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Entry version 172 (13 Feb 2019)
Sequence version 2 (15 Mar 2004)
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Protein

Cysteine desulfurase, mitochondrial

Gene

NFS1

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

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.5 Publications

Miscellaneous

Present with 504 molecules/cell in log phase SD medium.1 Publication

<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

<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

pyridoxal 5'-phosphateBy similarity

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>pH dependencei

Optimum pH is 8.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei248Pyridoxal phosphateBy similarity1
Binding sitei276Pyridoxal phosphateBy similarity1
Binding sitei336Pyridoxal phosphateBy similarity1
<p>This subsection of the ‘Function’ 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 sitei421Cysteine persulfide intermediateBy similarity1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi421Iron-sulfur (2Fe-2S); via persulfide groupBy similarity1

<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 functionTransferase
Biological processtRNA processing
LigandIron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G3O-29283-MONOMER
YEAST:G3O-29283-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1362409 Mitochondrial iron-sulfur cluster biogenesis
R-SCE-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se
R-SCE-947581 Molybdenum cofactor biosynthesis

<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:
Cysteine desulfurase, mitochondrial1 Publication (EC:2.8.1.71 Publication)
Alternative name(s):
tRNA-splicing protein SPL11 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:NFS1Imported
Synonyms:SPL11 Publication
Ordered Locus Names:YCL017CImported
<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 III

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YCL017C

Saccharomyces Genome Database

More...
SGDi
S000000522 NFS1

<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

Mitochondrion

<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

Impairs cysteine desulfurase activity of mitochondria. Leads to strong accumulation of free iron, not bound to heme or Fe/S clusters, in mitochondria, as well as to decreased amounts of the mitochondrial Fe/S proteins including aconitase and succinate dehydrogenase. Leads also to accumulation of 5-methoxycarbonylmethyluridine (mcm5U) and a concomitant decrease in 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs.4 Publications

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>Mutagenesisi191I → S: Exhibits constitutive up-regulation of the genes of the cellular iron uptake system. 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 transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 33MitochondrionSequence analysisAdd BLAST33
<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_000000130434 – 497Cysteine desulfurase, mitochondrialAdd BLAST464

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 residuei299N6-(pyridoxal phosphate)lysineBy similarity1

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P25374

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

More...
PaxDbi
P25374

PRoteomics IDEntifications database

More...
PRIDEi
P25374

<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%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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
30967, 416 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-392 NFS1-ISD11 cysteine desulphurase complex

Database of interacting proteins

More...
DIPi
DIP-2948N

Protein interaction database and analysis system

More...
IntActi
P25374, 14 interactors

Molecular INTeraction database

More...
MINTi
P25374

STRING: functional protein association networks

More...
STRINGi
4932.YCL017C

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

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P25374

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

More...
SMRi
P25374

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni168 – 169Pyridoxal phosphate bindingBy similarity2
Regioni296 – 298Pyridoxal phosphate bindingBy similarity3

<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

the N-terminal beta-strand formed by residues 99-104 is essential for the function.1 Publication

<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

Keywords - Domaini

Transit peptide

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155740

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000017510

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P25374

KEGG Orthology (KO)

More...
KOi
K04487

Identification of Orthologs from Complete Genome Data

More...
OMAi
EPIQSGG

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00331 Cys_desulf_IscS, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000192 Aminotrans_V_dom
IPR020578 Aminotrans_V_PyrdxlP_BS
IPR010240 Cys_deSase_IscS
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major

