Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P06168 (ILV5_YEAST)

Entry version 197 (12 Aug 2020)
Sequence version 1 (01 Jan 1988)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

Ketol-acid reductoisomerase, mitochondrial

Gene

ILV5

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

Miscellaneous

Present with 883000 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

Mg2+By similarityNote: Binds 2 magnesium ions per subunit.By similarity

<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: L-isoleucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-isoleucine from 2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-isoleucine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-isoleucine from 2-oxobutanoate, the pathway L-isoleucine biosynthesis and in Amino-acid biosynthesis.

Pathwayi: L-valine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-valine from pyruvate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Acetolactate synthase small subunit, mitochondrial (ILV6), Acetolactate synthase catalytic subunit, mitochondrial (ILV2)
  2. Ketol-acid reductoisomerase, mitochondrial (ILV5)
  3. Dihydroxy-acid dehydratase, mitochondrial (ILV3)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-valine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-valine from pyruvate, the pathway L-valine biosynthesis and in Amino-acid biosynthesis.

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 sitei171Sequence analysis1
<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 bindingi255Magnesium 1PROSITE-ProRule annotation1
Metal bindingi255Magnesium 2PROSITE-ProRule annotation1
Metal bindingi259Magnesium 1PROSITE-ProRule annotation1
Metal bindingi291Magnesium 2PROSITE-ProRule annotation1
Metal bindingi295Magnesium 2PROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei317SubstratePROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi84 – 93NADPSequence analysis10
Nucleotide bindingi108 – 113NADPBy similarity6
Nucleotide bindingi146 – 150NADPBy similarity5

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionOxidoreductase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis
LigandMagnesium, Metal-binding, NADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		YEAST:YLR355C-MONOMER

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

More...UniPathwayi		UPA00047;UER00056
UPA00049;UER00060

Protein family/group databases

MoonProt database of moonlighting proteins

More...MoonProti		P06168

<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:
Ketol-acid reductoisomerase, mitochondrial (EC:1.1.1.86)
Alternative name(s):
Acetohydroxy-acid reductoisomerase
Alpha-keto-beta-hydroxylacyl reductoisomerase
<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:ILV5
Ordered Locus Names:YLR355C
ORF Names:L9638.7
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XII

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		FungiDB:YLR355C

Saccharomyces Genome Database

More...SGDi		S000004347, ILV5

<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

Mitochondrion

<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 – 47MitochondrionSequence analysisAdd BLAST47
<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_000001563448 – 395Ketol-acid reductoisomerase, mitochondrialAdd BLAST348

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 residuei355PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P06168

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

More...PaxDbi		P06168

PRoteomics IDEntifications database

More...PRIDEi		P06168

Consortium for Top Down Proteomics

More...TopDownProteomicsi		P06168

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P06168

PTM databases

CarbonylDB database of protein carbonylation sites

More...CarbonylDBi		P06168

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P06168

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		31617, 132 interactors

Database of interacting proteins

More...DIPi		DIP-6463N

Protein interaction database and analysis system

More...IntActi		P06168, 38 interactors

Molecular INTeraction database

More...MINTi		P06168

STRING: functional protein association networks

More...STRINGi		4932.YLR355C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P06168, 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		P06168

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

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>Domaini57 – 246KARI N-terminal RossmannPROSITE-ProRule annotationAdd BLAST190
Domaini247 – 394KARI C-terminal knottedPROSITE-ProRule annotationAdd BLAST148

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>Regioni363 – 395HydrophilicAdd BLAST33

<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 ketol-acid reductoisomerase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		ENOG502QQBF, Eukaryota

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_033821_1_2_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P06168

KEGG Orthology (KO)

More...KOi		K00053

Identification of Orthologs from Complete Genome Data

More...OMAi		RAMFSWL

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.1040.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR013328, 6PGD_dom2
IPR013023, KARI
IPR000506, KARI_C
IPR013116, KARI_N
IPR016207, KetolA_reductoisomerase_fun
IPR036291, NAD(P)-bd_dom_sf

The PANTHER Classification System

More...PANTHERi		PTHR21371, PTHR21371, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF01450, IlvC, 1 hit
PF07991, IlvN, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF000119, Ilv5_fungal, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR00465, ilvC, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS51851, KARI_C, 1 hit
PS51850, KARI_N, 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.

