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 184 (23 Feb 2022)
Sequence version 2 (01 Feb 1995)
Previous versions | rss
Add a publicationFeedback
Protein

Arginine permease CAN1

Gene

CAN1

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

High-affinity permease for arginine (PubMed:8436127, PubMed:9231419, PubMed:10654085, PubMed:11746604).

4 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

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

Biological processAmino-acid transport, Transport

Protein family/group databases

Transport Classification Database

More...
TCDBi
2.A.3.10.4, the amino acid-polyamine-organocation (apc) family

<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:
Arginine permease CAN1
Alternative name(s):
Canavanine resistance protein 11 Publication
<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:CAN11 Publication
Ordered Locus Names:YEL063C
<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 V

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000000789, CAN1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YEL063C

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei93 – 113HelicalSequence analysisAdd BLAST21
Transmembranei117 – 137HelicalSequence analysisAdd BLAST21
Transmembranei172 – 192HelicalSequence analysisAdd BLAST21
Transmembranei199 – 219HelicalSequence analysisAdd BLAST21
Transmembranei235 – 255HelicalSequence analysisAdd BLAST21
Transmembranei283 – 303HelicalSequence analysisAdd BLAST21
Transmembranei324 – 344HelicalSequence analysisAdd BLAST21
Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Transmembranei420 – 440HelicalSequence analysisAdd BLAST21
Transmembranei449 – 469HelicalSequence analysisAdd BLAST21
Transmembranei498 – 518HelicalSequence analysisAdd BLAST21
Transmembranei524 – 544HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Cell membrane, Endosome, 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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Abolishes canavanine sensitivity (PubMed:3327612). Extends replicative lifespan and leads to distinct changes in transcriptional and translational profiles, including translational activation of the GCN4 transcription factor (PubMed:28228255).2 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi113P → L in CAN1-343; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi148P → L in CAN1-337; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, but not sensitivity to L-aspartic acid alpha-hydroxamate or p-fluoro-L-phenylalanine. 1 Publication1
Mutagenesisi149V → F in CAN1-315; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi152S → F in CAN1-342; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi173Y → D in CAN1-306; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi173Y → H in CAN1-327; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi308G → A in CAN1-341; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi313P → S in CAN1-329; confers citrulline transport activity in GAP1-deleted cells and leads to sensitivity to L-glutamic acid alpha-hydroxamate, alpha-aminoisobutyrate, 3-chloro-L-alanine, L-ethionine, L-allylglycine, and D-histidine, L-aspartic acid alpha-hydroxamate and p-fluoro-L-phenylalanine. 1 Publication1
Mutagenesisi354 – 355Missing in CAN1-318; confers citrulline transport activity in GAP1-deleted cells. 1 Publication2
Mutagenesisi356Y → H in CAN1-340; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi356Y → N in CAN1-339; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi451W → C in CAN1-328; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi451W → L in CAN1-316; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi451W → S in CAN1-335; confers citrulline transport activity in GAP1-deleted cells. 1 Publication1
Mutagenesisi461F → S in CAN1-307; confers citrulline transport activity in GAP1-deleted cells. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000541481 – 590Arginine permease CAN1Add BLAST590

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 residuei54PhosphoserineBy similarity1
Modified residuei66PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Phosphorylated probably at multiple sites (PubMed:9544242).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P04817

PRoteomics IDEntifications database

More...
PRIDEi
P04817

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P04817

<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

Interacts with RRT2 (PubMed:21880895).

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
36666, 74 interactors

Database of interacting proteins

More...
DIPi
DIP-4062N

Protein interaction database and analysis system

More...
IntActi
P04817, 45 interactors

Molecular INTeraction database

More...
MINTi
P04817

STRING: functional protein association networks

More...
STRINGi
4932.YEL063C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P04817, 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
P04817

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

<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

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1286, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176760

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_007946_12_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P04817

Identification of Orthologs from Complete Genome Data

More...
OMAi
CLCMVCG

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR004841, AA-permease/SLC12A_dom
IPR004762, Amino_acid_permease_fungi
IPR004840, Amoino_acid_permease_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00324, AA_permease, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00913, 2A0310, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00218, AMINO_ACID_PERMEASE_1, 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.

