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Protein

Guanine nucleotide-binding protein subunit beta-1

Gene

Gbeta13F

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: 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

GO - Biological processi

  • actin filament organization Source: FlyBase
  • apical protein localization Source: FlyBase
  • asymmetric neuroblast division Source: FlyBase
  • cell adhesion involved in heart morphogenesis Source: FlyBase
  • convergent extension involved in gastrulation Source: FlyBase
  • establishment or maintenance of cytoskeleton polarity involved in gastrulation Source: FlyBase
  • G-protein coupled receptor signaling pathway Source: FlyBase
  • mesectoderm development Source: FlyBase
  • regulation of gastrulation Source: FlyBase
  • regulation of myosin II filament organization Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Transducer

Enzyme and pathway databases

ReactomeiR-DME-1296041. Activation of G protein gated Potassium channels.
R-DME-418555. G alpha (s) signalling events.
R-DME-418594. G alpha (i) signalling events.
R-DME-418597. G alpha (z) signalling events.
R-DME-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
R-DME-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SignaLinkiP26308.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanine nucleotide-binding protein subunit beta-1
Gene namesi
Name:Gbeta13F
Synonyms:Gb13F
ORF Names:CG10545
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome X

Organism-specific databases

FlyBaseiFBgn0001105. Gbeta13F.

Subcellular locationi

GO - Cellular componenti

  • heterotrimeric G-protein complex Source: FlyBase
  • microtubule associated complex Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 340340Guanine nucleotide-binding protein subunit beta-1PRO_0000127715Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei29 – 291Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP26308.
PRIDEiP26308.

PTM databases

iPTMnetiP26308.

Expressioni

Tissue specificityi

In adults, expression is higher in the head than in the body.1 Publication

Developmental stagei

Expressed throughout development.1 Publication

Gene expression databases

BgeeiP26308.
ExpressionAtlasiP26308. differential.
GenevisibleiP26308. DM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi58892. 7 interactions.
DIPiDIP-18432N.
IntActiP26308. 1 interaction.
MINTiMINT-1016369.
STRINGi7227.FBpp0089182.

Structurei

3D structure databases

ProteinModelPortaliP26308.
SMRiP26308. Positions 3-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati53 – 8331WD 1Add
BLAST
Repeati95 – 12531WD 2Add
BLAST
Repeati141 – 17030WD 3Add
BLAST
Repeati182 – 21231WD 4Add
BLAST
Repeati224 – 25431WD 5Add
BLAST
Repeati268 – 29831WD 6Add
BLAST
Repeati310 – 34031WD 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

eggNOGiKOG0286. Eukaryota.
ENOG410XQUX. LUCA.
GeneTreeiENSGT00760000119239.
InParanoidiP26308.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
PhylomeDBiP26308.

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]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P26308-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNELDSLRQE AESLKNAIRD ARKAACDTSL LQAATSLEPI GRIQMRTRRT
60 70 80 90 100
LRGHLAKIYA MHWGNDSRNL VSASQDGKLI VWDSHTTNKV HAIPLRSSWV
110 120 130 140 150
MTCAYAPSGS YVACGGLDNM CSIYNLKTRE GNVRVSRELP GHGGYLSCCR
160 170 180 190 200
FLDDNQIVTS SGDMSCGLWD IETGLQVTSF LGHTGDVMAL SLAPQCKTFV
210 220 230 240 250
SGACDASAKL WDIREGVCKQ TFPGHESDIN AVTFFPNGQA FATGSDDATC
260 270 280 290 300
RLFDIRADQE LAMYSHDNII CGITSVAFSK SGRLLLAGYD DFNCNVWDTM
310 320 330 340
KAERSGILAG HDNRVSCLGV TENGMAVATG SWDSFLRVWN
Length:340
Mass (Da):37,133
Last modified:May 1, 1992 - v1
Checksum:i5A4B70DCB0A1C32C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22567 Genomic DNA. Translation: AAB59247.1.
AE014298 Genomic DNA. Translation: AAF48530.1.
AY058566 mRNA. Translation: AAL13795.1.
PIRiA40489. RGFFBH.
RefSeqiNP_001303567.1. NM_001316638.1.
NP_525090.1. NM_080351.6.
NP_727907.1. NM_167469.3.
NP_996459.1. NM_206736.2.
NP_996460.1. NM_206737.2.
NP_996461.1. NM_206738.2.
NP_996462.1. NM_206739.2.
UniGeneiDm.7041.

