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Q9U1K1

- SPIR_DROME

UniProt

Q9U1K1 - SPIR_DROME

Protein

Protein spire

Gene

spir

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 111 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    Acts as an actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Promotes dissociation of capu from the barbed end of actin filaments. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for localization of determinants within the developing oocyte to the posterior pole and to the dorsal anterior corner. Links Rho family signaling and Jnk function to the actin cytoskeleton.5 Publications

    GO - Molecular functioni

    1. actin binding Source: FlyBase
    2. microtubule binding Source: FlyBase
    3. protein binding Source: FlyBase

    GO - Biological processi

    1. actin cytoskeleton organization Source: FlyBase
    2. actin filament-based process Source: FlyBase
    3. actin filament network formation Source: FlyBase
    4. actin filament organization Source: FlyBase
    5. actin nucleation Source: FlyBase
    6. chorion-containing eggshell formation Source: FlyBase
    7. karyosome formation Source: FlyBase
    8. oogenesis Source: FlyBase
    9. pole plasm assembly Source: FlyBase
    10. pole plasm oskar mRNA localization Source: FlyBase
    11. pole plasm RNA localization Source: FlyBase
    12. protein transport Source: UniProtKB-KW
    13. regulation of cytoskeleton organization Source: FlyBase
    14. vesicle-mediated transport Source: FlyBase

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Protein transport, Transport

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein spire
    Gene namesi
    Name:spirImported
    Synonyms:p150-SpirImported
    ORF Names:CG10076
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 2L

    Organism-specific databases

    FlyBaseiFBgn0003475. spir.

    Subcellular locationi

    Cytoplasmcytoskeleton. Cytoplasmperinuclear region. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side
    Note: Punctate spots in perinuclear region and cytoplasm.1 Publication

    GO - Cellular componenti

    1. cell cortex Source: FlyBase
    2. cytoplasm Source: FlyBase
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. cytoskeleton Source: UniProtKB-SubCell
    5. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    6. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Cytoplasmic vesicle, Cytoskeleton, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Flies display premature microtubule-dependent cytoplasmic streaming; failure in the orientation of microtubule plus ends towards the posterior pole.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi232 – 2321Y → K: Abolishes interaction with capu. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10201020Protein spirePRO_0000309573Add
    BLAST

    Post-translational modificationi

    Phosphorylated by Jnk kinase (bsk).1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiQ9U1K1.
    PRIDEiQ9U1K1.

    Expressioni

    Developmental stagei

    Expressed both maternally and zygotically.1 Publication

    Gene expression databases

    BgeeiQ9U1K1.

    Interactioni

    Subunit structurei

    Interacts with bsk, Rho1, Rac1, Cdc42 and wash. Interacts with capu.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    bskP922081EBI-91672,EBI-74487
    CG14579Q9VRF51EBI-91672,EBI-99956
    saxQ7JQ361EBI-91672,EBI-121415

    Protein-protein interaction databases

    BioGridi69994. 13 interactions.
    DIPiDIP-17301N.
    IntActiQ9U1K1. 3 interactions.
    MINTiMINT-295231.

    Structurei

    Secondary structure

    1
    1020
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi374 – 38310
    Helixi400 – 4089
    Helixi431 – 4388
    Helixi463 – 47311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MMVX-ray2.80X429-447[»]
    3MN5X-ray1.50S448-485[»]
    3MN6X-ray2.00X/Y/Z397-415[»]
    3MN7X-ray2.00S441-479[»]
    3MN9X-ray2.00X372-390[»]
    3UE5X-ray2.76B428-485[»]
    4EFHX-ray2.48B428-485[»]
    ProteinModelPortaliQ9U1K1.
    SMRiQ9U1K1. Positions 222-331.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9U1K1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 327238KINDPROSITE-ProRule annotationAdd
    BLAST
    Domaini399 – 41719WH2 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini463 – 48018WH2 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni705 – 72521Spir-boxAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi205 – 22016His-richSequence AnalysisAdd
    BLAST
    Compositional biasi792 – 87786Ser-richSequence AnalysisAdd
    BLAST

    Domaini

    Binds to actin monomers via the WH2 domain.1 Publication
    The Spir-box targets binding to intracellular membrane structures.By similarity

    Sequence similaritiesi

    Belongs to the spire family.Curated
    Contains 1 KIND domain.PROSITE-ProRule annotation
    Contains 2 WH2 domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG69783.
    GeneTreeiENSGT00390000003058.
    InParanoidiQ9U1K1.
    KOiK02098.
    OMAiWALIYQF.
    OrthoDBiEOG7F511H.
    PhylomeDBiQ9U1K1.

