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UniProtKB - P15274 (AMPD_YEAST)

Entry version 192 (10 Feb 2021)
Sequence version 2 (01 Feb 1996)
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Protein

AMP deaminase

Gene

AMD1

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

AMP deaminase plays a critical role in energy metabolism.

Miscellaneous

Present with 3910 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: IMP biosynthesis via salvage pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from AMP.
Proteins known to be involved in this subpathway in this organism are:
  1. AMP deaminase (AMD1)
This subpathway is part of the pathway IMP biosynthesis via salvage pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from AMP, the pathway IMP biosynthesis via salvage pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi362Zinc; catalyticBy similarity1
Metal bindingi364Zinc; catalyticBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei364SubstrateBy similarity1
Metal bindingi630Zinc; catalyticBy similarity1
Binding sitei633SubstrateBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 sitei652Proton acceptorPROSITE-ProRule annotation1
Metal bindingi707Zinc; catalyticBy similarity1

<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

  • AMP deaminase activity Source: SGD
  • metal ion binding Source: UniProtKB-KW
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase
Biological processNucleotide metabolism
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-SCE-6798695, Neutrophil degranulation
R-SCE-74217, Purine salvage

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

More...UniPathwayi		UPA00591;UER00663

<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:
AMP deaminase (EC:3.5.4.6)
Alternative name(s):
Myoadenylate deaminase
<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:AMD1
Synonyms:AMD
Ordered Locus Names:YML035C
<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 lineageiEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces ›
<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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...SGDi		S000004498, AMD1

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		FungiDB:YML035C

<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>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_00001944141 – 810AMP deaminaseAdd BLAST810

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 residuei19PhosphoserineCombined sources1
Modified residuei58PhosphoserineCombined sources1
Modified residuei61PhosphoserineCombined sources1
Modified residuei138PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...MaxQBi		P15274

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

More...PaxDbi		P15274

PRoteomics IDEntifications database

More...PRIDEi		P15274

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P15274

<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

Homotetramer.

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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		35135, 217 interactors

Database of interacting proteins

More...DIPi		DIP-1949N

Protein interaction database and analysis system

More...IntActi		P15274, 11 interactors

Molecular INTeraction database

More...MINTi		P15274

STRING: functional protein association networks

More...STRINGi		4932.YML035C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P15274, protein

<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

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni433 – 438Substrate bindingBy similarity6
Regioni708 – 711Substrate bindingBy similarity4

<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 metallo-dependent hydrolases superfamily. Adenosine and AMP deaminases family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG1096, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00950000183011

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_003782_2_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P15274

Identification of Orthologs from Complete Genome Data

More...OMAi		QHVEWRI

Family and domain databases

Conserved Domains Database

More...CDDi		cd01319, AMPD, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR006650, A/AMP_deam_AS
IPR001365, A/AMP_deaminase_dom
IPR006329, AMPD
IPR032466, Metal_Hydrolase

The PANTHER Classification System

More...PANTHERi		PTHR11359, PTHR11359, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00962, A_deaminase, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001251, AMP_deaminase_met, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF51556, SSF51556, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01429, AMP_deaminase, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00485, A_DEAMINASE, 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.

