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Protein

Protein deltex

Gene

dx

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulator of Notch signaling, a signaling pathway involved in cell-cell communications that regulates a broad spectrum of cell-fate determinations. Mainly acts as a positive regulator of Notch, but it may also act as a negative regulator, depending on the developmental and cell context. Mediates the antineural activity of Notch. May function as a ubiquitin ligase protein in the Notch pathway.3 Publications

Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri548 – 60356RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • Notch binding Source: UniProtKB
  • ubiquitin protein ligase activity Source: FlyBase
  • zinc ion binding Source: FlyBase

GO - Biological processi

  • endocytosis Source: FlyBase
  • imaginal disc-derived leg joint morphogenesis Source: FlyBase
  • negative regulation of Notch signaling pathway Source: UniProtKB
  • Notch receptor processing Source: FlyBase
  • Notch signaling pathway Source: FlyBase
  • positive regulation of Notch signaling pathway Source: UniProtKB
  • protein ubiquitination Source: FlyBase
  • regulation of Notch signaling pathway Source: FlyBase
  • wing disc development Source: FlyBase
  • Wnt signaling pathway Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Notch signaling pathway, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
SignaLinkiQ23985.
UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein deltex
Alternative name(s):
Probable E3 ubiquitin-protein ligase deltex (EC:6.3.2.-)
Gene namesi
Name:dx
ORF Names:CG3929
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0000524. dx.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi476 – 4849Missing : Dominant-negative mutant that inhibits Notch signaling. 1 Publication
Mutagenesisi571 – 5711H → A: Loss of function. Abolishes homomultimerization; when associated with A-574. 1 Publication
Mutagenesisi574 – 5741H → A: Loss of function. Abolishes homomultimerization; when associated with A-571. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 738738Protein deltexPRO_0000219079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei425 – 4251Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ23985.

PTM databases

iPTMnetiQ23985.

Expressioni

Tissue specificityi

Ubiquitous. Expressed at low levels throughout embryogenesis and in larvae.1 Publication

Gene expression databases

BgeeiQ23985.
ExpressionAtlasiQ23985. differential.
GenevisibleiQ23985. DM.

Interactioni

Subunit structurei

Homomultimer; the oligomerization is required for its function. Interacts with the ankyrin repeats of Notch.2 Publications

GO - Molecular functioni

  • Notch binding Source: UniProtKB

Protein-protein interaction databases

BioGridi58076. 61 interactions.
DIPiDIP-18159N.
IntActiQ23985. 7 interactions.
MINTiMINT-333005.
STRINGi7227.FBpp0070876.

Structurei

Secondary structure

1
738
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi45 – 539Combined sources
Beta strandi56 – 594Combined sources
Helixi62 – 7312Combined sources
Beta strandi78 – 803Combined sources
Helixi81 – 833Combined sources
Beta strandi92 – 943Combined sources
Turni95 – 984Combined sources
Beta strandi99 – 1013Combined sources
Beta strandi115 – 1217Combined sources
Helixi126 – 1294Combined sources
Beta strandi131 – 1366Combined sources
Beta strandi138 – 1414Combined sources
Beta strandi144 – 1485Combined sources
Helixi151 – 16212Combined sources
Beta strandi166 – 1694Combined sources
Helixi170 – 1734Combined sources
Beta strandi179 – 1824Combined sources
Turni183 – 1864Combined sources
Beta strandi187 – 1904Combined sources
Turni191 – 1933Combined sources
Beta strandi196 – 2038Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A90X-ray2.15A26-261[»]
ProteinModelPortaliQ23985.
SMRiQ23985. Positions 43-211, 609-736.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ23985.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 11884WWE 1PROSITE-ProRule annotationAdd
BLAST
Domaini119 – 20183WWE 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 304304Interaction with NotchAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi480 – 4845SH3-bindingSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi251 – 30353Gln/His-rich (OPA repeat)Add
BLAST
Compositional biasi332 – 472141Ser-richAdd
BLAST
Compositional biasi489 – 51426Poly-Gln (OPA repeat)Add
BLAST

Domaini

The WWE domains are thought to mediate some protein-protein interaction, and are frequently found in ubiquitin ligases.By similarity

Sequence similaritiesi

Belongs to the Deltex family.Curated
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation
Contains 2 WWE domains.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri548 – 60356RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH3-binding, Zinc-finger

