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Entry version 229 (11 Dec 2019)
Sequence version 3 (29 Mar 2005)
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Protein

Insulin-like receptor

Gene

InR

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

Has a ligand-stimulated tyrosine-protein kinase activity. Required for cell survival. Regulates body size and organ size by altering cell number and cell size in a cell-autonomous manner. Involved in the development of the embryonic nervous system, and is necessary for axon guidance and targeting in the visual system. Also plays a role in life-span determination.6 Publications

<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 ‘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

Mn2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Autophosphorylation activates the kinase activity.

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 sitei1405ATPPROSITE-ProRule annotation1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">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 sitei1519Proton acceptorPROSITE-ProRule annotation1

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 bindingi1377 – 1385ATPPROSITE-ProRule annotation9

<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 functionDevelopmental protein, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processDifferentiation, Growth regulation, Neurogenesis
LigandATP-binding, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
2.7.10.1 1994

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110478 Insulin signaling pathway
R-DME-77387 Insulin receptor recycling
R-DME-9009391 Extra-nuclear estrogen signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

More...
SignaLinki
P09208

<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:
Insulin-like receptor (EC:2.7.10.1)
Short name:
dIR
Short name:
dInr
Alternative name(s):
dIRH
Cleaved into the following 3 chains:
<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:InR
Synonyms:dinr, Dir-a, Inr-a
ORF Names:CG18402
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 3R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0283499 InR

<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 Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1086 – 1310ExtracellularSequence analysisAdd BLAST225
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1311 – 1331HelicalSequence analysisAdd BLAST21
Topological domaini1332 – 2144CytoplasmicSequence analysisAdd BLAST813

Keywords - Cellular componenti

Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi1467R → C in allele 353; reduction in head size. 1 Publication1
Mutagenesisi1539G → E in allele 339; strong reduction in head size. 1 Publication1
Mutagenesisi1599G → R in allele 211; reduction in head size. 1 Publication1

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – ?Sequence analysis
<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_0000016715651 – 1081Insulin-like receptor subunit alphaAdd BLAST431
ChainiPRO_00000167161086 – 2144Insulin-like receptor subunit beta 1Add BLAST1059
ChainiPRO_00000167171086 – ?Insulin-like receptor subunit beta 2
ChainiPRO_0000016718? – 2144Insulin-like receptor

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi74N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi203N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi265N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi356N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi376N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi406N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi509N-linked (GlcNAc...) asparagineSequence analysis1
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi531 ↔ 539By similarity
Disulfide bondi535 ↔ 545By similarity
Disulfide bondi546 ↔ 554By similarity
Disulfide bondi550 ↔ 564By similarity
Glycosylationi561N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi567 ↔ 576By similarity
Glycosylationi569N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi580 ↔ 591By similarity
Disulfide bondi597 ↔ 618By similarity
Disulfide bondi635 ↔ 638By similarity
Glycosylationi751N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi810N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi824N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi839N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi864N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi898N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi946N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1053N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1147N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1218N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1265N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei1354Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1545Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1549Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1550Phosphotyrosine; by autocatalysisBy similarity1
Modified residuei1816Phosphoserine1 Publication1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The 280 kDa proreceptor is proteolytically processed to form a 120 kDa alpha subunit and a 170 kDa beta subunit. The beta subunit undergoes cell-specific cleavage to generate a 90 kDa beta subunit and a free 60 kDa C-terminal subunit. Both the 90 kDa and the 170 kDa beta subunits can assemble with the alpha subunits to form mature receptors.1 Publication
Autophosphorylated on tyrosine residues in response to exogenous insulin.1 Publication
Phosphorylation of Tyr-1354 is required for Chico-binding.By similarity

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P09208

PRoteomics IDEntifications database

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PRIDEi
P09208

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09208

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Widely distributed throughout the embryo. Expressed at high levels in the embryonic nervous system. Larval expression is limited to the nervous system and all imaginal disks. Expressed at high levels in the adult nervous system and ovaries.2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Expressed throughout development. Embryonic expression is most prominent 8 to 12 hours after egg laying.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0013984 Expressed in 28 organ(s), highest expression level in embryo

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P09208 DM

<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

Tetramer of 2 alpha and 2 beta chains linked by disulfide bonds. The alpha chains contribute to the formation of the ligand-binding domain, while the beta chains carry the kinase domain. When autophosphorylated, the beta-subunit binds the SH2 and SH3 domains of the adapter protein Dock. The beta subunit also binds and tyrosine phosphorylates the insulin receptor substrate Chico.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Show more details

