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Protein

DNA damage-inducible protein 1

Gene

DDI1

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

Aspartic protease (PubMed:21266539). Appears to act as negative regulator of constitutive exocytosis (PubMed:10330187, PubMed:12051757). May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly (PubMed:12925750). Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation (PubMed:17144915, PubMed:16478980). Required for S-phase checkpoint control (PubMed:11238935, PubMed:17144915).1 Publication7 Publications

Miscellaneous

Present with 6510 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Inhibited by the proteinase inhibitors indinavir, lopinavir, nelfinavir, isovaleryl pepstatin, ritonavir, saquinavir and tipranavir.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei220Curated1

<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

  • aspartic-type endopeptidase activity Source: UniProtKB-KW
  • SNARE binding Source: SGD
  • ubiquitin binding Source: SGD

GO - Biological processi

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

Molecular functionAspartyl protease, Hydrolase, Protease
Biological processProtein transport, Transport

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-30304-MONOMER

Protein family/group databases

MEROPS protease database

More...
MEROPSi
A28.001

<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:
DNA damage-inducible protein 1 (EC:3.4.23.-By similarity)
Alternative name(s):
v-SNARE-master 1
<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:DDI1
Synonyms:VSM1
Ordered Locus Names:YER143W
<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 V

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000000945 DDI1

<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

Cell membrane, Cytoplasm, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_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>Mutagenesisi220D → A: Increased protein secretion most likely due to reduced catalytic activity. Cells are larger and clump together. 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_00002109971 – 428DNA damage-inducible protein 1Add BLAST428

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki171Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki257Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P40087

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

More...
PaxDbi
P40087

PRoteomics IDEntifications database

More...
PRIDEi
P40087

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P40087

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By DNA damage via PDR3.4 Publications

<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

Forms homodimers. Interacts with RAD23. These interactions are mediated by the UBA domain. Is also able to bind ubiquitin and polyubiquitinated proteins. Interacts with the SNAREs SNC1, SNC2, SSO1, TLG1 and TLG2. Binding to SSO1 is promoted by the phosphorylation of 'Ser-49' of SSO1 by TKP1.7 Publications

<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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
36892, 107 interactors

Database of interacting proteins

More...
DIPi
DIP-1216N

Protein interaction database and analysis system

More...
IntActi
P40087, 6 interactors

Molecular INTeraction database

More...
MINTi
P40087

STRING: functional protein association networks

More...
STRINGi
4932.YER143W

<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

1428
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1AX-ray2.30A/B/C/D180-325[»]
2MR9NMR-A389-428[»]
2MRONMR-B389-428[»]
2MRPNMR-A2-80[»]
2MWSNMR-B2-80[»]
2N7ENMR-A1-80[»]
4Z2ZX-ray1.80A/B185-325[»]
5KESNMR-A86-196[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P40087

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

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SMRi
P40087

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P40087

<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_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 80Ubiquitin-likeAdd BLAST80
Domaini389 – 428UBAPROSITE-ProRule annotationAdd BLAST40

<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 DDI1 family.Curated

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153387

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000234736

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P40087

KEGG Orthology (KO)

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KOi
K11885

Identification of Orthologs from Complete Genome Data

More...
OMAi
NQARISE

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05479 RP_DDI, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.40.70.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR033322 DDI1
IPR001995 Peptidase_A2_cat
IPR019103 Peptidase_aspartic_DDI1-type
IPR021109 Peptidase_aspartic_dom_sf
IPR015940 UBA
IPR009060 UBA-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12917 PTHR12917, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF09668 Asp_protease, 1 hit
PF00627 UBA, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00165 UBA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46934 SSF46934, 1 hit
SSF50630 SSF50630, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50030 UBA, 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.

