Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 157 (31 Jul 2019)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Ribosomal RNA small subunit methyltransferase NEP1

Gene

EMG1

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

S-adenosyl-L-methionine-dependent pseudouridine N1-methyltransferase that methylates pseudouridine at position 1189 (Psi1189) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. N1-methylation is independent on acp-modification at the N3-position of U1191. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 (RPS19A/RPS19B) during the formation of pre-ribosomes.5 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei90Stabilizes Arg-881 Publication1
<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 sitei180S-adenosyl-L-methionine; via carbonyl oxygen2 Publications1
Binding sitei207S-adenosyl-L-methionine; via amide nitrogen2 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

Molecular functionMethyltransferase, Ribonucleoprotein, RNA-binding, rRNA-binding, Transferase
Biological processRibosome biogenesis, rRNA processing
LigandS-adenosyl-L-methionine

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-32309-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

<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:
Ribosomal RNA small subunit methyltransferase NEP11 Publication (EC:2.1.1.2601 Publication)
Alternative name(s):
18S rRNA (pseudouridine(1189)-N1)-methyltransferase1 Publication
Short name:
18S rRNA Psi1189 methyltransferase1 Publication
Essential for mitotic growth protein 11 Publication
Nucleolar essential protein 11 Publication
<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:EMG11 Publication
Synonyms:NEP11 Publication
Ordered Locus Names:YLR186WImported
ORF Names:L9470.5
<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

More...
EuPathDBi
FungiDB:YLR186W

Saccharomyces Genome Database

More...
SGDi
S000004176 EMG1

<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

<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

Depletion of EMG1 affects growth and leads to strong ribosome biogenesis defects, with defects in 20S pre-rRNA and mature 18S rRNA species.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>Mutagenesisi88R → A: Loss of substrate rRNA binding. 1 Publication1
Mutagenesisi88R → D: Loss of substrate rRNA binding. No effect on growth. 1 Publication1
Mutagenesisi90D → G: Loses its exclusive nucleolar localization and mislocalizes to the cytoplasm. 1 Publication1
Mutagenesisi129R → A: Loss of substrate rRNA binding. 1 Publication1
Mutagenesisi132R → A: Loss of substrate rRNA binding. 1 Publication1
Mutagenesisi136R → A: Loss of substrate rRNA binding. 1 Publication1
Mutagenesisi214D → R: Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. 1 Publication1
Mutagenesisi232L → S: Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. 1 Publication1
Mutagenesisi237A → D: Almost complete loss of SAM binding. No effect on growth and ribosome biogenesis. 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_00001586121 – 252Ribosomal RNA small subunit methyltransferase NEP1Add BLAST252

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q06287

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

More...
PaxDbi
Q06287

PRoteomics IDEntifications database

More...
PRIDEi
Q06287

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q06287

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q06287

<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

Homodimer.

Interacts with snoRNA U3.

Interacts with NOP14 and MPP10.

Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.

3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei88Interaction with substrate rRNA1 Publication1
Sitei129Interaction with substrate rRNA1 Publication1
Sitei132Interaction with substrate rRNA1 Publication1
Sitei136Interaction with substrate rRNA1 Publication1

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
31456, 449 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1604 Small ribosomal subunit processome, variant 1
CPX-1607 Small ribosomal subunit processome, variant 2
CPX-1608 Small ribosomal subunit processome, variant 3

Database of interacting proteins

More...
DIPi
DIP-6504N

Protein interaction database and analysis system

More...
IntActi
Q06287, 27 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YLR186W

<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

1252
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
Q06287

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q06287

<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>Regioni212 – 214S-adenosyl-L-methionine binding2 Publications3
Regioni227 – 232S-adenosyl-L-methionine binding2 Publications6

<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

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000000305

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q06287

KEGG Orthology (KO)

More...
KOi
K14568

Identification of Orthologs from Complete Genome Data

More...
OMAi
GCMKIGT

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.1280.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR029028 Alpha/beta_knot_MTases
IPR005304 Rbsml_bgen_MeTrfase_EMG1/NEP1
IPR029026 tRNA_m1G_MTases_N

The PANTHER Classification System

More...
PANTHERi
PTHR12636 PTHR12636, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03587 EMG1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF75217 SSF75217, 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.

