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Q24151

- STAT_DROME

UniProt

Q24151 - STAT_DROME

Protein

Signal transducer and transcription activator

Gene

Stat92E

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 1 (01 Nov 1997)
      Previous versions | rss
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    Functioni

    Signal transduction and activation of transcription. Plays an important role in the segmental pattern formation in the early embryo by activating specific stripes of pair rule gene expression. The Janus kinase-STAT pathway is connected to drosophila early development.

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. DNA binding Source: FlyBase
    3. protein binding Source: FlyBase
    4. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: FlyBase
    5. sequence-specific DNA binding transcription factor activity Source: FlyBase
    6. signal transducer activity Source: InterPro

    GO - Biological processi

    1. blastoderm segmentation Source: FlyBase
    2. border follicle cell migration Source: FlyBase
    3. cell dedifferentiation Source: FlyBase
    4. cellular response to lipopolysaccharide Source: FlyBase
    5. cellular response to X-ray Source: FlyBase
    6. compound eye development Source: FlyBase
    7. defense response Source: FlyBase
    8. epithelial cell fate determination, open tracheal system Source: FlyBase
    9. eye-antennal disc morphogenesis Source: FlyBase
    10. germ-line stem cell division Source: FlyBase
    11. germ-line stem cell maintenance Source: FlyBase
    12. hemocyte proliferation Source: FlyBase
    13. hemopoiesis Source: FlyBase
    14. hindgut morphogenesis Source: FlyBase
    15. humoral immune response Source: FlyBase
    16. imaginal disc-derived wing morphogenesis Source: FlyBase
    17. JAK-STAT cascade Source: FlyBase
    18. lamellocyte differentiation Source: FlyBase
    19. larval lymph gland hemopoiesis Source: FlyBase
    20. larval somatic muscle development Source: FlyBase
    21. long-term memory Source: FlyBase
    22. negative regulation of antimicrobial humoral response Source: FlyBase
    23. negative regulation of Wnt signaling pathway Source: FlyBase
    24. nervous system development Source: FlyBase
    25. oocyte localization involved in germarium-derived egg chamber formation Source: FlyBase
    26. oogenesis Source: FlyBase
    27. open tracheal system development Source: FlyBase
    28. ovarian follicle cell stalk formation Source: FlyBase
    29. positive regulation of cell proliferation Source: FlyBase
    30. positive regulation of defense response to virus by host Source: FlyBase
    31. positive regulation of transcription from RNA polymerase II promoter Source: GOC
    32. primary sex determination Source: FlyBase
    33. regulation of JAK-STAT cascade Source: FlyBase
    34. segment specification Source: FlyBase
    35. sex determination Source: FlyBase
    36. somatic stem cell division Source: FlyBase
    37. somatic stem cell maintenance Source: FlyBase
    38. stem cell division Source: FlyBase
    39. stem cell maintenance Source: FlyBase

    Keywords - Molecular functioni

    Activator, Developmental protein

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    ReactomeiREACT_180284. Growth hormone receptor signaling.
    REACT_180781. Signaling by FGFR1 fusion mutants.
    REACT_180816. Interleukin-7 signaling.
    REACT_219000. Interleukin-2 signaling.
    REACT_224431. Signaling by Leptin.
    REACT_85224. Interleukin-3, 5 and GM-CSF signaling.
    SignaLinkiQ24151.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Signal transducer and transcription activator
    Short name:
    d-STAT
    Alternative name(s):
    Protein marelle
    Gene namesi
    Name:Stat92E
    Synonyms:MARE, mrL, Stat
    ORF Names:CG4257
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3R

    Organism-specific databases

    FlyBaseiFBgn0016917. Stat92E.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Translocated into the nucleus in response to phosphorylation.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. nucleus Source: BHF-UCL

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Disruption phenotypei

    Flies exhibit aberrant expression of the pair rule gene even-skipped at the cellular blastoderm stage, leading to larval segmentation defects.2 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 761761Signal transducer and transcription activatorPRO_0000182435Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei711 – 7111Phosphotyrosine; by JAK2 Publications

    Post-translational modificationi

    Tyrosine phosphorylated by hopscotch. Phosphorylation is required for DNA-binding activity and dimerization.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ24151.
    PRIDEiQ24151.

    Expressioni

    Developmental stagei

    Expressed throughout embryonic, larval, pupal, and adult stages, with some decrease in the late embryonic stages. The expression is uniform in unfertilized or just fertilized eggs, suggesting maternally deposited mRNA. At blastoderm stage, expression pattern shows stripes, that are reminiscent of many pair rule genes pattern.

    Gene expression databases

    BgeeiQ24151.

    Interactioni

    Subunit structurei

    Forms a homodimer or a heterodimer with a related family member.