Phylogenomic databases

eggNOGiENOG410IEMS. Eukaryota.
ENOG4111EY2. LUCA.
GeneTreeiENSGT00440000035370.
InParanoidiQ23985.
KOiK06058.
OMAiLSHAHFS.
OrthoDBiEOG7G1V5R.
PhylomeDBiQ23985.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02825. WWE. 2 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00678. WWE. 2 hits.
[Graphical view]
PROSITEiPS50918. WWE. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q23985-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASSAGSAAS GSVVPGGGGS AASSCATMAL STAGSGGPPV NHAHAVCVWE
60 70 80 90 100
FESRGKWLPY SPAVSQHLER AHAKKLTRVM LSDADPSLEQ YYVNVRTMTQ
110 120 130 140 150
ESEAETAGSG LLTIGVRRMF YAPSSPAGKG TKWEWSGGSA DSNNDWRPYN
160 170 180 190 200
MHVQCIIEDA WARGEQTLDL CNTHIGLPYT INFCNLTQLR QPSGPMRSIR
210 220 230 240 250
RTQQAPYPLV KLTPQQANQL KSNSASVSSQ YNTLPKLGDT KSLHRVPMTR
260 270 280 290 300
QQHPLPTSHQ VQQQQHQHQH QQQQQQQHHH QHQQQQHQQQ QQHQMQHHQI
310 320 330 340 350
HHQTAPRKPP KKHSEISTTN LRQILNNLNI FSSSTKHQSN MSTAASASSS
360 370 380 390 400
SSSASLHHAN HLSHAHFSHA KNMLTASMNS HHSRCSEGSL QSQRSSRMGS
410 420 430 440 450
HRSRSRTRTS DTDTNSVKSH RRRPSVDTVS TYLSHESKES LRSRNFAISV
460 470 480 490 500
NDLLDCSLGS DEVFVPSLPP SSLGERAPVP PPLPLHPRQQ QQQQQQQQQL
510 520 530 540 550
QMQQQQQAQQ QQQQSIAGSI VGVDPASDMI SRFVKVVEPP LWPNAQPCPM
560 570 580 590 600
CMEELVHSAQ NPAISLSRCQ HLMHLQCLNG MIIAQQNEMN KNLFIECPVC
610 620 630 640 650
GIVYGEKVGN QPIGSMSWSI ISKNLPGHEG QNTIQIVYDI ASGLQTEEHP
660 670 680 690 700
HPGRAFFAVG FPRICYLPDC PLGRKVLRFL KIAFDRRLLF SIGRSVTTGR
710 720 730
EDVVIWNSVD HKTQFNMFPD PTYLQRTMQQ LVHLGVTD
Length:738
Mass (Da):82,186
Last modified:August 15, 2003 - v2
Checksum:i7B1CF29E024D26AF
GO

Sequence cautioni

The sequence AAO39479.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1082AG → R in AAA18501 (PubMed:8150285).Curated
Sequence conflicti120 – 1201F → L in AAA18501 (PubMed:8150285).Curated
Sequence conflicti188 – 1892QL → HV in AAA18501 (PubMed:8150285).Curated
Sequence conflicti268 – 2681H → L in AAA18501 (PubMed:8150285).Curated
Sequence conflicti444 – 4441R → S in AAO39479 (PubMed:12537569).Curated
Sequence conflicti468 – 4681L → V in AAA18501 (PubMed:8150285).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti511 – 5111Q → L in strain: ZW141. 1 Publication
Natural varianti514 – 5141Q → QQ in strain: ZW122. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09789 mRNA. Translation: AAA18501.1.
AE014298 Genomic DNA. Translation: AAF46170.1.
BT033059 mRNA. Translation: ACE82582.1.
BT003476 mRNA. Translation: AAO39479.1. Different initiation.
EU217842 Genomic DNA. Translation: ABW92761.1.
EU217843 Genomic DNA. Translation: ABW92762.1.
EU217844 Genomic DNA. Translation: ABW92763.1.
EU217845 Genomic DNA. Translation: ABW92764.1.
EU217846 Genomic DNA. Translation: ABW92765.1.
EU217847 Genomic DNA. Translation: ABW92766.1.
EU217848 Genomic DNA. Translation: ABW92767.1.
EU217849 Genomic DNA. Translation: ABW92768.1.
EU217850 Genomic DNA. Translation: ABW92769.1.
EU217851 Genomic DNA. Translation: ABW92770.1.
EU217852 Genomic DNA. Translation: ABW92771.1.
EU217853 Genomic DNA. Translation: ABW92772.1.
PIRiS47857.
RefSeqiNP_511064.2. NM_078509.3.
UniGeneiDm.2626.