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
67515, 76 interactors

Protein interaction database and analysis system

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IntActi
P09208, 5 interactors

STRING: functional protein association networks

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STRINGi
7227.FBpp0288669

<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
P09208

Database of comparative protein structure models

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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

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>Domaini825 – 927Fibronectin type-III 1PROSITE-ProRule annotationAdd BLAST103
Domaini928 – 1026Fibronectin type-III 2PROSITE-ProRule annotationAdd BLAST99
Domaini1210 – 1305Fibronectin type-III 3PROSITE-ProRule annotationAdd BLAST96
Domaini1371 – 1659Protein kinasePROSITE-ProRule annotationAdd BLAST289

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>Regioni1351 – 1354Chico-bindingBy similarity4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi176 – 252Gln-richAdd BLAST77
Compositional biasi177 – 197His-richAdd BLAST21
Compositional biasi521 – 580Cys-richAdd BLAST60

<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 protein kinase superfamily. Tyr protein kinase family. Insulin receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH3-binding, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4258 Eukaryota
COG0515 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000168802

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P09208

KEGG Orthology (KO)

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KOi
K05087

Identification of Orthologs from Complete Genome Data

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OMAi
KFRGYAF

Database of Orthologous Groups

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OrthoDBi
223327at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P09208

Family and domain databases

Conserved Domains Database

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CDDi
cd00063 FN3, 1 hit
cd00064 FU, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
2.60.40.10, 3 hits
3.80.20.20, 2 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR002011 Tyr_kinase_rcpt_2_CS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00757 Furin-like, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 1 hit
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF49265 SSF49265, 2 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50853 FN3, 3 hits
PS01352 HEMATOPO_REC_L_F1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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>. 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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P09208-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MFNMPRGVTK SKSKRGKIKM ENDMAAAATT TACTLGHICV LCRQEMLLDT
60 70 80 90 100
CCCRQAVEAV DSPASSEEAY SSSNSSSCQA SSEISAEEVW FLSHDDIVLC
110 120 130 140 150
RRPKFDEVET TGKKRDVKCS GHQCSNECDD GSTKNNRQQR ENFNIFSNCH
160 170 180 190 200
NILRTLQSLL LLMFNCGIFN KRRRRQHQQQ HHHHYQHHHQ QHHQQHHQRQ
210 220 230 240 250
QANVSYTKFL LLLQTLAAAT TRLSLSPKNY KQQQQLQHNQ QLPRATPQQK
260 270 280 290 300
QQEKDRHKCF HYKHNYSYSP GISLLLFILL ANTLAIQAVV LPAHQQHLLH
310 320 330 340 350
NDIADGLDKT ALSVSGTQSR WTRSESNPTM RLSQNVKPCK SMDIRNMVSH
360 370 380 390 400
FNQLENCTVI EGFLLIDLIN DASPLNRSFP KLTEVTDYII IYRVTGLHSL
410 420 430 440 450
SKIFPNLSVI RGNKLFDGYA LVVYSNFDLM DLGLHKLRSI TRGGVRIEKN
460 470 480 490 500