Genome annotation databases

EnsemblMetazoaiFBtr0074106; FBpp0073920; FBgn0001105.
FBtr0074107; FBpp0073921; FBgn0001105.
FBtr0074108; FBpp0089182; FBgn0001105.
FBtr0074110; FBpp0089184; FBgn0001105.
FBtr0074111; FBpp0089185; FBgn0001105.
FBtr0331597; FBpp0303987; FBgn0001105.
FBtr0346794; FBpp0312372; FBgn0001105.
GeneIDi32544.
KEGGidme:Dmel_CG10545.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M22567 Genomic DNA. Translation: AAB59247.1.
AE014298 Genomic DNA. Translation: AAF48530.1.
AY058566 mRNA. Translation: AAL13795.1.
PIRiA40489. RGFFBH.
RefSeqiNP_001303567.1. NM_001316638.1.
NP_525090.1. NM_080351.6.
NP_727907.1. NM_167469.3.
NP_996459.1. NM_206736.2.
NP_996460.1. NM_206737.2.
NP_996461.1. NM_206738.2.
NP_996462.1. NM_206739.2.
UniGeneiDm.7041.

3D structure databases

ProteinModelPortaliP26308.
SMRiP26308. Positions 3-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi58892. 7 interactions.
DIPiDIP-18432N.
IntActiP26308. 1 interaction.
MINTiMINT-1016369.
STRINGi7227.FBpp0089182.

PTM databases

iPTMnetiP26308.

Proteomic databases

PaxDbiP26308.
PRIDEiP26308.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0074106; FBpp0073920; FBgn0001105.
FBtr0074107; FBpp0073921; FBgn0001105.
FBtr0074108; FBpp0089182; FBgn0001105.
FBtr0074110; FBpp0089184; FBgn0001105.
FBtr0074111; FBpp0089185; FBgn0001105.
FBtr0331597; FBpp0303987; FBgn0001105.
FBtr0346794; FBpp0312372; FBgn0001105.
GeneIDi32544.
KEGGidme:Dmel_CG10545.

Organism-specific databases

CTDi32544.
FlyBaseiFBgn0001105. Gbeta13F.

Phylogenomic databases

eggNOGiKOG0286. Eukaryota.
ENOG410XQUX. LUCA.
GeneTreeiENSGT00760000119239.
InParanoidiP26308.
KOiK04536.
OMAiRIVMRPR.
OrthoDBiEOG7GN2N5.
PhylomeDBiP26308.

Enzyme and pathway databases

ReactomeiR-DME-1296041. Activation of G protein gated Potassium channels.
R-DME-418555. G alpha (s) signalling events.
R-DME-418594. G alpha (i) signalling events.
R-DME-418597. G alpha (z) signalling events.
R-DME-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.
R-DME-997272. Inhibition of voltage gated Ca2+ channels via Gbeta/gamma subunits.
SignaLinkiP26308.

Miscellaneous databases

ChiTaRSiGbeta13F. fly.
GenomeRNAii32544.
PROiP26308.

Gene expression databases

BgeeiP26308.
ExpressionAtlasiP26308. differential.
GenevisibleiP26308. DM.

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]
PANTHERiPTHR19850. PTHR19850. 1 hit.
PfamiPF00400. WD40. 6 hits.
[Graphical view]
PRINTSiPR00319. GPROTEINB.
PR00320. GPROTEINBRPT.
SMARTiSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF50978. SSF50978. 1 hit.
PROSITEiPS00678. WD_REPEATS_1. 3 hits.
PS50082. WD_REPEATS_2. 6 hits.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of a Drosophila melanogaster guanine nucleotide regulatory protein beta-subunit gene and characterization of its expression during development."
    Yarfitz S., Provost N.M., Hurley J.B.
    Proc. Natl. Acad. Sci. U.S.A. 85:7134-7138(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: Canton-S.
  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: Embryo.
  5. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-29, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiGBB1_DROME
AccessioniPrimary (citable) accession number: P26308
Secondary accession number(s): Q9VXM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: May 1, 1992
Last modified: July 6, 2016
This is version 143 of the entry and version 1 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

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.