Genome annotation databases

EnsemblMetazoaiFBtr0070914; FBpp0070876; FBgn0000524.
GeneIDi31589.
KEGGidme:Dmel_CG3929.
UCSCiCG3929-RA. d. melanogaster.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U09789 mRNA. Translation: AAA18501.1.
AE014298 Genomic DNA. Translation: AAF46170.1.
BT033059 mRNA. Translation: ACE82582.1.
BT003476 mRNA. Translation: AAO39479.1. Different initiation.
EU217842 Genomic DNA. Translation: ABW92761.1.
EU217843 Genomic DNA. Translation: ABW92762.1.
EU217844 Genomic DNA. Translation: ABW92763.1.
EU217845 Genomic DNA. Translation: ABW92764.1.
EU217846 Genomic DNA. Translation: ABW92765.1.
EU217847 Genomic DNA. Translation: ABW92766.1.
EU217848 Genomic DNA. Translation: ABW92767.1.
EU217849 Genomic DNA. Translation: ABW92768.1.
EU217850 Genomic DNA. Translation: ABW92769.1.
EU217851 Genomic DNA. Translation: ABW92770.1.
EU217852 Genomic DNA. Translation: ABW92771.1.
EU217853 Genomic DNA. Translation: ABW92772.1.
PIRiS47857.
RefSeqiNP_511064.2. NM_078509.3.
UniGeneiDm.2626.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A90X-ray2.15A26-261[»]
ProteinModelPortaliQ23985.
SMRiQ23985. Positions 43-211, 609-736.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58076. 61 interactions.
DIPiDIP-18159N.
IntActiQ23985. 7 interactions.
MINTiMINT-333005.
STRINGi7227.FBpp0070876.

PTM databases

iPTMnetiQ23985.

Proteomic databases

PaxDbiQ23985.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0070914; FBpp0070876; FBgn0000524.
GeneIDi31589.
KEGGidme:Dmel_CG3929.
UCSCiCG3929-RA. d. melanogaster.

Organism-specific databases

CTDi31589.
FlyBaseiFBgn0000524. dx.

Phylogenomic databases

eggNOGiENOG410IEMS. Eukaryota.
ENOG4111EY2. LUCA.
GeneTreeiENSGT00440000035370.
InParanoidiQ23985.
KOiK06058.
OMAiLSHAHFS.
OrthoDBiEOG7G1V5R.
PhylomeDBiQ23985.

Enzyme and pathway databases

UniPathwayiUPA00143.
ReactomeiR-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
SignaLinkiQ23985.

Miscellaneous databases

EvolutionaryTraceiQ23985.
GenomeRNAii31589.
NextBioi774342.
PROiQ23985.

Gene expression databases

BgeeiQ23985.
ExpressionAtlasiQ23985. differential.
GenevisibleiQ23985. DM.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR004170. WWE-dom.
IPR018123. WWE-dom_subgr.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PfamiPF02825. WWE. 2 hits.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00678. WWE. 2 hits.
[Graphical view]
PROSITEiPS50918. WWE. 2 hits.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A member of the Notch group of interacting loci, deltex encodes a cytoplasmic basic protein."
    Busseau I., Diederich R.J., Xu T., Artavanis-Tsakonas S.
    Genetics 136:585-596(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Strain: Oregon-R.
    Tissue: Embryo.
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Embryo.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 17-738.
    Strain: Berkeley.
    Tissue: Embryo.
  6. "Hitchhiking effects of recurrent beneficial amino acid substitutions in the Drosophila melanogaster genome."
    Andolfatto P.
    Genome Res. 17:1755-1762(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 326-567, VARIANTS LEU-511 AND GLN-514 INS.
    Strain: ZW104, ZW109, ZW122, ZW123, ZW133, ZW136, ZW139, ZW140, ZW141, ZW142, ZW143 and ZW144.
  7. "Deltex acts as a positive regulator of Notch signaling through interactions with the Notch ankyrin repeats."
    Matsuno K., Diederich R.J., Go M.J., Blaumueller C.M., Artavanis-Tsakonas S.
    Development 121:2633-2644(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH NOTCH.
  8. "Novel Notch alleles reveal a Deltex-dependent pathway repressing neural fate."
    Ramain P., Khechumian K., Seugnet L., Arbogast N., Ackermann C., Heitzler P.
    Curr. Biol. 11:1729-1738(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Involvement of a proline-rich motif and RING-H2 finger of Deltex in the regulation of Notch signaling."
    Matsuno K., Ito M., Hori K., Miyashita F., Suzuki S., Kishi N., Artavanis-Tsakonas S., Okano H.
    Development 129:1049-1059(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HOMOMULTIMERIZATION, MUTAGENESIS OF 476-ARG--PRO-484; HIS-571 AND HIS-574.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "Structure and Notch receptor binding of the tandem WWE domain of Deltex."
    Zweifel M.E., Leahy D.J., Barrick D.
    Structure 13:1599-1611(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 26-261, INTERACTION WITH NOTCH.

Entry informationi

Entry nameiDTX_DROME
AccessioniPrimary (citable) accession number: Q23985
Secondary accession number(s): A9YJA9
, A9YJB1, A9YJB7, B3LF71, Q86P53, Q9W3Z1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2003
Last sequence update: August 15, 2003
Last modified: May 11, 2016
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.