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Protein

Discs overgrown protein kinase

Gene

dco

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

Involved in circadian rhythms, viability and molecular oscillations of the clock genes period (per) and timeless (tim). Dbt reduces the stability and thus the accumulation of monomeric per proteins, probably through phosphorylation. No evident circadian oscillation is detected in head. Together with CkIalpha, regulates processing of ci by phosphorylating it which promotes its binding to slmb, the F-box recognition component of the SCF(slmb) E3 ubiquitin-protein ligase (PubMed:16326393).4 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

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 sitei38ATPPROSITE-ProRule annotation1
<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 sitei128Proton acceptorPROSITE-ProRule annotation1

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 bindingi15 – 23ATPPROSITE-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 functionKinase, Serine/threonine-protein kinase, Transferase
Biological processBiological rhythms
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.11.1 1994

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-201688 WNT mediated activation of DVL
R-DME-209155 Phosphorylation of AXN and APC
R-DME-209159 Assembly of the CI containing complexes
R-DME-209190 Phosphorylation of CI
R-DME-209214 Phosphorylation of SMO
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209396 Phosphorylation of ARM
R-DME-209413 Assembly of the 'destruction complex'
R-DME-209440 Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-390023 Subcellular localisation of D
R-DME-432395 Degradation of TIM
R-DME-432490 Nuclear import of PER and TIM
R-DME-432501 Transcription repression by PER and activation by PDP1
R-DME-432524 Degradation of PER
R-DME-432553 Phosphorylation of PER and TIM
R-DME-432620 Dephosphorylation of PER
R-DME-451850 Positive regulation of FT and DS
R-DME-538898 Dephosphorylation of TIM
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol

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

More...
SignaLinki
O76324

<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:
Discs overgrown protein kinase (EC:2.7.11.1)
Alternative name(s):
Protein double-time
<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:dco
Synonyms:dbt
ORF Names:CG2048
<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
FBgn0002413 dco

<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; Source: COMPARTMENTS

<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>Mutagenesisi47P → S in dbtS; shortens the behavioral period. 1 Publication1
Mutagenesisi80M → I in dbtL; lengthens the behavioral period. 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 describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001928491 – 440Discs overgrown protein kinaseAdd BLAST440

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 residuei333Phosphoserine1 Publication1
Modified residuei334Phosphoserine1 Publication1

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
O76324

PRoteomics IDEntifications database

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PRIDEi
O76324

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
O76324

<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

Expressed in photoreceptor cells of the eyes as well as in the region situated between the optic lobe and the central brain.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0002413 Expressed in 58 organ(s), highest expression level in egg chamber

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
O76324 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
O76324 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

Forms a complex with per (PubMed:9674431). Interacts with Dlish (PubMed:27692068).2 Publications

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
68523, 37 interactors

Database of interacting proteins

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DIPi
DIP-46048N

Protein interaction database and analysis system

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IntActi
O76324, 4 interactors

STRING: functional protein association networks

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STRINGi
7227.FBpp0085104

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
O76324

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

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SMRi
O76324

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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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

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>Domaini9 – 277Protein kinasePROSITE-ProRule annotationAdd BLAST269

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 biasi319 – 332Poly-AlaAdd BLAST14
Compositional biasi336 – 339Poly-Gln4
Compositional biasi347 – 351Poly-Gly5
Compositional biasi414 – 426Poly-GlyAdd BLAST13
Compositional biasi430 – 437Poly-Gly8

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1164 Eukaryota
ENOG410XPGP LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153536

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000148798

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
O76324

KEGG Orthology (KO)

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KOi
K08960

Identification of Orthologs from Complete Genome Data

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OMAi
RWYGTEC

Database of Orthologous Groups

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OrthoDBi
1097975at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
O76324

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS

Pfam protein domain database

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Pfami
View protein in Pfam
PF00069 Pkinase, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00220 S_TKc, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 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>Sequence (1+)i

<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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

O76324-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MELRVGNKYR LGRKIGSGSF GDIYLGTTIN TGEEVAIKLE CIRTKHPQLH
60 70 80 90 100
IESKFYKTMQ GGIGIPRIIW CGSEGDYNVM VMELLGPSLE DLFNFCSRRF
110 120 130 140 150
SLKTVLLLAD QMISRIDYIH SRDFIHRDIK PDNFLMGLGK KGNLVYIIDF
160 170 180 190 200
GLAKKFRDAR SLKHIPYREN KNLTGTARYA SINTHLGIEQ SRRDDLESLG
210 220 230 240 250
YVLMYFNLGA LPWQGLKAAN KRQKYERISE KKLSTSIVVL CKGFPSEFVN
260 270 280 290 300
YLNFCRQMHF DQRPDYCHLR KLFRNLFHRL GFTYDYVFDW NLLKFGGPRN
310 320 330 340 350
PQAIQQAQDG ADGQAGHDAV AAAAAVAAAA AASSHQQQQH KVNAALGGGG
360 370 380 390 400
GSAAQQQLQG GQTLAMLGGN GGGNGSQLIG GNGLNMDDSM AATNSSRPPY
410 420 430 440
DTPERRPSIR MRQGGGGGGG GVGVGGMPSG GGGGGVGNAK
Length:440
Mass (Da):47,958
Last modified:August 16, 2005 - 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:i0B67B83E44213902
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0B4KHX3A0A0B4KHX3_DROME
Discs overgrown, isoform D
dco 01, 02, 0538, 09, 0915
440Annotation 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 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 conflicti353A → R in AAC39134 (PubMed:9674431).Curated1
Sequence conflicti428P → Q in AAC39134 (PubMed:9674431).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