HKLCYDRTID WLEILAENET QLVVLTENGK EKECRLSKCP GEIRIEEGHD
510 520 530 540 550
TTAIEGELNA SCQLHNNRRL CWNSKLCQTK CPEKCRNNCI DEHTCCSQDC
560 570 580 590 600
LGGCVIDKNG NESCISCRNV SFNNICMDSC PKGYYQFDSR CVTANECITL
610 620 630 640 650
TKFETNSVYS GIPYNGQCIT HCPTGYQKSE NKRMCEPCPG GKCDKECSSG
660 670 680 690 700
LIDSLERARE FHGCTIITGT EPLTISIKRE SGAHVMDELK YGLAAVHKIQ
710 720 730 740 750
SSLMVHLTYG LKSLKFFQSL TEISGDPPMD ADKYALYVLD NRDLDELWGP
760 770 780 790 800
NQTVFIRKGG VFFHFNPKLC VSTINQLLPM LASKPKFFEK SDVGADSNGN
810 820 830 840 850
RGSCGTAVLN VTLQSVGANS AMLNVTTKVE IGEPQKPSNA TIVFKDPRAF
860 870 880 890 900
IGFVFYHMID PYGNSTKSSD DPCDDRWKVS SPEKSGVMVL SNLIPYTNYS
910 920 930 940 950
YYVRTMAISS ELTNAESDVK NFRTNPGRPS KVTEVVATAI SDSKINVTWS
960 970 980 990 1000
YLDKPYGVLT RYFIKAKLIN RPTRNNNRDY CTEPLVKAME NDLPATTPTK
1010 1020 1030 1040 1050
KISDPLAGDC KCVEGSKKTS SQEYDDRKVQ AGMEFENALQ NFIFVPNIRK
1060 1070 1080 1090 1100
SKNGSSDKSD GAEGAALDSN AIPNGGATNP SRRRRDVALE PELDDVEGSV
1110 1120 1130 1140 1150
LLRHVRSITD DTDAFFEKDD ENTYKDEEDL SSNKQFYEVF AKELPPNQTH
1160 1170 1180 1190 1200
FVFEKLRHFT RYAIFVVACR EEIPSEKLRD TSFKKSLCSD YDTVFQTTKR
1210 1220 1230 1240 1250
KKFADIVMDL KVDLEHANNT ESPVRVRWTP PVDPNGEIVT YEVAYKLQKP
1260 1270 1280 1290 1300
DQVEEKKCIP AADFNQTAGY LIKLNEGLYS FRVRANSIAG YGDFTEVEHI
1310 1320 1330 1340 1350
KVEPPPSYAK VFFWLLGIGL AFLIVSLFGY VCYLHKRKVP SNDLHMNTEV
1360 1370 1380 1390 1400
NPFYASMQYI PDDWEVLREN IIQLAPLGQG SFGMVYEGIL KSFPPNGVDR
1410 1420 1430 1440 1450
ECAIKTVNEN ATDRERTNFL SEASVMKEFD TYHVVRLLGV CSRGQPALVV
1460 1470 1480 1490 1500
MELMKKGDLK SYLRAHRPEE RDEAMMTYLN RIGVTGNVQP PTYGRIYQMA
1510 1520 1530 1540 1550
IEIADGMAYL AAKKFVHRDL AARNCMVADD LTVKIGDFGM TRDIYETDYY
1560 1570 1580 1590 1600
RKGTKGLLPV RWMPPESLRD GVYSSASDVF SFGVVLWEMA TLAAQPYQGL
1610 1620 1630 1640 1650
SNEQVLRYVI DGGVMERPEN CPDFLHKLMQ RCWHHRSSAR PSFLDIIAYL
1660 1670 1680 1690 1700
EPQCPNSQFK EVSFYHSEAG LQHREKERKE RNQLDAFAAV PLDQDLQDRE
1710 1720 1730 1740 1750
QQEDATTPLR MGDYQQNSSL DQPPESPIAM VDDQGSHLPF SLPSGFIASS
1760 1770 1780 1790 1800
TPDGQTVMAT AFQNIPAAQG DISATYVVPD ADALDGDRGY EIYDPSPKCA
1810 1820 1830 1840 1850
ELPTSRSGST GGGKLSGEQH LLPRKGRQPT IMSSSMPDDV IGGSSLQPST
1860 1870 1880 1890 1900
ASAGSSNASS HTGRPSLKKT VADSVRNKAN FINRHLFNHK RTGSNASHKS
1910 1920 1930 1940 1950
NASNAPSTSS NTNLTSHPVA MGNLGTIESG GSGSAGSYTG TPRFYTPSAT
1960 1970 1980 1990 2000
PGGGSGMAIS DNPNYRLLDE SIASEQATIL TTSSPNPNYE MMHPPTSLVS
2010 2020 2030 2040 2050
TNPNYMPMNE TPVQMAGVTI SHNPNYQPMQ APLNARQSQS SSDEDNEQEE
2060 2070 2080 2090 2100
DDEDEDDDVD DEHVEHIKME RMPLSRPRQR ALPSKTQPPR SRSVSQTRKS
2110 2120 2130 2140
PTNPNSGIGA TGAGNRSNLL KENWLRPAST PRPPPPNGFI GREA
Length:2,144
Mass (Da):239,776
Last modified:March 29, 2005 - v3
<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:iC4A8ECB08C70523A
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 AAA28644 differs from that shown. Reason: Frameshift.Curated
The sequence AAA68953 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 conflicti29T → ATTAK in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti89V → D in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti157Q → H in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti157Q → H in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti164F → C in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti197H → L in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti197H → L in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti319S → T in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti319S → T in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti322T → P in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti322T → P in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti470T → S in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti485R → S in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti501T → N in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti501T → N in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti653 – 660DSLERARE → PPPPPPPL in AAA28644 (PubMed:3099787).Curated8
Sequence conflicti679 – 681RES → GER in AAA28644 (PubMed:3099787).Curated3
Sequence conflicti723 – 727ISGDP → LAAI in AAA28644 (PubMed:3099787).Curated5
Sequence conflicti793V → E in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti822M → S in AAA68953 (PubMed:7628438).Curated1
Sequence conflicti864 – 877NSTKS…CDDRW → TQLKAVTIHAMIAG in AAA28644 (PubMed:3099787).CuratedAdd BLAST14
Sequence conflicti933 – 935Missing in AAA68953 (PubMed:7628438).Curated3
Sequence conflicti933 – 935Missing in AAA28644 (PubMed:3099787).Curated3
Sequence conflicti954 – 958KPYGV → NLMA in AAA68953 (PubMed:7628438).Curated5
Sequence conflicti954 – 958KPYGV → NLMA in AAA28644 (PubMed:3099787).Curated5
Sequence conflicti1161Missing in AAA28644 (PubMed:3099787).Curated1
Sequence conflicti1187 – 1192LCSDYD → SAAIIH in AAA28644 (PubMed:3099787).Curated6
Sequence conflicti1224 – 1232VRVRWTPPV → ATFSLGRHQL in AAA68953 (PubMed:7628438).Curated9
Sequence conflicti1224 – 1232VRVRWTPPV → ATFSLGRHQL in AAA28644 (PubMed:3099787).Curated9
Sequence conflicti1263 – 1282DFNQT…LYSFR → RLQPDCRLFNKAQRGPLQLQ in AAA28644 (PubMed:3099787).CuratedAdd BLAST20
Sequence conflicti1300 – 1303IKVE → LIQQ in AAA28645 (PubMed:7876183).Curated4
Sequence conflicti1457 – 1458GD → VE in AAA28644 (PubMed:3099787).Curated2
Sequence conflicti1469 – 1484EERDE…NRIGV → RSGMRPDDVSLIAWM in AAA28644 (PubMed:3099787).CuratedAdd BLAST16
Sequence conflicti1473 – 1479EAMMTYL → DGHDDVS in AAA28645 (PubMed:7876183).Curated7
Sequence conflicti1499M → V in AAA28644 (PubMed:3099787).Curated1
Sequence conflicti1519 – 1520DL → PF in AAA28645 (PubMed:7876183).Curated2
Sequence conflicti1569 – 1578RDGVYSSASD → QAWCLLLVPVT in AAA28645 (PubMed:7876183).Curated10
Sequence conflicti1591 – 1598TLAAQPYQ → ILSLWRSP in AAA28645 (PubMed:7876183).Curated8
Sequence conflicti1682N → H in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti1682N → H in AAA28644 (PubMed:3099787).Curated1
Sequence conflicti1706T → S in AAA28644 (PubMed:3099787).Curated1
Sequence conflicti1715Q → E in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti1792 – 1799IYDPSPKC → STIPVRNG in AAA28644 (PubMed:3099787).Curated8
Sequence conflicti1828Q → K in AAA28644 (PubMed:3099787).Curated1
Sequence conflicti1850 – 1851TA → GI in AAA28644 (PubMed:3099787).Curated2
Sequence conflicti1852 – 1854SAG → FTT in AAA68953 (PubMed:7628438).Curated3
Sequence conflicti1854G → A in AAC47458 (PubMed:7876183).Curated1
Sequence conflicti1887F → Y in AAA68953 (PubMed:7628438).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U28136 mRNA Translation: AAA68953.1 Frameshift.
U18351 Genomic DNA Translation: AAC47458.1
AE014297 Genomic DNA Translation: AAF55903.2
AE014297 Genomic DNA Translation: ACL83549.1
AE014297 Genomic DNA Translation: ACL83550.1
AE014297 Genomic DNA Translation: ACL83551.1
M14778 mRNA Translation: AAA28644.1 Frameshift.
M13568 Genomic DNA Translation: AAA28645.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A56081
S57245

