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Entry version 185 (18 Sep 2019)
Sequence version 1 (01 Apr 1990)
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Protein

Uridylate kinase

Gene

URA6

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 pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate donors, but can also use GTP, dGTP, dCTP, and dTTP to some degree.UniRule annotation4 Publications

Miscellaneous

Present with 1500 molecules/cell in log phase SD medium.1 Publication

Caution

There is controversy about the substrate specificity of the enzyme. Next to the primary substrate UMP, PubMed:1333436 and Ref. 8 report that the enzyme accepts also CMP and AMP as nucleoside monophosphates, but not GMP, whereas PubMed:2172245 and PubMed:8391780 report activity with GMP and dTMP, but not AMP or CMP.4 Publications

<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 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

Mg2+UniRule annotation2 PublicationsNote: Binds 1 Mg2+ ion per monomer.UniRule annotation2 Publications

<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=0.15 mM for UMP1 Publication
  2. KM=1.0 mM for dUMP1 Publication
  3. KM=1.8 mM for dTMP1 Publication
  4. KM=0.11 mM for ATP1 Publication
  5. KM=0.53 mM for dCMP1 Publication
  1. Vmax=120 µmol/min/mg enzyme (for dCDP synthesis)1 Publication

pH dependencei

Optimum pH is 6-9.5.1 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 sitei52NMPUniRule annotation2 Publications1
Binding sitei111NMPUniRule annotation2 Publications1
Binding sitei142ATPUniRule annotation2 Publications1
Binding sitei148NMPUniRule annotation2 Publications1
Binding sitei159NMPUniRule annotation2 Publications1
Binding sitei187ATP; via carbonyl oxygenUniRule annotation2 Publications1

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 bindingi26 – 31ATPUniRule annotation2 Publications6
Nucleotide bindingi74 – 76NMPUniRule annotation2 Publications3
Nucleotide bindingi104 – 107NMPUniRule annotation2 Publications4

<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 processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:YKL024C-MONOMER
YEAST:YKL024C-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.4.B1 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-499943 Interconversion of nucleotide di- and triphosphates

<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:
Uridylate kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Short name:
UKUniRule annotation
Alternative name(s):
ATP:UMP phosphotransferaseUniRule annotation
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Suppressor of cdc8 protein
Uridine monophosphate kinaseUniRule annotation
Short name:
UMP kinaseUniRule annotation
Short name:
UMPKUniRule annotation
<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:URA6UniRule annotation
Synonyms:SOC8
Ordered Locus Names:YKL024C
<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 XI

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YKL024C

Saccharomyces Genome Database

More...
SGDi
S000001507 URA6

<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

Cytoplasm, Nucleus

<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_and_biotech_section">'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>Mutagenesisi29K → E: Abolishes catalytic 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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001589471 – 204Uridylate kinaseAdd BLAST204

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P15700

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

More...
PaxDbi
P15700

PRoteomics IDEntifications database

More...
PRIDEi
P15700

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15700

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer.

UniRule annotation3 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34107, 230 interactors

Database of interacting proteins

More...
DIPi
DIP-4756N

Molecular INTeraction database

More...
MINTi
P15700

STRING: functional protein association networks

More...
STRINGi
4932.YKL024C

<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

1204
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
P15700

Database of comparative protein structure models

More...
ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P15700

<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

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>Regioni46 – 76NMPbindUniRule annotation2 PublicationsAdd BLAST31
Regioni141 – 151LIDUniRule annotation2 PublicationsAdd BLAST11

<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

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation2 Publications

<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 adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000238771

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P15700

KEGG Orthology (KO)

More...
KOi
K13800

Identification of Orthologs from Complete Genome Data

More...
OMAi
QFTHLSA

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01428 ADK, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_00235 Adenylate_kinase_Adk, 1 hit
MF_03172 Adenylate_kinase_UMP_CMP_kin, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR027417 P-loop_NTPase
IPR006266 UMP_CMP_kinase

The PANTHER Classification System

More...
PANTHERi
PTHR23359 PTHR23359, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00094 ADENYLTKNASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540 SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01359 UMP_CMP_kin_fam, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00113 ADENYLATE_KINASE, 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.

P15700-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTAATTSQPA FSPDQVSVIF VLGGPGAGKG TQCEKLVKDY SFVHLSAGDL
60 70 80 90 100
LRAEQGRAGS QYGELIKNCI KEGQIVPQEI TLALLRNAIS DNVKANKHKF
110 120 130 140 150
LIDGFPRKMD QAISFERDIV ESKFILFFDC PEDIMLERLL ERGKTSGRSD
160 170 180 190 200
DNIESIKKRF NTFKETSMPV IEYFETKSKV VRVRCDRSVE DVYKDVQDAI

RDSL
Length:204
Mass (Da):22,933
Last modified:April 1, 1990 - 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:iDDD7645EBCF4088D
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
M31455 Genomic DNA Translation: AAA35194.1
M69295 Genomic DNA Translation: AAA35200.1
Z28024 Genomic DNA Translation: CAA81859.1
AY558074 Genomic DNA Translation: AAS56400.1
BK006944 Genomic DNA Translation: DAA09130.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A33572

NCBI Reference Sequences

More...
RefSeqi
NP_012901.3, NM_001179590.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YKL024C_mRNA; YKL024C; YKL024C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
853844

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YKL024C

<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
M31455 Genomic DNA Translation: AAA35194.1
M69295 Genomic DNA Translation: AAA35200.1
Z28024 Genomic DNA Translation: CAA81859.1
AY558074 Genomic DNA Translation: AAS56400.1
BK006944 Genomic DNA Translation: DAA09130.1
PIRiA33572
RefSeqiNP_012901.3, NM_001179590.3

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
1UKYX-ray2.13A2-204[»]
1UKZX-ray1.90A2-204[»]
SMRiP15700
ModBaseiSearch...

Protein-protein interaction databases

BioGridi34107, 230 interactors
DIPiDIP-4756N
MINTiP15700
STRINGi4932.YKL024C

PTM databases

iPTMnetiP15700

Proteomic databases

MaxQBiP15700
PaxDbiP15700
PRIDEiP15700

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYKL024C_mRNA; YKL024C; YKL024C
GeneIDi853844
KEGGisce:YKL024C

Organism-specific databases

EuPathDBiFungiDB:YKL024C
SGDiS000001507 URA6

Phylogenomic databases

HOGENOMiHOG000238771
InParanoidiP15700
KOiK13800
OMAiQFTHLSA

Enzyme and pathway databases

BioCyciMetaCyc:YKL024C-MONOMER
YEAST:YKL024C-MONOMER
BRENDAi2.7.4.B1 984
ReactomeiR-SCE-499943 Interconversion of nucleotide di- and triphosphates

Miscellaneous databases

EvolutionaryTraceiP15700

Protein Ontology

More...
PROi
PR:P15700

Family and domain databases

CDDicd01428 ADK, 1 hit
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
MF_03172 Adenylate_kinase_UMP_CMP_kin, 1 hit
InterProiView protein in InterPro
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR027417 P-loop_NTPase
IPR006266 UMP_CMP_kinase
PANTHERiPTHR23359 PTHR23359, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01359 UMP_CMP_kin_fam, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 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 nameiKCY_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: P15700
Secondary accession number(s): D6VXR0
<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: April 1, 1990
Last sequence update: April 1, 1990
Last modified: September 18, 2019
This is version 185 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, Complete proteome, Reference proteome

Documents

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