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Protein

Maternal effect protein staufen

Gene

stau

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

Functioni

Required both for the localization of maternal determinants to the posterior pole of the egg, oskar (osk) RNA, and for correct localization to the anterior pole, anchoring bicoid (bcd) RNA. Osk protein is required to keep osk RNA and stau protein at the posterior pole. Stau-bcd complexes form particles that show a microtubule-dependent localization.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei606 – 6061RNA
Binding sitei608 – 6081RNA
Binding sitei628 – 6281RNA
Binding sitei629 – 6291RNA
Binding sitei632 – 6321RNA

GO - Molecular functioni

  • double-stranded RNA binding Source: FlyBase
  • microtubule binding Source: FlyBase
  • mRNA 3'-UTR binding Source: FlyBase
  • mRNA binding Source: FlyBase

GO - Biological processi

  • anterior/posterior axis specification, embryo Source: FlyBase
  • asymmetric neuroblast division Source: FlyBase
  • asymmetric protein localization involved in cell fate determination Source: FlyBase
  • bicoid mRNA localization Source: FlyBase
  • intracellular mRNA localization Source: FlyBase
  • long-term memory Source: FlyBase
  • microtubule-based process Source: FlyBase
  • neuroblast fate determination Source: FlyBase
  • oogenesis Source: FlyBase
  • pole plasm assembly Source: FlyBase
  • pole plasm mRNA localization Source: FlyBase
  • pole plasm oskar mRNA localization Source: FlyBase
  • pole plasm protein localization Source: FlyBase
  • pole plasm RNA localization Source: FlyBase
  • positive regulation of cytoplasmic mRNA processing body assembly Source: FlyBase
  • positive regulation of oskar mRNA translation Source: FlyBase
  • positive regulation of synaptic growth at neuromuscular junction Source: FlyBase
  • protein localization Source: FlyBase
  • protein localization to synapse Source: FlyBase
  • regulation of oskar mRNA translation Source: FlyBase
  • regulation of pole plasm oskar mRNA localization Source: FlyBase
  • RNA localization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Maternal effect protein staufen
Gene namesi
Name:stau
ORF Names:CG5753
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0003520. stau.

Subcellular locationi

GO - Cellular componenti

  • apical cortex Source: FlyBase
  • apical part of cell Source: FlyBase
  • apical plasma membrane Source: FlyBase
  • basal cortex Source: FlyBase
  • basal plasma membrane Source: FlyBase
  • cell cortex Source: FlyBase
  • cytoplasm Source: FlyBase
  • cytoplasmic mRNA processing body Source: FlyBase
  • germ plasm Source: BHF-UCL
  • microtubule associated complex Source: FlyBase
  • subsynaptic reticulum Source: FlyBase
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi581 – 5822SQ → AA: Affects RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi584 – 5852HE → AA: Affects RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi586 – 5861I → A: Crucial for the structure of DRBM 3. 1 Publication
Mutagenesisi596 – 5961F → A: Crucial for the structure of DRBM 3. 1 Publication
Mutagenesisi599 – 6024LREE → AAAA: Strongly reduces RNA binding. 1 Publication
Mutagenesisi606 – 6061H → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi608 – 6081K → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi628 – 6292KK → AA: Abolishes RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi632 – 6321K → A: Abolishes RNA binding without altering the conformation of the domain. 1 Publication
Mutagenesisi633 – 6342KR → AA: No effect on RNA binding. 1 Publication
Mutagenesisi635 – 6362AA → SS: Crucial for the structure of DRBM 3. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 10261026Maternal effect protein staufenPRO_0000072250Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei563 – 5631Phosphoserine1 Publication
Modified residuei570 – 5701Phosphoserine1 Publication
Modified residuei650 – 6501Phosphothreonine1 Publication
Modified residuei655 – 6551Phosphothreonine1 Publication
Modified residuei676 – 6761Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP25159.
PRIDEiP25159.

PTM databases

iPTMnetiP25159.

Expressioni

Tissue specificityi

Polar granules at the posterior pole of the oocyte, and by the time the egg is laid, at the anterior pole.2 Publications

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Gene expression databases

BgeeiP25159.
ExpressionAtlasiP25159. differential.
GenevisibleiP25159. DM.

Interactioni

GO - Molecular functioni

  • microtubule binding Source: FlyBase

Protein-protein interaction databases

BioGridi62749. 5 interactions.
IntActiP25159. 6 interactions.
MINTiMINT-112231.
STRINGi7227.FBpp0085962.