P40087-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDLTISNELT GEIYGPIEVS EDMALTDLIA LLQADCGFDK TKHDLYYNMD
60 70 80 90 100
ILDSNRTQSL KELGLKTDDL LLIRGKISNS IQTDAATLSD EAFIEQFRQE
110 120 130 140 150
LLNNQMLRSQ LILQIPGLND LVNDPLLFRE RLGPLILQRR YGGYNTAMNP
160 170 180 190 200
FGIPQDEYTR LMANPDDPDN KKRIAELLDQ QAIDEQLRNA IEYTPEMFTQ
210 220 230 240 250
VPMLYINIEI NNYPVKAFVD TGAQTTIMST RLAKKTGLSR MIDKRFIGEA
260 270 280 290 300
RGVGTGKIIG RIHQAQVKIE TQYIPCSFTV LDTDIDVLIG LDMLKRHLAC
310 320 330 340 350
VDLKENVLRI AEVETSFLSE AEIPKSFQEG LPAPTSVTTS SDKPLTPTKT
360 370 380 390 400
SSTLPPQPGA VPALAPRTGM GPTPTGRSTA GATTATGRTF PEQTIKQLMD
410 420
LGFPRDAVVK ALKQTNGNAE FAASLLFQ
Length:428
Mass (Da):47,354
Last modified:February 1, 1995 - 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:iB43425B029B7658B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U14002 Genomic DNA Translation: AAB82066.1
AF034895 Genomic DNA Translation: AAC18522.1
U18917 Genomic DNA Translation: AAB64670.1
AY692945 Genomic DNA Translation: AAT92964.1
BK006939 Genomic DNA Translation: DAA07804.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S50646

NCBI Reference Sequences

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RefSeqi
NP_011070.3, NM_001179033.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YER143W_mRNA; YER143W_mRNA; YER143W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856886

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YER143W

<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
U14002 Genomic DNA Translation: AAB82066.1
AF034895 Genomic DNA Translation: AAC18522.1
U18917 Genomic DNA Translation: AAB64670.1
AY692945 Genomic DNA Translation: AAT92964.1
BK006939 Genomic DNA Translation: DAA07804.1
PIRiS50646
RefSeqiNP_011070.3, NM_001179033.3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2I1AX-ray2.30A/B/C/D180-325[»]
2MR9NMR-A389-428[»]
2MRONMR-B389-428[»]
2MRPNMR-A2-80[»]
2MWSNMR-B2-80[»]
2N7ENMR-A1-80[»]
4Z2ZX-ray1.80A/B185-325[»]
5KESNMR-A86-196[»]
ProteinModelPortaliP40087
SMRiP40087
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36892, 107 interactors
DIPiDIP-1216N
IntActiP40087, 6 interactors
MINTiP40087
STRINGi4932.YER143W

Protein family/group databases

MEROPSiA28.001

PTM databases

iPTMnetiP40087

Proteomic databases

MaxQBiP40087
PaxDbiP40087
PRIDEiP40087

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYER143W_mRNA; YER143W_mRNA; YER143W
GeneIDi856886
KEGGisce:YER143W

Organism-specific databases

SGDiS000000945 DDI1

Phylogenomic databases

GeneTreeiENSGT00940000153387
HOGENOMiHOG000234736
InParanoidiP40087
KOiK11885
OMAiNQARISE

Enzyme and pathway databases

BioCyciYEAST:G3O-30304-MONOMER

Miscellaneous databases

EvolutionaryTraceiP40087

Protein Ontology

More...
PROi
PR:P40087

Family and domain databases

CDDicd05479 RP_DDI, 1 hit
Gene3Di2.40.70.10, 1 hit
InterProiView protein in InterPro
IPR033322 DDI1
IPR001995 Peptidase_A2_cat
IPR019103 Peptidase_aspartic_DDI1-type
IPR021109 Peptidase_aspartic_dom_sf
IPR015940 UBA
IPR009060 UBA-like_sf
PANTHERiPTHR12917 PTHR12917, 1 hit
PfamiView protein in Pfam
PF09668 Asp_protease, 1 hit
PF00627 UBA, 1 hit
SMARTiView protein in SMART
SM00165 UBA, 1 hit
SUPFAMiSSF46934 SSF46934, 1 hit
SSF50630 SSF50630, 1 hit
PROSITEiView protein in PROSITE
PS50030 UBA, 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 nameiDDI1_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: P40087
Secondary accession number(s): D3DM50
<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: February 1, 1995
Last sequence update: February 1, 1995
Last modified: January 16, 2019
This is version 176 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. SIMILARITY comments
    Index of protein domains and families
  2. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  3. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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