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DROME:Q9VB13

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) No Information Provided.
Protein Name(s) Microtubule-associated protein (ECO:0000256 with RuleBase:RU000686)
External Links
UniProt Q9VB13
EMBL AE014297
AY032977
AY102697
RefSeq NP_001263017.1
NP_651575.1
UniGene Dm.20268
EnsemblMetazoa FBtr0085197
FBtr0331366
GeneID 326116
KEGG dme:Dmel_CG31057
UCSC CG31057-RA
CTD 326116
FlyBase FBgn0266579
eggNOG NOG148882
GeneTree ENSGT00530000063491
KO K04380
OMA KDYLKNV
OrthoDB EOG7M98H1
PhylomeDB Q9VB13
Reactome REACT_236010
GenomeRNAi 326116
NextBio 847137
PRO PR:Q9VB13
Proteomes UP000000803
GO GO:0005737
GO:0005874
InterPro IPR027324
IPR001084
PANTHER PTHR11501
Pfam PF00418
PROSITE PS00229
PS51491

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

part_of

GO:0043005

neuron projection

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:97175
PANTHER:PTN000161190
RGD:3044
RGD:69329
WB:WBGene00004212

C

Seeded From UniProt

complete

involved_in

GO:0031175

neuron projection development

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000161190
UniProtKB:P11137

P

Seeded From UniProt

complete

enables

GO:0008017

microtubule binding

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0266579
MGI:MGI:97175
MGI:MGI:97178
MGI:MGI:97180
PANTHER:PTN000161190
RGD:3044
RGD:69329
UniProtKB:P10636
WB:WBGene00004212

F

Seeded From UniProt

complete

involved_in

GO:0000226

microtubule cytoskeleton organization

PMID:21873635[1]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0266579
MGI:MGI:97175
MGI:MGI:97178
MGI:MGI:97180
PANTHER:PTN000161190
UniProtKB:P10636

P

Seeded From UniProt

complete

part_of

GO:0005875

microtubule associated complex

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

NCBI_gi:1698712

C

Seeded From UniProt

complete

enables

GO:0008017

microtubule binding

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

NCBI_gi:517394

F

Seeded From UniProt

complete

enables

GO:0008017

microtubule binding

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

NCBI_gi:1698712

F

Seeded From UniProt

complete

involved_in

GO:0000226

microtubule cytoskeleton organization

PMID:24909306[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:1901215

negative regulation of neuron death

PMID:24909306[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0061541

rhabdomere morphogenesis

PMID:24909306[3]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0030424

axon

PMID:20881132[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0030425

dendrite

PMID:20881132[4]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

colocalizes_with

GO:0005881

cytoplasmic microtubule

PMID:20193038[5]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0007017

microtubule-based process

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

P

Seeded From UniProt

Missing: with/from

enables

GO:0008017

microtubule binding

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

part_of

GO:0005875

microtubule associated complex

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

C

Seeded From UniProt

Missing: with/from

part_of

GO:0005875

microtubule associated complex

PMID:10908588[2]

ECO:0000250

sequence similarity evidence used in manual assertion

NCBI_gi:517394

C

Seeded From UniProt

complete

enables

GO:0015631

tubulin binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR001084

F

Seeded From UniProt

complete

part_of

GO:0005874

microtubule

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0493

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0206

C

Seeded From UniProt

complete

part_of

GO:0005737

cytoplasm

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0963

C

Seeded From UniProt

complete

part_of

GO:0005856

cytoskeleton

GO_REF:0000040

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-SubCell:SL-0090

C

Seeded From UniProt

complete

Notes

References

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

  1. ↑ 1.0 1.1 1.2 1.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  2. ↑ 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Goldstein, LS & Gunawardena, S (2000) Flying through the drosophila cytoskeletal genome. J. Cell Biol. 150 F63-8 PubMed GONUTS page
  3. ↑ 3.0 3.1 3.2 Bolkan, BJ & Kretzschmar, D (2014) Loss of Tau results in defects in photoreceptor development and progressive neuronal degeneration in Drosophila. Dev Neurobiol 74 1210-25 PubMed GONUTS page
  4. ↑ 4.0 4.1 Lin, CH et al. (2010) LRRK2 G2019S mutation induces dendrite degeneration through mislocalization and phosphorylation of tau by recruiting autoactivated GSK3ß. J. Neurosci. 30 13138-49 PubMed GONUTS page
  5. ↑ Feuillette, S et al. (2010) Drosophila models of human tauopathies indicate that Tau protein toxicity in vivo is mediated by soluble cytosolic phosphorylated forms of the protein. J. Neurochem. 113 895-903 PubMed GONUTS page