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Entry version 171 (17 Jun 2020)
Sequence version 1 (01 Dec 1992)
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Protein

Isocitrate lyase

Gene

ICL1

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 formation of succinate and glyoxylate from isocitrate, a key step of the glyoxylate cycle, which operates as an anaplerotic route for replenishing the tricarboxylic acid cycle. Required for growth on ethanol or acetate, but dispensable when fermentable carbon sources are available. Acts also on 2-methylisocitrate.6 Publications

Miscellaneous

Yeast isocitrate lyase is the only eukaryotic member of this family that is located in the cytoplasm, instead of being targeted to the peroxisome or the glyoxysome.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

Mg2+By similarity

<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

Phosphorylated and inactivated after addition of glucose to the cell culture (repressing conditions).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

The Vmax with threo-D(S)-isocitrate as substrate is 5-fold higher than with threo-D(S)-2-methylisocitrate as substrate.2 Publications
  1. KM=1.4 mM for threo-D(S)-isocitrate (at pH 7.0)2 Publications
  2. KM=0.6 mM for threo-D(S)-2-methylisocitrate (at pH 7.0 and 30 degrees Celsius)2 Publications

    pH dependencei

    Optimum pH is 7.2 Publications

    Temperature dependencei

    Thermostable for 60 minutes up to 50 degrees Celsius.2 Publications

    <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: glyoxylate cycle

    This protein is involved in step 1 of the subpathway that synthesizes (S)-malate from isocitrate.2 Publications
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Isocitrate lyase (ICL1)
    2. Malate synthase 1 (MLS1)
    This subpathway is part of the pathway glyoxylate 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 (S)-malate from isocitrate, the pathway glyoxylate 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 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 bindingi179MagnesiumBy similarity1
    <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 sitei217Proton acceptorCurated1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei254SubstrateBy similarity1
    Binding sitei471SubstrateBy 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

    • isocitrate lyase activity Source: SGD
    • metal ion binding Source: UniProtKB-KW
    • methylisocitrate lyase activity Source: UniProtKB-EC

    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 functionLyase
    Biological processGlyoxylate bypass, Tricarboxylic acid cycle
    LigandMagnesium, Metal-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    YEAST:YER065C-MONOMER

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    P28240

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

    More...
    UniPathwayi
    UPA00703;UER00719

    <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:
    Isocitrate lyase1 Publication (EC:4.1.3.14 Publications)
    Short name:
    ICLCurated
    Alternative name(s):
    Methylisocitrate lyase1 Publication (EC:4.1.3.302 Publications)
    Short name:
    MICACurated
    Threo-D(S)-isocitrate glyoxylate-lyaseCurated
    <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:ICL11 Publication
    Ordered Locus Names:YER065CImported
    <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 V

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    FungiDB:YER065C

    Saccharomyces Genome Database

    More...
    SGDi
    S000000867 ICL1

    <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

    Cytoplasm, Extracellular matrix, Secreted, Vacuole

    <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 growth when acetate or ethanol are the sole carbon source. Leads to reduced chronological lifespan.5 Publications

    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>Mutagenesisi53T → A: Abolishes short-term enzyme inactivation by glucose addition. 1 Publication1
    Mutagenesisi216K → R: Reduces activity by 45%; when associated with L-220. 1 Publication1
    Mutagenesisi220M → L: Reduces activity by 45%; when associated with R-216. 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_00000687991 – 557Isocitrate lyaseAdd BLAST557

    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 residuei53PhosphothreonineSequence analysis1

    <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

    Phosphorylated in response to elevated glucose levels, leading first to reversible inactivation of the enzyme (short-term inactivation), and at a later stage to proteolytic degradation of the protein (long-term inactivation).1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    P28240

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

    More...
    PaxDbi
    P28240

    PRoteomics IDEntifications database

    More...
    PRIDEi
    P28240

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

    Repressed by glucose and induced by ethanol via the transcriptional activator CAT8. The promoter sequence located between -397 and -388 contains an upstream activating sequence (UAS)element whereas the sequence located between -261 and -242 contains an upstream repressing sequence (URS) element.5 Publications

    <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

    Homotetramer.

    1 Publication

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGRID)

    More...
    BioGRIDi
    36807, 80 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-1663N

    Protein interaction database and analysis system

    More...
    IntActi
    P28240, 2 interactors

    Molecular INTeraction database

    More...
    MINTi
    P28240

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YER065C

    Miscellaneous databases

    RNAct, Protein-RNA interaction predictions for model organisms.

    More...
    RNActi
    P28240 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
    P28240

    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

    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>Regioni106 – 108Substrate bindingBy similarity3
    Regioni218 – 219Substrate bindingBy similarity2
    Regioni437 – 441Substrate bindingBy similarity5

    <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

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    CLU_019214_2_2_1

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    P28240

    KEGG Orthology (KO)

    More...
    KOi
    K01637

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    LEKDWAE

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd00377 ICL_PEPM, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.20.20.60, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR039556 ICL/PEPM
    IPR006254 Isocitrate_lyase
    IPR018523 Isocitrate_lyase_ph_CS
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442 Pyrv_Kinase-like_dom_sf

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR21631 PTHR21631, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00463 ICL, 1 hit

    PIRSF; a whole-protein classification database

    More...
    PIRSFi
    PIRSF001362 Isocit_lyase, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF51621 SSF51621, 1 hit

    TIGRFAMs; a protein family database

    More...
    TIGRFAMsi
    TIGR01346 isocit_lyase, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS00161 ISOCITRATE_LYASE, 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.

