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Entry version 157 (02 Jun 2021)
Sequence version 1 (01 Nov 1996)
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Protein

Sphingosine-1-phosphate lyase

Gene

DPL1

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

Sphingosine-1-phosphate lyase that cleaves phosphorylated sphingoid bases (PSBs), such as sphingosine-1-phosphate, into fatty aldehydes and phosphoethanolamine (PubMed:20696404, PubMed:25345524, PubMed:9334171).

Prefers C-16 dihydrosphingosine-l-phosphate (DHS-P) as a substrate. Regulates intracellular levels of sphingolipid long-chain base phosphates (LCBPs) (PubMed:11795842).

Plays a role in the regulation of global responses to nutrient deprivation in yeast (PubMed:10329480).

5 Publications

Miscellaneous

Present with 13100 molecules/cell in log phase SD medium.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

pyridoxal 5'-phosphate1 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=19.6 µM for dihydrosphingosin 1-phosphate1 Publication
  2. KM=10.6 µM for phytosphingosin 1-phosphate1 Publication
  1. Vmax=28.3 nmol/min/µg enzyme toward dihydrosphingosin 1-phosphate1 Publication
  2. Vmax=8.9 nmol/min/µg enzyme toward phytosphingosin 1-phosphate1 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: sphingolipid metabolism

This protein is involved in the pathway sphingolipid metabolism, which is part of Lipid metabolism.
View all proteins of this organism that are known to be involved in the pathway sphingolipid metabolism and in Lipid metabolism.

<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 functionLyase
Biological processLipid metabolism, Sphingolipid metabolism
LigandPyridoxal phosphate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YDR294C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.2.27, 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1660661, Sphingolipid de novo biosynthesis

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

More...
UniPathwayi
UPA00222

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...
SwissLipidsi
SLP:000000071
SLP:000000196

<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:
Sphingosine-1-phosphate lyase1 Publication (EC:4.1.2.-1 Publication, EC:4.1.2.272 Publications)
Short name:
S1PL1 Publication
Short name:
SP-lyase1 Publication
Short name:
ySPL1 Publication
Alternative name(s):
Bestowed of sphingosine tolerance 11 Publication
Sphingosine-1-phosphate aldolase1 Publication
<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:DPL11 Publication
Synonyms:BST11 Publication
Ordered Locus Names:YDR294C
ORF Names:D9819.5
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002702, DPL1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YDR294C

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 58LumenalCuratedAdd BLAST58
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei59 – 76HelicalSequence analysisAdd BLAST18
Topological domaini77 – 589CytoplasmicCuratedAdd BLAST513

Keywords - Cellular componenti

Endoplasmic reticulum, 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

Leads to the accumulation of endogenous phosphorylated sphingoid bases, and exhibits unregulated proliferation upon approach to stationary phase (PubMed:10329480). Causes a reduction in total C15 and C17 phosphatidylcholine levels (PubMed:25345524).2 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>Mutagenesisi65 – 71CYKLISN → LYLLILL in Dpl1CKSN_LLLL; impairs the formation of higher oder oligomeric complexes and consequently reduces catalytic activity. 1 Publication7
Mutagenesisi67K → L: Reduces catalytic activity. 1 Publication1
Mutagenesisi172A → P: Loss of enzyme activity. 1 Publication1
Mutagenesisi174Y → F: Mildly decreased enzyme activity. 1 Publication1
Mutagenesisi198H → A: Decreased enzyme activity. 1 Publication1
Mutagenesisi380K → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi386K → A: Loss of enzyme activity. 1 Publication1
Mutagenesisi554Y → F: Decreased enzyme activity. 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_00001470181 – 589Sphingosine-1-phosphate lyaseAdd BLAST589

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi6N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
<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 residuei380N6-(pyridoxal phosphate)lysine1

<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

Glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q05567

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

More...
PaxDbi
Q05567

PRoteomics IDEntifications database

More...
PRIDEi
Q05567

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q05567

<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

Homodimer.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Q05567
With#Exp.IntAct
itself3EBI-33743,EBI-33743

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
32346, 157 interactors

Database of interacting proteins

More...
DIPi
DIP-49371N

Protein interaction database and analysis system

More...
IntActi
Q05567, 2 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YDR294C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q05567, 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

Secondary structure

1589
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
Q05567

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q05567

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1383, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000000046

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_028929_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q05567

Identification of Orthologs from Complete Genome Data

More...
OMAi
DPHKMGL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002129, PyrdxlP-dep_de-COase
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00282, Pyridoxal_deC, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383, SSF53383, 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.

