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Entry version 197 (16 Oct 2019)
Sequence version 3 (01 Dec 2000)
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Protein

ATP-dependent RNA helicase vasa

Gene

vas

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 translational control mechanisms operating in early stages of oogenesis. Required maternally in many stages of oogenesis, including cystocyte differentiation, oocyte differentiation, and specification of anterior-posterior polarity in the developing cysts. Essential for the formation and/or structural integrity of perinuclear nuage particles during germ cell formation. Required for gus, Fsn and aub accumulation at the posterior pole of the embryo. Required for the localization of vas to the perinuclear region of nurse cells.11 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

Mg2+1 Publication

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 bindingi289 – 296ATPPROSITE-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
  • RNA binding Source: GO_Central
  • RNA helicase activity Source: UniProtKB

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, Helicase, Hydrolase, RNA-binding
Biological processDifferentiation, Oogenesis
LigandATP-binding, Magnesium, Nucleotide-binding

<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:
ATP-dependent RNA helicase vasa1 Publication (EC:3.6.4.131 Publication)
Alternative name(s):
Antigen Mab46F11
<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:vasImported
Synonyms:vasa1 Publication
ORF Names:CG46283Imported
<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 2L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0283442 vas

<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

Cytoplasm

<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

Defective growth of germline cysts. Fails to efficiently accumulate many localized RNAs, such as Bic-D, orb, osk and nos, but still accumulates grk RNA.3 Publications

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>Mutagenesisi184 – 188DINNN → AAAAA: Enhances protein stability. Does not affect protein distribution in the oocyte. 1 Publication5
Mutagenesisi184D → A: Decreases interaction with gus. 2 Publications1
Mutagenesisi185I → A: Decreases interaction with gus. 1 Publication1
Mutagenesisi186 – 189NNNN → ANNA: Strongly decreases interaction with gus. 1 Publication4
Mutagenesisi186 – 188NNN → AAA: Abolishes interaction with gus. 1 Publication3
Mutagenesisi187N → A: Strongly decreases interaction with gus. 2 Publications1
Mutagenesisi188N → A: Strongly decreases interaction with gus. 2 Publications1
Mutagenesisi189N → A: Does not affect interaction with gus. 2 Publications1
Mutagenesisi256I → N: Fails to bind and unwind RNA. 1 Publication1
Mutagenesisi271I → M: Fails to bind and unwind RNA. 1 Publication1
Mutagenesisi328R → A: Reduction in RNA-binding, reduced RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi329E → A: Increase in RNA-binding and no significant change to RNA-dependent ATPase or unwinding activities. 1 Publication1
Mutagenesisi333Q → A: Reduction in RNA-binding, drastic reduction in unwinding activities, no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi378R → A: Reduction in RNA-binding, significantly reduced RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi381D → A: Increase in RNA-binding. 1 Publication1
Mutagenesisi525Q → A: Reduction in RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi528R → A: Reduction in RNA-binding, barely detectable RNA-dependent ATPase activity and completely defective unwinding activity. 1 Publication1
Mutagenesisi546T → A: Moderately decreased the RNA binding, abolished both the RNA-dependent ATPase and unwinding activities. 1 Publication1
Mutagenesisi551R → A: Reduction in RNA-binding, drastic reduction in unwinding activities and no significant change to RNA-dependent ATPase activity. 1 Publication1
Mutagenesisi552G → E: Fails to unwind RNA. 1 Publication1
Mutagenesisi554D → A: No change to RNA-binding, abolished unwinding activities and no significant change to RNA-dependent ATPase activity. 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_00000549761 – 661ATP-dependent RNA helicase vasaAdd BLAST661

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 residuei22Phosphoserine1 Publication1
Modified residuei27Phosphothreonine1 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

Ubiquitinated during oogenesis. Deubiquitinated by faf, which protects this protein from proteasome-mediated degradation.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P09052

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P09052

<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

Abundantly expressed in the female germline. Gus and faf are required for vas expression in the posterior pole of the oocyte.5 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 both maternally and zygotically.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
FBgn0262526 Expressed in 10 organ(s), highest expression level in egg chamber

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P09052 differential

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_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

Interacts with eIF5B and faf.

Interacts with gus (via B30.2/SPRY domain) and Fsn (via B30.2/SPRY domain).

Interacts with aub, me31B, eIF-4a and TER94.

Interacts with piwi; this interaction is RNA independent.

Interacts with Dcr-1 and Fmr1; these interactions occur in the polar granules.

8 Publications

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
60902, 7 interactors

Database of interacting proteins

More...
DIPi
DIP-20604N

The Eukaryotic Linear Motif resource for Functional Sites in Proteins

More...
ELMi
P09052

Protein interaction database and analysis system

More...
IntActi
P09052, 9 interactors

Molecular INTeraction database

More...
MINTi
P09052

<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

1661
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

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SMRi
P09052

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P09052

<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 ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati93 – 9917
Repeati100 – 10627
Repeati107 – 11337
Repeati114 – 12047
Repeati121 – 12757
<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>Domaini276 – 453Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST178
Domaini477 – 624Helicase C-terminalPROSITE-ProRule annotationAdd BLAST148

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>Regioni93 – 1275 X 7 AA tandem repeats of [FS]-R-G-G-[EQ]-G-GAdd BLAST35
Regioni184 – 203Required for posterior localization in oocyteAdd BLAST20

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>Motifi184 – 188B30.2/SPRY domain-binding motif2 Publications5
Motifi245 – 273Q motifAdd BLAST29
Motifi399 – 402DEAD box4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The B30.2/SPRY domain-binding motif mediates recognition by proteins containing a B30.2/SPRY domain.2 Publications

<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

Keywords - Domaini

Repeat

Phylogenomic databases

Ensembl GeneTree

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GeneTreei
ENSGT00940000157507

KEGG Orthology (KO)

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KOi
K13982

Identification of Orthologs from Complete Genome Data

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OMAi
PGMPSKD

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P09052

Family and domain databases

Integrated resource of protein families, domains and functional sites

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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

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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

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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_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>Sequences (2+)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 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.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform vasImported (identifier: P09052-1) [UniParc]FASTAAdd to basket
Also known as: A

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
MSDDWDDEPI VDTRGARGGD WSDDEDTAKS FSGEAEGDGV GGSGGEGGGY
60 70 80 90 100
QGGNRDVFGR IGGGRGGGAG GYRGGNRDGG GFHGGRREGE RDFRGGEGGF
110 120 130 140 150
RGGQGGSRGG QGGSRGGQGG FRGGEGGFRG RLYENEDGDE RRGRLDREER
160 170 180 190 200
GGERRGRLDR EERGGERGER GDGGFARRRR NEDDINNNNN IVEDVERKRE
210 220 230 240 250
FYIPPEPSND AIEIFSSGIA SGIHFSKYNN IPVKVTGSDV PQPIQHFTSA
260 270 280 290 300
DLRDIIIDNV NKSGYKIPTP IQKCSIPVIS SGRDLMACAQ TGSGKTAAFL
310 320 330 340 350
LPILSKLLED PHELELGRPQ VVIVSPTREL AIQIFNEARK FAFESYLKIG
360 370 380 390 400
IVYGGTSFRH QNECITRGCH VVIATPGRLL DFVDRTFITF EDTRFVVLDE
410 420 430 440 450
ADRMLDMGFS EDMRRIMTHV TMRPEHQTLM FSATFPEEIQ RMAGEFLKNY
460 470 480 490 500
VFVAIGIVGG ACSDVKQTIY EVNKYAKRSK LIEILSEQAD GTIVFVETKR
510 520 530 540 550
GADFLASFLS EKEFPTTSIH GDRLQSQREQ ALRDFKNGSM KVLIATSVAS
560 570 580 590 600
RGLDIKNIKH VINYDMPSKI DDYVHRIGRT GRVGNNGRAT SFFDPEKDRA
610 620 630 640 650
IAADLVKILE GSGQTVPDFL RTCGAGGDGG YSNQNFGGVD VRGRGNYVGD
660
ATNVEEEEQW D
Length:661
Mass (Da):72,331
Last modified:December 1, 2000 - 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:i8617C25CCB3130B9
GO
Isoform solo (identifier: B6JUP5-1) [UniParc]FASTAAdd to basket
The sequence of this isoform can be found in the external entry B6JUP5.
Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
Length:1,031
Mass (Da):112,515
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
M9PBB5M9PBB5_DROME
Vasa, isoform B
vas BG:DS00929.14, CG3506, CG43081, cgt, Dmel\CG46283
661Annotation 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>

