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DROME:SING

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) sn
Protein Name(s) Protein singed
External Links
UniProt Q24524
EMBL X17549
X17550
AE014298
RefSeq NP_001162697.1
NP_511076.3
NP_727226.1
NP_727227.1
UniGene Dm.7274
ProteinModelPortal Q24524
SMR Q24524
BioGrid 58189
MINT MINT-295848
STRING 7227.FBpp0071056
PaxDb Q24524
PRIDE Q24524
EnsemblMetazoa FBtr0071101
FBtr0071102
FBtr0301676
FBtr0301677
FBtr0301678
FBtr0301679
GeneID 31717
KEGG dme:Dmel_CG32858
UCSC CG32858-RA
CTD 31717
FlyBase FBgn0003447
eggNOG NOG85029
GeneTree ENSGT00530000063373
InParanoid Q24524
KO K17455
OMA HRWALRT
OrthoDB EOG761BV4
PhylomeDB Q24524
GenomeRNAi 31717
NextBio 774985
PRO PR:Q24524
Proteomes UP000000803
Bgee Q24524
ExpressionAtlas Q24524
GO GO:0015629
GO:0005737
GO:0043005
GO:0043025
GO:0003779
GO:0051015
GO:0030036
GO:0051017
GO:0007015
GO:0048800
GO:0008407
GO:0035017
GO:0016358
GO:0009913
GO:0007163
GO:0046847
GO:0035099
GO:0035317
GO:0030034
GO:0048812
GO:0048477
GO:0042060
InterPro IPR008999
IPR010431
IPR022768
IPR024703
PANTHER PTHR10551
Pfam PF06268
PIRSF PIRSF005682
SUPFAM SSF50405

Annotations

Qualifier GO ID GO term name Reference Evidence Code with/from Aspect Notes Status

Colocalizes with

GO:0034399

nuclear periphery

PMID:25808493[1]

IDA: Inferred from Direct Assay

C

Figure 1: Live imaging of late stage follicles reveals GFP-Fascin, is in the nucleus during S10B-S12 (F-H) and at the nuclear periphery during S13 (I, J).

complete
CACAO 10877

GO:0003779

actin binding

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q16658

F

Seeded From UniProt

complete

GO:0003779

actin binding

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0009

F

Seeded From UniProt

complete

GO:0003779

actin binding

PMID:10908588[2]

ISS: Inferred from Sequence or Structural Similarity

F

Seeded From UniProt

Missing: with/from

GO:0005737

cytoplasm

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

GO:0005737

cytoplasm

PMID:8163553[3]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0005856

cytoskeleton

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

GO:0005856

cytoskeleton

GO_REF:0000039

IEA: Inferred from Electronic Annotation

UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

GO:0007015

actin filament organization

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010431

P

Seeded From UniProt

complete

GO:0007015

actin filament organization

PMID:11139280[4]

TAS: Traceable Author Statement

P

Seeded From UniProt

complete

GO:0007163

establishment or maintenance of cell polarity

PMID:19592575[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0007275

multicellular organismal development

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0217

P

Seeded From UniProt

complete

GO:0008407

chaeta morphogenesis

PMID:12975350[6]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0009913

epidermal cell differentiation

PMID:16933974[7]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0015629

actin cytoskeleton

PMID:19592575[5]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0016358

dendrite development

PMID:22764047[8]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0030034

microvillar actin bundle assembly

PMID:15226373[9]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0030036

actin cytoskeleton organization

PMID:19592575[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0030154

cell differentiation

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0221

P

Seeded From UniProt

complete

GO:0030674

protein binding, bridging

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR022768
InterPro:IPR024703

F

Seeded From UniProt

complete

GO:0035017

cuticle pattern formation

PMID:16933974[7]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0035099

hemocyte migration

PMID:19592575[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0035317

imaginal disc-derived wing hair organization

PMID:15917291[10]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0042060

wound healing

PMID:19592575[5]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0043005

neuron projection

PMID:22764047[8]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0043025

neuronal cell body

PMID:22764047[8]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

GO:0046847

filopodium assembly

PMID:22564415[11]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0048477

oogenesis

GO_REF:0000037

IEA: Inferred from Electronic Annotation

UniProtKB-KW:KW-0896

P

Seeded From UniProt

complete

GO:0048477

oogenesis

PMID:3089870[12]

TAS: Traceable Author Statement

P

Seeded From UniProt

complete

GO:0048800

antennal morphogenesis

PMID:12070612[13]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0048812

neuron projection morphogenesis

PMID:16928862[14]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0051015

actin filament binding

GO_REF:0000002

IEA: Inferred from Electronic Annotation

InterPro:IPR010431
InterPro:IPR022768
InterPro:IPR024703

F

Seeded From UniProt

complete

GO:0051015

actin filament binding

GO_REF:0000024

ISS: Inferred from Sequence or Structural Similarity

UniProtKB:Q16658

F

Seeded From UniProt

complete

GO:0051017

actin filament bundle assembly

PMID:14517310[15]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0051017

actin filament bundle assembly

PMID:15917291[10]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

GO:0051017

actin filament bundle assembly

PMID:22564415[11]

IMP: Inferred from Mutant Phenotype

P

Seeded From UniProt

complete

colocalizes_with

GO:0031941

filamentous actin

PMID:16933974[7]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

colocalizes_with

GO:0034399

nuclear periphery

PMID:25808493[1]

IDA: Inferred from Direct Assay

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. 1.0 1.1 Groen, CM et al. (2015) Prostaglandins regulate nuclear localization of Fascin and its function in nucleolar architecture. Mol. Biol. Cell 26 1901-17 PubMed GONUTS page
  2. Goldstein, LS & Gunawardena, S (2000) Flying through the drosophila cytoskeletal genome. J. Cell Biol. 150 F63-8 PubMed GONUTS page
  3. Cant, K et al. (1994) Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. J. Cell Biol. 125 369-80 PubMed GONUTS page
  4. Buszczak, M & Cooley, L (2000) Eggs to die for: cell death during Drosophila oogenesis. Cell Death Differ. 7 1071-4 PubMed GONUTS page
  5. 5.0 5.1 5.2 5.3 5.4 Zanet, J et al. (2009) Fascin is required for blood cell migration during Drosophila embryogenesis. Development 136 2557-65 PubMed GONUTS page
  6. Guild, GM et al. (2003) Long continuous actin bundles in Drosophila bristles are constructed by overlapping short filaments. J. Cell Biol. 162 1069-77 PubMed GONUTS page
  7. 7.0 7.1 7.2 Chanut-Delalande, H et al. (2006) Shavenbaby couples patterning to epidermal cell shape control. PLoS Biol. 4 e290 PubMed GONUTS page
  8. 8.0 8.1 8.2 Nagel, J et al. (2012) Fascin controls neuronal class-specific dendrite arbor morphology. Development 139 2999-3009 PubMed GONUTS page
  9. Tilney, LG et al. (2004) Microvilli appear to represent the first step in actin bundle formation in Drosophila bristles. J. Cell. Sci. 117 3531-8 PubMed GONUTS page
  10. 10.0 10.1 Guild, GM et al. (2005) Actin filament bundles in Drosophila wing hairs: hairs and bristles use different strategies for assembly. Mol. Biol. Cell 16 3620-31 PubMed GONUTS page
  11. 11.0 11.1 Zanet, J et al. (2012) Fascin promotes filopodia formation independent of its role in actin bundling. J. Cell Biol. 197 477-86 PubMed GONUTS page
  12. Perrimon, N et al. (1986) X-linked female-sterile loci in Drosophila melanogaster. Genetics 113 695-712 PubMed GONUTS page
  13. He, B & Adler, PN (2002) The genetic control of arista lateral morphogenesis in Drosophila. Dev. Genes Evol. 212 218-29 PubMed GONUTS page
  14. Kraft, R et al. (2006) Phenotypes of Drosophila brain neurons in primary culture reveal a role for fascin in neurite shape and trajectory. J. Neurosci. 26 8734-47 PubMed GONUTS page
  15. Tilney, LG et al. (2003) Actin filament turnover regulated by cross-linking accounts for the size, shape, location, and number of actin bundles in Drosophila bristles. Mol. Biol. Cell 14 3953-66 PubMed GONUTS page