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Protein

Protein gustavus

Gene

gus

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

Functioni

Involved in the localization of vas to the posterior pole of the oocyte. Required maternally in the germ line for efficient primordial germ cell formation.2 Publications

GO - Biological processi

  • cuticle pattern formation Source: UniProtKB
  • dorsal appendage formation Source: FlyBase
  • germ cell development Source: UniProtKB
  • intracellular signal transduction Source: InterPro
  • oocyte anterior/posterior axis specification Source: FlyBase
  • pole cell migration Source: UniProtKB
  • pole plasm assembly Source: UniProtKB
  • positive regulation of protein catabolic process Source: FlyBase
  • protein localization Source: UniProtKB
  • wing disc morphogenesis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Enzyme and pathway databases

ReactomeiR-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein gustavusImported
Gene namesi
Name:gus
ORF Names:CG2944
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2R

Organism-specific databases

FlyBaseiFBgn0026238. gus.

Subcellular locationi

  • Cytoplasm 2 Publications
  • Nucleus 2 Publications

  • Note: Component of the cytoplasmic ribonucleoprotein (RNP) bodies which concentrate at the perinuclear region of the nurse cell and in punctate aggregates throughout the cytoplasm. Some cortical enrichment of these aggregates is also observed. At stage 7, accumulates in the anterior cytoplasm of the oocyte, whereas during stage 10 accumulates at the posterior pole. This posterior distribution is not maintained in later developmental stages.2 Publications

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • Cul5-RING ubiquitin ligase complex Source: FlyBase
  • cytoplasm Source: UniProtKB
  • elongin complex Source: UniProtKB
  • nucleus Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
  • pole plasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Homozygous females produce defective eggs, which desiccate and collapse soon after egg laying, or embryos, which hatch very rarely. Mutants exhibit wing morphology defects, including blistering, formation of ectopic vein material, and loss of material at the margin.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi131 – 1311Y → A: Does not affect binding to Elongin BC complex. Abolishes interaction with vas. 1 Publication
Mutagenesisi147 – 1471G → Y: Does not affect binding to Elongin BC complex. Abolishes interaction with vas. 1 Publication
Mutagenesisi148 – 1481R → W: Does not affect binding to Elongin BC complex. Abolishes interaction with vas. 1 Publication
Mutagenesisi187 – 1871E → A: Does not affect binding to Elongin BC complex or vas. 1 Publication
Mutagenesisi204 – 2041R → S: Does not affect binding to Elongin BC complex or vas. 1 Publication
Mutagenesisi219 – 2191W → L: Does not affect binding to Elongin BC complex. Decreases interaction with vas. 3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 279279Protein gustavusPRO_0000422158Add
BLAST

Proteomic databases

PaxDbiA1Z6E0.
PRIDEiA1Z6E0.

Expressioni

Tissue specificityi

Expressed in ovaries, primarily in nurse cells and oocytes (at protein level).2 Publications

Developmental stagei

Expressed during oogenesis, in early embryos (0 to 4 hours) and in fertile adult females (at protein level).2 Publications

Gene expression databases

BgeeiA1Z6E0.
GenevisibleiA1Z6E0. DM.

Interactioni

Subunit structurei

Interacts (via B30.2/SPRY domain) with vas; this interaction may be necessary for the transport of vas to the posterior pole of the oocyte. Interacts with Cul-5. May associate with the Elongin BC complex composed of Elongin-B and Elongin-C.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
stumpsO967573EBI-75338,EBI-74922
vasP090525EBI-75338,EBI-134067

Protein-protein interaction databases

BioGridi61396. 47 interactions.
IntActiA1Z6E0. 35 interactions.
STRINGi7227.FBpp0301582.

Structurei

Secondary structure

1
279
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi37 – 448Combined sources
Helixi50 – 556Combined sources
Beta strandi57 – 637Combined sources
Beta strandi67 – 704Combined sources
Beta strandi73 – 797Combined sources
Beta strandi85 – 928Combined sources
Beta strandi97 – 1059Combined sources
Helixi108 – 1103Combined sources
Beta strandi116 – 1205Combined sources
Beta strandi126 – 1316Combined sources
Beta strandi141 – 1455Combined sources
Turni146 – 1494Combined sources
Beta strandi150 – 1545Combined sources
Turni155 – 1573Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi177 – 1848Combined sources
Turni185 – 1884Combined sources
Beta strandi189 – 1946Combined sources
Beta strandi197 – 2037Combined sources
Beta strandi211 – 2177Combined sources
Beta strandi223 – 23210Combined sources
Helixi239 – 2479Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FNJX-ray1.80A27-251[»]
2IHSX-ray2.20A/B27-232[»]
ProteinModelPortaliA1Z6E0.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA1Z6E0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 233198B30.2/SPRYPROSITE-ProRule annotationAdd
BLAST
Domaini234 – 27946SOCS boxPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni236 – 27944Involved in binding to the Elongin BC complex1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the SPSB family.Curated
Contains 1 B30.2/SPRY domain.PROSITE-ProRule annotation
Contains 1 SOCS box domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
InParanoidiA1Z6E0.
KOiK10343.
OrthoDBiEOG72C513.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1Z6E0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQKISGGVK TVSRNDSQST FKPIIPRELQ ADFVKPARID ILLDMPPASR
60 70 80 90 100
DLQLKHSWNS EDRSLNIFVK EDDKLTFHRH PVAQSTDCIR GKVGLTKGLH
110 120 130 140 150
IWEIYWPTRQ RGTHAVVGVC TADAPLHSVG YQSLVGSTEQ SWGWDLGRNK
160 170 180 190 200
LYHDSKNCAG VTYPAILKND EAFLVPDKFL VALDMDEGTL SFIVDQQYLG
210 220 230 240 250
IAFRGLRGKK LYPIVSAVWG HCEITMRYIG GLDPEPLPLM DLCRRTIRQK
260 270
IGRTNLEEHI QQLQLPLSMK TYLLYKNRR
Length:279
Mass (Da):31,713
Last modified:March 16, 2016 - v2
Checksum:iDCA657FEEA83D785
GO

