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Q7KN62

- TERA_DROME

UniProt

Q7KN62 - TERA_DROME

Protein

Transitional endoplasmic reticulum ATPase TER94

Gene

TER94

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 91 (01 Oct 2014)
      Sequence version 1 (03 Oct 2006)
      Previous versions | rss
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    Functioni

    Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/or anchoring during oogenesis. Involved in germ cell formation.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei345 – 3451ATPBy similarity
    Binding sitei381 – 3811ATPBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi244 – 2507ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-triphosphatase activity Source: InterPro
    3. protein binding Source: FlyBase

    GO - Biological processi

    1. ATP catabolic process Source: FlyBase
    2. cellular response to virus Source: FlyBase
    3. dendrite morphogenesis Source: FlyBase
    4. endoplasmic reticulum membrane fusion Source: FlyBase
    5. endoplasmic reticulum organization Source: FlyBase
    6. ER-associated ubiquitin-dependent protein catabolic process Source: FlyBase
    7. Golgi organization Source: FlyBase
    8. microtubule cytoskeleton organization Source: FlyBase
    9. oogenesis Source: UniProtKB-KW
    10. positive regulation of neuron apoptotic process Source: FlyBase
    11. positive regulation of proteasomal ubiquitin-dependent protein catabolic process Source: FlyBase
    12. positive regulation of viral entry into host cell Source: FlyBase
    13. proteolysis Source: FlyBase
    14. regulation of neuron apoptotic process Source: FlyBase
    15. regulation of pole plasm oskar mRNA localization Source: FlyBase
    16. transport Source: UniProtKB-KW
    17. ubiquitin-dependent protein catabolic process Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein, Hydrolase

    Keywords - Biological processi

    Differentiation, Oogenesis, Transport, Ubl conjugation pathway

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Transitional endoplasmic reticulum ATPase TER94 (EC:3.6.4.6)
    Alternative name(s):
    Valosin-containing protein homolog
    Gene namesi
    Name:TER94
    Synonyms:VCP
    ORF Names:CG2331
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2R

    Organism-specific databases

    FlyBaseiFBgn0261014. TER94.

    Subcellular locationi

    Cytoplasm. Nucleus
    Note: Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.

    GO - Cellular componenti

    1. cytoplasm Source: FlyBase
    2. fusome Source: FlyBase
    3. lipid particle Source: FlyBase
    4. microtubule associated complex Source: FlyBase
    5. nucleus Source: UniProtKB-SubCell
    6. proteasome complex Source: FlyBase

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi437 – 4371E → A in ter94-26-8; arrests early in oogenesis. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 801801Transitional endoplasmic reticulum ATPase TER94PRO_0000347178Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei716 – 7161Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ7KN62.
    PRIDEiQ7KN62.

    Expressioni

    Tissue specificityi

    Present in the mushroom bodies of the protocerebrum and in the glomeruli of the antennal lobe. Present in nurse cells, oocytes and sperm bundles (at protein level).3 Publications

    Developmental stagei

    Present in egg, pupa and imago but not larva (at protein level).1 Publication

    Gene expression databases

    BgeeiQ7KN62.

    Interactioni

    Subunit structurei

    Homohexamer. Interacts with tud, vas, papi and AGO3.3 Publications

    Protein-protein interaction databases

    BioGridi61868. 79 interactions.
    IntActiQ7KN62. 5 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliQ7KN62.
    SMRiQ7KN62. Positions 14-761.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family.Curated

    Phylogenomic databases

    eggNOGiCOG0464.
    GeneTreeiENSGT00740000115575.
    InParanoidiQ7KN62.
    KOiK13525.
    OMAiHACADIK.
    OrthoDBiEOG7H4DSW.
    PhylomeDBiQ7KN62.

    Family and domain databases

    Gene3Di3.10.330.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR005938. AAA_ATPase_CDC48.
    IPR009010. Asp_de-COase-like_dom.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR004201. Cdc48_dom2.
    IPR029067. CDC48_domain_2-like.
    IPR003338. CDC4_N-term_subdom.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view]
    PfamiPF00004. AAA. 2 hits.
    PF02933. CDC48_2. 1 hit.
    PF02359. CDC48_N. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 2 hits.
    SM01072. CDC48_2. 1 hit.
    SM01073. CDC48_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF50692. SSF50692. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF54585. SSF54585. 1 hit.
    TIGRFAMsiTIGR01243. CDC48. 1 hit.
    PROSITEiPS00674. AAA. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform A (identifier: Q7KN62-1) [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