    Family and domain databases

    Gene3Di3.30.40.10. 1 hit.
    InterProiIPR011019. KIND.
    IPR003124. WH2_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view]
    SMARTiSM00750. KIND. 1 hit.
    SM00246. WH2. 2 hits.
    [Graphical view]
    SUPFAMiSSF57903. SSF57903. 2 hits.
    PROSITEiPS51377. KIND. 1 hit.
    PS51082. WH2. 2 hits.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform A1 Publication (identifier: Q9U1K1-1) [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

    MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ     50
    HKLPADQLAM SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK 100
    APLSEDQAWA LIHQFAGLYH QVAVQAHTCA ADYEAALPTG FELHFHRDGS 150
    VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV DQPDHSASSS GDSSVINRAF 200
    DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP EDEECQVSQE 250
    LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC 300
    RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES 350
    SATTQQELAK LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY 400
    EILMGDIRAK KYQLRKVMVN GDIPPRVKKD AHAMILEFIR SRPPLKKASD 450
    RQLGPPRMCE PSPREQLMES IRKGKELKQI TPPEAPTLRE RVLPSANSTL 500
    SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH PHFAEMHRCS 550
    QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTMEPAKQ VPPPEEPSFT 600
    KDEYHKFYDT ALESYDLATQ CESRRASLRR HTIVGCQSNL DETHSMPPTR 650
    PESRQSDDVS KETPKRSPAE QTHPSDEGSS TSSLGPWNKS FMDKQTWMER 700
    GDDRLSVTLA EIVHIRSVMT KAELEGLPMD VRVKEDVEKR RVCFLCLRTR 750
    FSFFGPWGIQ CKLCQRTVCA KCYTKMRIPS EHFRNVPLVL ISPSLLSSPA 800
    SSSTPSPSHH AQQAHSSSTG NIMDDQFPKS LIERLLRSES DRKTRSTVGS 850
    APSSPKHQRS NMSTPGISVG PGASSSSAAA TGQAVEALHD QATMSSSYSA 900
    AMRPSGVHQQ QKQHYNNAMS RSMEGPRSLP VHSPAYRPLS NNSTLERKSR 950
    FSRGFNLFSS GSHLAQTQEQ KENLRGEQVT VCNDCQGLVN EITSSVKQKR 1000
    SSARNRTIQN LTLDLTPVWK 1020
    Length:1,020
    Mass (Da):114,867
    Last modified:May 1, 2000 - v1
    Checksum:i010CD024F9ABC078
    GO
    Isoform B1 Publication (identifier: Q9U1K1-2) [UniParc]FASTAAdd to Basket

    Also known as: Long1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         585-614: MEPAKQVPPPEEPSFTKDEYHKFYDTALES → T

    Show »
    Length:991
    Mass (Da):111,475
    Checksum:i5A39B9F07136E212
    GO
    Isoform C1 Publication (identifier: Q9U1K1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2-96: TEHQAEEQAD...EQCVTLHDIL → EARPAKRSTA...KPRQAIRSSK
         97-491: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:625
    Mass (Da):69,401
    Checksum:i6B020E5746568D77
    GO
    Isoform D1 Publication (identifier: Q9U1K1-4) [UniParc]FASTAAdd to Basket

    Also known as: Short1 Publication

    The sequence of this isoform differs from the canonical sequence as follows:
         338-338: Missing.
         585-586: ME → SI
         587-1020: Missing.

    Show »
    Length:585
    Mass (Da):66,418
    Checksum:i8F2F09E9AB96CF7F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531L → M in AAF23615. (PubMed:10556052)Curated
    Sequence conflicti53 – 531L → M in AAF23616. (PubMed:10556052)Curated
    Sequence conflicti885 – 8851V → A in AAF23615. (PubMed:10556052)Curated

    RNA editingi

    Partially edited. Target of Adar.1 Publication

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti734 – 7341K → R in RNA edited version. 1 Publication

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2 – 9695TEHQA…LHDIL → EARPAKRSTAASVFRSHHMP RESDLVDIGSDASLYCGSDG ESSQAQSTSTSTPNPQTSSD QDLDQPQPTPRAAPRASASN NPPTPKPRQAIRSSK in isoform C. 2 PublicationsVSP_052599Add
    BLAST
    Alternative sequencei97 – 491395Missing in isoform C. 2 PublicationsVSP_052600Add
    BLAST
    Alternative sequencei338 – 3381Missing in isoform D. 2 PublicationsVSP_052601
    Alternative sequencei585 – 61430MEPAK…TALES → T in isoform B. 2 PublicationsVSP_052602Add
    BLAST
    Alternative sequencei585 – 5862ME → SI in isoform D. 2 PublicationsVSP_052603
    Alternative sequencei587 – 1020434Missing in isoform D. 2 PublicationsVSP_052604Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184975 mRNA. Translation: AAF23615.1.
    AF184976 mRNA. Translation: AAF23616.1.
    AJ238876 mRNA. Translation: CAB62901.1.
    AE014134 Genomic DNA. Translation: AAF53884.2.
    AE014134 Genomic DNA. Translation: AAN11070.1.
    AE014134 Genomic DNA. Translation: AAN11071.1.
    AE014134 Genomic DNA. Translation: AAN11072.2.
    AY075586 mRNA. Translation: AAL68390.1.
    AY089503 mRNA. Translation: AAL90241.1.
    BT016094 mRNA. Translation: AAV36979.1.
    RefSeqiNP_001246102.1. NM_001259173.1.
    NP_524854.2. NM_080115.3. [Q9U1K1-2]
    NP_724254.1. NM_165323.2. [Q9U1K1-1]
    NP_724255.1. NM_165324.2. [Q9U1K1-4]
    NP_724256.2. NM_165325.2. [Q9U1K1-3]
    UniGeneiDm.3356.

    Genome annotation databases

    EnsemblMetazoaiFBtr0081352; FBpp0080884; FBgn0003475. [Q9U1K1-1]
    GeneIDi45931.
    KEGGidme:Dmel_CG10076.
    UCSCiCG10076-RA. d. melanogaster. [Q9U1K1-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, RNA editing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF184975 mRNA. Translation: AAF23615.1 .
    AF184976 mRNA. Translation: AAF23616.1 .
    AJ238876 mRNA. Translation: CAB62901.1 .
    AE014134 Genomic DNA. Translation: AAF53884.2 .
    AE014134 Genomic DNA. Translation: AAN11070.1 .
    AE014134 Genomic DNA. Translation: AAN11071.1 .
    AE014134 Genomic DNA. Translation: AAN11072.2 .
    AY075586 mRNA. Translation: AAL68390.1 .
    AY089503 mRNA. Translation: AAL90241.1 .
    BT016094 mRNA. Translation: AAV36979.1 .
    RefSeqi NP_001246102.1. NM_001259173.1.
    NP_524854.2. NM_080115.3. [Q9U1K1-2 ]
    NP_724254.1. NM_165323.2. [Q9U1K1-1 ]
    NP_724255.1. NM_165324.2. [Q9U1K1-4 ]
    NP_724256.2. NM_165325.2. [Q9U1K1-3 ]
    UniGenei Dm.3356.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MMV X-ray 2.80 X 429-447 [» ]
    3MN5 X-ray 1.50 S 448-485 [» ]
    3MN6 X-ray 2.00 X/Y/Z 397-415 [» ]
    3MN7 X-ray 2.00 S 441-479 [» ]
    3MN9 X-ray 2.00 X 372-390 [» ]
    3UE5 X-ray 2.76 B 428-485 [» ]
    4EFH X-ray 2.48 B 428-485 [» ]
    ProteinModelPortali Q9U1K1.
    SMRi Q9U1K1. Positions 222-331.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 69994. 13 interactions.
    DIPi DIP-17301N.
    IntActi Q9U1K1. 3 interactions.
    MINTi MINT-295231.

    Proteomic databases

    PaxDbi Q9U1K1.
    PRIDEi Q9U1K1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0081352 ; FBpp0080884 ; FBgn0003475 . [Q9U1K1-1 ]
    GeneIDi 45931.
    KEGGi dme:Dmel_CG10076.
    UCSCi CG10076-RA. d. melanogaster. [Q9U1K1-1 ]

    Organism-specific databases

    CTDi 45931.
    FlyBasei FBgn0003475. spir.

