Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 167 (29 Sep 2021)
Sequence version 1 (01 Nov 1996)
Previous versions | rss
Add a publicationFeedback
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, PubMed:25345524).

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).

9 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 <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei266ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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

<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

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1660661, Sphingolipid de novo biosynthesis
R-SCE-390471, Association of TriC/CCT with target proteins during biosynthesis
R-SCE-5218921, VEGFR2 mediated cell proliferation
R-SCE-9009391, Extra-nuclear estrogen signaling

SABIO-RK: Biochemical Reaction Kinetics Database

More...
SABIO-RKi
Q12246

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:2.7.1.912 Publications)
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

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YOR171C

<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

Keywords - Cellular componenti

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

<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

Completely abolishes the conversion of phytosphingosin to glycerophospholipid.1 Publication

<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_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 cysteine; by AKR11 Publication1
Lipidationi46S-palmitoyl cysteine; by AKR11 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
Palmitoylated by palmitoyltransferase AKR1; this anchors the protein to the plasma membrane.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, 156 interactors

Database of interacting proteins

More...
DIPi
DIP-2844N

Protein interaction database and analysis system

More...
IntActi
Q12246, 3 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YOR171C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q12246, 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

<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>Regioni95 – 162DisorderedSequence analysisAdd BLAST68
Regioni291 – 294Substrate bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular type of amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi95 – 130Polar residuesSequence analysisAdd BLAST36
Compositional biasi131 – 146Basic and acidic residuesSequence analysisAdd BLAST16
Compositional biasi147 – 162Polar residuesSequence analysisAdd BLAST16

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1116, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000167991

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_013399_0_2_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q12246

Identification of Orthologs from Complete Genome Data

More...
OMAi
QRFTIWT

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>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

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; 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

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi34565, 156 interactors
DIPiDIP-2844N
IntActiQ12246, 3 interactors
STRINGi4932.YOR171C

Chemistry databases

SwissLipidsiSLP:000000109

PTM databases

iPTMnetiQ12246
SwissPalmiQ12246

Proteomic databases

MaxQBiQ12246
PaxDbiQ12246
PRIDEiQ12246

Genome annotation databases

EnsemblFungiiYOR171C_mRNA; YOR171C; YOR171C
GeneIDi854342
KEGGisce:YOR171C

Organism-specific databases

SGDiS000005697, LCB4
VEuPathDBiFungiDB:YOR171C

Phylogenomic databases

eggNOGiKOG1116, Eukaryota
GeneTreeiENSGT00940000167991
HOGENOMiCLU_013399_0_2_1
InParanoidiQ12246
OMAiQRFTIWT

Enzyme and pathway databases

BioCyciMetaCyc:YOR171C-MONOMER
ReactomeiR-SCE-1660661, Sphingolipid de novo biosynthesis
R-SCE-390471, Association of TriC/CCT with target proteins during biosynthesis
R-SCE-5218921, VEGFR2 mediated cell proliferation
R-SCE-9009391, Extra-nuclear estrogen signaling
SABIO-RKiQ12246

Miscellaneous databases

Protein Ontology

More...
PROi
PR:Q12246
RNActiQ12246, protein

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

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 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: September 29, 2021
This is version 167 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. 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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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

Do not show this banner again