    P28240-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MPIPVGNTKN DFAALQAKLD ADAAEIEKWW SDSRWSKTKR NYSARDIAVR
    60 70 80 90 100
    RGTFPPIEYP SSVMARKLFK VLEKHHNEGT VSKTFGALDP VQISQMAKYL
    110 120 130 140 150
    DTIYISGWQC SSTASTSNEP GPDLADYPMD TVPNKVEHLF KAQLFHDRKQ
    160 170 180 190 200
    LEARSKAKSQ EELDEMGAPI DYLTPIVADA DAGHGGLTAV FKLTKMFIER
    210 220 230 240 250
    GAAGIHMEDQ TSTNKKCGHM AGRCVIPVQE HVNRLVTIRM CADIMHSDLI
    260 270 280 290 300
    VVARTDSEAA TLISSTIDTR DHYFIVGATN PNIEPFAEVL NDAIMSGASG
    310 320 330 340 350
    QELADIEQKW CRDAGLKLFH EAVIDEIERS ALSNKQELIK KFTSKVGPLT
    360 370 380 390 400
    ETSHREAKKL AKEILGHEIF FDWELPRVRE GLYRYRGGTQ CSIMRARAFA
    410 420 430 440 450
    PYADLVWMES NYPDFQQAKE FAEGVKEKFP DQWLAYNLSP SFNWPKAMSV
    460 470 480 490 500
    DEQHTFIQRL GDLGYIWQFI TLAGLHTNAL AVHNFSRDFA KDGMKAYAQN
    510 520 530 540 550
    VQQREMDDGV DVLKHQKWSG AEYIDGLLKL AQGGVSATAA MGTGVTEDQF

    KENGVKK
    Length:557
    Mass (Da):62,409
    Last modified:December 1, 1992 - 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:i15CC5A169CCEBE8B
    GO

    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
    X61271 Genomic DNA Translation: CAA43575.1
    X65554 Genomic DNA Translation: CAA46523.1
    U18813 Genomic DNA Translation: AAB64601.1
    BK006939 Genomic DNA Translation: DAA07724.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S22386 WZBYI

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_010987.3, NM_001178956.3

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YER065C_mRNA; YER065C; YER065C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    856794

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YER065C

    <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
    X61271 Genomic DNA Translation: CAA43575.1
    X65554 Genomic DNA Translation: CAA46523.1
    U18813 Genomic DNA Translation: AAB64601.1
    BK006939 Genomic DNA Translation: DAA07724.1
    PIRiS22386 WZBYI
    RefSeqiNP_010987.3, NM_001178956.3

    3D structure databases

    SMRiP28240
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGRIDi36807, 80 interactors
    DIPiDIP-1663N
    IntActiP28240, 2 interactors
    MINTiP28240
    STRINGi4932.YER065C

    Proteomic databases

    MaxQBiP28240
    PaxDbiP28240
    PRIDEiP28240

    Genome annotation databases

    EnsemblFungiiYER065C_mRNA; YER065C; YER065C
    GeneIDi856794
    KEGGisce:YER065C

    Organism-specific databases

    EuPathDBiFungiDB:YER065C
    SGDiS000000867 ICL1

    Phylogenomic databases

    HOGENOMiCLU_019214_2_2_1
    InParanoidiP28240
    KOiK01637
    OMAiLEKDWAE

    Enzyme and pathway databases

    UniPathwayiUPA00703;UER00719
    BioCyciYEAST:YER065C-MONOMER
    SABIO-RKiP28240

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:P28240
    RNActiP28240 protein

    Family and domain databases

    CDDicd00377 ICL_PEPM, 1 hit
    Gene3Di3.20.20.60, 1 hit
    InterProiView protein in InterPro
    IPR039556 ICL/PEPM
    IPR006254 Isocitrate_lyase
    IPR018523 Isocitrate_lyase_ph_CS
    IPR015813 Pyrv/PenolPyrv_Kinase-like_dom
    IPR040442 Pyrv_Kinase-like_dom_sf
    PANTHERiPTHR21631 PTHR21631, 1 hit
    PfamiView protein in Pfam
    PF00463 ICL, 1 hit
    PIRSFiPIRSF001362 Isocit_lyase, 1 hit
    SUPFAMiSSF51621 SSF51621, 1 hit
    TIGRFAMsiTIGR01346 isocit_lyase, 1 hit
    PROSITEiView protein in PROSITE
    PS00161 ISOCITRATE_LYASE, 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 nameiACEA_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: P28240
    Secondary accession number(s): D3DLX0
    <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: December 1, 1992
    Last sequence update: December 1, 1992
    Last modified: June 17, 2020
    This is version 171 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

    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 V
      Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
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