    Phylogenomic databases

    eggNOGi NOG69783.
    GeneTreei ENSGT00390000003058.
    InParanoidi Q9U1K1.
    KOi K02098.
    OMAi WALIYQF.
    OrthoDBi EOG7F511H.
    PhylomeDBi Q9U1K1.

    Miscellaneous databases

    ChiTaRSi spir. drosophila.
    EvolutionaryTracei Q9U1K1.
    GenomeRNAii 45931.
    NextBioi 838510.
    PROi Q9U1K1.

    Gene expression databases

    Bgeei Q9U1K1.

    Family and domain databases

    Gene3Di 3.30.40.10. 1 hit.
    InterProi IPR011019. KIND.
    IPR003124. WH2_dom.
    IPR011011. Znf_FYVE_PHD.
    IPR013083. Znf_RING/FYVE/PHD.
    [Graphical view ]
    SMARTi SM00750. KIND. 1 hit.
    SM00246. WH2. 2 hits.
    [Graphical view ]
    SUPFAMi SSF57903. SSF57903. 2 hits.
    PROSITEi PS51377. KIND. 1 hit.
    PS51082. WH2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Spire contains actin binding domains and is related to ascidian posterior end mark-5."
      Wellington A., Emmons S., James B., Calley J., Grover M., Tolias P., Manseau L.
      Development 126:5267-5274(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS B AND D), FUNCTION, INTERACTION WITH RHO1; RAC1 AND CDC42, DEVELOPMENTAL STAGE, ACTIN-BINDING, DISRUPTION PHENOTYPE.
      Tissue: Ovary1 Publication.
    2. "The p150-Spir protein provides a link between c-Jun N-terminal kinase function and actin reorganization."
      Otto I.M., Raabe T., Rennefahrt U.E.E., Bork P., Rapp U.R., Kerkhoff E.
      Curr. Biol. 10:345-348(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, INTERACTION WITH BSK, SUBCELLULAR LOCATION, PHOSPHORYLATION.
      Tissue: Embryo1 Publication.
    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: Berkeley1 Publication.
    4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
      Strain: Berkeley.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS C AND D), RNA EDITING OF POSITION 734.
      Strain: Berkeley1 Publication.
      Tissue: Embryo1 Publication and Head1 Publication.
    6. Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Rubin G.M., Celniker S.E.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 196-1020 (ISOFORM B).
      Strain: BerkeleyImported.
      Tissue: Embryo.
    7. "Drosophila Spire is an actin nucleation factor."
      Quinlan M.E., Heuser J.E., Kerkhoff E., Mullins R.D.
      Nature 433:382-388(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "RNA editing in Drosophila melanogaster: new targets and functional consequences."
      Stapleton M., Carlson J.W., Celniker S.E.
      RNA 12:1922-1932(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA EDITING OF POSITION 734.
    9. "Wash functions downstream of Rho and links linear and branched actin nucleation factors."
      Liu R., Abreu-Blanco M.T., Barry K.C., Linardopoulou E.V., Osborn G.E., Parkhurst S.M.
      Development 136:2849-2860(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH WASH.
    10. "Structure and function of the interacting domains of Spire and Fmn-family formins."
      Vizcarra C.L., Kreutz B., Rodal A.A., Toms A.V., Lu J., Zheng W., Quinlan M.E., Eck M.J.
      Proc. Natl. Acad. Sci. U.S.A. 108:11884-11889(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CAPU, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-232.
    11. "Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation."
      Ducka A.M., Joel P., Popowicz G.M., Trybus K.M., Schleicher M., Noegel A.A., Huber R., Holak T.A., Sitar T.
      Proc. Natl. Acad. Sci. U.S.A. 107:11757-11762(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 448-485 IN COMPLEX WITH ACTIN, FUNCTION.
    12. "Multiple forms of Spire-actin complexes and their functional consequences."
      Chen C.K., Sawaya M.R., Phillips M.L., Reisler E., Quinlan M.E.
      J. Biol. Chem. 287:10684-10692(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.76 ANGSTROMS) OF 428-485 IN COMPLEX WITH ACTIN.

    Entry informationi

    Entry nameiSPIR_DROME
    AccessioniPrimary (citable) accession number: Q9U1K1
    Secondary accession number(s): Q5U0Z8
    , Q8INV3, Q8INV4, Q8INV5, Q8SXP3, Q8T8P8, Q9U4F0, Q9U4F1, Q9VIN3, Q9VIN4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 13, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 111 of the entry and version 1 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

    External Data

    Dasty 3