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Entry version 182 (08 May 2019)
Sequence version 1 (01 Jan 1990)
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Protein

Aspartate-semialdehyde dehydrogenase

Gene

HOM2

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

Catalyzes the NADPH-dependent formation of L-aspartate-semialdehyde (L-ASA) by the reductive dephosphorylation of L-aspartyl-4-phosphate.By similarity

Miscellaneous

Present with 18400 molecules/cell in log phase SD medium.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: L-lysine biosynthesis via DAP pathway

This protein is involved in step 2 of the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate.
Proteins known to be involved in the 4 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. no protein annotated in this organism
  4. no protein annotated in this organism
This subpathway is part of the pathway L-lysine biosynthesis via DAP pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-tetrahydrodipicolinate from L-aspartate, the pathway L-lysine biosynthesis via DAP pathway and in Amino-acid biosynthesis.

Pathwayi: L-methionine biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes L-homoserine from L-aspartate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. Homoserine dehydrogenase (HOM6)
This subpathway is part of the pathway L-methionine biosynthesis via de novo pathway, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-homoserine from L-aspartate, the pathway L-methionine biosynthesis via de novo pathway and in Amino-acid biosynthesis.

Pathwayi: L-threonine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-threonine from L-aspartate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. Aspartokinase (HOM3)
  2. Aspartate-semialdehyde dehydrogenase (HOM2)
  3. Homoserine dehydrogenase (HOM6)
  4. Homoserine kinase (THR1)
  5. Threonine synthase (THR4)
This subpathway is part of the pathway L-threonine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-threonine from L-aspartate, the pathway L-threonine biosynthesis and in Amino-acid biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 sitei112PhosphateBy similarity1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei156Acyl-thioester intermediateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei211SubstrateBy similarity1
Binding sitei214PhosphateBy similarity1
Binding sitei249SubstrateBy similarity1
Active sitei256Proton acceptorBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ 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 bindingi13 – 16NADPBy similarity4
Nucleotide bindingi40 – 41NADPBy similarity2
Nucleotide bindingi187 – 188NADPBy similarity2
Nucleotide bindingi343 – 344NADPBy similarity2

<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

Molecular functionOxidoreductase
Biological processAmino-acid biosynthesis, Lysine biosynthesis, Methionine biosynthesis, Threonine biosynthesis
LigandNADP

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
YEAST:YDR158W-MONOMER

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

More...
UniPathwayi
UPA00034;UER00016

UPA00050;UER00463

UPA00051;UER00464

<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:
Aspartate-semialdehyde dehydrogenase (EC:1.2.1.11)
Short name:
ASA dehydrogenase
Short name:
ASADH
Alternative name(s):
Aspartate-beta-semialdehyde dehydrogenase
<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:HOM2
Ordered Locus Names:YDR158W
ORF Names:YD8358.12
<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 IV

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
FungiDB:YDR158W

Saccharomyces Genome Database

More...
SGDi
S000002565 HOM2

<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.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001414001 – 365Aspartate-semialdehyde dehydrogenaseAdd BLAST365

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 residuei13PhosphothreonineCombined sources1
Modified residuei318PhosphoserineCombined sources1
Modified residuei323PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
P13663

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

More...
PaxDbi
P13663

PRoteomics IDEntifications database

More...
PRIDEi
P13663

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...
SWISS-2DPAGEi
P13663

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P13663

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

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

By high concentrations of Met (general AA biosynthesis control).

<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

Homodimer.

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
32209, 342 interactors

Database of interacting proteins

More...
DIPi
DIP-5204N

Protein interaction database and analysis system

More...
IntActi
P13663, 22 interactors

Molecular INTeraction database

More...
MINTi
P13663

STRING: functional protein association networks

More...
STRINGi
4932.YDR158W

<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
P13663

Database of comparative protein structure models

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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

<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

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000013358

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P13663

KEGG Orthology (KO)

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KOi
K00133

Identification of Orthologs from Complete Genome Data

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OMAi
CEEEMKM

Family and domain databases

HAMAP database of protein families

More...
HAMAPi
MF_02121 ASADH, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000319 Asp-semialdehyde_DH_CS
IPR005676 Asp_semi-ald_DH_pep-lack
IPR012080 Asp_semialdehyde_DH
IPR036291 NAD(P)-bd_dom_sf
IPR000534 Semialdehyde_DH_NAD-bd
IPR012280 Semialdhyde_DH_dimer_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF01118 Semialdhyde_dh, 1 hit
PF02774 Semialdhyde_dhC, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00859 Semialdhyde_dh, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51735 SSF51735, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR00978 asd_EA, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS01103 ASD, 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.