P06168-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MLRTQAARLI CNSRVITAKR TFALATRAAA YSRPAARFVK PMITTRGLKQ 
        60         70         80         90        100
INFGGTVETV YERADWPREK LLDYFKNDTF ALIGYGSQGY GQGLNLRDNG 
       110        120        130        140        150
LNVIIGVRKD GASWKAAIED GWVPGKNLFT VEDAIKRGSY VMNLLSDAAQ 
       160        170        180        190        200
SETWPAIKPL LTKGKTLYFS HGFSPVFKDL THVEPPKDLD VILVAPKGSG 
       210        220        230        240        250
RTVRSLFKEG RGINSSYAVW NDVTGKAHEK AQALAVAIGS GYVYQTTFER 
       260        270        280        290        300
EVNSDLYGER GCLMGGIHGM FLAQYDVLRE NGHSPSEAFN ETVEEATQSL 
       310        320        330        340        350
YPLIGKYGMD YMYDACSTTA RRGALDWYPI FKNALKPVFQ DLYESTKNGT 
       360        370        380        390 
ETKRSLEFNS QPDYREKLEK ELDTIRNMEI WKVGKEVRKL RPENQ
Length:395
Mass (Da):44,368
Last modified:January 1, 1988 - 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:iD76419A6AD68E85E
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
X04969 Genomic DNA Translation: CAA28643.1
U19102 Genomic DNA Translation: AAB67753.1
BK006945 Genomic DNA Translation: DAA09659.1

Protein sequence database of the Protein Information Resource

More...PIRi		A24709

NCBI Reference Sequences

More...RefSeqi		NP_013459.1, NM_001182244.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YLR355C_mRNA; YLR355C; YLR355C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		851069

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YLR355C

<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
X04969 Genomic DNA Translation: CAA28643.1
U19102 Genomic DNA Translation: AAB67753.1
BK006945 Genomic DNA Translation: DAA09659.1
PIRiA24709
RefSeqiNP_013459.1, NM_001182244.1

3D structure databases

SMRiP06168
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi31617, 132 interactors
DIPiDIP-6463N
IntActiP06168, 38 interactors
MINTiP06168
STRINGi4932.YLR355C

Protein family/group databases

MoonProtiP06168

PTM databases

CarbonylDBiP06168
iPTMnetiP06168

2D gel databases

SWISS-2DPAGEiP06168

Proteomic databases

MaxQBiP06168
PaxDbiP06168
PRIDEiP06168
TopDownProteomicsiP06168

Genome annotation databases

EnsemblFungiiYLR355C_mRNA; YLR355C; YLR355C
GeneIDi851069
KEGGisce:YLR355C

Organism-specific databases

EuPathDBiFungiDB:YLR355C
SGDiS000004347, ILV5

Phylogenomic databases

eggNOGiENOG502QQBF, Eukaryota
HOGENOMiCLU_033821_1_2_1
InParanoidiP06168
KOiK00053
OMAiRAMFSWL

Enzyme and pathway databases

UniPathwayiUPA00047;UER00056
UPA00049;UER00060
BioCyciYEAST:YLR355C-MONOMER

Miscellaneous databases

Protein Ontology

More...PROi		PR:P06168
RNActiP06168, protein

Family and domain databases

Gene3Di1.10.1040.10, 3 hits
InterProiView protein in InterPro
IPR008927, 6-PGluconate_DH-like_C_sf
IPR013328, 6PGD_dom2
IPR013023, KARI
IPR000506, KARI_C
IPR013116, KARI_N
IPR016207, KetolA_reductoisomerase_fun
IPR036291, NAD(P)-bd_dom_sf
PANTHERiPTHR21371, PTHR21371, 1 hit
PfamiView protein in Pfam
PF01450, IlvC, 1 hit
PF07991, IlvN, 1 hit
PIRSFiPIRSF000119, Ilv5_fungal, 1 hit
SUPFAMiSSF48179, SSF48179, 1 hit
SSF51735, SSF51735, 1 hit
TIGRFAMsiTIGR00465, ilvC, 1 hit
PROSITEiView protein in PROSITE
PS51851, KARI_C, 1 hit
PS51850, KARI_N, 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 nameiILV5_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: P06168
Secondary accession number(s): D6VYZ3
<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: January 1, 1988
Last sequence update: January 1, 1988
Last modified: August 12, 2020
This is version 197 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

Direct protein sequencing, Reference proteome

Documents

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