<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 AAL89864 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 conflicti35A → R in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti153 – 165Missing in AAA29013 (PubMed:3052853).CuratedAdd BLAST13
Sequence conflicti192V → A in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti192V → A in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti265Y → F in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti322V → C in AAA29013 (PubMed:3052853).Curated1
Sequence conflicti452F → S in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti582R → C in CAA31405 (PubMed:3140040).Curated1
Sequence conflicti594D → H in AAA29013 (PubMed:3052853).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
X12945, X12946 Genomic DNA Translation: CAA31405.1
M23560 mRNA Translation: AAA29013.1
AE014134 Genomic DNA Translation: AAF53438.1
AY084126 mRNA Translation: AAL89864.1 Frameshift.

Protein sequence database of the Protein Information Resource

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PIRi
A58768

NCBI Reference Sequences

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RefSeqi
NP_001260458.1, NM_001273529.2 [P09052-1]
NP_001303322.1, NM_001316393.1 [P09052-1]
NP_723899.1, NM_165103.3 [P09052-1]

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
FBtr0445185; FBpp0401445; FBgn0283442 [P09052-1]
FBtr0445186; FBpp0401446; FBgn0283442 [P09052-1]
FBtr0445187; FBpp0401447; FBgn0283442 [P09052-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
26067080

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG46283

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
X12945, X12946 Genomic DNA Translation: CAA31405.1
M23560 mRNA Translation: AAA29013.1
AE014134 Genomic DNA Translation: AAF53438.1
AY084126 mRNA Translation: AAL89864.1 Frameshift.
PIRiA58768
RefSeqiNP_001260458.1, NM_001273529.2 [P09052-1]
NP_001303322.1, NM_001316393.1 [P09052-1]
NP_723899.1, NM_165103.3 [P09052-1]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DB3X-ray2.20A/B/C/D200-623[»]
2IHSX-ray2.20C/D184-203[»]
3EMWX-ray1.80B184-203[»]
3F2OX-ray2.05C/D184-203[»]
5NT7X-ray1.40B/D463-623[»]
SMRiP09052
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi60902, 7 interactors
DIPiDIP-20604N
ELMiP09052
IntActiP09052, 9 interactors
MINTiP09052

PTM databases

iPTMnetiP09052

Proteomic databases

PRIDEiP09052

Genome annotation databases

EnsemblMetazoaiFBtr0445185; FBpp0401445; FBgn0283442 [P09052-1]
FBtr0445186; FBpp0401446; FBgn0283442 [P09052-1]
FBtr0445187; FBpp0401447; FBgn0283442 [P09052-1]
GeneIDi26067080
KEGGidme:Dmel_CG46283

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
26067080
FlyBaseiFBgn0283442 vas

Phylogenomic databases

GeneTreeiENSGT00940000157507
KOiK13982
OMAiPGMPSKD
PhylomeDBiP09052

Miscellaneous databases

EvolutionaryTraceiP09052

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

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GenomeRNAii
26067080

Gene expression databases

BgeeiFBgn0262526 Expressed in 10 organ(s), highest expression level in egg chamber
ExpressionAtlasiP09052 differential

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiVASA1_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: P09052
Secondary accession number(s): Q24582, Q8SXU8, Q9V3Q8
<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: November 1, 1988
Last sequence update: December 1, 2000
Last modified: October 16, 2019
This is version 197 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, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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