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DDBJi
Links Updated
AF055583 mRNA Translation: AAC39134.1
AF192484 Genomic DNA Translation: AAF27346.1
AE014297 Genomic DNA Translation: AAF57109.1
AE014297 Genomic DNA Translation: AAF57110.1
AF132558 mRNA Translation: AAD27857.1

NCBI Reference Sequences

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RefSeqi
NP_001263132.1, NM_001276203.1
NP_524602.1, NM_079863.3
NP_733414.1, NM_170535.2
NP_733415.1, NM_170536.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Dm.1901

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0085742; FBpp0085104; FBgn0002413
FBtr0085743; FBpp0085105; FBgn0002413
FBtr0085744; FBpp0085106; FBgn0002413
FBtr0334548; FBpp0306615; FBgn0002413

Database of genes from NCBI RefSeq genomes

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GeneIDi
43673

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG2048

UCSC genome browser

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UCSCi
CG2048-RC 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
AF055583 mRNA Translation: AAC39134.1
AF192484 Genomic DNA Translation: AAF27346.1
AE014297 Genomic DNA Translation: AAF57109.1
AE014297 Genomic DNA Translation: AAF57110.1
AF132558 mRNA Translation: AAD27857.1
RefSeqiNP_001263132.1, NM_001276203.1
NP_524602.1, NM_079863.3
NP_733414.1, NM_170535.2
NP_733415.1, NM_170536.3
UniGeneiDm.1901

3D structure databases

ProteinModelPortaliO76324
SMRiO76324
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68523, 37 interactors
DIPiDIP-46048N
IntActiO76324, 4 interactors
STRINGi7227.FBpp0085104

PTM databases

iPTMnetiO76324

Proteomic databases

PaxDbiO76324
PRIDEiO76324

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0085742; FBpp0085104; FBgn0002413
FBtr0085743; FBpp0085105; FBgn0002413
FBtr0085744; FBpp0085106; FBgn0002413
FBtr0334548; FBpp0306615; FBgn0002413
GeneIDi43673
KEGGidme:Dmel_CG2048
UCSCiCG2048-RC d. melanogaster

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
43673
FlyBaseiFBgn0002413 dco

Phylogenomic databases

eggNOGiKOG1164 Eukaryota
ENOG410XPGP LUCA
GeneTreeiENSGT00940000153536
HOGENOMiHOG000148798
InParanoidiO76324
KOiK08960
OMAiRWYGTEC
OrthoDBi1097975at2759
PhylomeDBiO76324

Enzyme and pathway databases

BRENDAi2.7.11.1 1994
ReactomeiR-DME-201688 WNT mediated activation of DVL
R-DME-209155 Phosphorylation of AXN and APC
R-DME-209159 Assembly of the CI containing complexes
R-DME-209190 Phosphorylation of CI
R-DME-209214 Phosphorylation of SMO
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209396 Phosphorylation of ARM
R-DME-209413 Assembly of the 'destruction complex'
R-DME-209440 Recruitment of the 'destruction complex' to the receptor complex, the degradation of AXN and release of ARM
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-390023 Subcellular localisation of D
R-DME-432395 Degradation of TIM
R-DME-432490 Nuclear import of PER and TIM
R-DME-432501 Transcription repression by PER and activation by PDP1
R-DME-432524 Degradation of PER
R-DME-432553 Phosphorylation of PER and TIM
R-DME-432620 Dephosphorylation of PER
R-DME-451850 Positive regulation of FT and DS
R-DME-538898 Dephosphorylation of TIM
R-DME-6791226 Major pathway of rRNA processing in the nucleolus and cytosol
SignaLinkiO76324

Miscellaneous databases

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

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ChiTaRSi
dco fly

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

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GenomeRNAii
43673

Protein Ontology

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PROi
PR:O76324

Gene expression databases

BgeeiFBgn0002413 Expressed in 58 organ(s), highest expression level in egg chamber
ExpressionAtlasiO76324 baseline and differential
GenevisibleiO76324 DM

Family and domain databases

InterProiView protein in InterPro
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR008271 Ser/Thr_kinase_AS
PfamiView protein in Pfam
PF00069 Pkinase, 1 hit
SMARTiView protein in SMART
SM00220 S_TKc, 1 hit
SUPFAMiSSF56112 SSF56112, 1 hit
PROSITEiView protein in PROSITE
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00108 PROTEIN_KINASE_ST, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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<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 nameiDCO_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: O76324
Secondary accession number(s): A4V3P5, Q0KHY4, Q9V462
<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 15, 1999
Last sequence update: August 16, 2005
Last modified: January 16, 2019
This is version 160 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 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

Complete proteome, 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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