The PANTHER Classification System

More...
PANTHERi
PTHR11601:SF34 PTHR11601:SF34, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00266 Aminotran_5, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383 SSF53383, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR02006 IscS, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00595 AA_TRANSFER_CLASS_5, 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>.<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P25374-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLKSTATRSI TRLSQVYNVP AATYRACLVS RRFYSPPAAG VKLDDNFSLE
60 70 80 90 100
THTDIQAAAK AQASARASAS GTTPDAVVAS GSTAMSHAYQ ENTGFGTRPI
110 120 130 140 150
YLDMQATTPT DPRVLDTMLK FYTGLYGNPH SNTHSYGWET NTAVENARAH
160 170 180 190 200
VAKMINADPK EIIFTSGATE SNNMVLKGVP RFYKKTKKHI ITTRTEHKCV
210 220 230 240 250
LEAARAMMKE GFEVTFLNVD DQGLIDLKEL EDAIRPDTCL VSVMAVNNEI
260 270 280 290 300
GVIQPIKEIG AICRKNKIYF HTDAAQAYGK IHIDVNEMNI DLLSISSHKI
310 320 330 340 350
YGPKGIGAIY VRRRPRVRLE PLLSGGGQER GLRSGTLAPP LVAGFGEAAR
360 370 380 390 400
LMKKEFDNDQ AHIKRLSDKL VKGLLSAEHT TLNGSPDHRY PGCVNVSFAY
410 420 430 440 450
VEGESLLMAL RDIALSSGSA CTSASLEPSY VLHALGKDDA LAHSSIRFGI
460 470 480 490
GRFSTEEEVD YVVKAVSDRV KFLRELSPLW EMVQEGIDLN SIKWSGH
Length:497
Mass (Da):54,467
Last modified:March 15, 2004 - 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:iD709E326B3921BCC
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 conflicti150H → Y in AAA34814 (PubMed:8444805).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
M98808 Genomic DNA Translation: AAA34814.1
X59720 Genomic DNA Translation: CAA42344.2
M12909 Genomic DNA Translation: AAA66918.1
BK006937 Genomic DNA Translation: DAA07466.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S19343

NCBI Reference Sequences

More...
RefSeqi
NP_009912.2, NM_001178664.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YCL017C_mRNA; YCL017C_mRNA; YCL017C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
850343

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YCL017C

<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
M98808 Genomic DNA Translation: AAA34814.1
X59720 Genomic DNA Translation: CAA42344.2
M12909 Genomic DNA Translation: AAA66918.1
BK006937 Genomic DNA Translation: DAA07466.1
PIRiS19343
RefSeqiNP_009912.2, NM_001178664.1

3D structure databases

ProteinModelPortaliP25374
SMRiP25374
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi30967, 416 interactors
ComplexPortaliCPX-392 NFS1-ISD11 cysteine desulphurase complex
DIPiDIP-2948N
IntActiP25374, 14 interactors
MINTiP25374
STRINGi4932.YCL017C

Proteomic databases

MaxQBiP25374
PaxDbiP25374
PRIDEiP25374

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYCL017C_mRNA; YCL017C_mRNA; YCL017C
GeneIDi850343
KEGGisce:YCL017C

Organism-specific databases

EuPathDBiFungiDB:YCL017C
SGDiS000000522 NFS1

Phylogenomic databases

GeneTreeiENSGT00940000155740
HOGENOMiHOG000017510
InParanoidiP25374
KOiK04487
OMAiEPIQSGG

Enzyme and pathway databases

BioCyciMetaCyc:G3O-29283-MONOMER
YEAST:G3O-29283-MONOMER
ReactomeiR-SCE-1362409 Mitochondrial iron-sulfur cluster biogenesis
R-SCE-2408508 Metabolism of ingested SeMet, Sec, MeSec into H2Se
R-SCE-947581 Molybdenum cofactor biosynthesis

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P25374

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
HAMAPiMF_00331 Cys_desulf_IscS, 1 hit
InterProiView protein in InterPro
IPR000192 Aminotrans_V_dom
IPR020578 Aminotrans_V_PyrdxlP_BS
IPR010240 Cys_deSase_IscS
IPR015424 PyrdxlP-dep_Trfase
IPR015422 PyrdxlP-dep_Trfase_dom1
IPR015421 PyrdxlP-dep_Trfase_major
PANTHERiPTHR11601:SF34 PTHR11601:SF34, 1 hit
PfamiView protein in Pfam
PF00266 Aminotran_5, 1 hit
SUPFAMiSSF53383 SSF53383, 1 hit
TIGRFAMsiTIGR02006 IscS, 1 hit
PROSITEiView protein in PROSITE
PS00595 AA_TRANSFER_CLASS_5, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiNFS1_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: P25374
Secondary accession number(s): D6VQZ7
<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 1, 1992
Last sequence update: March 15, 2004
Last modified: February 13, 2019
This is version 172 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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