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 197 (17 Jun 2020)
Sequence version 3 (01 Oct 1996)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

3-isopropylmalate dehydratase

Gene

LEU1

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 isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate.

Miscellaneous

Present with 96300 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

[4Fe-4S] clusterBy similarityNote: Binds 1 [4Fe-4S] cluster 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-leucine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-leucine from 3-methyl-2-oxobutanoate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. 2-isopropylmalate synthase (LEU4), 2-isopropylmalate synthase 2, mitochondrial (LEU9)
  2. 3-isopropylmalate dehydratase (LEU1)
  3. 3-isopropylmalate dehydrogenase (LEU2)
  4. Branched-chain-amino-acid aminotransferase, cytosolic (BAT2), Branched-chain-amino-acid aminotransferase, mitochondrial (BAT1)
This subpathway is part of the pathway L-leucine 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-leucine from 3-methyl-2-oxobutanoate, the pathway L-leucine 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 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 bindingi360Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi421Iron-sulfur (4Fe-4S)By similarity1
Metal bindingi424Iron-sulfur (4Fe-4S)By 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

  • 3-isopropylmalate dehydratase activity Source: SGD
  • 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionLyase
Biological processAmino-acid biosynthesis, Branched-chain amino acid biosynthesis, Leucine biosynthesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YGL009C-MONOMER

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

More...
UniPathwayi
UPA00048;UER00071

<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:
3-isopropylmalate dehydratase (EC:4.2.1.33)
Alternative name(s):
Alpha-IPM isomerase
Short name:
IPMI
Isopropylmalate isomerase
<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:LEU1
Ordered Locus Names:YGL009C
<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:YGL009C

Saccharomyces Genome Database

More...
SGDi
S000002977 LEU1

<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

<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_00000768941 – 7793-isopropylmalate dehydrataseAdd BLAST779

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 residuei488PhosphoserineCombined sources1
Modified residuei494PhosphothreonineCombined sources1
Modified residuei495PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P07264

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

More...
PaxDbi
P07264

PRoteomics IDEntifications database

More...
PRIDEi
P07264

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P07264

<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

Monomer.

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33237, 94 interactors

Database of interacting proteins

More...
DIPi
DIP-6715N

Protein interaction database and analysis system

More...
IntActi
P07264, 10 interactors

Molecular INTeraction database

More...
MINTi
P07264

STRING: functional protein association networks

More...
STRINGi
4932.YGL009C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P07264 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

<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 aconitase/IPM isomerase family.Curated

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_006714_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P07264

KEGG Orthology (KO)

More...
KOi
K01702

Identification of Orthologs from Complete Genome Data

More...
OMAi
ETDFVLN

Family and domain databases

Conserved Domains Database

More...
CDDi
cd01583 IPMI, 1 hit
cd01577 IPMI_Swivel, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.20.19.10, 1 hit
3.30.499.10, 1 hit

HAMAP database of protein families

More...
HAMAPi
MF_01026 LeuC_type1, 1 hit
MF_01031 LeuD_type1, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004430 3-IsopropMal_deHydase_lsu
IPR004431 3-IsopropMal_deHydase_ssu
IPR012235 3-IsopropMal_deHydtase_ssu/lsu
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl
IPR033941 IPMI_cat
IPR033940 IPMI_Swivel

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF001418 ACN, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00415 ACONITASE

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53732 SSF53732, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00170 leuC, 1 hit
TIGR00171 leuD, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 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.

