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 178 (17 Jun 2020)
Sequence version 1 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Phosphatidylserine decarboxylase proenzyme 2

Gene

PSD2

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:7890740, PubMed:7890739, PubMed:24366873). Phosphatidylethanolamine produced by PSD2 is insufficient to completely provide the PtdEtn pool required by mitochondria under respiratory conditions (PubMed:11294902). PSD2 is also involved in the PtdSer transport step to the site of PtdEtn synthesis on the Golgi/endosome membranes (PubMed:24366873). Required for normal heavy metal resistance (PubMed:20016005).UniRule annotation5 Publications

<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

Protein has several cofactor binding sites:

<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 indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi571CalciumPROSITE-ProRule annotation1
Metal bindingi574CalciumPROSITE-ProRule annotation1
Metal bindingi577CalciumPROSITE-ProRule annotation1
<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 sitei899Charge relay system; for autoendoproteolytic cleavage activityUniRule annotationBy similarity1
Active sitei956Charge relay system; for autoendoproteolytic cleavage activityUniRule annotationBy similarity1
Active sitei1043Charge relay system; for autoendoproteolytic cleavage activityUniRule annotationBy similarity1
Active sitei1043Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activityUniRule annotationBy similarity1

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

  • metal ion binding Source: UniProtKB-KW
  • 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
LigandCalcium, Metal-binding, Pyruvate

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YGR170W-MONOMER

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 2UniRule annotation1 Publication (EC:4.1.1.65UniRule annotation1 Publication)
Cleaved into the following 2 chains:
Phosphatidylserine decarboxylase 2 beta chainUniRule annotation1 Publication
Phosphatidylserine decarboxylase 2 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:PSD21 PublicationUniRule annotation
Ordered Locus Names:YGR170WImported
<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 VII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YGR170W

Saccharomyces Genome Database

More...
SGDi
S000003402 PSD2

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

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

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>Mutagenesisi1041 – 1043GGS → AAA: No processing of the proenzyme, complete loss of activity. 1 Publication3

<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_00000452001 – 1138Phosphatidylserine decarboxylase proenzyme 2Add BLAST1138
ChainiPRO_00000452011 – 1042Phosphatidylserine decarboxylase 2 beta chainUniRule annotationAdd BLAST1042
ChainiPRO_00000452021043 – 1138Phosphatidylserine decarboxylase 2 alpha chainUniRule annotationAdd BLAST96

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 residuei1043Pyruvic acid (Ser); by autocatalysisUniRule annotationBy similarity1

<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

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. 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.UniRule annotation

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>Sitei1042 – 1043Cleavage (non-hydrolytic); by autocatalysisUniRule annotationBy similarity2

Keywords - PTMi

Zymogen

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P53037

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

More...
PaxDbi
P53037

PRoteomics IDEntifications database

More...
PRIDEi
P53037

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P53037

<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 (By similarity).

Interacts with pstB2/PDR17 (PubMed:20016005, PubMed:24366873). This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2/PDR17 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis (PubMed:24366873).

By similarity1 Publication2 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection%27">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33422, 185 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-1319 PSTB lipid transfer acceptor membrane complex

Database of interacting proteins

More...
DIPi
DIP-6756N

Protein interaction database and analysis system

More...
IntActi
P53037, 3 interactors

Molecular INTeraction database

More...
MINTi
P53037

STRING: functional protein association networks

More...
STRINGi
4932.YGR170W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P53037 protein

<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%5Fand%5Fdomains%5Fsection">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>Domaini1 – 122C2 1PROSITE-ProRule annotationAdd BLAST122
Domaini478 – 600C2 2PROSITE-ProRule annotationAdd BLAST123

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 amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi108 – 159Ser-richPROSITE-ProRule annotationAdd BLAST52

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C2 domains have an essential, but non-catalytic function (Probable) (PubMed:24366873). Both C2-1 and C2-2 facilitate interaction with PstB2/PDR17 and are required for lipid transport function (PubMed:24366873).1 Publication1 Publication

<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 II sub-subfamily.UniRule annotationBy similarity

Keywords - Domaini

Repeat

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000013484

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_002661_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P53037

KEGG Orthology (KO)

More...
KOi
K01613

Identification of Orthologs from Complete Genome Data

More...
OMAi
KTSWRKH

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.150, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00663 PS_decarb_PSD_B_type2, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR003817 PS_Dcarbxylase
IPR033177 PSD
IPR033179 PSD_type2_pro

The PANTHER Classification System

More...
PANTHERi
PTHR10067 PTHR10067, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00168 C2, 2 hits
PF02666 PS_Dcarbxylase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00239 C2, 2 hits

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00163 PS_decarb, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50004 C2, 2 hits

<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.