    MADSKGEDLA TAILKRKDRP NRLIVEEAQN DDNSVVSLSQ AKMDELQLFR    50
    GDTVILKGKR RKETVCIVLS DDTCPDEKIR MNRVVRNNLC VHLSDVVSVQ 100
    SCPDVKYGKR VRILPIDEST EGVTGNLFEI YLKPYFLEAY RPIHMGDNFI 150
    VRAAMRPIEF KVVLTDPEPY CIVAPETVIF CDGDPIKREE EEESLNAVGY 200
    DDIGGCRKQL AQIKEMVELP LRHPSLFKAI GVKPPRGILM YGPPGTGKTL 250
    IARAVANETG AFFFLINGPE IMSKLAGESE SNLRKAFEEA EKNSPAIIFI 300
    DEIDAIAPKR DKTHGEVERR IVSQLLTLMD GMKKSSHLIV MAATNRPNSI 350
    DPALRRFGRF DREIDIGIPD ATGRLEVLRI HTKNMKLHDD VDLEQIAAES 400
    HGHVGADLAS LCSEAALQQI REKMDLIDLE DDKIDAEVLA SLAVTMENFR 450
    YAMTKSSPSA LRETVVEVPN TTWTDIGGLE SVKKELQELV QYPVEHPDKF 500
    LKFGMQPSRG VLFYGPPGCG KTLLAKAIAN ECQANFISVK GPELLTMWFG 550
    ESEANVRDIF DKARSAAPCV LFFDELDSIA KARGGNVGDA GGAADRVINQ 600
    ILTEMDGMGA KKNVFIIGAT NRPDIIDPAI LRPGRLDQLI YIPLPDDKSR 650
    EAILKANLRK SPLAKEVDLT YIAKVTQGFS GADLTEICQR ACKLAIRQAI 700
    EAEIRREKER AENQNSAMDM DEDDPVPEIT SAHFEEAMKF ARRSVSDNDI 750
    RKYEMFAQTL QQSRGFGQNF RFPGQTGNTS GSGNNLPVNS PGDNGDDDLY 800
    S 801
    Length:801
    Mass (Da):88,859
    Last modified:October 3, 2006 - v1
    Checksum:iECF8F173B3B10B07
    GO
    Isoform D (identifier: Q7KN62-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-42: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:759
    Mass (Da):84,250
    Checksum:i3C3B83366776697E
    GO
    Isoform C (identifier: Q7KN62-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-6: MADSKG → MDHDGDTRDFMRGYHSEQDEKMKPKDSFDKR

    Note: No experimental confirmation available.

    Show »
    Length:826
    Mass (Da):92,055
    Checksum:iB6D5F85ECE7BCA33
    GO

    Sequence cautioni

    The sequence AAF17568.1 differs from that shown. Reason: Frameshift at positions 136, 142, 757 and 761.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti524 – 5241L → P in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti563 – 5642AR → GP in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti582 – 5843ARG → SRC in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti590 – 5912AG → C in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti661 – 6622SP → FA in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti662 – 6621P → A in AAC27447. (PubMed:9639875)Curated
    Sequence conflicti720 – 7201Missing in AAF17568. (PubMed:10656772)Curated
    Sequence conflicti735 – 7351E → Q in AAC27447. (PubMed:9639875)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4242Missing in isoform D. CuratedVSP_035052Add
    BLAST
    Alternative sequencei1 – 66MADSKG → MDHDGDTRDFMRGYHSEQDE KMKPKDSFDKR in isoform C. CuratedVSP_035053

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047037 mRNA. Translation: AAC27447.1.
    AF202034 mRNA. Translation: AAF17568.1. Frameshift.
    AE013599 Genomic DNA. Translation: ABV53745.1.
    AE013599 Genomic DNA. Translation: ABV53746.1.
    AE013599 Genomic DNA. Translation: AAF58863.1.
    AF132553 mRNA. Translation: AAD27852.1.
    RefSeqiNP_001097249.1. NM_001103779.2. [Q7KN62-3]
    NP_001097250.1. NM_001103780.2. [Q7KN62-2]
    NP_477369.1. NM_058021.4. [Q7KN62-1]
    UniGeneiDm.2968.

    Genome annotation databases

    EnsemblMetazoaiFBtr0088391; FBpp0087479; FBgn0261014. [Q7KN62-1]
    GeneIDi36040.
    KEGGidme:Dmel_CG2331.
    UCSCiCG2331-RA. d. melanogaster. [Q7KN62-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF047037 mRNA. Translation: AAC27447.1 .
    AF202034 mRNA. Translation: AAF17568.1 . Frameshift.
    AE013599 Genomic DNA. Translation: ABV53745.1 .
    AE013599 Genomic DNA. Translation: ABV53746.1 .
    AE013599 Genomic DNA. Translation: AAF58863.1 .
    AF132553 mRNA. Translation: AAD27852.1 .
    RefSeqi NP_001097249.1. NM_001103779.2. [Q7KN62-3 ]
    NP_001097250.1. NM_001103780.2. [Q7KN62-2 ]
    NP_477369.1. NM_058021.4. [Q7KN62-1 ]
    UniGenei Dm.2968.