P04817-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MTNSKEDADI EEKHMYNEPV TTLFHDVEAS QTHHRRGSIP LKDEKSKELY
60 70 80 90 100
PLRSFPTRVN GEDTFSMEDG IGDEDEGEVQ NAEVKRELKQ RHIGMIALGG
110 120 130 140 150
TIGTGLFIGL STPLTNAGPV GALISYLFMG SLAYSVTQSL GEMATFIPVT
160 170 180 190 200
SSFTVFSQRF LSPAFGAANG YMYWFSWAIT FALELSVVGQ VIQFWTYKVP
210 220 230 240 250
LAAWISIFWV IITIMNLFPV KYYGEFEFWV ASIKVLAIIG FLIYCFCMVC
260 270 280 290 300
GAGVTGPVGF RYWRNPGAWG PGIISKDKNE GRFLGWVSSL INAAFTFQGT
310 320 330 340 350
ELVGITAGEA ANPRKSVPRA IKKVVFRILT FYIGSLLFIG LLVPYNDPKL
360 370 380 390 400
TQSTSYVSTS PFIIAIENSG TKVLPHIFNA VILTTIISAA NSNIYVGSRI
410 420 430 440 450
LFGLSKNKLA PKFLSRTTKG GVPYIAVFVT AAFGALAYME TSTGGDKVFE
460 470 480 490 500
WLLNITGVAG FFAWLFISIS HIRFMQALKY RGISRDELPF KAKLMPGLAY
510 520 530 540 550
YAATFMTIII IIQGFTAFAP KFNGVSFAAA YISIFLFLAV WILFQCIFRC
560 570 580 590
RFIWKIGDVD IDSDRRDIEA IVWEDHEPKT FWDKFWNVVA
Length:590
Mass (Da):65,785
Last modified:February 1, 1995 - v2
<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:i4E5A21C77145330D
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 conflicti534I → V in CAA27416 (PubMed:3327612).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
X03784 Genomic DNA Translation: CAA27416.1
M11724 Genomic DNA Translation: AAA34467.1
U18795 Genomic DNA Translation: AAB65024.1
BK006939 Genomic DNA Translation: DAA07591.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A23922, QRBYPR

NCBI Reference Sequences

More...
RefSeqi
NP_010851.1, NM_001178878.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YEL063C_mRNA; YEL063C; YEL063C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
856646

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YEL063C

<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
X03784 Genomic DNA Translation: CAA27416.1
M11724 Genomic DNA Translation: AAA34467.1
U18795 Genomic DNA Translation: AAB65024.1
BK006939 Genomic DNA Translation: DAA07591.1
PIRiA23922, QRBYPR
RefSeqiNP_010851.1, NM_001178878.1

3D structure databases

SMRiP04817
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi36666, 74 interactors
DIPiDIP-4062N
IntActiP04817, 45 interactors
MINTiP04817
STRINGi4932.YEL063C

Protein family/group databases

TCDBi2.A.3.10.4, the amino acid-polyamine-organocation (apc) family

PTM databases

iPTMnetiP04817

Proteomic databases

PaxDbiP04817
PRIDEiP04817

Genome annotation databases

EnsemblFungiiYEL063C_mRNA; YEL063C; YEL063C
GeneIDi856646
KEGGisce:YEL063C

Organism-specific databases

SGDiS000000789, CAN1
VEuPathDBiFungiDB:YEL063C

Phylogenomic databases

eggNOGiKOG1286, Eukaryota
GeneTreeiENSGT00940000176760
HOGENOMiCLU_007946_12_1_1
InParanoidiP04817
OMAiCLCMVCG

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P04817
RNActiP04817, protein

Family and domain databases

InterProiView protein in InterPro
IPR004841, AA-permease/SLC12A_dom
IPR004762, Amino_acid_permease_fungi
IPR004840, Amoino_acid_permease_CS
PfamiView protein in Pfam
PF00324, AA_permease, 1 hit
TIGRFAMsiTIGR00913, 2A0310, 1 hit
PROSITEiView protein in PROSITE
PS00218, AMINO_ACID_PERMEASE_1, 1 hit

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 nameiCAN1_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: P04817
Secondary accession number(s): D3DLI7
<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: August 13, 1987
Last sequence update: February 1, 1995
Last modified: February 23, 2022
This is version 184 of the entry and version 2 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. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome V
    Yeast (Saccharomyces cerevisiae) chromosome V: entries and gene names
  3. 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