLQELRYLM
160 170 180 190 200
FDCLAINGRC LTQSPTSSRL AHLGKEFFKP YFDLRAAYPN RCTTFPFKIS
210 220 230 240 250
MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG KDSLLLKWKP
260 270 280 290 300
EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD
310 320 330 340 350
VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR
360 370 380 390 400
IVECAKNQET GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI
410 420 430 440 450
VGDIKRCWDE RRANMAGGSG RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK

YVDEDDWSD
Length:459
Mass (Da):52,764
Last modified:February 1, 1995 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF7F5A3E59EEFA15F
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 conflicti45G → S (PubMed:7500935).Curated1
Sequence conflicti300D → N (PubMed:7500935).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
D10263 Genomic DNA Translation: BAA01103.1
X87252 Genomic DNA Translation: CAA60705.1
Z72652 Genomic DNA Translation: CAA96839.1
BK006941 Genomic DNA Translation: DAA07979.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S59731

NCBI Reference Sequences

More...
RefSeqi
NP_011385.3, NM_001180995.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL130W_mRNA; YGL130W; YGL130W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852747

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL130W

<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
D10263 Genomic DNA Translation: BAA01103.1
X87252 Genomic DNA Translation: CAA60705.1
Z72652 Genomic DNA Translation: CAA96839.1
BK006941 Genomic DNA Translation: DAA07979.1
PIRiS59731
RefSeqiNP_011385.3, NM_001180995.3

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
3KYHX-ray3.00C/D1-459[»]
SMRiQ01159
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33121, 592 interactors
ComplexPortaliCPX-580, mRNA cap methyltransferase complex
DIPiDIP-2298N
IntActiQ01159, 27 interactors
MINTiQ01159
STRINGi4932.YGL130W

PTM databases

iPTMnetiQ01159

Proteomic databases

MaxQBiQ01159
PaxDbiQ01159
PRIDEiQ01159

Genome annotation databases

EnsemblFungiiYGL130W_mRNA; YGL130W; YGL130W
GeneIDi852747
KEGGisce:YGL130W

Organism-specific databases

EuPathDBiFungiDB:YGL130W
SGDiS000003098, CEG1

Phylogenomic databases

eggNOGiKOG2386, Eukaryota
GeneTreeiENSGT00940000156953
HOGENOMiCLU_021710_0_2_1
InParanoidiQ01159
KOiK00987
OMAiDPHILKW

Enzyme and pathway databases

BioCyciMetaCyc:G3O-30626-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ01159

Protein Ontology

More...
PROi
PR:Q01159
RNActiQ01159, protein

Family and domain databases

InterProiView protein in InterPro
IPR001339, mRNA_cap_enzyme
IPR017075, mRNA_cap_enzyme_alpha
IPR013846, mRNA_cap_enzyme_C
IPR012340, NA-bd_OB-fold
PfamiView protein in Pfam
PF03919, mRNA_cap_C, 1 hit
PF01331, mRNA_cap_enzyme, 1 hit
PIRSFiPIRSF036959, mRNA_cap_alpha, 1 hit
SUPFAMiSSF50249, SSF50249, 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 nameiMCE1_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: Q01159
Secondary accession number(s): D6VU18, Q9URD1
<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: April 1, 1993
Last sequence update: February 1, 1995
Last modified: October 7, 2020
This is version 188 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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