Sequence cautioni

The sequence AAM50263.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ACU12389.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ACX32987.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence ADZ74173.1 differs from that shown. Reason: Frameshift at position 210. Curated
The sequence ADZ74173.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57346.2.
AE013599 Genomic DNA. Translation: AAF57347.3.
AE013599 Genomic DNA. Translation: AAG22337.2.
AE013599 Genomic DNA. Translation: AAM68372.1.
AE013599 Genomic DNA. Translation: AAM68373.2.
AE013599 Genomic DNA. Translation: AAM68374.2.
AY119609 mRNA. Translation: AAM50263.1. Different initiation.
BT089043 mRNA. Translation: ACU12389.1. Different initiation.
BT099916 mRNA. Translation: ACX32987.1. Different initiation.
BT126146 mRNA. Translation: ADZ74173.1. Sequence problems.
RefSeqiNP_001246140.1. NM_001259211.2.
NP_610158.3. NM_136314.4.
NP_724398.2. NM_165418.3.
NP_724399.2. NM_165419.3.
NP_724400.2. NM_165420.3.
NP_724401.2. NM_165421.3.
NP_724402.2. NM_165422.3.
UniGeneiDm.7323.

Genome annotation databases

GeneIDi35478.
KEGGidme:Dmel_CG2944.
UCSCiCG2944-RA. d. melanogaster.
CG2944-RB. d. melanogaster.
CG2944-RD. d. melanogaster.
CG2944-RE. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE013599 Genomic DNA. Translation: AAF57346.2.
AE013599 Genomic DNA. Translation: AAF57347.3.
AE013599 Genomic DNA. Translation: AAG22337.2.
AE013599 Genomic DNA. Translation: AAM68372.1.
AE013599 Genomic DNA. Translation: AAM68373.2.
AE013599 Genomic DNA. Translation: AAM68374.2.
AY119609 mRNA. Translation: AAM50263.1. Different initiation.
BT089043 mRNA. Translation: ACU12389.1. Different initiation.
BT099916 mRNA. Translation: ACX32987.1. Different initiation.
BT126146 mRNA. Translation: ADZ74173.1. Sequence problems.
RefSeqiNP_001246140.1. NM_001259211.2.
NP_610158.3. NM_136314.4.
NP_724398.2. NM_165418.3.
NP_724399.2. NM_165419.3.
NP_724400.2. NM_165420.3.
NP_724401.2. NM_165421.3.
NP_724402.2. NM_165422.3.
UniGeneiDm.7323.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2FNJX-ray1.80A27-251[»]
2IHSX-ray2.20A/B27-232[»]
ProteinModelPortaliA1Z6E0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi61396. 47 interactions.
IntActiA1Z6E0. 35 interactions.
STRINGi7227.FBpp0301582.

Proteomic databases

PaxDbiA1Z6E0.
PRIDEiA1Z6E0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi35478.
KEGGidme:Dmel_CG2944.
UCSCiCG2944-RA. d. melanogaster.
CG2944-RB. d. melanogaster.
CG2944-RD. d. melanogaster.
CG2944-RE. d. melanogaster.

Organism-specific databases

CTDi35478.
FlyBaseiFBgn0026238. gus.

Phylogenomic databases

eggNOGiKOG3953. Eukaryota.
ENOG410XQC1. LUCA.
InParanoidiA1Z6E0.
KOiK10343.
OrthoDBiEOG72C513.

Enzyme and pathway databases

ReactomeiR-DME-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiA1Z6E0.
GenomeRNAii35478.
PROiA1Z6E0.

Gene expression databases

BgeeiA1Z6E0.
GenevisibleiA1Z6E0. DM.

Family and domain databases

InterProiIPR001870. B30.2/SPRY.
IPR013320. ConA-like_dom.
IPR001496. SOCS_box.
IPR003877. SPRY_dom.
[Graphical view]
PfamiPF07525. SOCS_box. 1 hit.
PF00622. SPRY. 1 hit.
[Graphical view]
SMARTiSM00969. SOCS_box. 1 hit.
SM00449. SPRY. 1 hit.
[Graphical view]
SUPFAMiSSF158235. SSF158235. 1 hit.
SSF49899. SSF49899. 1 hit.
PROSITEiPS50188. B302_SPRY. 1 hit.
PS50225. SOCS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley1 Publication.
    Tissue: Embryo1 Publication.
  4. Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.
    Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BerkeleyImported.
    Tissue: Embryo.
  5. "VASA localization requires the SPRY-domain and SOCS-box containing protein, GUSTAVUS."
    Styhler S., Nakamura A., Lasko P.
    Dev. Cell 3:865-876(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAS, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  6. "Regulation of Drosophila vasa in vivo through paralogous cullin-RING E3 ligase specificity receptors."
    Kugler J.M., Woo J.S., Oh B.H., Lasko P.
    Mol. Cell. Biol. 30:1769-1782(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH VAS AND CUL-5, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF TRP-219.
  7. "Structural and functional insights into the B30.2/SPRY domain."
    Woo J.S., Imm J.H., Min C.K., Kim K.J., