Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 189 (02 Dec 2020)
Sequence version 3 (02 Feb 2004)
Previous versions | rss
Add a publicationFeedback
Protein

ATP-dependent RNA helicase me31b

Gene

me31B

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

ATP-dependent RNA helicase which is a core component of a variety of ribonucleoprotein complexes (RNPs) that play critical roles in translational repression and mRNA decapping during embryogenesis, oogenesis, neurogenesis and neurotransmission (PubMed:11546740, PubMed:16256742, PubMed:17178403, PubMed:18590813, PubMed:21267420, PubMed:21447556, PubMed:28875934, PubMed:28388438, PubMed:17982591). Recruits core components and translational repressors to some RNP complexes, and mediates RNP aggregation into processing granules such as P-bodies (PubMed:28875934, PubMed:11546740, PubMed:16256742, PubMed:17178403, PubMed:21267420, PubMed:21447556, PubMed:17982591). As part of a RNP complex containing tral, eIF4E1, cup, and pAbp, involved in RNP-mediated translational repression of maternal mRNAs during oogenesis and embryogenesis (PubMed:28875934). As part of a RNP complex containing tral and the RNA localization factors exu and yps, mediates translational silencing of mRNAs such as osk/oskar and bcd/bicoid during their transport to the oocyte in order to prevent their translation until they reach their positional destinations (PubMed:11546740). In neurons and possibly imaginal disks, involved in miRNA-mediated translational repression, possibly in association with components of the piRNA transposon silencing pathway (PubMed:21447556, PubMed:17178403, PubMed:21267420, PubMed:17982591, PubMed:21081899). Involved in RNA localization and protein trafficking in the oocyte (PubMed:11546740, PubMed:16256742). As part of an ER-associated RNP containing tral, cup and yps, required for tral-dependent ER exit site formation and consequently efficient trafficking of proteins such as grk and yl through the secretory pathway (PubMed:16256742). Component of neuron RNPs that mediate transport and translation of neuronal RNAs, including translation repression of synaptic transcripts in preparation for their dendritic targeting (PubMed:17178403, PubMed:21267420, PubMed:28388438). As part of the Atx2-Not1 repressor complex promotes Not1-dependent post-transcriptional gene silencing in adult circadian pacemaker neurons in order to sustain high-amplitude circadian rhythms and Pdf cycling in a per-independent manner (PubMed:28388438). Promotes the interaction between Atx2 and Not1 within the Atx2-Not1 RNP complex (PubMed:28388438).10 Publications

<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

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 bindingi102 – 109ATPPROSITE-ProRule annotation8

<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

  • ATP binding Source: UniProtKB-KW
  • mRNA binding Source: GO_Central
  • RNA binding Source: FlyBase
  • RNA helicase activity Source: UniProtKB-EC

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 functionHelicase, Hydrolase, Repressor, RNA-binding
Biological processTranslation regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-430039, mRNA decay by 5' to 3' exoribonuclease

<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:
ATP-dependent RNA helicase me31b (EC:3.6.4.13)
Alternative name(s):
Maternal expression at 31B
<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:me31B
ORF Names:CG4916
<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)
<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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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 2L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0004419, me31B

<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

Keywords - Cellular componenti

Cell projection, Cytoplasm, Endoplasmic reticulum

<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

Larvae lethal at the second- or third-instar stage (PubMed:11546740). RNAi-mediated knockdown in adult pigment dispersing factor (Pdf)-expressing clock neurons results in poor circadian locomotor rhythms under constant dark (DD) conditions (PubMed:28388438). The axonal terminus of s-LNv neurons display a loss of Pdf circadian daily oscillations which is consistent with their behavioral arrhythmicity (PubMed:28388438). However, there is no effect on the daily oscillations of pir and tim proteins in Pdf neurons (PubMed:28388438). Double knockdown with Atx2 enhances the behavioral arrhythmicity (PubMed:28388438). RNAi-mediated knockdown in the dorsal-most class IV neurons frequently results in defects in terminal dendrite morphology and dendritic tiling (PubMed:17178403). RNAi-mediated knockdown in adult projection neurons increases levels of the translational reporter protein CaMKII in the antennal lobe (PubMed:21267420). RNAi-mediated knockdown in the anterior/posterior boundary of the wing imaginal disk causes loss of DCP1- and pcm-expressing P-bodies (PubMed:17982591).5 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi281Q → A: Abolishes interaction with Edc3; when associated with A-284; A-288 and A-292. 1 Publication1
Mutagenesisi284H → A: Abolishes interaction with Edc3; when associated with A-281; A-288 and A-292. 1 Publication1
Mutagenesisi288T → A: Abolishes interaction with Edc3; when associated with A-281; A-284 and A-292. 1 Publication1
Mutagenesisi292K → A: Abolishes interaction with Edc3; when associated with A-281; A-284 and A-288. 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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000549821 – 459ATP-dependent RNA helicase me31bAdd BLAST459

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 residuei8Phosphoserine1 Publication1
Modified residuei29Phosphoserine1 Publication1
Modified residuei450Phosphoserine1 Publication1

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

Symmetrically dimethylated on arginine residues.1 Publication

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P23128

PRoteomics IDEntifications database

More...
PRIDEi
P23128

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P23128

<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

Ubiquitously expressed throughout the brain (at protein level) (PubMed:21267420, PubMed:17178403). Expressed in the olfactory system including the antennal lobes, projection neurons, local interneurons, mushroom-body Kenyon cells and glial cells (at protein level) (PubMed:21267420).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

First detected at low levels in the germarium region 2B where it is concentrated in the pro-oocytes (at protein level) (PubMed:11546740). Remains concentrated in the oocyte until mid-oogenesis (at protein level) (PubMed:11546740). In early egg chambers detected in nurse cells and oocytes, and later accumulates at the posterior pole of stage 10 oocytes (at protein level) (PubMed:11546740). Expression decreases during the first 5 hours of embryogenesis; expression levels are high during the first 2 hours of embryogenesis then sharply decrease at 2-3 hours and remains low (at protein level) (PubMed:28875934). Ubiquitously expressed in cleavage embryos but is not detected at the cellular blastoderm stage (at protein level) (PubMed:11546740). Expressed both maternally and zygotically (PubMed:1900936).3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0004419, Expressed in embryo and 40 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P23128, 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%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

Conserved component of different types of multiprotein ribonucleoprotein complexes (RNPs) that form distinct germ granules (P-body, nuage, sponge body or polar granules) and P-body-like neuronal RNPs (PubMed:11546740, PubMed:16256742, PubMed:18765641, PubMed:18590813, PubMed:19285948, PubMed:28388438). Consequently it interacts with a wide variety of proteins, some of which appear to be common interactive partners in almost all RNPs types i.e. cup and tral, whereas other interactions are specific to a germ granule/RNP (PubMed:28945271). Core functional components in me31B-containing RNPs include RNA regulatory proteins (such as translational repressor, RNA-decapping and exonuclease proteins), RNA localization proteins and additional proteins depending on the biological context of the RNPs (PubMed:17178403, PubMed:28945271). In the P-body RNPs, interacts with at least the translation repressor proteins tral, cup and Edc3, and the mRNA localization factor yps (PubMed:16256742, PubMed:18765641, PubMed:18590813, PubMed:19285948). Interaction with tral or Edc3 is required for translation repression and possibly RNA decapping; binding to tral and Edc3 is mutually exclusive (PubMed:18765641, PubMed:19285948). In the nuage and germ plasm polar granule RNPs, interacts with at least tral, cup, and additional proteins required for assembly and function of the germ granules such as tud, vas and aub (PubMed:18765641, PubMed:18590813, PubMed:19285948, PubMed:28945271).

Interacts (when dimethylated on Arg residues) with tud; interaction is RNA-independent (PubMed:28945271).

Component of the osk RNP complex, which is composed of at least me31B, exu, yps, aret/bruno, cup, and the mRNA of osk (PubMed:10662770).

Component of the nos RNP complex, which is composed of at least smg, cup, tral, me31B, the CCR4-NOT complex members Rga/NOT2 and Caf1-55, and the mRNA of nos (PubMed:21081899).

Interacts with tral and piRNA pathway components papi and AGO3; promotes interaction between nuage RNPs and the piRNA-mediated transposon silencing (PubMed:21447556).

Forms a RNP containing at least me31B, eIF4E1, cup, tral and pAbp; this interaction is required for the translational silencing of maternal mRNAs during the maternal-to-zygotic transition (PubMed:28875934). In the sponge body, forms a RNP containing at least me31B, exu, yps and the mRNA of osk; interactions with exu and yps are RNA dependent (PubMed:11546740).

Component of a neuronal RNP, at least composed of me31B, tral and Fmr1 (PubMed:17178403).

Component of the Atx2-Not1 repressor complex, composed of at least me31B, Atx2, tyf and pAbp (PubMed:28388438).

Interacts (via the C-terminus) with Atx2, tyf, pAbp and Lsm12a (PubMed:28388438).

12 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
60455, 35 interactors

Protein interaction database and analysis system

More...
IntActi
P23128, 14 interactors

Molecular INTeraction database

More...
MINTi
P23128

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0079565

<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

Secondary structure

1459
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...
SMRi
P23128

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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%5Fand%5Fdomains%5Fsection">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>Domaini89 – 259Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini269 – 429Helicase C-terminalPROSITE-ProRule annotationAdd BLAST161

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi58 – 86Q motifPROSITE-ProRule annotationAdd BLAST29
Motifi207 – 210DEAD boxPROSITE-ProRule annotation4

<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
KOG0326, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000170366

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P23128

Identification of Orthologs from Complete Genome Data

More...
OMAi
DWNLMSS

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P23128

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 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>Sequences (2)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform A (identifier: P23128-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MMTEKLNSGH TNLTSKGIIN DLQIAGNTSD DMGWKSKLKL PPKDNRFKTT
60 70 80 90 100
DVTDTRGNEF EEFCLKRELL MGIFEKGWER PSPIQEAAIP IALSGKDVLA
110 120 130 140 150
RAKNGTGKTG AYCIPVLEQI DPTKDYIQAL VMVPTRELAL QTSQICIELA
160 170 180 190 200
KHLDIRVMVT TGGTILKDDI LRIYQKVQLI IATPGRILDL MDKKVADMSH
210 220 230 240 250
CRILVLDEAD KLLSLDFQGM LDHVILKLPK DPQILLFSAT FPLTVKNFME
260 270 280 290 300
KHLREPYEIN LMEELTLKGV TQYYAFVQER QKVHCLNTLF SKLQINQSII
310 320 330 340 350
FCNSTQRVEL LAKKITELGY CCYYIHAKMA QAHRNRVFHD FRQGLCRNLV
360 370 380 390 400
CSDLFTRGID VQAVNVVINF DFPRMAETYL HRIGRSGRFG HLGIAINLIT
410 420 430 440 450
YEDRFDLHRI EKELGTEIKP IPKVIDPALY VANVGASVGD TCNNSDLNNS

ANEEGNVSK
Length:459
Mass (Da):51,945
Last modified:February 2, 2004 - 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:iB783E8185EF11E86
GO
Isoform B (identifier: P23128-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-31: Missing.

Show »
Length:428
Mass (Da):48,644
Checksum:i34E61B3C97D11A2A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti39 – 45KLPPKDN → NCRQRTT in AAA28603 (PubMed:1900936).Curated7

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0192861 – 31Missing in isoform B. CuratedAdd BLAST31

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
M59926 mRNA Translation: AAA28603.1
AE014134 Genomic DNA Translation: AAF52881.2
AE014134 Genomic DNA Translation: AAN10728.1
AY051663 mRNA Translation: AAK93087.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A39157

NCBI Reference Sequences

More...
RefSeqi
NP_523533.2, NM_078809.4 [P23128-1]
NP_723539.1, NM_164898.2 [P23128-2]

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0079975; FBpp0079565; FBgn0004419 [P23128-1]
FBtr0079976; FBpp0079566; FBgn0004419 [P23128-2]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
34364

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG4916

Keywords - Coding sequence diversityi

Alternative splicing

<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
M59926 mRNA Translation: AAA28603.1
AE014134 Genomic DNA Translation: AAF52881.2
AE014134 Genomic DNA Translation: AAN10728.1
AY051663 mRNA Translation: AAK93087.1
PIRiA39157
RefSeqiNP_523533.2, NM_078809.4 [P23128-1]
NP_723539.1, NM_164898.2 [P23128-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6S8RX-ray2.41A264-431[»]
SMRiP23128
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi60455, 35 interactors
IntActiP23128, 14 interactors
MINTiP23128
STRINGi7227.FBpp0079565

PTM databases

iPTMnetiP23128

Proteomic databases

PaxDbiP23128
PRIDEiP23128

Protocols and materials databases

ABCD curated depository of sequenced antibodies

More...
ABCDi
P23128, 6 sequenced antibodies

Genome annotation databases

EnsemblMetazoaiFBtr0079975; FBpp0079565; FBgn0004419 [P23128-1]
FBtr0079976; FBpp0079566; FBgn0004419 [P23128-2]
GeneIDi34364
KEGGidme:Dmel_CG4916

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
34364
FlyBaseiFBgn0004419, me31B

Phylogenomic databases

eggNOGiKOG0326, Eukaryota
GeneTreeiENSGT00940000170366
InParanoidiP23128
OMAiDWNLMSS
PhylomeDBiP23128

Enzyme and pathway databases

ReactomeiR-DME-430039, mRNA decay by 5' to 3' exoribonuclease

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
34364, 1 hit in 1 CRISPR screen

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

More...
ChiTaRSi
me31B, fly

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

More...
GenomeRNAii
34364

Protein Ontology

More...
PROi
PR:P23128

Gene expression databases

BgeeiFBgn0004419, Expressed in embryo and 40 other tissues
GenevisibleiP23128, DM

Family and domain databases

InterProiView protein in InterPro
IPR011545, DEAD/DEAH_box_helicase_dom
IPR014001, Helicase_ATP-bd
IPR001650, Helicase_C
IPR027417, P-loop_NTPase
IPR000629, RNA-helicase_DEAD-box_CS
IPR014014, RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF00270, DEAD, 1 hit
PF00271, Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487, DEXDc, 1 hit
SM00490, HELICc, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS00039, DEAD_ATP_HELICASE, 1 hit
PS51192, HELICASE_ATP_BIND_1, 1 hit
PS51194, HELICASE_CTER, 1 hit
PS51195, Q_MOTIF, 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 nameiDDX6_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: P23128
Secondary accession number(s): Q8IPC9, Q961D2, Q9VL17
<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: November 1, 1991
Last sequence update: February 2, 2004
Last modified: December 2, 2020
This is version 189 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

3D-structure, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again