Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein
Submitted name:

FI01544p

Gene

Rab1

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

Functioni

GO - Molecular functioni

  • GTPase activity Source: FlyBase
  • GTP binding Source: InterPro

GO - Biological processi

  • actin filament organization Source: FlyBase
  • anterograde axonal transport Source: FlyBase
  • carbohydrate homeostasis Source: FlyBase
  • cell adhesion Source: FlyBase
  • ER to Golgi vesicle-mediated transport Source: FlyBase
  • intracellular protein transport Source: InterPro
  • nucleocytoplasmic transport Source: InterPro
  • positive regulation of dendrite morphogenesis Source: FlyBase
  • positive regulation of insulin secretion Source: FlyBase
  • protein secretion Source: FlyBase
  • Rab protein signal transduction Source: FlyBase
  • regulation of cell migration Source: FlyBase
  • regulation of cell shape Source: FlyBase
  • vesicle-mediated transport Source: FlyBase
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-DME-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-DME-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-DME-6807878. COPI-mediated anterograde transport.
R-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Names & Taxonomyi

Protein namesi
Submitted name:
FI01544pImported
Submitted name:
Rab1Imported
Gene namesi
Name:Rab1Imported
Synonyms:Rab1-RAImported
ORF Names:CG3320Imported, Dmel_CG3320Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0016700. Rab1.

Subcellular locationi

GO - Cellular componenti

  • axon cytoplasm Source: GOC
  • cytoplasm Source: FlyBase
  • lipid particle Source: FlyBase
  • membrane Source: InterPro
  • neuronal cell body Source: FlyBase
  • vesicle Source: FlyBase
Complete GO annotation...

Interactioni

Protein-protein interaction databases

DIPiDIP-51950N.
IntActiO18332. 3 interactions.
MINTiMINT-990386.
STRINGi7227.FBpp0083503.

Structurei

3D structure databases

SMRiO18332. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
GeneTreeiENSGT00840000129698.
HOGENOMiHOG000208217.
KOiK07874.
OMAiKERMGNT.
OrthoDBiEOG7VB2H4.
PhylomeDBiO18332.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.

Sequencei

Sequence statusi: Complete.

O18332-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSVNPEYDY LFKLLLIGDS GVGKSCLLLR FADDTYTESY ISTIGVDFKI
60 70 80 90 100
RTIELDGKTI KLQIWDTAGQ ERFRTITSSY YRGAHGIIVV YDCTDQESFN
110 120 130 140 150
NVKQWLEEIE RYACENVNKL LVGNKSDLTT KKVVDHTTAA EYAAQLGIPF
160 170 180 190 200
LETSAKSATN VEQAFMTMAA EIKNRVGPPS SATDNASKVK IDQGRPVENT

KSGCC
Length:205
Mass (Da):22,763
Last modified:January 1, 1998 - v1
Checksum:i9CE2691205FAE343
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF55873.1.
BT046126 mRNA. Translation: ACI46514.1.
D84312 mRNA. Translation: BAA21705.1.
RefSeqiNP_732610.1. NM_169953.3.
UniGeneiDm.2386.

Genome annotation databases

EnsemblMetazoaiFBtr0084104; FBpp0083503; FBgn0016700.
GeneIDi42524.
KEGGidme:Dmel_CG3320.
UCSCiCG3320-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAF55873.1.
BT046126 mRNA. Translation: ACI46514.1.
D84312 mRNA. Translation: BAA21705.1.
RefSeqiNP_732610.1. NM_169953.3.
UniGeneiDm.2386.

3D structure databases

SMRiO18332. Positions 6-176.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-51950N.
IntActiO18332. 3 interactions.
MINTiMINT-990386.
STRINGi7227.FBpp0083503.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0084104; FBpp0083503; FBgn0016700.
GeneIDi42524.
KEGGidme:Dmel_CG3320.
UCSCiCG3320-RA. d. melanogaster.

Organism-specific databases

CTDi42524.
FlyBaseiFBgn0016700. Rab1.

Phylogenomic databases

eggNOGiKOG0084. Eukaryota.
ENOG410XQN5. LUCA.
GeneTreeiENSGT00840000129698.
HOGENOMiHOG000208217.
KOiK07874.
OMAiKERMGNT.
OrthoDBiEOG7VB2H4.
PhylomeDBiO18332.

Enzyme and pathway databases

ReactomeiR-DME-162658. Golgi Cisternae Pericentriolar Stack Reorganization.
R-DME-204005. COPII (Coat Protein 2) Mediated Vesicle Transport.
R-DME-6807878. COPI-mediated anterograde transport.
R-DME-6811434. COPI-dependent Golgi-to-ER retrograde traffic.

Miscellaneous databases

GenomeRNAii42524.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
[Graphical view]
PfamiPF00071. Ras. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rab proteins of Drosophila melanogaster: novel members of the Rab-protein family."
    Satoh A.K., Tokunaga F., Ozaki K.
    FEBS Lett. 404:65-69(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Oregon RImported.
    Tissue: HeadImported.
  2. "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., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Gabor G.L., 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., 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., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J., 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., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., 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., WoodageT, 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., 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: BerkeleyImported.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  5. "The transposable elements of the Drosophila melanogaster euchromatin: a genomics perspective."
    Kaminker J.S., Bergman C.M., Kronmiller B., Carlson J., Svirskas R., Patel S., Frise E., Wheeler D.A., Lewis S.E., Rubin G.M., Ashburner M., Celniker S.E.
    Genome Biol. 3:RESEARCH0084.1-RESEARCH0084.20(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  6. "Heterochromatic sequences in a Drosophila whole-genome shotgun assembly."
    Hoskins R.A., Smith C.D., Carlson J.W., Carvalho A.B., Halpern A., Kaminker J.S., Kennedy C., Mungall C.J., Sullivan B.A., Sutton G.G., Yasuhara J.C., Wakimoto B.T., Myers E.W., Celniker S.E., Rubin G.M., Karpen G.H.
    Genome Biol. 3:RESEARCH0085-RESEARCH0085(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  7. "Combined evidence annotation of transposable elements in genome sequences."
    Quesneville H., Bergman C.M., Andrieu O., Autard D., Nouaud D., Ashburner M., Anxolabehere D.
    PLoS Comput. Biol. 1:166-175(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  8. "Drosophila melanogaster release 4 sequence."
    Berkeley Drosophila Genome Project
    Celniker S., Carlson J., Wan K., Pfeiffer B., Frise E., George R., Hoskins R., Stapleton M., Pacleb J., Park S., Svirskas R., Smith E., Yu C., Rubin G.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  9. Celniker S., Carlson J., Wan K., Frise E., Hoskins R., Park S., Svirskas R., Rubin G.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  10. "The Release 5.1 annotation of Drosophila melanogaster heterochromatin."
    Smith C.D., Shu S., Mungall C.J., Karpen G.H.
    Science 316:1586-1591(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  12. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  13. FlyBase
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO18332_DROME
AccessioniPrimary (citable) accession number: O18332
Entry historyi
Integrated into UniProtKB/TrEMBL: January 1, 1998
Last sequence update: January 1, 1998
Last modified: June 8, 2016
This is version 136 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.