    3D structure databases

    ProteinModelPortali Q7KN62.
    SMRi Q7KN62. Positions 14-761.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 61868. 79 interactions.
    IntActi Q7KN62. 5 interactions.

    Proteomic databases

    PaxDbi Q7KN62.
    PRIDEi Q7KN62.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0088391 ; FBpp0087479 ; FBgn0261014 . [Q7KN62-1 ]
    GeneIDi 36040.
    KEGGi dme:Dmel_CG2331.
    UCSCi CG2331-RA. d. melanogaster. [Q7KN62-1 ]

    Organism-specific databases

    CTDi 36040.
    FlyBasei FBgn0261014. TER94.

    Phylogenomic databases

    eggNOGi COG0464.
    GeneTreei ENSGT00740000115575.
    InParanoidi Q7KN62.
    KOi K13525.
    OMAi HACADIK.
    OrthoDBi EOG7H4DSW.
    PhylomeDBi Q7KN62.

    Miscellaneous databases

    GenomeRNAii 36040.
    NextBioi 796507.
    PROi Q7KN62.

    Gene expression databases

    Bgeei Q7KN62.

    Family and domain databases

    Gene3Di 3.10.330.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR005938. AAA_ATPase_CDC48.
    IPR009010. Asp_de-COase-like_dom.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR004201. Cdc48_dom2.
    IPR029067. CDC48_domain_2-like.
    IPR003338. CDC4_N-term_subdom.
    IPR027417. P-loop_NTPase.
    IPR015415. Vps4_C.
    [Graphical view ]
    Pfami PF00004. AAA. 2 hits.
    PF02933. CDC48_2. 1 hit.
    PF02359. CDC48_N. 1 hit.
    PF09336. Vps4_C. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 2 hits.
    SM01072. CDC48_2. 1 hit.
    SM01073. CDC48_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50692. SSF50692. 1 hit.
    SSF52540. SSF52540. 2 hits.
    SSF54585. SSF54585. 1 hit.
    TIGRFAMsi TIGR01243. CDC48. 1 hit.
    PROSITEi PS00674. AAA. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "TER94, a Drosophila homolog of the membrane fusion protein CDC48/p97, is accumulated in nonproliferating cells: in the reproductive organs and in the brain of the imago."
      Pinter M., Jekely G., Szepesi R.J., Farkas A., Theopold U., Meyer H.E., Lindholm D., Nassel D.R., Hultmark D., Friedrich P.
      Insect Biochem. Mol. Biol. 28:91-98(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 163-176; 214-220; 229-245; 294-308; 456-479; 485-499; 503-520; 563-580; 613-632; 666-687; 694-707 AND 740-748, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
      Strain: Canton-S.
    2. "Membrane fusion proteins are required for oskar mRNA localization in the Drosophila egg chamber."
      Ruden D.M., Sollars V., Wang X., Mori D., Alterman M., Lu X.
      Dev. Biol. 218:314-325(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), TISSUE SPECIFICITY, MUTAGENESIS OF GLU-437.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
      Strain: Berkeley.
      Tissue: Ovary.
    6. "Identification of TER94, an AAA ATPase protein, as a Bam-dependent component of the Drosophila fusome."
      Leon A., McKearin D.
      Mol. Biol. Cell 10:3825-3834(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, SUBUNIT, SUBCELLULAR LOCATION.
    7. "RNA interference of valosin-containing protein (VCP/p97) reveals multiple cellular roles linked to ubiquitin/proteasome-dependent proteolysis."
      Wojcik C., Yano M., DeMartino G.N.
      J. Cell Sci. 117:281-292(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "An integrated chemical, mass spectrometric and computational strategy for (quantitative) phosphoproteomics: application to Drosophila melanogaster Kc167 cells."
      Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A., Eng J.K., Aebersold R., Tao W.A.
      Mol. Biosyst. 3:275-286(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-716, IDENTIFICATION BY MASS SPECTROMETRY.
    9. "Isolation of new polar granule components in Drosophila reveals P body and ER associated proteins."
      Thomson T., Liu N., Arkov A., Lehmann R., Lasko P.
      Mech. Dev. 125:865-873(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TUD AND VAS, SUBCELLULAR LOCATION.
    10. "PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition."
      Liu L., Qi H., Wang J., Lin H.
      Development 138:1863-1873(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PAPI AND AGO3.

    Entry informationi

    Entry nameiTERA_DROME
    AccessioniPrimary (citable) accession number: Q7KN62
    Secondary accession number(s): A8DY85
    , A8DY86, O76279, Q9U463
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 2, 2008
    Last sequence update: October 3, 2006
    Last modified: October 1, 2014
    This is version 91 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, Direct protein sequencing, 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