Structurei

Secondary structure

1
1026
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi579 – 58911Combined sources
Beta strandi595 – 6017Combined sources
Beta strandi604 – 6063Combined sources
Beta strandi610 – 6167Combined sources
Beta strandi619 – 6235Combined sources
Beta strandi630 – 6323Combined sources
Helixi633 – 64311Combined sources
Helixi953 – 96210Combined sources
Beta strandi967 – 9726Combined sources
Beta strandi977 – 98610Combined sources
Beta strandi992 – 10009Combined sources
Helixi1001 – 101818Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKZNMR-A571-646[»]
1STUNMR-A579-646[»]
5CFFX-ray2.50E/F/G/H953-1019[»]
ProteinModelPortaliP25159.
SMRiP25159. Positions 571-646, 712-776.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP25159.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini311 – 37868DRBM 1PROSITE-ProRule annotationAdd
BLAST
Domaini490 – 55768DRBM 2PROSITE-ProRule annotationAdd
BLAST
Domaini578 – 64568DRBM 3PROSITE-ProRule annotationAdd
BLAST
Domaini711 – 78171DRBM 4PROSITE-ProRule annotationAdd
BLAST
Domaini951 – 101868DRBM 5PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3 – 8280Gln/His/Pro-richAdd
BLAST
Compositional biasi134 – 17744Pro-richAdd
BLAST
Compositional biasi421 – 521101Pro-richAdd
BLAST
Compositional biasi873 – 94775Ser-richAdd
BLAST

Domaini

Contains a proline-rich domain. The insertion of this domain in the DRBM 2 domain is required for stau-oskar mRNA localization.
DRBM 3 domain binds optimally to stem-loops containing 12 bp (in vitro).

Sequence similaritiesi

Contains 5 DRBM (double-stranded RNA-binding) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
InParanoidiP25159.
KOiK17597.
OMAiERGPAHC.
OrthoDBiEOG7NGQCG.
PhylomeDBiP25159.

Family and domain databases

Gene3Di3.30.160.20. 5 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: P25159-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' 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
MQHNVHAARP APHIRAAHHH SHSHAHMHLH PGMEQHLGPS LQQQQQPPPP
60 70 80 90 100
PQQPPHRDLH ARLNHHHLHA QQQQQQQTSS NQAGAVAAAG AAYHHGNINS
110 120 130 140 150
NSGSNISSNS NQMQKIRQQH QHLSSSNGLL GNQPPGPPPQ AFNPLAGNPA
160 170 180 190 200
ALAYNQLPPH PPHHMAAHLG SYAAPPPHYY MSQAKPAKYN HYGSNANSNS
210 220 230 240 250
GSNNSNSNYA PKAILQNTYR NQKVVVPPVV QEVTPVPEPP VTTNNATTNS
260 270 280 290 300
TSNSTVIASE PVTQEDTSQK PETRQEPASA DDHVSTGNID ATGALSNEDT
310 320 330 340 350
SSSGRGGKDK TPMCLVNELA RYNKITHQYR LTEERGPAHC KTFTVTLMLG
360 370 380 390 400
DEEYSADGFK IKKAQHLAAS KAIEETMYKH PPPKIRRSEE GGPMRTHITP
410 420 430 440 450
TVELNALAMK LGQRTFYLLD PTQIPPTDSI VPPEFAGGHL LTAPGPGMPQ
460 470 480 490 500
PPPPPAYALR QRLGNGFVPI PSQPMHPHFF HGPGQRPFPP KFPSRFALPP
510 520 530 540 550
PLGAHVHHGP NGPFPSVPTP PSKITLFVGK QKFVGIGRTL QQAKHDAAAR
560 570 580 590 600
ALQVLKTQAI SASEEALEDS MDEGDKKSPI SQVHEIGIKR NMTVHFKVLR
610 620 630 640 650
EEGPAHMKNF ITACIVGSIV TEGEGNGKKV SKKRAAEKML VELQKLPPLT
660 670 680 690 700
PTKQTPLKRI KVKTPGKSGA AAREGSVVSG TDGPTQTGKP ERRKRLNPPK
710 720 730 740 750
DKLIDMDDAD NPITKLIQLQ QTRKEKEPIF ELIAKNGNET ARRREFVMEV
760 770 780 790 800
SASGSTARGT GNSKKLAKRN AAQALFELLE AVQVTPTNET QSSEECSTSA
810 820 830 840 850
TMSAVTAPAV EATAEGKVPM VATPVGPMPG ILILRQNKKP AKKRDQIVIV
860 870 880 890 900
KSNVESKEEE ANKEVAVAAE ENSNNSANSG DSSNSSSGDS QATEAASESA
910 920 930 940 950
LNTSTGSNTS GVSSNSSNVG ANTDGNNHAE SKNNTESSSN STSNTQSAGV
960 970 980 990 1000
HMKEQLLYLS KLLDFEVNFS DYPKGNHNEF LTIVTLSTHP PQICHGVGKS
1010 1020
SEESQNDAAS NALKILSKLG LNNAMK
Length:1,026
Mass (Da):110,283
Last modified:July 19, 2005 - v2
Checksum:i3D390391F988B0A2
GO
Isoform B (identifier: P25159-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.