NCBI Reference Sequences

More...
RefSeqi
NP_001138093.1, NM_001144621.3
NP_001138094.1, NM_001144622.2
NP_001138095.1, NM_001144623.2
NP_524436.2, NM_079712.6

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0084121; FBpp0083519; FBgn0283499
FBtr0290230; FBpp0288669; FBgn0283499
FBtr0290231; FBpp0288670; FBgn0283499
FBtr0290232; FBpp0288671; FBgn0283499

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
42549

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG18402

<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
U28136 mRNA Translation: AAA68953.1 Frameshift.
U18351 Genomic DNA Translation: AAC47458.1
AE014297 Genomic DNA Translation: AAF55903.2
AE014297 Genomic DNA Translation: ACL83549.1
AE014297 Genomic DNA Translation: ACL83550.1
AE014297 Genomic DNA Translation: ACL83551.1
M14778 mRNA Translation: AAA28644.1 Frameshift.
M13568 Genomic DNA Translation: AAA28645.1
PIRiA56081
S57245
RefSeqiNP_001138093.1, NM_001144621.3
NP_001138094.1, NM_001144622.2
NP_001138095.1, NM_001144623.2
NP_524436.2, NM_079712.6

3D structure databases

SMRiP09208
ModBaseiSearch...

Protein-protein interaction databases

BioGridi67515, 76 interactors
IntActiP09208, 5 interactors
STRINGi7227.FBpp0288669

PTM databases

iPTMnetiP09208

Proteomic databases

PaxDbiP09208
PRIDEiP09208

Genome annotation databases

EnsemblMetazoaiFBtr0084121; FBpp0083519; FBgn0283499
FBtr0290230; FBpp0288669; FBgn0283499
FBtr0290231; FBpp0288670; FBgn0283499
FBtr0290232; FBpp0288671; FBgn0283499
GeneIDi42549
KEGGidme:Dmel_CG18402

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
42549
FlyBaseiFBgn0283499 InR

Phylogenomic databases

eggNOGiKOG4258 Eukaryota
COG0515 LUCA
GeneTreeiENSGT00940000168802
InParanoidiP09208
KOiK05087
OMAiKFRGYAF
OrthoDBi223327at2759
PhylomeDBiP09208

Enzyme and pathway databases

BRENDAi2.7.10.1 1994
ReactomeiR-DME-110478 Insulin signaling pathway
R-DME-77387 Insulin receptor recycling
R-DME-9009391 Extra-nuclear estrogen signaling
SignaLinkiP09208

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
InR fly

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

More...
GenomeRNAii
42549

Protein Ontology

More...
PROi
PR:P09208

Gene expression databases

BgeeiFBgn0013984 Expressed in 28 organ(s), highest expression level in embryo
GenevisibleiP09208 DM

Family and domain databases

CDDicd00063 FN3, 1 hit
cd00064 FU, 1 hit
Gene3Di2.60.40.10, 3 hits
3.80.20.20, 2 hits
InterProiView protein in InterPro
IPR003961 FN3_dom
IPR036116 FN3_sf
IPR006211 Furin-like_Cys-rich_dom
IPR006212 Furin_repeat
IPR009030 Growth_fac_rcpt_cys_sf
IPR013783 Ig-like_fold
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR000494 Rcpt_L-dom
IPR036941 Rcpt_L-dom_sf
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom
IPR002011 Tyr_kinase_rcpt_2_CS
PfamiView protein in Pfam
PF00757 Furin-like, 1 hit
PF07714 Pkinase_Tyr, 1 hit
PF01030 Recep_L_domain, 2 hits
PRINTSiPR00109 TYRKINASE
SMARTiView protein in SMART
SM00060 FN3, 3 hits
SM00261 FU, 1 hit
SM00219 TyrKc, 1 hit
SUPFAMiSSF49265 SSF49265, 2 hits
SSF56112 SSF56112, 1 hit
SSF57184 SSF57184, 1 hit
PROSITEiView protein in PROSITE
PS50853 FN3, 3 hits
PS01352 HEMATOPO_REC_L_F1, 1 hit
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 1 hit
PS00239 RECEPTOR_TYR_KIN_II, 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 nameiINSR_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: P09208
Secondary accession number(s): B7Z0N6
, Q24023, Q24089, Q9VD94
<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: July 1, 1989
Last sequence update: March 29, 2005
Last modified: December 11, 2019
This is version 229 of the entry and version 3 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. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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