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Entry version 193 (17 Jun 2020)
Sequence version 2 (01 Feb 1994)
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Protein

Citrate synthase, mitochondrial

Gene

CIT1

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

Specific citrate synthase with catalytic activity only with acetyl-CoA.2 Publications

Miscellaneous

Citrate synthase is found in nearly all cells capable of oxidative metabolism.Curated

<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 <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Phosphorylation at Ser-462 inhibits catalytic activity. Dephosphorylation at Ser-462 by PTC7 enhances catalytic activity.1 Publication

<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>Kineticsi

  1. KM=76 µM for acetyl-CoA1 Publication
  2. KM=9.86 µM for oxaloacetate1 Publication
  1. Vmax=1.92 µM/sec/µg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: tricarboxylic acid cycle

This protein is involved in step 1 of the subpathway that synthesizes isocitrate from oxaloacetate.Curated
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Citrate synthase 3, mitochondrial (CIT3), Citrate synthase, mitochondrial (CIT1), Citrate synthase, peroxisomal (CIT2)
  2. Aconitate hydratase, mitochondrial (ACO1)
This subpathway is part of the pathway tricarboxylic acid cycle, which is itself part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes isocitrate from oxaloacetate, the pathway tricarboxylic acid cycle and in Carbohydrate metabolism.

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 sitei312PROSITE-ProRule annotation1
Active sitei358PROSITE-ProRule annotation1
Active sitei413PROSITE-ProRule annotation1

<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 processTricarboxylic acid cycle

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YNR001C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.3.3.16 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-71403 Citric acid cycle (TCA cycle)

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00223;UER00717

<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:
Citrate synthase, mitochondrial1 Publication (EC:2.3.3.12 Publications)
<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:CIT11 Publication
Synonyms:GLU3, LYS6
Ordered Locus Names:YNR001C
ORF Names:N2019
<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 XIV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YNR001C

Saccharomyces Genome Database

More...
SGDi
S000005284 CIT1

<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

Decreased growth related to mitochondrial dysfunction.1 Publication

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>Mutagenesisi462S → A: Loss of phosphorylation. Greatly increases catalytic activity and promotes homodimerization. 1 Publication1
Mutagenesisi462S → E: Phosphomimetic mutant. Inhibits catalytic activity and homodimerization. 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 – 37MitochondrionAdd BLAST37
<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_000000547938 – 479Citrate synthase, mitochondrialAdd BLAST442

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 residuei462Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation at Ser-462. Dephosphorylated at Ser-462 by PTC7.1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P00890

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

More...
PaxDbi
P00890

PRoteomics IDEntifications database

More...
PRIDEi
P00890

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P00890

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P00890

<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

Monomer and homodimer (PubMed:28076776). Exists as an inactive monomer when phosphorylated (PubMed:28076776). Homodimerization is dependent on dephosphorylation of Ser-462 by PTC7 and is required for activity (PubMed:28076776).

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35825, 146 interactors

Database of interacting proteins

More...
DIPi
DIP-4597N

Protein interaction database and analysis system

More...
IntActi
P00890, 31 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YNR001C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P00890 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

3D structure databases

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

More...
SMRi
P00890

Database of comparative protein structure models

More...
ModBasei
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

<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 citrate synthase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000006813

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_022049_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P00890

KEGG Orthology (KO)

More...
KOi
K01647

Identification of Orthologs from Complete Genome Data

More...
OMAi
TVGWCAQ

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.230.10, 1 hit
1.10.580.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR019810 Citrate_synthase_AS
IPR010109 Citrate_synthase_euk
IPR036969 Citrate_synthase_sf

The PANTHER Classification System

More...
PANTHERi
PTHR11739 PTHR11739, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00285 Citrate_synt, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00143 CITRTSNTHASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48256 SSF48256, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01793 cit_synth_euk, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00480 CITRATE_SYNTHASE, 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.

<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 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.