Q05567-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSGVSNKTVS INGWYGMPIH LLREEGDFAQ FMILTINELK IAIHGYLRNT
60 70 80 90 100
PWYNMLKDYL FVIFCYKLIS NFFYLLKVYG PVRLAVRTYE HSSRRLFRWL
110 120 130 140 150
LDSPFLRGTV EKEVTKVKQS IEDELIRSDS QLMNFPQLPS NGIPQDDVIE
160 170 180 190 200
ELNKLNDLIP HTQWKEGKVS GAVYHGGDDL IHLQTIAYEK YCVANQLHPD
210 220 230 240 250
VFPAVRKMES EVVSMVLRMF NAPSDTGCGT TTSGGTESLL LACLSAKMYA
260 270 280 290 300
LHHRGITEPE IIAPVTAHAG FDKAAYYFGM KLRHVELDPT TYQVDLGKVK
310 320 330 340 350
KFINKNTILL VGSAPNFPHG IADDIEGLGK IAQKYKLPLH VDSCLGSFIV
360 370 380 390 400
SFMEKAGYKN LPLLDFRVPG VTSISCDTHK YGFAPKGSSV IMYRNSDLRM
410 420 430 440 450
HQYYVNPAWT GGLYGSPTLA GSRPGAIVVG CWATMVNMGE NGYIESCQEI
460 470 480 490 500
VGAAMKFKKY IQENIPDLNI MGNPRYSVIS FSSKTLNIHE LSDRLSKKGW
510 520 530 540 550
HFNALQKPVA LHMAFTRLSA HVVDEICDIL RTTVQELKSE SNSKPSPDGT
560 570 580
SALYGVAGSV KTAGVADKLI VGFLDALYKL GPGEDTATK
Length:589
Mass (Da):65,566
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:i75FAF8182AF72266
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
U51031 Genomic DNA Translation: AAB64470.1
BK006938 Genomic DNA Translation: DAA12133.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S70123

NCBI Reference Sequences

More...
RefSeqi
NP_010580.1, NM_001180602.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR294C_mRNA; YDR294C; YDR294C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851888

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR294C

<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
U51031 Genomic DNA Translation: AAB64470.1
BK006938 Genomic DNA Translation: DAA12133.1
PIRiS70123
RefSeqiNP_010580.1, NM_001180602.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3MC6X-ray3.15A/C103-589[»]
SMRiQ05567
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi32346, 157 interactors
DIPiDIP-49371N
IntActiQ05567, 2 interactors
STRINGi4932.YDR294C

Chemistry databases

SwissLipidsiSLP:000000071
SLP:000000196

PTM databases

iPTMnetiQ05567

Proteomic databases

MaxQBiQ05567
PaxDbiQ05567
PRIDEiQ05567

Genome annotation databases

EnsemblFungiiYDR294C_mRNA; YDR294C; YDR294C
GeneIDi851888
KEGGisce:YDR294C

Organism-specific databases

SGDiS000002702, DPL1
VEuPathDBiFungiDB:YDR294C

Phylogenomic databases

eggNOGiKOG1383, Eukaryota
GeneTreeiENSGT00390000000046
HOGENOMiCLU_028929_1_0_1
InParanoidiQ05567
OMAiDPHKMGL

Enzyme and pathway databases

UniPathwayiUPA00222
BioCyciMetaCyc:YDR294C-MONOMER
BRENDAi4.1.2.27, 984
ReactomeiR-SCE-1660661, Sphingolipid de novo biosynthesis

Miscellaneous databases

EvolutionaryTraceiQ05567

Protein Ontology

More...
PROi
PR:Q05567
RNActiQ05567, protein

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR002129, PyrdxlP-dep_de-COase
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major
PfamiView protein in Pfam
PF00282, Pyridoxal_deC, 1 hit
SUPFAMiSSF53383, SSF53383, 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 nameiSGPL_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: Q05567
Secondary accession number(s): D6VSS3
<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: October 24, 2003
Last sequence update: November 1, 1996
Last modified: June 2, 2021
This is version 157 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

3D-structure, Reference proteome

Documents

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