Note: No experimental confirmation available.
Show »
Length:914
Mass (Da):98,029
Checksum:iAB307F84F318C6E5
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti84 – 841G → A in AAA73062 (PubMed:1712672).Curated
Sequence conflicti684 – 6852PT → TM in AAA73062 (PubMed:1712672).Curated
Sequence conflicti797 – 7971S → C in AAA73062 (PubMed:1712672).Curated
Sequence conflicti841 – 8411Missing in AAQ23615 (Ref. 4) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 112112Missing in isoform B. 1 PublicationVSP_014781Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69111 mRNA. Translation: AAA73062.1.
AE013599 Genomic DNA. Translation: AAF57752.1.
AE013599 Genomic DNA. Translation: AAF57753.1.
BT003228 mRNA. Translation: AAO24983.1.
BT010297 mRNA. Translation: AAQ23615.1.
PIRiA40315.
RefSeqiNP_001163185.1. NM_001169714.2.
NP_476751.1. NM_057403.4. [P25159-1]
NP_725748.1. NM_166263.2. [P25159-2]
UniGeneiDm.4722.

Genome annotation databases

EnsemblMetazoaiFBtr0086783; FBpp0085962; FBgn0003520. [P25159-1]
GeneIDi37065.
KEGGidme:Dmel_CG5753.
UCSCiCG5753-RA. d. melanogaster. [P25159-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M69111 mRNA. Translation: AAA73062.1.
AE013599 Genomic DNA. Translation: AAF57752.1.
AE013599 Genomic DNA. Translation: AAF57753.1.
BT003228 mRNA. Translation: AAO24983.1.
BT010297 mRNA. Translation: AAQ23615.1.
PIRiA40315.
RefSeqiNP_001163185.1. NM_001169714.2.
NP_476751.1. NM_057403.4. [P25159-1]
NP_725748.1. NM_166263.2. [P25159-2]
UniGeneiDm.4722.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EKZNMR-A571-646[»]
1STUNMR-A579-646[»]
5CFFX-ray2.50E/F/G/H953-1019[»]
ProteinModelPortaliP25159.
SMRiP25159. Positions 571-646, 712-776.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi62749. 5 interactions.
IntActiP25159. 6 interactions.
MINTiMINT-112231.
STRINGi7227.FBpp0085962.

PTM databases

iPTMnetiP25159.

Proteomic databases

PaxDbiP25159.
PRIDEiP25159.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0086783; FBpp0085962; FBgn0003520. [P25159-1]
GeneIDi37065.
KEGGidme:Dmel_CG5753.
UCSCiCG5753-RA. d. melanogaster. [P25159-1]

Organism-specific databases

CTDi37065.
FlyBaseiFBgn0003520. stau.

Phylogenomic databases

eggNOGiKOG3732. Eukaryota.
ENOG410XSCK. LUCA.
GeneTreeiENSGT00830000128290.
InParanoidiP25159.
KOiK17597.
OMAiERGPAHC.
OrthoDBiEOG7NGQCG.
PhylomeDBiP25159.

Miscellaneous databases

EvolutionaryTraceiP25159.
GenomeRNAii37065.
NextBioi801768.
PROiP25159.

Gene expression databases

BgeeiP25159.
ExpressionAtlasiP25159. differential.
GenevisibleiP25159. DM.

Family and domain databases

Gene3Di3.30.160.20. 5 hits.
InterProiIPR014720. dsRBD_dom.
IPR032478. Staufen_C.
[Graphical view]
PfamiPF00035. dsrm. 4 hits.
PF16482. Staufen_C. 1 hit.
[Graphical view]
SMARTiSM00358. DSRM. 4 hits.
[Graphical view]
PROSITEiPS50137. DS_RBD. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Staufen, a gene required to localize maternal RNAs in the Drosophila egg."
    St Johnston D., Beuchle D., Nuesslein-Volhard C.
    Cell 66:51-63(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  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, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS A AND B).
    Strain: Berkeley.
    Tissue: Embryo, Larva and Pupae.
  5. "Staufen protein associates with the 3'UTR of bicoid mRNA to form particles that move in a microtubule-dependent manner."
    Ferrandon D., Elphick L., Nusslein-Volhard C., St Johnston D.
    Cell 79:1221-1232(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. "Distinct roles of two conserved Staufen domains in oskar mRNA localization and translation."
    Micklem D.R., Adams J., Grunert S., St Johnston D.
    EMBO J. 19:1366-1377(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF DRBM DOMAINS.
  7. "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-563; SER-570; THR-650; THR-655 AND SER-676, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  8. "NMR solution structure of a dsRNA binding domain from Drosophila staufen protein reveals homology to the N-terminal domain of ribosomal protein S5."
    Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.
    EMBO J. 14:3563-3571(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 579-646.
  9. Erratum
    Bycroft M., Grunert S., Murzin A.G., Proctor M., St Johnston D.
    EMBO J. 14:4385-4385(1995)
  10. Cited for: STRUCTURE BY NMR OF 571-646, FUNCTION, MUTAGENESIS OF 581-SER--GLN-582; 584-HIS--GLU-585; ILE-586; PHE-596; 599-LEU--GLU-602; HIS-606; LYS-608; 628-LYS--LYS-629; LYS-632; 633-LYS--ALA-634 AND 635-ALA--ALA-636.

Entry informationi

Entry nameiSTAU_DROME
AccessioniPrimary (citable) accession number: P25159
Secondary accession number(s): Q6NQY8
, Q86PB7, Q9V8B8, Q9V8B9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: July 19, 2005
Last modified: May 11, 2016
This is version 146 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.