P13663-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAGKKIAGVL GATGSVGQRF ILLLANHPHF ELKVLGASSR SAGKKYVDAV
60 70 80 90 100
NWKQTDLLPE SATDIIVSEC KSEFFKECDI VFSGLDADYA GAIEKEFMEA
110 120 130 140 150
GIAIVSNAKN YRREQDVPLI VPVVNPEHLD IVAQKLDTAK AQGKPRPGFI
160 170 180 190 200
ICISNCSTAG LVAPLKPLIE KFGPIDALTT TTLQAISGAG FSPGVPGIDI
210 220 230 240 250
LDNIIPYIGG EEDKMEWETK KILAPLAEDK THVKLLTPEE IKVSAQCNRV
260 270 280 290 300
AVSDGHTECI SLRFKNRPAP SVEQVKTCLK EYVCDAYKLG CHSAPKQTIH
310 320 330 340 350
VLEQPDRPQP RLDRNRDSGY GVSVGRIRED PLLDFKMVVL SHNTIIGAAG
360
SGVLIAEILL ARNLI
Length:365
Mass (Da):39,544
Last modified:January 1, 1990 - 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:iD33096DA8C2B6424
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
X15649 Genomic DNA Translation: CAA33675.1
Z50046 Genomic DNA Translation: CAA90378.1
AY557698 Genomic DNA Translation: AAS56024.1
BK006938 Genomic DNA Translation: DAA11998.1

Protein sequence database of the Protein Information Resource

More...
PIRi
JQ0198

NCBI Reference Sequences

More...
RefSeqi
NP_010442.3, NM_001180465.3

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YDR158W_mRNA; YDR158W_mRNA; YDR158W

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
851736

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YDR158W

<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
X15649 Genomic DNA Translation: CAA33675.1
Z50046 Genomic DNA Translation: CAA90378.1
AY557698 Genomic DNA Translation: AAS56024.1
BK006938 Genomic DNA Translation: DAA11998.1
PIRiJQ0198
RefSeqiNP_010442.3, NM_001180465.3

3D structure databases

SMRiP13663
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi32209, 342 interactors
DIPiDIP-5204N
IntActiP13663, 22 interactors
MINTiP13663
STRINGi4932.YDR158W

PTM databases

iPTMnetiP13663

2D gel databases

SWISS-2DPAGEiP13663

Proteomic databases

MaxQBiP13663
PaxDbiP13663
PRIDEiP13663

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDR158W_mRNA; YDR158W_mRNA; YDR158W
GeneIDi851736
KEGGisce:YDR158W

Organism-specific databases

EuPathDBiFungiDB:YDR158W
SGDiS000002565 HOM2

Phylogenomic databases

HOGENOMiHOG000013358
InParanoidiP13663
KOiK00133
OMAiCEEEMKM

Enzyme and pathway databases

UniPathwayi
UPA00034;UER00016

UPA00050;UER00463

UPA00051;UER00464

BioCyciYEAST:YDR158W-MONOMER

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P13663

Family and domain databases

HAMAPiMF_02121 ASADH, 1 hit
InterProiView protein in InterPro
IPR000319 Asp-semialdehyde_DH_CS
IPR005676 Asp_semi-ald_DH_pep-lack
IPR012080 Asp_semialdehyde_DH
IPR036291 NAD(P)-bd_dom_sf
IPR000534 Semialdehyde_DH_NAD-bd
IPR012280 Semialdhyde_DH_dimer_dom
PfamiView protein in Pfam
PF01118 Semialdhyde_dh, 1 hit
PF02774 Semialdhyde_dhC, 1 hit
SMARTiView protein in SMART
SM00859 Semialdhyde_dh, 1 hit
SUPFAMiSSF51735 SSF51735, 1 hit
TIGRFAMsiTIGR00978 asd_EA, 1 hit
PROSITEiView protein in PROSITE
PS01103 ASD, 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 nameiDHAS_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: P13663
Secondary accession number(s): D6VSD8
<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: January 1, 1990
Last sequence update: January 1, 1990
Last modified: May 8, 2019
This is version 182 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

Complete proteome, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome IV
    Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families
  4. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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