P15274-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MDNQATQRLN DLSLEPAPSH DEQDGSGLVI DIDQRKIGDE QAGVVVDDET 
        60         70         80         90        100
PPLEQQDSHE SLAADSRNAN FSYHENQQLL ENGTKQLALD EHDSHSAILE 
       110        120        130        140        150
QPSHSTNCSS SNIAAMNKGH DSADHASQNS GGKPRTLSAS AQHILPETLK 
       160        170        180        190        200
SFAGAPVVNK QVRTSASYKM GMLADDASQQ FLDDPSSELI DLYSKVAECR 
       210        220        230        240        250
NLRAKYQTIS VQNDDQNPKN KPGWVVYPPP PKPSYNSDTK TVVPVTNKPD 
       260        270        280        290        300
AEVFDFTKCE IPGEDPDWEF TLNDDDSYVV HRSGKTDELI AQIPTLRDYY 
       310        320        330        340        350
LDLEKMISIS SDGPAKSFAY RRLQYLEARW NLYYLLNEYQ ETSVSKRNPH 
       360        370        380        390        400
RDFYNVRKVD THVHHSACMN QKHLLRFIKH KLRHSKDEKV IFRDGKLLTL 
       410        420        430        440        450
DEVFRSLHLT GYDLSIDTLD MHAHKDTFHR FDKFNLKYNP IGESRLREIF 
       460        470        480        490        500
LKTNNYIKGT YLADITKQVI FDLENSKYQN CEYRISVYGR SLDEWDKLAS 
       510        520        530        540        550
WVIDNKVISH NVRWLVQIPR LYDIYKKTGI VQSFQDICKN LFQPLFEVTK 
       560        570        580        590        600
NPQSHPKLHV FLQRVIGFDS VDDESKVDRR FHRKYPKPSL WEAPQNPPYS 
       610        620        630        640        650
YYLYYLYSNV ASLNQWRAKR GFNTLVLRPH CGEAGDPEHL VSAYLLAHGI 
       660        670        680        690        700
SHGILLRKVP FVQYLYYLDQ VGIAMSPLSN NALFLTYDKN PFPRYFKRGL 
       710        720        730        740        750
NVSLSTDDPL QFSYTREPLI EEYSVAAQIY KLSNVDMCEL ARNSVLQSGW 
       760        770        780        790        800
EAQIKKHWIG KDFDKSGVEG NDVVRTNVPD IRINYRYDTL STELELVNHF 
       810
ANFKRTIEEK
Length:810
Mass (Da):93,302
Last modified:February 1, 1996 - 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:i7A6DCB43B9B45C93
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 conflicti568F → C in AAA34420 (PubMed:2690949).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
M30449 Genomic DNA Translation: AAA34420.1
Z46659 Genomic DNA Translation: CAA86620.1
BK006946 Genomic DNA Translation: DAA09864.1

Protein sequence database of the Protein Information Resource

More...PIRi		S49744

NCBI Reference Sequences

More...RefSeqi		NP_013677.1, NM_001182392.1

Genome annotation databases

Ensembl fungal genome annotation project

More...EnsemblFungii		YML035C_mRNA; YML035C; YML035C

Database of genes from NCBI RefSeq genomes

More...GeneIDi		854973

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		sce:YML035C

<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
M30449 Genomic DNA Translation: AAA34420.1
Z46659 Genomic DNA Translation: CAA86620.1
BK006946 Genomic DNA Translation: DAA09864.1
PIRiS49744
RefSeqiNP_013677.1, NM_001182392.1

3D structure databases

Database of comparative protein structure models

More...ModBasei		Search...

SWISS-MODEL Interactive Workspace

More...SWISS-MODEL-Workspacei		Submit a new modelling project...

Protein-protein interaction databases

BioGRIDi35135, 217 interactors
DIPiDIP-1949N
IntActiP15274, 11 interactors
MINTiP15274
STRINGi4932.YML035C

PTM databases

iPTMnetiP15274

Proteomic databases

MaxQBiP15274
PaxDbiP15274
PRIDEiP15274

Genome annotation databases

EnsemblFungiiYML035C_mRNA; YML035C; YML035C
GeneIDi854973
KEGGisce:YML035C

Organism-specific databases

SGDiS000004498, AMD1
VEuPathDBiFungiDB:YML035C

Phylogenomic databases

eggNOGiKOG1096, Eukaryota
GeneTreeiENSGT00950000183011
HOGENOMiCLU_003782_2_1_1
InParanoidiP15274
OMAiQHVEWRI

Enzyme and pathway databases

UniPathwayiUPA00591;UER00663
ReactomeiR-SCE-6798695, Neutrophil degranulation
R-SCE-74217, Purine salvage

Miscellaneous databases

Protein Ontology

More...PROi		PR:P15274
RNActiP15274, protein

Family and domain databases

CDDicd01319, AMPD, 1 hit
InterProiView protein in InterPro
IPR006650, A/AMP_deam_AS
IPR001365, A/AMP_deaminase_dom
IPR006329, AMPD
IPR032466, Metal_Hydrolase
PANTHERiPTHR11359, PTHR11359, 1 hit
PfamiView protein in Pfam
PF00962, A_deaminase, 1 hit
PIRSFiPIRSF001251, AMP_deaminase_met, 1 hit
SUPFAMiSSF51556, SSF51556, 1 hit
TIGRFAMsiTIGR01429, AMP_deaminase, 1 hit
PROSITEiView protein in PROSITE
PS00485, A_DEAMINASE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

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 nameiAMPD_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: P15274
Secondary accession number(s): D6VZE0
<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: April 1, 1990
Last sequence update: February 1, 1996
Last modified: February 10, 2021
This is version 192 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 XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families
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