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Protein

Cofilin/actin-depolymerizing factor homolog

Gene

tsr

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

Exhibits F-actin depolymerizing activity and regulates actin cytoskeleton dynamics (PubMed:21205790). Required for cytokinesis in both mitotic and meiotic cells and for aster migration and separation (PubMed:8522587). Promotes cell motility during ovary development and oogenesis (PubMed:11175754). During larval development, required for the cell rearrangement needed for formation of terminal filaments which are stacks of somatic cells that are important for the initiation of ovarioles (PubMed:11175754). Also required for border cell migration during oogenesis (PubMed:11175754). During border cell migration, required for actin turnover and lamellipodial protrusion (PubMed:21205790). Required for the establishment of planar cell polarity (PCP) where cells adopt a uniform orientation within the plane of an epithelium (PubMed:16571634). During establishment of PCP, required for the redistribution of the PCP core proteins fz and stan/fmi to the proximodistal cell boundary (PubMed:16571634). During pupal development, required for elongation of the retinal cell body and for rhabdomere morphogenesis (PubMed:18423434). Required for mushroom body neuroblast proliferation and axon growth (PubMed:15572110). Plays a role in the positive regulation of protein secretion (PubMed:20026655). Plays a role in the regulation of nuclear localization of actin (PubMed:22323606). Required for the maintenance of epithelial integrity by controlling cell junctions and is also necessary for cell survival and tissue growth through regulation of JNK and yki signaling (PubMed:27041568).9 Publications

Miscellaneous

The name 'twinstar' derives from the characteristic aberrant arrangement of asters seen in mutants.1 Publication

<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

  • actin binding Source: FlyBase

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 functionActin-binding
Biological processCell cycle, Cell division

<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:
Cofilin/actin-depolymerizing factor homolog
Alternative name(s):
Protein D61
Protein twinstar1 Publication
<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:tsr1 PublicationImported
Synonyms:Cadf
ORF Names:CG4254Imported
<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 2R

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0011726 tsr

<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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

<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

Late larval or pupal lethality with mutants showing defects in cytokinesis in both mitotic and meiotic cells, abnormal accumulation of F-actin in mature primary spermatocytes, and defective aster migration where the asters remain in close proximity to each other rather than separating from each other and migrating around the periphery of the nuclear envelope as in the wild type (PubMed:8522587). Failure of terminal filament formation in the ovary at the third larval instar at 25 degrees Celsius but formation occurs at 18 degrees Celsius (PubMed:11175754). Significantly thinner retina than controls, significantly increased F-actin levels in pupal eye disks and defective rhabdomere morphogenesis (PubMed:18423434). Defective mushroom body neuroblast proliferation with newly hatched larvae containing significantly fewer neurons than controls and severe axon growth defects with mutants failing to extend axons beyond the peduncle (PubMed:15572110). RNAi-mediated knockdown in the wing results in increased F-actin levels, altered subcellular location of the transcriptional coactivator yki, strong expression of the yki target genes wg and ex, cell extrusion from the basement membrane, reduced levels of the junction proteins dlg1, arm and shg, up-regulation of Rho1, apoptosis and JNK signaling (PubMed:27041568).5 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>Mutagenesisi3S → A: Abolishes in vitro phosphorylation by LIMK1. Partial rescue of both the defective neuroblast proliferation and defective axon growth seen in null mutants. 2 Publications1
Mutagenesisi3S → E: No rescue of the defective neuroblast proliferation seen in null mutants but partial rescue of the defective axon growth. 1 Publication1
Mutagenesisi27V → Q: Defective distal orientation of wing hairs and incorrect localization of the planar cell polarity proteins fz and stan/fmi; when associated with 139-AAALA-143. 1 Publication1
Mutagenesisi139 – 143EEKLR → AAALA: Defective distal orientation of wing hairs and incorrect localization of the planar cell polarity proteins fz and stan/fmi; when associated with Q-27. 1 Publication5

<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_00002149161 – 148Cofilin/actin-depolymerizing factor homologAdd BLAST148

<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

Phosphorylated in vitro by protein kinase LIMK1 (PubMed:20026655). Phosphorylation is required for inactivation of tsr and for cell proliferation and axon growth (PubMed:15572110). Phosphorylation is negatively regulated by the panthothenate kinase fbl which catalyzes the first step in the conversion of panthothenic acid to coenzyme A (PubMed:22912811).3 Publications
Dephosphorylated by protein phosphatase ssh which activates tsr.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

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

More...
PaxDbi
P45594

PRoteomics IDEntifications database

More...
PRIDEi
P45594

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P45594

<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 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 during all stages of development and peaks in late larval and pupal stages. Expressed in both male and female adults.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
FBgn0011726 Expressed in 31 organ(s), highest expression level in embryo

