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Protein

Ubiquitin-activating enzyme E1-like

Gene

UBA2

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

The dimeric enzyme acts as a SMT3 E1 ligase. It mediates ATP-dependent activation of SMT3 and formation of a thioester with a conserved cysteine residue on AOS1.1 Publication

Miscellaneous

Present with 18800 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei52ATPBy similarity1
Binding sitei76ATPBy similarity1
<p>This subsection of the ‘Function’ 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 bindingi162ZincBy similarity1
Metal bindingi165ZincBy similarity1
<p>This subsection of the ‘Function’ 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 sitei177Glycyl thioester intermediatePROSITE-ProRule annotation1
Metal bindingi435ZincBy similarity1
Metal bindingi438ZincBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi28 – 33ATPBy similarity6
Nucleotide bindingi60 – 63ATPBy similarity4
Nucleotide bindingi121 – 126ATPBy similarity6

<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

  • acid-amino acid ligase activity Source: InterPro
  • ATP binding Source: UniProtKB-KW
  • metal ion binding Source: UniProtKB-KW
  • SUMO activating enzyme activity Source: GO_Central

GO - Biological processi

  • protein sumoylation Source: SGD

<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 functionLigase
Biological processUbl conjugation pathway
LigandATP-binding, Metal-binding, Nucleotide-binding, Zinc

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-29938-MONOMER

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
6.2.1.B9 984

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-SCE-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)

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

More...
UniPathwayi
UPA00886

<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:
Ubiquitin-activating enzyme E1-like
Alternative name(s):
Polymerase-interacting protein 2
SMT3-activating enzyme subunit 2
<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:UBA2
Synonyms:PIP2, UAL1
Ordered Locus Names:YDR390C
ORF Names:D9509.10
<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 IV

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000002798 UBA2

<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; Source: COMPARTMENTS

Keywords - Cellular componenti

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>Mutagenesisi177C → A or S: Loss of function. 1

<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_00001949791 – 636Ubiquitin-activating enzyme E1-likeAdd BLAST636

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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

Multiubiquitinated in vivo.

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P52488

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

More...
PaxDbi
P52488

PRoteomics IDEntifications database

More...
PRIDEi
P52488

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
P52488

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P52488

<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

Heterodimer of UBA2 and AOS1. The complex binds SMT3.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<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
32451, 31 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-3238 SUMO activating enzyme complex

Database of interacting proteins

More...
DIPi
DIP-2296N

Protein interaction database and analysis system

More...
IntActi
P52488, 10 interactors

Molecular INTeraction database

More...
MINTi
P52488

STRING: functional protein association networks

More...
STRINGi
4932.YDR390C

<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

1636
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P52488

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P52488

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
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

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi619 – 622Nuclear localization signalSequence analysis4

<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 ubiquitin-activating E1 family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00550000074924

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000216514

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P52488

KEGG Orthology (KO)

More...
KOi
K10685

Identification of Orthologs from Complete Genome Data

More...
OMAi
CITWAKE

Database of Orthologous Groups

More...
OrthoDBi
EOG092C3FGE

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.520, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000594 ThiF_NAD_FAD-bd
IPR023318 Ub_act_enz_dom_a_sf
IPR030661 Uba2
IPR019572 UBA_E1_Cys
IPR035985 Ubiquitin-activating_enz
IPR033127 UBQ-activ_enz_E1_Cys_AS

The PANTHER Classification System

More...
PANTHERi
PTHR10953:SF5 PTHR10953:SF5, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00899 ThiF, 1 hit
PF10585 UBA_e1_thiolCys, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF039133 SUMO_E1B, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF69572 SSF69572, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00865 UBIQUITIN_ACTIVAT_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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<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.