P07264-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MVYTPSKGPR TLYDKVFDAH VVHQDENGSF LLYIDRHLVH EVTSPQAFEG
60 70 80 90 100
LENAGRKVRR VDCTLATVDH NIPTESRKNF KSLDTFIKQT DSRLQVKTLE
110 120 130 140 150
NNVKQFGVPY FGMSDARQGI VHTIGPEEGF TLPGTTVVCG DSHTSTHGAF
160 170 180 190 200
GSLAFGIGTS EVEHVLATQT IIQAKSKNMR ITVNGKLSPG ITSKDLILYI
210 220 230 240 250
IGLIGTAGGT GCVIEFAGEA IEALSMEARM SMCNMAIEAG ARAGMIKPDE
260 270 280 290 300
TTFQYTKGRP LAPKGAEWEK AVAYWKTLKT DEGAKFDHEI NIEAVDVIPT
310 320 330 340 350
ITWGTSPQDA LPITGSVPDP KNVTDPIKKS GMERALAYMG LEPNTPLKSI
360 370 380 390 400
KVDKVFIGSC TNGRIEDLRS AAAVVRGQKL ASNIKLAMVV PGSGLVKKQA
410 420 430 440 450
EAEGLDKIFQ EAGFEWREAG CSICLGMNPD ILDAYERCAS TSNRNFEGRQ
460 470 480 490 500
GALSRTHLMS PAMAAAAGIA GHFVDIREFE YKDQDQSSPK VEVTSEDEKE
510 520 530 540 550
LESAAYDHAE PVQPEDAPQD IANDELKDIP VKSDDTPAKP SSSGMKPFLT
560 570 580 590 600
LEGISAPLDK ANVDTDAIIP KQFLKTIKRT GLKKGLFYEW RFRKDDQGKD
610 620 630 640 650
QETDFVLNVE PWREAEILVV TGDNFGCGSS REHAPWALKD FGIKSIIAPS
660 670 680 690 700
YGDIFYNNSF KNGLLPIRLD QQIIIDKLIP IANKGGKLCV DLPNQKILDS
710 720 730 740 750
DGNVLVDHFE IEPFRKHCLV NGLDDIGITL QKEEYISRYE ALRREKYSFL
760 770
EGGSKLLKFD NVPKRKAVTT TFDKVHQDW
Length:779
Mass (Da):85,794
Last modified:October 1, 1996 - v3
<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:iBD409A9702AE3E57
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 conflicti291N → TLKH in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti423I → M in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti459M → I in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti744R → K in AAB19612 (PubMed:1840714).Curated1
Sequence conflicti744R → K in S58126 (PubMed:1882553).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
S57886 Genomic DNA Translation: AAB19612.1
Z72531 Genomic DNA Translation: CAA96709.1
K01969 Genomic DNA Translation: AAA34742.1
S58126 Genomic DNA No translation available.
BK006941 Genomic DNA Translation: DAA08089.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S64011

NCBI Reference Sequences

More...
RefSeqi
NP_011506.1, NM_001180874.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL009C_mRNA; YGL009C; YGL009C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852875

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL009C

<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
S57886 Genomic DNA Translation: AAB19612.1
Z72531 Genomic DNA Translation: CAA96709.1
K01969 Genomic DNA Translation: AAA34742.1
S58126 Genomic DNA No translation available.
BK006941 Genomic DNA Translation: DAA08089.1
PIRiS64011
RefSeqiNP_011506.1, NM_001180874.1

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

BioGRIDi33237, 94 interactors
DIPiDIP-6715N
IntActiP07264, 10 interactors
MINTiP07264
STRINGi4932.YGL009C

PTM databases

iPTMnetiP07264

Proteomic databases

MaxQBiP07264
PaxDbiP07264
PRIDEiP07264

Genome annotation databases

EnsemblFungiiYGL009C_mRNA; YGL009C; YGL009C
GeneIDi852875
KEGGisce:YGL009C

Organism-specific databases

EuPathDBiFungiDB:YGL009C
SGDiS000002977 LEU1

Phylogenomic databases

HOGENOMiCLU_006714_1_0_1
InParanoidiP07264
KOiK01702
OMAiETDFVLN

Enzyme and pathway databases

UniPathwayiUPA00048;UER00071
BioCyciYEAST:YGL009C-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P07264
RNActiP07264 protein

Family and domain databases

CDDicd01583 IPMI, 1 hit
cd01577 IPMI_Swivel, 1 hit
Gene3Di3.20.19.10, 1 hit
3.30.499.10, 1 hit
HAMAPiMF_01026 LeuC_type1, 1 hit
MF_01031 LeuD_type1, 1 hit
InterProiView protein in InterPro
IPR004430 3-IsopropMal_deHydase_lsu
IPR004431 3-IsopropMal_deHydase_ssu
IPR012235 3-IsopropMal_deHydtase_ssu/lsu
IPR015931 Acnase/IPM_dHydase_lsu_aba_1/3
IPR001030 Acoase/IPM_deHydtase_lsu_aba
IPR015928 Aconitase/3IPM_dehydase_swvl
IPR018136 Aconitase_4Fe-4S_BS
IPR036008 Aconitase_4Fe-4S_dom
IPR000573 AconitaseA/IPMdHydase_ssu_swvl
IPR033941 IPMI_cat
IPR033940 IPMI_Swivel
PfamiView protein in Pfam
PF00330 Aconitase, 1 hit
PF00694 Aconitase_C, 1 hit
PIRSFiPIRSF001418 ACN, 1 hit
PRINTSiPR00415 ACONITASE
SUPFAMiSSF53732 SSF53732, 1 hit
TIGRFAMsiTIGR00170 leuC, 1 hit
TIGR00171 leuD, 1 hit
PROSITEiView protein in PROSITE
PS00450 ACONITASE_1, 1 hit
PS01244 ACONITASE_2, 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 nameiLEUC_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: P07264
Secondary accession number(s): D6VUC8
<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: April 1, 1988
Last sequence update: October 1, 1996
Last modified: June 17, 2020
This is version 197 of the entry and version 3 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