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P45594 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P45594 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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
63422, 45 interactors

Database of interacting proteins

More...
DIPi
DIP-20149N

Protein interaction database and analysis system

More...
IntActi
P45594, 37 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0072097

<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

1148
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P45594

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

More...
SMRi
P45594

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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>Domaini4 – 143ADF-HPROSITE-ProRule annotationAdd BLAST140

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>Motifi19 – 23Nuclear localization signalSequence analysis5

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the actin-binding proteins ADF family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1735 Eukaryota
ENOG41122P5 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154567

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P45594

KEGG Orthology (KO)

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KOi
K05765

Identification of Orthologs from Complete Genome Data

More...
OMAi
QMLPEKD

Database of Orthologous Groups

More...
OrthoDBi
EOG091G0TDH

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P45594

Family and domain databases

Conserved Domains Database

More...
CDDi
cd11286 ADF_cofilin_like, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.20.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR017904 ADF/Cofilin

The PANTHER Classification System

More...
PANTHERi
PTHR11913 PTHR11913, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00241 Cofilin_ADF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00102 ADF, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS51263 ADF_H, 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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

P45594-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MASGVTVSDV CKTTYEEIKK DKKHRYVIFY IRDEKQIDVE TVADRNAEYD
60 70 80 90 100
QFLEDIQKCG PGECRYGLFD FEYMHQCQGT SESSKKQKLF LMSWCPDTAK
110 120 130 140
VKKKMLYSSS FDALKKSLVG VQKYIQATDL SEASREAVEE KLRATDRQ
Length:148
Mass (Da):17,153
Last modified:November 1, 1995 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i24F7216033859620
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U08217 mRNA Translation: AAA19856.1
U24490 mRNA Translation: AAC46962.1
U24676 Genomic DNA Translation: AAC46963.1
AE013599 Genomic DNA Translation: AAF47146.1
BT089017 mRNA Translation: ACT98664.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A57569

NCBI Reference Sequences

More...
RefSeqi
NP_477034.1, NM_057686.4

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Dm.763

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0072188; FBpp0072097; FBgn0011726

Database of genes from NCBI RefSeq genomes

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GeneIDi
37841

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
dme:Dmel_CG4254

<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
U08217 mRNA Translation: AAA19856.1
U24490 mRNA Translation: AAC46962.1
U24676 Genomic DNA Translation: AAC46963.1
AE013599 Genomic DNA Translation: AAF47146.1
BT089017 mRNA Translation: ACT98664.1
PIRiA57569
RefSeqiNP_477034.1, NM_057686.4
UniGeneiDm.763

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
2MV2NMR-A1-148[»]
ProteinModelPortaliP45594
SMRiP45594
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi63422, 45 interactors
DIPiDIP-20149N
IntActiP45594, 37 interactors
STRINGi7227.FBpp0072097

PTM databases

iPTMnetiP45594

Proteomic databases

PaxDbiP45594
PRIDEiP45594

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0072188; FBpp0072097; FBgn0011726
GeneIDi37841
KEGGidme:Dmel_CG4254

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
37841
FlyBaseiFBgn0011726 tsr

Phylogenomic databases

eggNOGiKOG1735 Eukaryota
ENOG41122P5 LUCA
GeneTreeiENSGT00940000154567
InParanoidiP45594
KOiK05765
OMAiQMLPEKD
OrthoDBiEOG091G0TDH
PhylomeDBiP45594

Miscellaneous databases

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

More...
ChiTaRSi
tsr fly

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

More...
GenomeRNAii
37841

Protein Ontology

More...
PROi
PR:P45594

Gene expression databases

BgeeiFBgn0011726 Expressed in 31 organ(s), highest expression level in embryo
ExpressionAtlasiP45594 baseline and differential
GenevisibleiP45594 DM

Family and domain databases

CDDicd11286 ADF_cofilin_like, 1 hit
Gene3Di3.40.20.10, 1 hit
InterProiView protein in InterPro
IPR002108 ADF-H
IPR029006 ADF-H/Gelsolin-like_dom_sf
IPR017904 ADF/Cofilin
PANTHERiPTHR11913 PTHR11913, 1 hit
PfamiView protein in Pfam
PF00241 Cofilin_ADF, 1 hit
SMARTiView protein in SMART
SM00102 ADF, 1 hit
PROSITEiView protein in PROSITE
PS51263 ADF_H, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
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 nameiCADF_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: P45594
Secondary accession number(s): C6SV25, Q9W1C4
<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, 1995
Last sequence update: November 1, 1995
Last modified: December 5, 2018
This is version 155 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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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