P52488-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPRETSLVTI IGEDSYKKLR SSRCLLVGAG GIGSELLKDI ILMEFGEIHI
60 70 80 90 100
VDLDTIDLSN LNRQFLFRQK DIKQPKSTTA VKAVQHFNNS KLVPYQGNVM
110 120 130 140 150
DISTFPLHWF EQFDIIFNAL DNLAARRYVN KISQFLSLPL IESGTAGFDG
160 170 180 190 200
YMQPIIPGKT ECFECTKKET PKTFPVCTIR STPSQPIHCI VWAKNFLFNQ
210 220 230 240 250
LFASETSGNE DDNNQDWGTD DAEEIKRIKQ ETNELYELQK IIISRDASRI
260 270 280 290 300
PEILNKLFIQ DINKLLAIEN LWKTRTKPVP LSDSQINTPT KTAQSASNSV
310 320 330 340 350
GTIQEQISNF INITQKLMDR YPKEQNHIEF DKDDADTLEF VATAANIRSH
360 370 380 390 400
IFNIPMKSVF DIKQIAGNII PAIATTNAIV AGASSLISLR VLNLLKYAPT
410 420 430 440 450
TKYTDLNMAF TAKASNLSQN RYLSNPKLAP PNKNCPVCSK VCRGVIKLSS
460 470 480 490 500
DCLNKMKLSD FVVLIREKYS YPQDISLLDA SNQRLLFDYD FEDLNDRTLS
510 520 530 540 550
EINLGNGSII LFSDEEGDTM IRKAIELFLD VDDELPCNTC SLPDVEVPLI
560 570 580 590 600
KANNSPSKNE EEEKNEKGAD VVATTNSHGK DGIVILDDDE GEITIDAEPI
610 620 630
NGSKKRPVDT EISEAPSNKR TKLVNEPTNS DIVELD
Length:636
Mass (Da):71,259
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:iDBF800E1458B3B10
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence CAA82980 differs from that shown. Reason: Frameshift at positions 180 and 268.Curated

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
Z48725 Genomic DNA Translation: CAA88617.1
Z30326 Genomic DNA Translation: CAA82980.1 Frameshift.
U17263 Genomic DNA Translation: AAB46626.1
U32274 Genomic DNA Translation: AAB64832.1
BK006938 Genomic DNA Translation: DAA12234.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A57178

NCBI Reference Sequences

More...
RefSeqi
NP_010678.3, NM_001180698.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR390C_mRNA; YDR390C_mRNA; YDR390C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851998

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR390C

<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
Z48725 Genomic DNA Translation: CAA88617.1
Z30326 Genomic DNA Translation: CAA82980.1 Frameshift.
U17263 Genomic DNA Translation: AAB46626.1
U32274 Genomic DNA Translation: AAB64832.1
BK006938 Genomic DNA Translation: DAA12234.1
PIRiA57178
RefSeqiNP_010678.3, NM_001180698.3

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
3ONGX-ray2.30A/C439-563[»]
3ONHX-ray1.60A439-563[»]
ProteinModelPortaliP52488
SMRiP52488
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32451, 31 interactors
ComplexPortaliCPX-3238 SUMO activating enzyme complex
DIPiDIP-2296N
IntActiP52488, 10 interactors
MINTiP52488
STRINGi4932.YDR390C

PTM databases

iPTMnetiP52488

Proteomic databases

MaxQBiP52488
PaxDbiP52488
PRIDEiP52488
TopDownProteomicsiP52488

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR390C_mRNA; YDR390C_mRNA; YDR390C
GeneIDi851998
KEGGisce:YDR390C

Organism-specific databases

SGDiS000002798 UBA2

Phylogenomic databases

GeneTreeiENSGT00550000074924
HOGENOMiHOG000216514
InParanoidiP52488
KOiK10685
OMAiCITWAKE
OrthoDBiEOG092C3FGE

Enzyme and pathway databases

UniPathwayi
UPA00886

BioCyciYEAST:G3O-29938-MONOMER
BRENDAi6.2.1.B9 984
ReactomeiR-SCE-3065676 SUMO is conjugated to E1 (UBA2:SAE1)
R-SCE-3065678 SUMO is transferred from E1 to E2 (UBE2I, UBC9)

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P52488

Family and domain databases

Gene3Di1.10.10.520, 1 hit
InterProiView protein in InterPro
IPR000594 ThiF_NAD_FAD-bd
IPR023318 Ub_act_enz_dom_a_sf
IPR030661 Uba2
IPR019572 UBA_E1_Cys
IPR035985 Ubiquitin-activating_enz
IPR033127 UBQ-activ_enz_E1_Cys_AS
PANTHERiPTHR10953:SF5 PTHR10953:SF5, 1 hit
PfamiView protein in Pfam
PF00899 ThiF, 1 hit
PF10585 UBA_e1_thiolCys, 1 hit
PIRSFiPIRSF039133 SUMO_E1B, 1 hit
SUPFAMiSSF69572 SSF69572, 1 hit
PROSITEiView protein in PROSITE
PS00865 UBIQUITIN_ACTIVAT_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiUBA2_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: P52488
Secondary accession number(s): D6VT24
<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: October 1, 1996
Last sequence update: October 1, 1996
Last modified: December 5, 2018
This is version 181 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. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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