Q06287-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVEDSRVRDA LKGGDQKALP ASLVPQAPPV LTSKDKITKR MIVVLAMASL
60 70 80 90 100
ETHKISSNGP GGDKYVLLNC DDHQGLLKKM GRDISEARPD ITHQCLLTLL
110 120 130 140 150
DSPINKAGKL QVYIQTSRGI LIEVNPTVRI PRTFKRFSGL MVQLLHKLSI
160 170 180 190 200
RSVNSEEKLL KVIKNPITDH LPTKCRKVTL SFDAPVIRVQ DYIEKLDDDE
210 220 230 240 250
SICVFVGAMA RGKDNFADEY VDEKVGLSNY PLSASVACSK FCHGAEDAWN

IL
Length:252
Mass (Da):27,895
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:i4A8FCDA812051AD1
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 conflicti114I → T in AAS56267 (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
U17246 Genomic DNA Translation: AAB67457.1
AY557941 Genomic DNA Translation: AAS56267.1
BK006945 Genomic DNA Translation: DAA09505.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S51431

NCBI Reference Sequences

More...
RefSeqi
NP_013287.1, NM_001182073.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YLR186W_mRNA; YLR186W_mRNA; YLR186W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850883

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YLR186W

<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
U17246 Genomic DNA Translation: AAB67457.1
AY557941 Genomic DNA Translation: AAS56267.1
BK006945 Genomic DNA Translation: DAA09505.1
PIRiS51431
RefSeqiNP_013287.1, NM_001182073.1

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
2V3JX-ray2.00A1-252[»]
2V3KX-ray2.00A1-252[»]
3OIIX-ray1.85A/B1-252[»]
3OIJX-ray3.00A/B1-252[»]
3OINX-ray1.90A/B1-252[»]
5JPQelectron microscopy7.30e/f1-252[»]
5TZSelectron microscopy5.10j/k1-252[»]
5WLCelectron microscopy3.80SJ/SK1-252[»]
5WYJelectron microscopy8.70E1/E21-252[»]
5WYKelectron microscopy4.50E1/E21-252[»]
SMRiQ06287
ModBaseiSearch...

Protein-protein interaction databases

BioGridi31456, 449 interactors
ComplexPortaliCPX-1604 Small ribosomal subunit processome, variant 1
CPX-1607 Small ribosomal subunit processome, variant 2
CPX-1608 Small ribosomal subunit processome, variant 3
DIPiDIP-6504N
IntActiQ06287, 27 interactors
STRINGi4932.YLR186W

PTM databases

iPTMnetiQ06287

Proteomic databases

MaxQBiQ06287
PaxDbiQ06287
PRIDEiQ06287
TopDownProteomicsiQ06287

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR186W_mRNA; YLR186W_mRNA; YLR186W
GeneIDi850883
KEGGisce:YLR186W

Organism-specific databases

EuPathDBiFungiDB:YLR186W
SGDiS000004176 EMG1

Phylogenomic databases

GeneTreeiENSGT00390000000305
InParanoidiQ06287
KOiK14568
OMAiGCMKIGT

Enzyme and pathway databases

BioCyciYEAST:G3O-32309-MONOMER
ReactomeiR-SCE-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

Miscellaneous databases

EvolutionaryTraceiQ06287

Protein Ontology

More...
PROi
PR:Q06287

Family and domain databases

Gene3Di3.40.1280.10, 1 hit
InterProiView protein in InterPro
IPR029028 Alpha/beta_knot_MTases
IPR005304 Rbsml_bgen_MeTrfase_EMG1/NEP1
IPR029026 tRNA_m1G_MTases_N
PANTHERiPTHR12636 PTHR12636, 1 hit
PfamiView protein in Pfam
PF03587 EMG1, 1 hit
SUPFAMiSSF75217 SSF75217, 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 nameiNEP1_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: Q06287
Secondary accession number(s): D6VYI9, E9P8U2
<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: May 10, 2002
Last sequence update: November 1, 1996
Last modified: July 31, 2019
This is version 157 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names
  4. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again