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Entry version 190 (29 Sep 2021)
Sequence version 1 (01 Oct 1989)
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Protein

5'-AMP-activated protein kinase subunit gamma

Gene

SNF4

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

Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming processes: inhibits protein, carbohydrate and lipid biosynthesis, as well as cell growth and proliferation. AMPK acts via direct phosphorylation of metabolic enzymes, and by longer-term effects via phosphorylation of transcription regulators. Gamma non-catalytic subunit mediates binding to AMP, ADP and ATP, leading to activate or inhibit AMPK: AMP-binding results in allosteric activation of alpha catalytic subunit (SNF1) both by inducing phosphorylation and preventing dephosphorylation of catalytic subunits.

18 Publications

Miscellaneous

Present with 11700 molecules/cell in log phase SD medium.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei42ADP 1; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei146ADP 1By similarity1
Binding sitei195ADP 2By similarity1
Binding sitei195AMPCombined sources1 Publication1
Binding sitei195ATPCombined sources1 Publication1
Binding sitei200AMP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1
Binding sitei200ATP; via amide nitrogen and carbonyl oxygenCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi166 – 169ADP 1By similarity4
Nucleotide bindingi221 – 222ADP 2By similarity2
Nucleotide bindingi221 – 222AMPCombined sources1 Publication2
Nucleotide bindingi221 – 222ATPCombined sources1 Publication2
Nucleotide bindingi291 – 293ADP 1By similarity3
Nucleotide bindingi309 – 312ADP 2By similarity4
Nucleotide bindingi309 – 312AMPCombined sources1 Publication4
Nucleotide bindingi309 – 312ATPCombined sources1 Publication4

<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 processCarbohydrate metabolism, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-SCE-1632852, Macroautophagy
R-SCE-163680, AMPK inhibits chREBP transcriptional activation activity
R-SCE-200425, Carnitine metabolism
R-SCE-380972, Energy dependent regulation of mTOR by LKB1-AMPK

<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:
5'-AMP-activated protein kinase subunit gamma
Short name:
AMPK gamma
Short name:
AMPK subunit gamma
Alternative name(s):
Regulatory protein CAT3
Sucrose non-fermenting protein 4
<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:SNF4
Synonyms:CAT3, SCI1
Ordered Locus Names:YGL115W
<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 VII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000003083, SNF4

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YGL115W

<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

Keywords - Cellular componenti

Cytoplasm, 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

<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

Leads to a decrease in the length of G1 with respect to the wild-type strain along with a smaller difference in the cell cycle length of parent and daughter cells.1 Publication

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>Mutagenesisi63V → Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi136C → Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi145G → E: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi146R → A or Q: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi166T → N: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi177N → A or Y: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi242L → E: Decreases SNF1-activation efficiency; when associated with A-291 and E-293. 1 Publication1
Mutagenesisi251N → I: Leads to resistance to 2-deoxyglucose. 1 Publication1
Mutagenesisi291R → A: Decreases SNF1-activation efficiency; when associated with E-242 and E-293. 1 Publication1
Mutagenesisi293H → A: Reduces glucose inhibition of SNF1 and leads to resistance to 2-deoxyglucose. 2 Publications1
Mutagenesisi293H → E: Decreases SNF1-activation efficiency; when associated with E-242 and A-291. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002043891 – 3225'-AMP-activated protein kinase subunit gammaAdd BLAST322

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P12904

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

More...
PaxDbi
P12904

PRoteomics IDEntifications database

More...
PRIDEi
P12904

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P12904

<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

AMPK is a heterotrimer of an alpha catalytic subunit (SNF1), a beta (SIP1, SIP2 or GAL83) and a gamma non-catalytic subunits (SNF4). Note=Interaction between SNF1 and SNF4 is inhibited by high levels of glucose.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
33136, 674 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...
ComplexPortali
CPX-231, Snf1 protein kinase complex variant GAL83
CPX-232, Snf1 protein kinase complex variant SIP1
CPX-2800, Snf1 protein kinase complex variant SIP2

Database of interacting proteins

More...
DIPi
DIP-592N

Protein interaction database and analysis system

More...
IntActi
P12904, 43 interactors

Molecular INTeraction database

More...
MINTi
P12904

STRING: functional protein association networks

More...
STRINGi
4932.YGL115W

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P12904, 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

Secondary structure

1322
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P12904

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P12904

<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>Domaini37 – 97CBS 1PROSITE-ProRule annotationAdd BLAST61
Domaini118 – 181CBS 2PROSITE-ProRule annotationAdd BLAST64
Domaini194 – 253CBS 3PROSITE-ProRule annotationAdd BLAST60
Domaini262 – 322CBS 4PROSITE-ProRule annotationAdd BLAST61

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The 4 CBS domains mediate binding to nucleotides. Of the 4 potential nucleotide-binding sites, 2 are occupied, designated as sites 2 and 3 based on the CBS modules that provide the acidic residue for coordination with the 2'- and 3'-hydroxyl groups of the ribose of AMP. Site 3 can bind either AMP, ADP or ATP (AMP, ADP or ATP 2). Site 2 binds specifically ADP (ADP 1) and is likely to be responsible for protection of a conserved threonine in the activation loop of the alpha catalytic subunit through conformational changes induced by binding of ADP (PubMed:22019086).1 Publication

<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

CBS domain, Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1764, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00950000183019

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_021740_1_0_1

Identification of Orthologs from Complete Genome Data

More...
OMAi
LNCKETK

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000644, CBS_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00571, CBS, 3 hits

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00116, CBS, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51371, CBS, 4 hits

<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>. 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_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.

