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Entry version 161 (08 May 2019)
Sequence version 1 (01 Feb 1995)
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Protein

Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1

Gene

SLM1

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

Together with SLM2, effector of the TORC2- and calcineurin-signaling pathways. Phosphorylated and activated by TORC2 under favorable growth conditions. Mediates actin polarization via inhibition of calcineurin-dependent transcription. Upon nutrient limitation or environmental stress, gets dephosphorylated by calcineurin. Dephosphorylation inhibits its interaction with TORC2, thereby antagonizing TORC2 signaling and mediating calcineurin-dependent actin depolarization. Also functions in heat-induced, calcineurin-mediated uracil permease (FUR4) endocytosis.4 Publications

Miscellaneous

Present with 5190 molecules/cell in log phase SD medium.1 Publication

<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

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:G3O-31361-MONOMER

<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:
Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
Alternative name(s):
Synthetic lethal with MSS4 protein 1
TORC2 effector protein SLM1
<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:SLM1
Synonyms:LIT2
Ordered Locus Names:YIL105C
<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 IX

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YIL105C

Saccharomyces Genome Database

More...
SGDi
S000001367 SLM1

<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>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>Keywords - Cellular componenti

Cell membrane, 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>Mutagenesisi477 – 478RR → AA in SLM1-PHM2; reduces phosphoinositide binding by 95%; when associated with A-487. 1 Publication2
Mutagenesisi483K → A in SLM1-PHM1; reduces phosphoinositide binding by 80% and causes mislocalization to the cytoplasm; when associated with A-487. 2 Publications1
Mutagenesisi487K → A in SLM1-PHM1; reduces phosphoinositide binding by 80% and causes mislocalization to the cytoplasm; when associated with A-483. In SLM1-PHM2; reduces phosphoinositide binding by 95%; when associated with 477-AA-478. 2 Publications1

<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_00002029651 – 686Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1Add BLAST686

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 residuei145PhosphoserineCombined sources1
Modified residuei150PhosphoserineCombined sources1
Modified residuei153PhosphoserineCombined sources1

<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

Phosphorylated by the target of rapamycin complex 2 (TORC2) and dephosphorylated by serine/threonine-protein phosphatase 2B (calcineurin).1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P40485

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

More...
PaxDbi
P40485

PRoteomics IDEntifications database

More...
PRIDEi
P40485

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P40485

<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 SLM1-SLM2. Binds phosphatidylinositol 4,5-bisphosphate, which is required for function. Interacts with the TORC2 subunits AVO2, BIT61 and TOR2. Interacts with the calcineurin catalytic subunits CNA1 and CNA2.4 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

WithEntry#Exp.IntActNotes
itself3EBI-25172,EBI-25172

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
34886, 151 interactors

Database of interacting proteins

More...
DIPi
DIP-1353N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P40485

Protein interaction database and analysis system

More...
IntActi
P40485, 27 interactors

Molecular INTeraction database

More...
MINTi
P40485

STRING: functional protein association networks

More...
STRINGi
4932.YIL105C

<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

1686
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

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
3NSUX-ray2.00A/B469-583[»]
4A5KX-ray1.76A/B/C/D469-583[»]
4A6FX-ray1.68A/B469-583[»]
4A6HX-ray1.45A/B/C/D469-583[»]
4A6KX-ray1.80A/B/C/D469-583[»]

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

More...
SMRi
P40485

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

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>Domaini468 – 581PHPROSITE-ProRule annotationAdd BLAST114

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili296 – 381Sequence analysisAdd BLAST86

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>Motifi673 – 678PXIXIT-like, required for interaction with CNA1 and CNA2, and calcineurin-dependent dephosphorylation6

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi45 – 63Poly-GlnAdd BLAST19
Compositional biasi133 – 136Poly-Asn4
Compositional biasi166 – 172Poly-Gln7

Keywords - Domaini

Coiled coil

Phylogenomic databases

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000176324

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000066129

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P40485

Identification of Orthologs from Complete Genome Data

More...
OMAi
PFRSGNQ

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.1270.60, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR033191 Slm1/Slm2

The PANTHER Classification System

More...
PANTHERi
PTHR31941:SF12 PTHR31941:SF12, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00169 PH, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00233 PH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF103657 SSF103657, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50003 PH_DOMAIN, 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.

