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Protein

Sphingoid long chain base kinase 4

Gene

LCB4

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 phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively (PubMed:9677363, PubMed:11102354, PubMed:11795842, PubMed:16141212). Involved in the biosynthesis of sphingolipids and ceramides (PubMed:12493772). Required with LCB3 for an effective incorporation of DHS into ceramides through a phosphorylation-dephosphorylation cycle. Involved in heat-induced transient cell cycle arrest (PubMed:11056159). Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling (PubMed:11278643). Involved in heat-stress resistance (PubMed:11967828).8 Publications

Miscellaneous

Present with 2840 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 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=7.7 µM for sphinganine1 Publication
  2. KM=25 µM for ATP1 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 sitei266ATPPROSITE-ProRule annotation1
    <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 sitei293Proton donor/acceptorBy similarity1
    Binding sitei298ATPPROSITE-ProRule annotation1
    Binding sitei392ATPPROSITE-ProRule annotation1
    Binding sitei398ATPPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi234 – 236ATPPROSITE-ProRule annotation3
    Nucleotide bindingi324 – 326ATPPROSITE-ProRule annotation3
    Nucleotide bindingi589 – 591ATPPROSITE-ProRule annotation3

    <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

    • calcium-mediated signaling Source: SGD
    • sphingolipid metabolic process Source: SGD

    <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 functionKinase, Transferase
    Biological processLipid metabolism, Sphingolipid metabolism
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyc Collection of Pathway/Genome Databases

    More...
    BioCyci
    MetaCyc:YOR171C-MONOMER
    YEAST:YOR171C-MONOMER

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-SCE-1483206 Glycerophospholipid biosynthesis
    R-SCE-1660661 Sphingolipid de novo biosynthesis
    R-SCE-1660662 Glycosphingolipid metabolism
    R-SCE-390471 Association of TriC/CCT with target proteins during biosynthesis
    R-SCE-5218921 VEGFR2 mediated cell proliferation

    Chemistry databases

    SwissLipids knowledge resource for lipid biology

    More...
    SwissLipidsi
    SLP:000000109

    <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:
    Sphingoid long chain base kinase 41 Publication (EC:2.7.1.911 Publication)
    Short name:
    LCB kinase 41 Publication
    Alternative name(s):
    Sphinganine kinase 4Curated
    <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:LCB41 Publication
    Ordered Locus Names:YOR171CImported
    ORF Names:O3615
    <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 XV

    Organism-specific databases

    Saccharomyces Genome Database

    More...
    SGDi
    S000005697 LCB4

    <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; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Golgi apparatus, Membrane

    <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_00002559561 – 624Sphingoid long chain base kinase 4Add BLAST624

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi43S-palmitoyl cysteine1 Publication1
    Lipidationi46S-palmitoyl cysteine1 Publication1
    <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 residuei111PhosphoserineCombined sources1
    Modified residuei120PhosphoserineCombined sources1
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki148Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)Combined sources
    Modified residuei154PhosphoserineCombined sources1
    Modified residuei160PhosphoserineCombined sources1
    Modified residuei451Phosphoserine; by PHO85Combined sources1 Publication1
    Modified residuei454PhosphoserineCombined sources1
    Modified residuei455Phosphoserine; by PHO85Combined sources1 Publication1
    Modified residuei460PhosphoserineCombined sources1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 by the cyclin-CDKs PCL1-PHO85 and PCL2-PHO85. Phosphorylation is a prerequisite to ubiquitination. The phosphorylation level depends on sterol composition and may also be involved in subcellular location (PubMed:16141212).2 Publications
    Ubiquitinated. The ubiquitination leads to degradation in the vacuole.1 Publication

    Keywords - PTMi

    Isopeptide bond, Lipoprotein, Palmitate, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQB - The MaxQuant DataBase

    More...
    MaxQBi
    Q12246

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

    More...
    PaxDbi
    Q12246

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q12246

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q12246

    SwissPalm database of S-palmitoylation events

    More...
    SwissPalmi
    Q12246

    <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

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    34565, 152 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-2844N

    Protein interaction database and analysis system

    More...
    IntActi
    Q12246, 3 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q12246

    STRING: functional protein association networks

    More...
    STRINGi
    4932.YOR171C

    <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
    Q12246

    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

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini224 – 363DAGKcPROSITE-ProRule annotationAdd BLAST140

    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>Regioni291 – 294Substrate bindingBy similarity4

    Phylogenomic databases

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000167991

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000207396

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q12246

    KEGG Orthology (KO)

    More...
    KOi
    K04718

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    FYCGNMA

    Database of Orthologous Groups

    More...
    OrthoDBi
    EOG092C1LMZ

    Family and domain databases

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    3.40.50.10330, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR017438 ATP-NAD_kinase_N
    IPR001206 Diacylglycerol_kinase_cat_dom
    IPR016064 NAD/diacylglycerol_kinase_sf

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00781 DAGK_cat, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00046 DAGKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF111331 SSF111331, 1 hit

    PROSITE; a protein domain and family database

    More...
    PROSITEi
    View protein in PROSITE
    PS50146 DAGK, 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.

