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Q9U1K1

- SPIR_DROME

UniProt

Q9U1K1 - SPIR_DROME

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Protein

Protein spire

Gene

spir

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

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

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
Complete GO annotation...

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 Source: UniProtKB-KW
  4. cytoskeleton Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

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.
ExpressionAtlasiQ9U1K1. differential.

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 – 38310Combined sources
Helixi400 – 4089Combined sources
Helixi431 – 4388Combined sources
Helixi463 – 47311Combined sources

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

        10         20         30         40         50
MTEHQAEEQA DTPPTKVKAT PTPTPSGKFK DAKEDAFLST SPDSANGDAQ
60 70 80 90 100
HKLPADQLAM SSSAHPQQAG QARPLILQAF HRCSSPEQCV TLHDILDSFK
110 120 130 140 150
APLSEDQAWA LIHQFAGLYH QVAVQAHTCA ADYEAALPTG FELHFHRDGS
160 170 180 190 200
VHFSGPDQLT PKEQLQQEQI PLPPQHDVIV DQPDHSASSS GDSSVINRAF
210 220 230 240 250
DNSNHHHHHQ HHHPPLVVSH RKIISELAEI VYTALDYNLP EDEECQVSQE
260 270 280 290 300
LENLFNFMTA DETDDDCIDE GIDEGDKRWD DESEEERNDT KELEHIIETC
310 320 330 340 350
RNHIKTTLPE NHYRAVCRAL VTETIELRVF LQQVLNNEAG AEKLIKASES
360 370 380 390 400
SATTQQELAK LGFNDWARFW VQVIDELRRG VRLKKSNHER TPIEYELTPY
410 420 430 440 450
EILMGDIRAK KYQLRKVMVN GDIPPRVKKD AHAMILEFIR SRPPLKKASD
460 470 480 490 500
RQLGPPRMCE PSPREQLMES IRKGKELKQI TPPEAPTLRE RVLPSANSTL
510 520 530 540 550
SRSRQRLIKV DFSKFQDDDL FYDENSISSS HSTAATHQHH PHFAEMHRCS
560 570 580 590 600
QPKMPPYPFG GYMVPSQARQ DCRETASLMR PRRTMEPAKQ VPPPEEPSFT
610 620 630 640 650
KDEYHKFYDT ALESYDLATQ CESRRASLRR HTIVGCQSNL DETHSMPPTR
660 670 680 690 700
PESRQSDDVS KETPKRSPAE QTHPSDEGSS TSSLGPWNKS FMDKQTWMER
710 720 730 740 750
GDDRLSVTLA EIVHIRSVMT KAELEGLPMD VRVKEDVEKR RVCFLCLRTR
760 770 780 790 800
FSFFGPWGIQ CKLCQRTVCA KCYTKMRIPS EHFRNVPLVL ISPSLLSSPA
810 820 830 840 850
SSSTPSPSHH AQQAHSSSTG NIMDDQFPKS LIERLLRSES DRKTRSTVGS
860 870 880 890 900
APSSPKHQRS NMSTPGISVG PGASSSSAAA TGQAVEALHD QATMSSSYSA
910 920 930 940 950
AMRPSGVHQQ QKQHYNNAMS RSMEGPRSLP VHSPAYRPLS NNSTLERKSR
960 970 980 990 1000
FSRGFNLFSS GSHLAQTQEQ KENLRGEQVT VCNDCQGLVN EITSSVKQKR
1010 1020
SSARNRTIQN LTLDLTPVWK
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_165323.3. [Q9U1K1-1]
NP_724255.1. NM_165324.2. [Q9U1K1-4]
NP_724256.2. NM_165325.3. [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_165323.3. [Q9U1K1-1 ]
NP_724255.1. NM_165324.2. [Q9U1K1-4 ]
NP_724256.2. NM_165325.3. [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.
ExpressionAtlasi Q9U1K1. differential.

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

« Hide 'large scale' publications
  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 29, 2014
This is version 112 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