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Entry version 177 (10 Feb 2021)
Sequence version 1 (01 Feb 1995)
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Protein

Phosphatidylserine decarboxylase proenzyme 1, mitochondrial

Gene

PSD1

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 phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (PubMed:8227017, PubMed:8407984, PubMed:17976194, PubMed:23124206, PubMed:25829489). Phosphatidylethanolamine formed in the mitochondria is exported to other membranes to fullfill their requirements for PtdEtn (PubMed:8530379, PubMed:11294902). Required for normal mitochondrial morphology and proper mitochondrial fusion during yeast mating (PubMed:23045528).UniRule annotation8 Publications

Miscellaneous

Present with 1080 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

pyruvateUniRule annotationNote: Binds 1 pyruvoyl group covalently per subunit.UniRule annotation

<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: phosphatidylethanolamine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol.UniRule annotation1 Publication
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. CDP-diacylglycerol--serine O-phosphatidyltransferase (CHO1)
  2. Phosphatidylserine decarboxylase proenzyme 2 (PSD2), Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (PSD1)
This subpathway is part of the pathway phosphatidylethanolamine biosynthesis, which is itself part of Phospholipid metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes phosphatidylethanolamine from CDP-diacylglycerol, the pathway phosphatidylethanolamine biosynthesis and in Phospholipid metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei210Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei348Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei463Charge relay system; for autoendoproteolytic cleavage activityUniRule annotation1
Active sitei463Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activityUniRule annotation1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • histone binding Source: SGD
  • phosphatidylserine decarboxylase activity Source: SGD

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 functionDecarboxylase, Lyase
Biological processLipid biosynthesis, Lipid metabolism, Phospholipid biosynthesis, Phospholipid metabolism
LigandPyruvate

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
4.1.1.65, 984

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

More...
UniPathwayi
UPA00558;UER00616

<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:
Phosphatidylserine decarboxylase proenzyme 1, mitochondrialUniRule annotation1 Publication (EC:4.1.1.65UniRule annotation1 Publication1 Publication)
Cleaved into the following 2 chains:
Phosphatidylserine decarboxylase 1 beta chainUniRule annotation1 Publication
Phosphatidylserine decarboxylase 1 alpha chainUniRule annotation1 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:PSD11 PublicationUniRule annotation
Ordered Locus Names:YNL169CImported
ORF Names:N1692
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome XIV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000005113, PSD1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YNL169C

<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 domaini45 – 79Mitochondrial matrixUniRule annotation1 PublicationAdd BLAST35
<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>Transmembranei80 – 98HelicalUniRule annotationAdd BLAST19
Topological domaini99 – 500Mitochondrial intermembraneUniRule annotation1 PublicationAdd BLAST402

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner 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

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>Mutagenesisi81 – 100Missing in PSD1deltaIM; Mislocalizes to the mitochondrial matrix. 1 PublicationAdd BLAST20
Mutagenesisi461 – 463LGS → AAA: No processing of the proenzyme, complete loss of activity. 1 Publication3
Mutagenesisi461L → A: No effect. 1 Publication1
Mutagenesisi462G → A: Significantly impairs processing of the proenzyme, retains some activity. 1 Publication1
Mutagenesisi463S → A: No processing of the proenzyme, complete loss of activity. 2 Publications1
Mutagenesisi464T → I: No effect. 1 Publication1

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a transit peptide.<p><a href='/help/transit' target='_top'>More...</a></p>Transit peptidei1 – 44MitochondrionUniRule annotationAdd BLAST44
<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_000002984345 – 500Phosphatidylserine decarboxylase proenzyme 1, mitochondrialAdd BLAST456
ChainiPRO_000002984445 – 462Phosphatidylserine decarboxylase 1 beta chainUniRule annotationAdd BLAST418
ChainiPRO_0000029845463 – 500Phosphatidylserine decarboxylase 1 alpha chainUniRule annotationAdd BLAST38

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 residuei463Pyruvic acid (Ser); by autocatalysisUniRule annotation1

<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

The precursor is imported via the TOM complex into mitochondria, where the N-terminal presequence is cleaved by the matrix-located proteases MPP (MAS1-MAS2) and OCT1.1 Publication1 Publication
Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme (PubMed:25829489). The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase (By similarity).UniRule annotation1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei462 – 463Cleavage (non-hydrolytic); by autocatalysisUniRule annotation2

Keywords - PTMi

Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P39006

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

More...
PaxDbi
P39006

PRoteomics IDEntifications database

More...
PRIDEi
P39006

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P39006

<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

Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit.