P12904-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKPTQDSQEK VSIEQQLAVE SIRKFLNSKT SYDVLPVSYR LIVLDTSLLV
60 70 80 90 100
KKSLNVLLQN SIVSAPLWDS KTSRFAGLLT TTDFINVIQY YFSNPDKFEL
110 120 130 140 150
VDKLQLDGLK DIERALGVDQ LDTASIHPSR PLFEACLKML ESRSGRIPLI
160 170 180 190 200
DQDEETHREI VVSVLTQYRI LKFVALNCRE THFLKIPIGD LNIITQDNMK
210 220 230 240 250
SCQMTTPVID VIQMLTQGRV SSVPIIDENG YLINVYEAYD VLGLIKGGIY
260 270 280 290 300
NDLSLSVGEA LMRRSDDFEG VYTCTKNDKL STIMDNIRKA RVHRFFVVDD
310 320
VGRLVGVLTL SDILKYILLG SN
Length:322
Mass (Da):36,401
Last modified:October 1, 1989 - 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:i51B387E346EE9561
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
M21760 Genomic DNA Translation: AAA34472.1
M30470 Genomic DNA Translation: AAA35061.1
Z72637 Genomic DNA Translation: CAA96823.1
D16506 Genomic DNA Translation: BAA03958.1
BK006941 Genomic DNA Translation: DAA07993.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A38906, RGBYC3

NCBI Reference Sequences

More...
RefSeqi
NP_011400.1, NM_001180980.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YGL115W_mRNA; YGL115W; YGL115W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
852763

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YGL115W

<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
M21760 Genomic DNA Translation: AAA34472.1
M30470 Genomic DNA Translation: AAA35061.1
Z72637 Genomic DNA Translation: CAA96823.1
D16506 Genomic DNA Translation: BAA03958.1
BK006941 Genomic DNA Translation: DAA07993.1
PIRiA38906, RGBYC3
RefSeqiNP_011400.1, NM_001180980.1

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
2NYCX-ray1.90A179-322[»]
2NYEX-ray2.50A/B179-322[»]
2QLVX-ray2.60C/F7-321[»]
3T4NX-ray2.30C2-322[»]
3TDHX-ray2.30C2-322[»]
3TE5X-ray2.50C2-322[»]
SMRiP12904
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi33136, 674 interactors
ComplexPortaliCPX-231, Snf1 protein kinase complex variant GAL83
CPX-232, Snf1 protein kinase complex variant SIP1
CPX-2800, Snf1 protein kinase complex variant SIP2
DIPiDIP-592N
IntActiP12904, 43 interactors
MINTiP12904
STRINGi4932.YGL115W

PTM databases

iPTMnetiP12904

Proteomic databases

MaxQBiP12904
PaxDbiP12904
PRIDEiP12904

Genome annotation databases

EnsemblFungiiYGL115W_mRNA; YGL115W; YGL115W
GeneIDi852763
KEGGisce:YGL115W

Organism-specific databases

SGDiS000003083, SNF4
VEuPathDBiFungiDB:YGL115W

Phylogenomic databases

eggNOGiKOG1764, Eukaryota
GeneTreeiENSGT00950000183019
HOGENOMiCLU_021740_1_0_1
OMAiLNCKETK

Enzyme and pathway databases

ReactomeiR-SCE-1632852, Macroautophagy
R-SCE-163680, AMPK inhibits chREBP transcriptional activation activity
R-SCE-200425, Carnitine metabolism
R-SCE-380972, Energy dependent regulation of mTOR by LKB1-AMPK

Miscellaneous databases

EvolutionaryTraceiP12904

Protein Ontology

More...
PROi
PR:P12904
RNActiP12904, protein

Family and domain databases

InterProiView protein in InterPro
IPR000644, CBS_dom
PfamiView protein in Pfam
PF00571, CBS, 3 hits
SMARTiView protein in SMART
SM00116, CBS, 4 hits
PROSITEiView protein in PROSITE
PS51371, CBS, 4 hits

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 nameiAAKG_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: P12904
Secondary accession number(s): D6VU32
<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, 1989
Last sequence update: October 1, 1989
Last modified: September 29, 2021
This is version 190 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, Direct protein sequencing, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: 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
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