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DROME:O46034

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Species (Taxon ID) Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s) No Information Provided. (synonyms: cbl (ECO:0000313 with EMBL:CAA11149.1))
Protein Name(s) CG7037-PA, isoform A (ECO:0000313 with EMBL:AAF50417.1)

Cbl protein (ECO:0000313 with EMBL:CAA11149.1) LD46082p (ECO:0000313 with EMBL:AAM49962.1)

External Links
UniProt O46034
EMBL AE003555
AY118593
AJ223175
RefSeq NP_729382.1
UniGene Dm.2332
SMR O46034
MINT MINT-312379
EnsemblMetazoa FBtr0076614
GeneID 38961
KEGG dme:Dmel_CG7037
UCSC CG7037-RA
CTD 867
FlyBase FBgn0020224
eggNOG NOG242251
GeneTree ENSGT00390000011617
KO K04707
OrthoDB EOG7M0NQX
Reactome REACT_180238
REACT_180240
REACT_180243
REACT_250163
REACT_261064
REACT_262116
GenomeRNAi 38961
NextBio 811201
Proteomes UP000000803
GO GO:0005938
GO:0005737
GO:0005634
GO:0005509
GO:0016874
GO:0001784
GO:0030971
GO:0004871
GO:0004842
GO:0008270
GO:0007298
GO:0009950
GO:0008069
GO:0006897
GO:0007173
GO:0001754
GO:0048134
GO:0007476
GO:0042059
GO:0007175
GO:0032353
GO:0006508
GO:0007465
GO:0006109
GO:0010941
GO:0042127
Gene3D 1.10.238.10
1.20.930.20
3.30.40.10
3.30.505.10
InterPro IPR024162
IPR014741
IPR003153
IPR014742
IPR024159
IPR011992
IPR000980
IPR001841
IPR013083
IPR017907
PANTHER PTHR23007
Pfam PF02262
PF02761
PF02762
SMART SM00184
SUPFAM SSF47668
SSF55550
PROSITE PS51506
PS00518
PS50089

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0055131

C3HC4-type RING finger domain binding

PMID:21340027[1]

ECO:0000314

F

Table 3 Figure 4

complete

enables

GO:0061630

ubiquitin protein ligase activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001124099
RGD:1561386
UniProtKB:Q9ULV8

F

Seeded From UniProt

complete

part_of

GO:0045121

membrane raft

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001124099
RGD:1561386
RGD:620535

C

Seeded From UniProt

complete

enables

GO:0030971

receptor tyrosine kinase binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0020224
PANTHER:PTN000544009

F

Seeded From UniProt

complete

enables

GO:0017124

SH3 domain binding

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:88279
PANTHER:PTN001124099
RGD:1561386
UniProtKB:P22681
UniProtKB:Q9ULV8

F

Seeded From UniProt

complete

involved_in

GO:0007175

negative regulation of epidermal growth factor-activated receptor activity

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000544009
UniProtKB:Q9ULV8

P

Seeded From UniProt

complete

involved_in

GO:0007165

signal transduction

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001124099
RGD:620535

P

Seeded From UniProt

complete

part_of

GO:0005886

plasma membrane

PMID:21873635[2]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN001124099
RGD:1561386
UniProtKB:P22681

C

Seeded From UniProt

complete

enables

GO:0008270

zinc ion binding

PMID:21912646[3]

ECO:0000255

match to sequence model evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

involved_in

GO:0032353

negative regulation of hormone biosynthetic process

PMID:22778134[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006109

regulation of carbohydrate metabolic process

PMID:22778134[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0042127

regulation of cell population proliferation

PMID:19306863[5]

ECO:0000316

genetic interaction evidence used in manual assertion

FB:FBgn0028734

P

Seeded From UniProt

complete

involved_in

GO:0048134

germ-line cyst formation

PMID:19306863[5]

