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Entry version 164 (02 Jun 2021)
Sequence version 1 (01 May 2000)
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Protein

Alanine--glyoxylate aminotransferase

Gene

Agxt

Organism
Drosophila melanogaster (Fruit fly)
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 pyridoxal 5'-phosphate-dependent transamination of alanine with glyoxylate as an amino group acceptor (PubMed:12220660).

Can also catalyze, although with much less efficiency, the transamination of amino-butyrate, phenylalanine and serine with glyoxylate or pyruvate as an amino group acceptor (PubMed:12220660).

Does not catalyze the transamination of both 3-hydroxykynurenine and L-kynurenine (PubMed:12220660).

May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the fly diet (Probable).

1 Publication1 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

pyridoxal 5'-phosphateUniRule annotation

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

kcat is 6800 min(-1) for glyoxylate (at 50 degrees Celsius, pH 7 and with alanine as cosubstrate) (PubMed:12220660). kcat is 7880 min(-1) for alanine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:12220660).1 Publication
  1. KM=64 mM for glyoxylate (at 50 degrees Celsius, pH 7 and with alanine as cosubstrate)1 Publication
  2. KM=149 mM for alanine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)1 Publication
  1. Vmax=170 µmol/min/mg enzyme toward glyoxylate (at 50 degrees Celsius, pH 7 and with alanine as cosubstrate)1 Publication
  2. Vmax=197 µmol/min/mg enzyme toward alanine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)1 Publication

pH dependencei

Optimum pH is 9 with alanine and glyoxylate as substrates.1 Publication

Temperature dependencei

Optimum temperature is between 30 and 80 degrees Celsius with alanine and glyoxylate as substrates.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 sitei153Pyridoxal phosphateBy similarity1
Binding sitei153SubstrateBy similarity1
Binding sitei204Pyridoxal phosphateBy similarity1
Binding sitei256Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei259Pyridoxal phosphate; shared with dimeric partnerBy similarity1
Binding sitei356SubstrateBy 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

  • alanine-glyoxylate transaminase activity Source: FlyBase
  • serine-pyruvate transaminase activity Source: GO_Central

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 functionAminotransferase, Transferase
LigandPyridoxal phosphate, Pyruvate

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-389661, Glyoxylate metabolism and glycine degradation
R-DME-9033241, Peroxisomal protein import

<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:
Alanine--glyoxylate aminotransferaseUniRule annotation (EC:2.6.1.44UniRule annotation1 Publication)
Short name:
AGTCurated
<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:Agxt1 PublicationImported
Synonyms:SpatImported
ORF Names:CG3926Imported
<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>OrganismiDrosophila melanogaster (Fruit fly)Imported
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 X

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0014031, Agxt

<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

Peroxisome

<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

RNAi-mediated knockdown causes accumulation of calcium oxalate crystals in Malpighian tubules.1 Publication

<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_00004521871 – 394Alanine--glyoxylate aminotransferaseAdd BLAST394

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 residuei205N6-(pyridoxal phosphate)lysineUniRule annotation1

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0014031, Expressed in Malpighian tubule and 30 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
Q9W3Z3, baseline and differential

<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

Homodimer.

1 Publication

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0070875

<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
Q9W3Z3

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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>Regioni76 – 78Pyridoxal phosphate bindingBy similarity3

<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 class-V pyridoxal-phosphate-dependent aminotransferase family.UniRule annotation

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2862, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000153241

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_027686_0_0_1

Identification of Orthologs from Complete Genome Data

More...
OMAi
GQTHSTP

Database of Orthologous Groups

More...
OrthoDBi
984738at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.640.10, 1 hit
3.90.1150.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000192, Aminotrans_V_dom
IPR020578, Aminotrans_V_PyrdxlP_BS
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major
IPR024169, SP_NH2Trfase/AEP_transaminase

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00266, Aminotran_5, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000524, SPT, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF53383, SSF53383, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00595, AA_TRANSFER_CLASS_5, 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.