    Protein-protein interaction databases

    BioGridi67407. 18 interactions.
    DIPiDIP-29510N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ24151.
    SMRiQ24151. Positions 235-695.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini594 – 65865SH2PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the transcription factor STAT family.Curated
    Contains 1 SH2 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH2 domain

    Phylogenomic databases

    eggNOGiNOG245085.
    GeneTreeiENSGT00740000115175.
    InParanoidiQ24151.
    KOiK11224.
    OMAiALNIKFG.
    OrthoDBiEOG73JKTT.
    PhylomeDBiQ24151.

    Family and domain databases

    Gene3Di1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProiIPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view]
    PANTHERiPTHR11801. PTHR11801. 1 hit.
    PfamiPF00017. SH2. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view]
    SMARTiSM00252. SH2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47655. SSF47655. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS50001. SH2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform F (identifier: Q24151-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MSLWKRISSH VDCEQRMAAY YEEKGMLELR LCLAPWIEDR IMSEQITPNT    50
    TDQLERVALK FNEDLQQKLL STRTASDQAL KFRVVELCAL IQRISAVELY 100
    THLRSGLQKE LQLVTEKSVA ATAGQSMPLN PYNMNNTPMV TGYMVDPSDL 150
    LAVSNSCNPP VVQGIGPIHN VQNTGIASPA LGMVTPKVEL YEVQHQIMQS 200
    LNEFGNCANA LKLLAQNYSY MLNSTSSPNA EAAYRSLIDE KAAIVLTMRR 250
    SFMYYESLHE MVIHELKNWR HQQAQAGNGA PFNEGSLDDI QRCFEMLESF 300
    IAHMLAAVKE LMRVRLVTEE PELTHLLEQV QNAQKNLVCS AFIVDKQPPQ 350
    VMKTNTRFAA SVRWLIGSQL GIHNNPPTVE CIIMSEIQSQ RFVTRNTQMD 400
    NSSLSGQSSG EIQNASSTME YQQNNHVFSA SFRNMQLKKI KRAEKKGTES 450
    VMDEKFALFF YTTTTVNDFQ IRVWTLSLPV VVIVHGNQEP QSWATITWDN 500
    AFAEIVRDPF MITDRVTWAQ LSVALNIKFG SCTGRSLTID NLDFLYEKLQ 550
    REERSEYITW NQFCKEPMPD RSFTFWEWFF AIMKLTKDHM LGMWKAGCIM 600
    GFINKTKAQT DLLRSVYGIG TFLLRFSDSE LGGVTIAYVN ENGLVTMLAP 650
    WTARDFQVLN LADRIRDLDV LCWLHPSDRN ASPVKRDVAF GEFYSKRQEP 700
    EPLVLDPVTG YVKSTLHVHV CRNGENGSTS GTPHHAQESM QLGNGDFGMA 750
    DFDTITNFEN F 761
    Length:761
    Mass (Da):86,415
    Last modified:November 1, 1997 - v1
    Checksum:iBF3A622A29899161
    GO
    Isoform B (identifier: Q24151-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.
         699-705: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:628
    Mass (Da):71,198
    Checksum:i841208C04B2A91D0
    GO
    Isoform C (identifier: Q24151-2) [UniParc]FASTAAdd to Basket

    Also known as: E, Short

    The sequence of this isoform differs from the canonical sequence as follows:
         699-705: Missing.

    Show »
    Length:754
    Mass (Da):85,637
    Checksum:iB607B3328A4A4956
    GO
    Isoform G (identifier: Q24151-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-126: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:635
    Mass (Da):71,976
    Checksum:iA3B0A8FFC32BCCF3
    GO

    Sequence cautioni

    The sequence AAM11192.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti105 – 1051S → T in AAB02195. (PubMed:8608596)Curated
    Sequence conflicti648 – 6481L → H in AAB02195. (PubMed:8608596)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 126126Missing in isoform B and isoform G. CuratedVSP_012752Add
    BLAST
    Alternative sequencei699 – 7057Missing in isoform B and isoform C. 1 PublicationVSP_006290

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40070 mRNA. Translation: AAC46984.1.
    U46688 mRNA. Translation: AAB02195.1.
    AE014297 Genomic DNA. Translation: AAN14350.2.
    AE014297 Genomic DNA. Translation: AAN14351.2.
    AE014297 Genomic DNA. Translation: AAS65180.1.
    AE014297 Genomic DNA. Translation: AAX52969.1.
    BT021314 mRNA. Translation: AAX33462.1.
    AY094839 mRNA. Translation: AAM11192.1. Different initiation.
    RefSeqiNP_001014643.1. NM_001014643.2. [Q24151-4]
    NP_001262757.1. NM_001275828.1. [Q24151-4]
    NP_001262762.1. NM_001275833.1. [Q24151-1]
    NP_732516.2. NM_169899.3. [Q24151-2]
    NP_732517.2. NM_169900.3. [Q24151-3]
    NP_996242.1. NM_206520.2. [Q24151-2]
    NP_996243.1. NM_206521.2. [Q24151-1]
    UniGeneiDm.2627.