P53037-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRIIKGRKRG KNKKPTLILK IHVIQAENIE ALKTFNCNPV CFVTTNTFYS
60 70 80 90 100
QKTNKLKNSN THWNQTLRIK LPRNPTSEWL RIIVYDALPT GAPPTTPSRP
110 120 130 140 150
RTTTANTSSS TLSNSGLSSH SHSSRNLNVT SKGNQTSTSI NSVSSSATPA
160 170 180 190 200
PSHSSSSLST TGPGSTHKNR INSYLYLGEA KISLLDLFKR KDTTTSYKFS
210 220 230 240 250
IEAQRYHLYD MKGGKDQDSL NCNFLVGDIL LGFKLECNVK RTPTFQAFNA
260 270 280 290 300
WRNELNTYLG RIDRNKARMR SSSSLPPPLE DMLSNSSAVS GNEIRREKPY
310 320 330 340 350
SDTDLAHDEE VNAEDEIDAE ESIEDMNSSG SICTERRYDI DNDTIFDSIS
360 370 380 390 400
EVVSLNDEEL DILNDFEEAD HPNVPDINVH DIDEDTRISL SSMITALDEY
410 420 430 440 450
DIVEPEDVAK LPAVSENDIT SVDDEESENQ QESDEEFDIY NEDEREDSDF
460 470 480 490 500
QSKEYIGSRL LHLQRGKHNK SYANYLYRRA KSNFFISKKE HAMGVVFMHI
510 520 530 540 550
GAIKNLPALR NRLSKTNYEM DPFIVISFGR RVFKTSWRKH TLNPEFNEYA
560 570 580 590 600
AFEVFPHETN FAFSIKVVDK DSFSFNDDVA KCELAWFDML QQQQHENEWI
610 620 630 640 650
PYEIPLDLTV EPAHAPKQPV LYSSFKYVSY PFLKKSFWKE AVDTSVNLER
660 670 680 690 700
LDIIQVMLYL ERLGSFTMAD SFELFQHFNK SAWAGQSITR SQLVEGLQSW
710 720 730 740 750
RKSTNFKRIW TCPRCMRSCK PTRNARRSKL VLENDLITHF AICTFSKEHK
760 770 780 790 800
TLKPSYVSSA FASKRWFSKV LIKLTYGKYA LGSNNANILV QDRDTGIIIE
810 820 830 840 850
EKISAHVKLG MRIIYNGKSP ESKKFRSLLK TLSIRQGKKF DSTASAKQIE
860 870 880 890 900
PFIKFHSLDL SQCRDKDFKT FNEFFYRKLK PGSRLPESNN KEILFSPADS
910 920 930 940 950
RCTVFPTIQE SKEIWVKGRK FSIKKLANNY NPETFNDNNC SIGIFRLAPQ
960 970 980 990 1000
DYHRFHSPCN GTIGKPVYVD GEYYTVNPMA VRSELDVFGE NIRVIIPIDS
1010 1020 1030 1040 1050
PQFGKLLYIP IGAMMVGSIL LTCKENDVVE SGQELGYFKF GGSTIIIIIP
1060 1070 1080 1090 1100
HNNFMFDSDL VKNSSERIET LVKVGMSIGH TSNVNELKRI RIKVDDPKKI
1110 1120 1130
ERIKRTISVS DENAKSTGNV TWEYHTLREM MNKDFAGL
Length:1,138
Mass (Da):130,065
Last modified:October 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:i934BA6579E121053
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti801E → G in AAA69819 (PubMed:7890740).Curated1
Sequence conflicti974Y → N in AAA69819 (PubMed:7890740).Curated1

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
U19910 Genomic DNA Translation: AAA69819.1
Z72955 Genomic DNA Translation: CAA97196.1
BK006941 Genomic DNA Translation: DAA08265.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64484

NCBI Reference Sequences

More...
RefSeqi
NP_011686.1, NM_001181299.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGR170W_mRNA; YGR170W; YGR170W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853080

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGR170W

<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
U19910 Genomic DNA Translation: AAA69819.1
Z72955 Genomic DNA Translation: CAA97196.1
BK006941 Genomic DNA Translation: DAA08265.1
PIRiS64484
RefSeqiNP_011686.1, NM_001181299.1

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

BioGRIDi33422, 185 interactors
ComplexPortaliCPX-1319 PSTB lipid transfer acceptor membrane complex
DIPiDIP-6756N
IntActiP53037, 3 interactors
MINTiP53037
STRINGi4932.YGR170W

PTM databases

iPTMnetiP53037

Proteomic databases

MaxQBiP53037
PaxDbiP53037
PRIDEiP53037

Genome annotation databases

EnsemblFungiiYGR170W_mRNA; YGR170W; YGR170W
GeneIDi853080
KEGGisce:YGR170W

Organism-specific databases

EuPathDBiFungiDB:YGR170W
SGDiS000003402 PSD2

Phylogenomic databases

GeneTreeiENSGT00390000013484
HOGENOMiCLU_002661_1_0_1
InParanoidiP53037
KOiK01613
OMAiKTSWRKH

Enzyme and pathway databases

UniPathwayiUPA00558;UER00616
BioCyciYEAST:YGR170W-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P53037
RNActiP53037 protein

Family and domain databases

Gene3Di2.60.40.150, 1 hit
HAMAPiMF_00663 PS_decarb_PSD_B_type2, 1 hit
InterProiView protein in InterPro
IPR000008 C2_dom
IPR035892 C2_domain_sf
IPR003817 PS_Dcarbxylase
IPR033177 PSD
IPR033179 PSD_type2_pro
PANTHERiPTHR10067 PTHR10067, 1 hit
PfamiView protein in Pfam
PF00168 C2, 2 hits
PF02666 PS_Dcarbxylase, 1 hit
SMARTiView protein in SMART
SM00239 C2, 2 hits
TIGRFAMsiTIGR00163 PS_decarb, 1 hit
PROSITEiView protein in PROSITE
PS50004 C2, 2 hits

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 nameiPSD2_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: P53037
Secondary accession number(s): D6VUV4
<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 1, 1996
Last sequence update: October 1, 1996
Last modified: June 17, 2020
This is version 178 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

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