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P29829

- GBB2_DROME

UniProt

P29829 - GBB2_DROME

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Protein

Guanine nucleotide-binding protein subunit beta-2

Gene

Gbeta76C

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

Functioni

Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.

GO - Molecular functioni

  1. GTPase activity Source: FlyBase
  2. protein heterodimerization activity Source: FlyBase
  3. signal transducer activity Source: UniProtKB-KW

GO - Biological processi

  1. activation of phospholipase C activity Source: FlyBase
  2. deactivation of rhodopsin mediated signaling Source: FlyBase
  3. G-protein coupled receptor signaling pathway Source: FlyBase
  4. GTP catabolic process Source: GOC
  5. phototransduction Source: FlyBase
  6. rhodopsin mediated signaling pathway Source: FlyBase
  7. visual perception Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Sensory transduction, Vision

Enzyme and pathway databases

ReactomeiREACT_248289. Activation of G protein gated Potassium channels.
REACT_251262. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SignaLinkiP29829.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit beta-2
Gene namesi
Name:Gbeta76C
Synonyms:Gb76C, Gbe
ORF Names:CG8770
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0004623. Gbeta76C.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: FlyBase
  2. heterotrimeric G-protein complex Source: FlyBase
  3. plasma membrane Source: FlyBase
  4. rhabdomere Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 346346Guanine nucleotide-binding protein subunit beta-2PRO_0000127716Add
BLAST

Proteomic databases

PaxDbiP29829.

Expressioni

Tissue specificityi

In the Drosophila compound eye.

Gene expression databases

BgeeiP29829.

Interactioni

Subunit structurei

G proteins are composed of 3 units, alpha, beta and gamma.

Binary interactionsi

WithEntry#Exp.IntActNotes
Ggamma30AQ9NFZ32EBI-128499,EBI-2695634

Protein-protein interaction databases

BioGridi65418. 4 interactions.
IntActiP29829. 3 interactions.
MINTiMINT-938155.
STRINGi7227.FBpp0074717.

Structurei

3D structure databases

ProteinModelPortaliP29829.
SMRiP29829. Positions 21-345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati57 – 9640WD 1Add
BLAST
Repeati99 – 13840WD 2Add
BLAST
Repeati147 – 18539WD 3Add
BLAST
Repeati188 – 22740WD 4Add
BLAST
Repeati230 – 26940WD 5Add
BLAST
Repeati274 – 31340WD 6Add
BLAST
Repeati316 – 34530WD 7Add
BLAST

Sequence similaritiesi

Belongs to the WD repeat G protein beta family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiCOG2319.
GeneTreeiENSGT00760000119239.
InParanoidiP29829.
KOiK07972.
OMAiIIWDTWT.
OrthoDBiEOG71ZP1T.
PhylomeDBiP29829.

Family and domain databases

Gene3Di2.130.10.10. 1 hit.
InterProiIPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view]
PfamiPF00400. WD40. 6 hits.
[Graphical view]
PIRSFiPIRSF002394. GN-bd_beta. 1 hit.
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29829-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPKIDPETQK LYDEINGMIQ KFKDDQKSKA DCTLADKCGD MGDVPKIRFS
60 70 80 90 100
SKKILKGHIN KVNSVHFAGD SRHCVTGSLD GKLIIWDTWT ANKVQIIPLR
110 120 130 140 150
SAWVMTVAFS PSGNFVACGG MDNQCTVYDV NNRDASGVAK MVKELMGYEG
160 170 180 190 200
FLSSCRFLDD GHLITGSGDM KICHWDLEKG VKTMDFNGHA GDIAGLSLSP
210 220 230 240 250
DMKTYITGSV DKTAKLWDVR EEGHKQMFFG HDMDVSSVCY HPSGFGFASC
260 270 280 290 300
SEDQTARMYD LRADQQIAQY EPPQKNTGFT SCALSTSGRY LMCGGIEGNV
310 320 330 340
HSWDTMKQRH TGTLSGHENR ITCISLCPNG MCLASTSWDQ QVRLWL
Length:346
Mass (Da):38,336
Last modified:March 15, 2004 - v3
Checksum:iE9B22D937EC3A707
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161V → E in AAA73103. (PubMed:1910788)Curated
Sequence conflicti136 – 1361S → P in AAA73103. (PubMed:1910788)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76593 mRNA. Translation: AAA73103.1.
AE014296 Genomic DNA. Translation: AAF49124.1.
AY118886 mRNA. Translation: AAM50746.1.
PIRiJU0269. RGFFB.
RefSeqiNP_523720.2. NM_078996.3.
UniGeneiDm.9760.

Genome annotation databases

EnsemblMetazoaiFBtr0074949; FBpp0074717; FBgn0004623.
GeneIDi40148.
KEGGidme:Dmel_CG8770.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M76593 mRNA. Translation: AAA73103.1 .
AE014296 Genomic DNA. Translation: AAF49124.1 .
AY118886 mRNA. Translation: AAM50746.1 .
PIRi JU0269. RGFFB.
RefSeqi NP_523720.2. NM_078996.3.
UniGenei Dm.9760.

3D structure databases

ProteinModelPortali P29829.
SMRi P29829. Positions 21-345.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 65418. 4 interactions.
IntActi P29829. 3 interactions.
MINTi MINT-938155.
STRINGi 7227.FBpp0074717.

Proteomic databases

PaxDbi P29829.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0074949 ; FBpp0074717 ; FBgn0004623 .
GeneIDi 40148.
KEGGi dme:Dmel_CG8770.

Organism-specific databases

CTDi 40148.
FlyBasei FBgn0004623. Gbeta76C.

Phylogenomic databases

eggNOGi COG2319.
GeneTreei ENSGT00760000119239.
InParanoidi P29829.
KOi K07972.
OMAi IIWDTWT.
OrthoDBi EOG71ZP1T.
PhylomeDBi P29829.

Enzyme and pathway databases

Reactomei REACT_248289. Activation of G protein gated Potassium channels.
REACT_251262. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SignaLinki P29829.

Miscellaneous databases

ChiTaRSi Gbeta76C. fly.
GenomeRNAii 40148.
NextBioi 817248.

Gene expression databases

Bgeei P29829.

Family and domain databases

Gene3Di 2.130.10.10. 1 hit.
InterProi IPR020472. G-protein_beta_WD-40_rep.
IPR001632. Gprotein_B.
IPR016346. Guanine_nucleotide-bd_bsu.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR019775. WD40_repeat_CS.
IPR017986. WD40_repeat_dom.
[Graphical view ]
Pfami PF00400. WD40. 6 hits.
[Graphical view ]
PIRSFi PIRSF002394. GN-bd_beta. 1 hit.
PRINTSi PR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTi SM00320. WD40. 7 hits.
[Graphical view ]
SUPFAMi SSF50978. SSF50978. 1 hit.
PROSITEi PS00678. WD_REPEATS_1. 1 hit.
PS50082. WD_REPEATS_2. 4 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A G beta protein in the Drosophila compound eye is different from that in the brain."
    Yarfitz S., Niemi G.A., McConnell J.L., Fitch C.L., Hurley J.B.
    Neuron 7:429-438(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Eye.
  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.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: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Head.

Entry informationi

Entry nameiGBB2_DROME
AccessioniPrimary (citable) accession number: P29829
Secondary accession number(s): Q9VW29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: March 15, 2004
Last modified: November 26, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3