ECO:0000316

genetic interaction evidence used in manual assertion

FB:FBgn0028734

P

Seeded From UniProt

complete

involved_in

GO:0006511

ubiquitin-dependent protein catabolic process

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

HGNC:15961

P

Seeded From UniProt

complete

enables

GO:0004842

ubiquitin-protein transferase activity

GO_REF:0000024

ECO:0000250

sequence similarity evidence used in manual assertion

HGNC:15961

F

Seeded From UniProt

complete

involved_in

GO:0042059

negative regulation of epidermal growth factor receptor signaling pathway

PMID:16844358[6]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005938

cell cortex

PMID:16844358[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0007476

imaginal disc-derived wing morphogenesis

PMID:16648592[7]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0001784

phosphotyrosine residue binding

PMID:9178769[8]

ECO:0000255

match to sequence model evidence used in manual assertion

F

Seeded From UniProt

Missing: with/from

part_of

GO:0005737

cytoplasm

PMID:9178769[8]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:1903688

positive regulation of border follicle cell migration

PMID:16054027[9]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0004842

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0004842

P

Seeded From UniProt

complete

involved_in

GO:0016567

protein ubiquitination

GO_REF:0000108

ECO:0000364

evidence based on logical inference from manual annotation used in automatic assertion

GO:0061630

P

Seeded From UniProt

complete

enables

GO:0001784

phosphotyrosine residue binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR024159

F

Seeded From UniProt

complete

enables

GO:0004842

ubiquitin-protein transferase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR024162

F

Seeded From UniProt

complete

enables

GO:0005509

calcium ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR014741

F

Seeded From UniProt

complete

involved_in

GO:0007166

cell surface receptor signaling pathway

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003153
InterPro:IPR036537

P

Seeded From UniProt

complete

involved_in

GO:0023051

regulation of signaling

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR024162

P

Seeded From UniProt

complete

enables

GO:0016874

ligase activity

GO_REF:0000038

ECO:0000323

imported automatically asserted information used in automatic assertion

UniProtKB-KW:KW-0436

F

Seeded From UniProt

complete

Notes

References

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

  1. Wang, PY & Pai, LM (2011) D-Cbl binding to Drk leads to dose-dependent down-regulation of EGFR signaling and increases receptor-ligand endocytosis. PLoS ONE 6 e17097 PubMed GONUTS page
  2. 2.0 2.1 2.2 2.3 2.4 2.5 2.6 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  3. Ying, M et al. (2011) Comprehensively surveying structure and function of RING domains from Drosophila melanogaster. PLoS ONE 6 e23863 PubMed GONUTS page
  4. 4.0 4.1 Yu, Y et al. (2012) Neuronal Cbl controls biosynthesis of insulin-like peptides in Drosophila melanogaster. Mol. Cell. Biol. 32 3610-23 PubMed GONUTS page
  5. 5.0 5.1 Epstein, AM et al. (2009) Drosophila Fragile X protein controls cellular proliferation by regulating cbl levels in the ovary. Dev. Biol. 330 83-92 PubMed GONUTS page
  6. 6.0 6.1 Pai, LM et al. (2006) Differential effects of Cbl isoforms on Egfr signaling in Drosophila. Mech. Dev. 123 450-62 PubMed GONUTS page
  7. Dworkin, I & Gibson, G (2006) Epidermal growth factor receptor and transforming growth factor-beta signaling contributes to variation for wing shape in Drosophila melanogaster. Genetics 173 1417-31 PubMed GONUTS page
  8. 8.0 8.1 Hime, GR et al. (1997) D-Cbl, the Drosophila homologue of the c-Cbl proto-oncogene, interacts with the Drosophila EGF receptor in vivo, despite lacking C-terminal adaptor binding sites. Oncogene 14 2709-19 PubMed GONUTS page
  9. Jékely, G et al. (2005) Regulators of endocytosis maintain localized receptor tyrosine kinase signaling in guided migration. Dev. Cell 9 197-207 PubMed GONUTS page