UniRule annotation

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35659, 485 interactors

Database of interacting proteins

More...
DIPi
DIP-4599N

Protein interaction database and analysis system

More...
IntActi
P39006, 6 interactors

Molecular INTeraction database

More...
MINTi
P39006

STRING: functional protein association networks

More...
STRINGi
4932.YNL169C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P39006, 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
P39006

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily.UniRule annotation

Keywords - Domaini

Transit peptide, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2420, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013484

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_029061_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P39006

Identification of Orthologs from Complete Genome Data

More...
OMAi
YTEAVYS

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_03208, PS_decarb_PSD_B_type1_euk, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR003817, PS_Dcarbxylase
IPR033177, PSD
IPR033661, PSD_type1_euk

The PANTHER Classification System

More...
PANTHERi
PTHR10067, PTHR10067, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF02666, PS_Dcarbxylase, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00163, PS_decarb, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P39006-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSIMPVKNAL AQGRTLLMGR MPAVKFSTRM QLRNRTAVLW NRKFSTRLFV
60 70 80 90 100
QQRRSSGEIV DRAKAAAANS GRKQVSMKWV VLTSFTIVLG TILLVSRNDS
110 120 130 140 150
TEEDATEGKK GRRTRKIKIF NNNWLFFCYS TLPLNAMSRL WGQVNSLTLP
160 170 180 190 200
IWVRPWGYRL YSFLFGVNLD EMEDPDLTHY ANLSEFFYRN IKPGTRPVAQ
210 220 230 240 250
GEDVIASPSD GKILQVGIIN SETGEIEQVK GMTYSIKEFL GTHSHPLMSK
260 270 280 290 300
SASSLDLTSD EEKHREFARV NRIQLAGSED TEQPLLNFKN EGDQSVREFK
310 320 330 340 350
PSVSKNIHLL SQLSLNYFSN GFSCSEPHDT ELFFAVIYLA PGDYHHFHSP
360 370 380 390 400
VDWVCKVRRH FPGDLFSVAP YFQRNFPNLF VLNERVALLG SWKYGFFSMT
410 420 430 440 450
PVGATNVGSI KLNFDQEFVT NSKSDKHLEP HTCYQAVYEN ASKILGGMPL
460 470 480 490 500
VKGEEMGGFE LGSTVVLCFE APTEFKFDVR VGDKVKMGQK LGIIGKNDLK
Length:500
Mass (Da):56,595
Last modified:February 1, 1995 - 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:iD57047C5AD11777A
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
L20973 Genomic DNA Translation: AAA34918.1
Z71444 Genomic DNA Translation: CAA96056.1
Z71448 Genomic DNA Translation: CAA96063.1
X92517 Genomic DNA Translation: CAA63270.1
BK006947 Genomic DNA Translation: DAA10379.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A48053

NCBI Reference Sequences

More...
RefSeqi
NP_014230.1, NM_001183007.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YNL169C_mRNA; YNL169C; YNL169C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
855552

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YNL169C

<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
L20973 Genomic DNA Translation: AAA34918.1
Z71444 Genomic DNA Translation: CAA96056.1
Z71448 Genomic DNA Translation: CAA96063.1
X92517 Genomic DNA Translation: CAA63270.1
BK006947 Genomic DNA Translation: DAA10379.1
PIRiA48053
RefSeqiNP_014230.1, NM_001183007.1

3D structure databases

SMRiP39006
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi35659, 485 interactors
DIPiDIP-4599N
IntActiP39006, 6 interactors
MINTiP39006
STRINGi4932.YNL169C

PTM databases

iPTMnetiP39006

Proteomic databases

MaxQBiP39006
PaxDbiP39006
PRIDEiP39006

Genome annotation databases

EnsemblFungiiYNL169C_mRNA; YNL169C; YNL169C
GeneIDi855552
KEGGisce:YNL169C

Organism-specific databases

SGDiS000005113, PSD1
VEuPathDBiFungiDB:YNL169C

Phylogenomic databases

eggNOGiKOG2420, Eukaryota
GeneTreeiENSGT00390000013484
HOGENOMiCLU_029061_1_0_1
InParanoidiP39006
OMAiYTEAVYS

Enzyme and pathway databases

UniPathwayiUPA00558;UER00616
BRENDAi4.1.1.65, 984

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P39006
RNActiP39006, protein

Family and domain databases

HAMAPiMF_03208, PS_decarb_PSD_B_type1_euk, 1 hit
InterProiView protein in InterPro
IPR003817, PS_Dcarbxylase
IPR033177, PSD
IPR033661, PSD_type1_euk
PANTHERiPTHR10067, PTHR10067, 1 hit
PfamiView protein in Pfam
PF02666, PS_Dcarbxylase, 1 hit
TIGRFAMsiTIGR00163, PS_decarb, 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 nameiPSD1_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: P39006
Secondary accession number(s): D6W113
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: February 10, 2021
This is version 177 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 XIV
    Yeast (Saccharomyces cerevisiae) chromosome XIV: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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