    Genome annotation databases

    EnsemblMetazoaiFBtr0089486; FBpp0088489; FBgn0016917. [Q24151-1]
    GeneIDi42428.
    KEGGidme:Dmel_CG4257.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U40070 mRNA. Translation: AAC46984.1 .
    U46688 mRNA. Translation: AAB02195.1 .
    AE014297 Genomic DNA. Translation: AAN14350.2 .
    AE014297 Genomic DNA. Translation: AAN14351.2 .
    AE014297 Genomic DNA. Translation: AAS65180.1 .
    AE014297 Genomic DNA. Translation: AAX52969.1 .
    BT021314 mRNA. Translation: AAX33462.1 .
    AY094839 mRNA. Translation: AAM11192.1 . Different initiation.
    RefSeqi NP_001014643.1. NM_001014643.2. [Q24151-4 ]
    NP_001262757.1. NM_001275828.1. [Q24151-4 ]
    NP_001262762.1. NM_001275833.1. [Q24151-1 ]
    NP_732516.2. NM_169899.3. [Q24151-2 ]
    NP_732517.2. NM_169900.3. [Q24151-3 ]
    NP_996242.1. NM_206520.2. [Q24151-2 ]
    NP_996243.1. NM_206521.2. [Q24151-1 ]
    UniGenei Dm.2627.

    3D structure databases

    ProteinModelPortali Q24151.
    SMRi Q24151. Positions 235-695.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 67407. 18 interactions.
    DIPi DIP-29510N.

    Proteomic databases

    PaxDbi Q24151.
    PRIDEi Q24151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0089486 ; FBpp0088489 ; FBgn0016917 . [Q24151-1 ]
    GeneIDi 42428.
    KEGGi dme:Dmel_CG4257.

    Organism-specific databases

    CTDi 42428.
    FlyBasei FBgn0016917. Stat92E.

    Phylogenomic databases

    eggNOGi NOG245085.
    GeneTreei ENSGT00740000115175.
    InParanoidi Q24151.
    KOi K11224.
    OMAi ALNIKFG.
    OrthoDBi EOG73JKTT.
    PhylomeDBi Q24151.

    Enzyme and pathway databases

    Reactomei REACT_180284. Growth hormone receptor signaling.
    REACT_180781. Signaling by FGFR1 fusion mutants.
    REACT_180816. Interleukin-7 signaling.
    REACT_219000. Interleukin-2 signaling.
    REACT_224431. Signaling by Leptin.
    REACT_85224. Interleukin-3, 5 and GM-CSF signaling.
    SignaLinki Q24151.

    Miscellaneous databases

    GenomeRNAii 42428.
    NextBioi 828722.

    Gene expression databases

    Bgeei Q24151.

    Family and domain databases

    Gene3Di 1.10.238.10. 1 hit.
    1.10.532.10. 1 hit.
    1.20.1050.20. 1 hit.
    2.60.40.630. 1 hit.
    3.30.505.10. 1 hit.
    InterProi IPR011992. EF-hand-dom_pair.
    IPR008967. p53-like_TF_DNA-bd.
    IPR000980. SH2.
    IPR001217. STAT.
    IPR013800. STAT_TF_alpha.
    IPR015988. STAT_TF_coiled-coil.
    IPR013801. STAT_TF_DNA-bd.
    IPR012345. STAT_TF_DNA-bd_sub.
    IPR013799. STAT_TF_prot_interaction.
    [Graphical view ]
    PANTHERi PTHR11801. PTHR11801. 1 hit.
    Pfami PF00017. SH2. 1 hit.
    PF01017. STAT_alpha. 1 hit.
    PF02864. STAT_bind. 1 hit.
    PF02865. STAT_int. 1 hit.
    [Graphical view ]
    SMARTi SM00252. SH2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47655. SSF47655. 1 hit.
    SSF49417. SSF49417. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS50001. SH2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Marelle acts downstream of the Drosophila HOP/JAK kinase and encodes a protein similar to the mammalian STATs."
      Hou X.S., Melnick M.B., Perrimon N.
      Cell 84:411-419(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM F), DISRUPTION PHENOTYPE.
      Tissue: Embryo.
    2. "Identification of a Stat gene that functions in Drosophila development."
      Yan R., Small S., Desplan C., Dearolf C.R., Darnell J.E. Jr.
      Cell 84:421-430(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), PHOSPHORYLATION AT TYR-711, DISRUPTION PHENOTYPE.
      Tissue: Embryo.
    3. "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.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
      Strain: Berkeley.
      Tissue: Embryo.
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 267-761 (ISOFORM F).
      Strain: Berkeley.
      Tissue: Larva and Pupae.
    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 TYR-711, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Embryo.

    Entry informationi

    Entry nameiSTAT_DROME
    AccessioniPrimary (citable) accession number: Q24151
    Secondary accession number(s): Q0KI43
    , Q24181, Q59DV7, Q5BIB0, Q8IN54, Q8SX55, Q9VDL8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 141 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3