P40485-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSKNNTMTSA VSDMLSQQQL NLQHLHNLQQ HTRSMTSADH ANVLQQQQQQ
60 70 80 90 100
QQQQQQQQQQ QQQSASFQNG SLTSDINQQS YLNGQPVPST SNSTFQNNRT
110 120 130 140 150
LTMNSGGLQG IISNGSPNID SNTNVTIAVP DPNNNNGKQL QGKNSLTNTS
160 170 180 190 200
ILSRARSSLQ RQRLAQQQQQ QQDPRSPLVI LVPTAAQPTD ILAARFSAWR
210 220 230 240 250
NVIKSVIVYL TEIASIQDEI VRQQLRLSHA VQFPFFSIEN QYQPSSQEDK
260 270 280 290 300
SVQKFFLPLG NGSIQDLPTI LNQYHESLAS SASKASRELT NDVIPRLEDL
310 320 330 340 350
RRDLIVKIKE IKSLQSDFKN SCSKELQQTK QAMKQFQESL KDARYSVPKQ
360 370 380 390 400
DPFLTKLALD RQIKKQLQEE NFLHEAFDNL ETSGAELEKI VVMEIQNSLT
410 420 430 440 450
IYARLLGQEA QLVFDILISK LDSGFFNVDP QFEWDNFISR DPNFLLPNLP
460 470 480 490 500
MRTFKEIVYK YQFDPLTYEI KSGFLERRSK FLKSYSKGYY VLTPNFLHEF
510 520 530 540 550
KTADRKKDLV PVMSLALSEC TVTEHSRKNS TSSPNSTGSD AKFVLHAKQN
560 570 580 590 600
GIIRRGHNWV FKADSYESMM SWFDNLKILT STSNIQDKYK FITQKLNLNS
610 620 630 640 650
DGKPKLTNNH TSINKYQLSN ANSTMVENDE NDDINSNYVG STVTPKLDNQ
660 670 680
TNTNTSMSSL PDTNDSELQD QVPNIYIQTP INDFKS
Length:686
Mass (Da):77,995
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:i849C82CC0960014B
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z38125 Genomic DNA Translation: CAA86275.1
BK006942 Genomic DNA Translation: DAA08448.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S48467

NCBI Reference Sequences

More...
RefSeqi
NP_012161.1, NM_001179453.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YIL105C_mRNA; YIL105C_mRNA; YIL105C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854701

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YIL105C

<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
Z38125 Genomic DNA Translation: CAA86275.1
BK006942 Genomic DNA Translation: DAA08448.1
PIRiS48467
RefSeqiNP_012161.1, NM_001179453.1

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NSUX-ray2.00A/B469-583[»]
4A5KX-ray1.76A/B/C/D469-583[»]
4A6FX-ray1.68A/B469-583[»]
4A6HX-ray1.45A/B/C/D469-583[»]
4A6KX-ray1.80A/B/C/D469-583[»]
SMRiP40485
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi34886, 151 interactors
DIPiDIP-1353N
ELMiP40485
IntActiP40485, 27 interactors
MINTiP40485
STRINGi4932.YIL105C

PTM databases

iPTMnetiP40485

Proteomic databases

MaxQBiP40485
PaxDbiP40485
PRIDEiP40485

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYIL105C_mRNA; YIL105C_mRNA; YIL105C
GeneIDi854701
KEGGisce:YIL105C

Organism-specific databases

EuPathDBiFungiDB:YIL105C
SGDiS000001367 SLM1

Phylogenomic databases

GeneTreeiENSGT00940000176324
HOGENOMiHOG000066129
InParanoidiP40485
OMAiPFRSGNQ

Enzyme and pathway databases

BioCyciYEAST:G3O-31361-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P40485

Family and domain databases

Gene3Di1.20.1270.60, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR027267 AH/BAR_dom_sf
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
IPR033191 Slm1/Slm2
PANTHERiPTHR31941:SF12 PTHR31941:SF12, 1 hit
PfamiView protein in Pfam
PF00169 PH, 1 hit
SMARTiView protein in SMART
SM00233 PH, 1 hit
SUPFAMiSSF103657 SSF103657, 1 hit
PROSITEiView protein in PROSITE
PS50003 PH_DOMAIN, 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 nameiSLM1_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: P40485
Secondary accession number(s): D6VVI2
<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: May 8, 2019
This is version 161 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Yeast chromosome IX
    Yeast (Saccharomyces cerevisiae) chromosome IX: entries and gene names
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