Q9W3Z3-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MEVPPPLVLK RPLYVPSKTL MGPGPSNCSH RVLEAMSNPV LGHMHPECLQ
60 70 80 90 100
IMDEVKEGIK YIFQTLNDAT MCISGAGHSG MEAALCNLIE DGDVVLMGIT
110 120 130 140 150
GVWGHRAGDM ARRYGAEVHY VEASFGRALS HEEITFAFEA HRPKVFFIAQ
160 170 180 190 200
GDSSTGIIQQ NIRELGELCR KYDCFLIVDT VASLGGTEFL MDEWKVDVAY
210 220 230 240 250
TGSQKSLGGP AGLTPISFSK RALTRIRKRK TKPKVYYFDI LLIGQYWGCY
260 270 280 290 300
GTPRIYHHTI SSTLLYGLRE ALAHFCAVGL KAVVRRHQEC SKRLQLGIEE
310 320 330 340 350
LGLEMFVSRE EERLPTVNTI KVPFGVDWKK VAEYAMRKYS VEISGGLGPT
360 370 380 390
VEHVFRIGLM GENATVERVD MVLSILNEAI QSSKLGIKTD LSKI
Length:394
Mass (Da):43,800
Last modified:May 1, 2000 - 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:iFB4695B4733C1B11
GO

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL39372 differs from that shown. Intron retention.Curated
The sequence AAL39372 differs from that shown. Reason: Frameshift.Curated

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 conflicti184L → P in ACU24744 (Ref. 4) 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
AE014298 Genomic DNA Translation: AAF46168.1
AY069227 mRNA Translation: AAL39372.1 Sequence problems.
BT099504 mRNA Translation: ACU24744.1
BT133279 mRNA Translation: AFC38910.1

NCBI Reference Sequences

More...
RefSeqi
NP_511062.1, NM_078507.2

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0070913; FBpp0070875; FBgn0014031

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
31587

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG3926

UCSC genome browser

More...
UCSCi
CG3926-RA, d. melanogaster

<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
AE014298 Genomic DNA Translation: AAF46168.1
AY069227 mRNA Translation: AAL39372.1 Sequence problems.
BT099504 mRNA Translation: ACU24744.1
BT133279 mRNA Translation: AFC38910.1
RefSeqiNP_511062.1, NM_078507.2

3D structure databases

SMRiQ9W3Z3
ModBaseiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0070875

Genome annotation databases

EnsemblMetazoaiFBtr0070913; FBpp0070875; FBgn0014031
GeneIDi31587
KEGGidme:Dmel_CG3926
UCSCiCG3926-RA, d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
31587
FlyBaseiFBgn0014031, Agxt

Phylogenomic databases

eggNOGiKOG2862, Eukaryota
GeneTreeiENSGT00940000153241
HOGENOMiCLU_027686_0_0_1
OMAiGQTHSTP
OrthoDBi984738at2759

Enzyme and pathway databases

ReactomeiR-DME-389661, Glyoxylate metabolism and glycine degradation
R-DME-9033241, Peroxisomal protein import

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
31587, 0 hits in 3 CRISPR screens

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
31587

Gene expression databases

BgeeiFBgn0014031, Expressed in Malpighian tubule and 30 other tissues
ExpressionAtlasiQ9W3Z3, baseline and differential

Family and domain databases

Gene3Di3.40.640.10, 1 hit
3.90.1150.10, 1 hit
InterProiView protein in InterPro
IPR000192, Aminotrans_V_dom
IPR020578, Aminotrans_V_PyrdxlP_BS
IPR015424, PyrdxlP-dep_Trfase
IPR015422, PyrdxlP-dep_Trfase_dom1
IPR015421, PyrdxlP-dep_Trfase_major
IPR024169, SP_NH2Trfase/AEP_transaminase
PfamiView protein in Pfam
PF00266, Aminotran_5, 1 hit
PIRSFiPIRSF000524, SPT, 1 hit
SUPFAMiSSF53383, SSF53383, 1 hit
PROSITEiView protein in PROSITE
PS00595, AA_TRANSFER_CLASS_5, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAGT_DROME
<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: Q9W3Z3
Secondary accession number(s): C6TP18, Q8T0J1
<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 7, 2021
Last sequence update: May 1, 2000
Last modified: June 2, 2021
This is version 164 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 programDrosophila annotation project

<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. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families
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