    Q12246-1 [UniParc]FASTAAdd to basket
    « Hide
            10         20         30         40         50
    MVVQKKLRAI LTDEGVLIKS QSHHMFNKHG QLRSGDSLSL LSCLSCLDDG
    60 70 80 90 100
    TLSSDGGSFD EDDSLELLPL NTTIPFNRIL NAKYVNVGQK GFNNGKISSN
    110 120 130 140 150
    PFQTENLSSS SENDDVENHS LSNDKAPVSE SQSFPKKDKW DTKTNTVKVS
    160 170 180 190 200
    PDDSQDNSPS LGIKDNQQLI ELTFAVPKGH DVIPQKLTLL IDHVSRKSRA
    210 220 230 240 250
    NTGEENISSG TVEEILEKSY ENSKRNRSIL VIINPHGGKG TAKNLFLTKA
    260 270 280 290 300
    RPILVESGCK IEIAYTKYAR HAIDIAKDLD ISKYDTIACA SGDGIPYEVI
    310 320 330 340 350
    NGLYRRPDRV DAFNKLAVTQ LPCGSGNAMS ISCHWTNNPS YAALCLVKSI
    360 370 380 390 400
    ETRIDLMCCS QPSYMNEWPR LSFLSQTYGV IAESDINTEF IRWMGPVRFN
    410 420 430 440 450
    LGVAFNIIQG KKYPCEVFVK YAAKSKKELK VHFLENKDKN KGCLTFEPNP
    460 470 480 490 500
    SPNSSPDLLS KNNINNSTKD ELSPNFLNED NFKLKYPMTE PVPRDWEKMD
    510 520 530 540 550
    SELTDNLTIF YTGKMPYIAK DTKFFPAALP ADGTIDLVIT DARIPVTRMT
    560 570 580 590 600
    PILLSLDKGS HVLEPEVIHS KILAYKIIPK VESGLFSVDG EKFPLEPLQV
    610 620
    EIMPMLCKTL LRNGRYIDTE FESM
    Length:624
    Mass (Da):69,639
    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:iE033A3BAC604D4BB
    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
    U55021 Genomic DNA Translation: AAB47416.1
    Z75078 Genomic DNA Translation: CAA99378.1
    BK006948 Genomic DNA Translation: DAA10943.1

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    S67059

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_014814.1, NM_001183590.1

    Genome annotation databases

    Ensembl fungal genome annotation project

    More...
    EnsemblFungii
    YOR171C_mRNA; YOR171C_mRNA; YOR171C

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    854342

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    sce:YOR171C

    <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
    U55021 Genomic DNA Translation: AAB47416.1
    Z75078 Genomic DNA Translation: CAA99378.1
    BK006948 Genomic DNA Translation: DAA10943.1
    PIRiS67059
    RefSeqiNP_014814.1, NM_001183590.1

    3D structure databases

    ProteinModelPortaliQ12246
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi34565, 152 interactors
    DIPiDIP-2844N
    IntActiQ12246, 3 interactors
    MINTiQ12246
    STRINGi4932.YOR171C

    Chemistry databases

    SwissLipidsiSLP:000000109

    PTM databases

    iPTMnetiQ12246
    SwissPalmiQ12246

    Proteomic databases

    MaxQBiQ12246
    PaxDbiQ12246
    PRIDEiQ12246

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblFungiiYOR171C_mRNA; YOR171C_mRNA; YOR171C
    GeneIDi854342
    KEGGisce:YOR171C

    Organism-specific databases

    SGDiS000005697 LCB4

    Phylogenomic databases

    GeneTreeiENSGT00940000167991
    HOGENOMiHOG000207396
    InParanoidiQ12246
    KOiK04718
    OMAiFYCGNMA
    OrthoDBiEOG092C1LMZ

    Enzyme and pathway databases

    BioCyciMetaCyc:YOR171C-MONOMER
    YEAST:YOR171C-MONOMER
    ReactomeiR-SCE-1483206 Glycerophospholipid biosynthesis
    R-SCE-1660661 Sphingolipid de novo biosynthesis
    R-SCE-1660662 Glycosphingolipid metabolism
    R-SCE-390471 Association of TriC/CCT with target proteins during biosynthesis
    R-SCE-5218921 VEGFR2 mediated cell proliferation

    Miscellaneous databases

    Protein Ontology

    More...
    PROi
    PR:Q12246

    Family and domain databases

    Gene3Di3.40.50.10330, 1 hit
    InterProiView protein in InterPro
    IPR017438 ATP-NAD_kinase_N
    IPR001206 Diacylglycerol_kinase_cat_dom
    IPR016064 NAD/diacylglycerol_kinase_sf
    PfamiView protein in Pfam
    PF00781 DAGK_cat, 1 hit
    SMARTiView protein in SMART
    SM00046 DAGKc, 1 hit
    SUPFAMiSSF111331 SSF111331, 1 hit
    PROSITEiView protein in PROSITE
    PS50146 DAGK, 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 nameiLCB4_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: Q12246
    Secondary accession number(s): D6W2M7
    <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: October 31, 2006
    Last sequence update: November 1, 1996
    Last modified: December 5, 2018
    This is version 151 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

    Complete proteome, Reference proteome

    Documents

    1. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    2. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names
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