P00890-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSAILSTTSK SFLSRGSTRQ CQNMQKALFA LLNARHYSSA SEQTLKERFA
60 70 80 90 100
EIIPAKAEEI KKFKKEHGKT VIGEVLLEQA YGGMRGIKGL VWEGSVLDPE
110 120 130 140 150
EGIRFRGRTI PEIQRELPKA EGSTEPLPEA LFWLLLTGEI PTDAQVKALS
160 170 180 190 200
ADLAARSEIP EHVIQLLDSL PKDLHPMAQF SIAVTALESE SKFAKAYAQG
210 220 230 240 250
VSKKEYWSYT FEDSLDLLGK LPVIASKIYR NVFKDGKITS TDPNADYGKN
260 270 280 290 300
LAQLLGYENK DFIDLMRLYL TIHSDHEGGN VSAHTTHLVG SALSSPYLSL
310 320 330 340 350
AAGLNGLAGP LHGRANQEVL EWLFKLREEV KGDYSKETIE KYLWDTLNAG
360 370 380 390 400
RVVPGYGHAV LRKTDPRYTA QREFALKHFP DYELFKLVST IYEVAPGVLT
410 420 430 440 450
KHGKTKNPWP NVDSHSGVLL QYYGLTEASF YTVLFGVARA IGVLPQLIID
460 470
RAVGAPIERP KSFSTEKYKE LVKKIESKN
Length:479
Mass (Da):53,360
Last modified:February 1, 1994 - 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:i280661B1CB248F14
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 conflicti58E → Q in CAA25359 (PubMed:6090126).Curated1
Sequence conflicti78E → EE in CAA25359 (PubMed:6090126).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
X00782 Genomic DNA Translation: CAA25359.1
Z23259 Genomic DNA Translation: CAA80781.1
X77395 Genomic DNA Translation: CAA54569.1
Z71616 Genomic DNA Translation: CAA96277.1
BK006947 Genomic DNA Translation: DAA10543.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S35390 YKBY

NCBI Reference Sequences

More...
RefSeqi
NP_014398.1, NM_001183178.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNR001C_mRNA; YNR001C; YNR001C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855732

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNR001C

<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
X00782 Genomic DNA Translation: CAA25359.1
Z23259 Genomic DNA Translation: CAA80781.1
X77395 Genomic DNA Translation: CAA54569.1
Z71616 Genomic DNA Translation: CAA96277.1
BK006947 Genomic DNA Translation: DAA10543.1
PIRiS35390 YKBY
RefSeqiNP_014398.1, NM_001183178.1

3D structure databases

SMRiP00890
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35825, 146 interactors
DIPiDIP-4597N
IntActiP00890, 31 interactors
STRINGi4932.YNR001C

PTM databases

iPTMnetiP00890

Proteomic databases

MaxQBiP00890
PaxDbiP00890
PRIDEiP00890
TopDownProteomicsiP00890

Genome annotation databases

EnsemblFungiiYNR001C_mRNA; YNR001C; YNR001C
GeneIDi855732
KEGGisce:YNR001C

Organism-specific databases

EuPathDBiFungiDB:YNR001C
SGDiS000005284 CIT1

Phylogenomic databases

GeneTreeiENSGT00390000006813
HOGENOMiCLU_022049_2_1_1
InParanoidiP00890
KOiK01647
OMAiTVGWCAQ

Enzyme and pathway databases

UniPathwayiUPA00223;UER00717
BioCyciYEAST:YNR001C-MONOMER
BRENDAi2.3.3.16 984
ReactomeiR-SCE-71403 Citric acid cycle (TCA cycle)

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P00890
RNActiP00890 protein

Family and domain databases

Gene3Di1.10.230.10, 1 hit
1.10.580.10, 1 hit
InterProiView protein in InterPro
IPR016142 Citrate_synth-like_lrg_a-sub
IPR016143 Citrate_synth-like_sm_a-sub
IPR002020 Citrate_synthase
IPR019810 Citrate_synthase_AS
IPR010109 Citrate_synthase_euk
IPR036969 Citrate_synthase_sf
PANTHERiPTHR11739 PTHR11739, 1 hit
PfamiView protein in Pfam
PF00285 Citrate_synt, 1 hit
PRINTSiPR00143 CITRTSNTHASE
SUPFAMiSSF48256 SSF48256, 1 hit
TIGRFAMsiTIGR01793 cit_synth_euk, 1 hit
PROSITEiView protein in PROSITE
PS00480 CITRATE_SYNTHASE, 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 nameiCISY1_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: P00890
Secondary accession number(s): D6W1H7
<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: July 21, 1986
Last sequence update: February 1, 1994
Last modified: June 17, 2020
This is version 193 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

Direct protein sequencing, Reference proteome

Documents

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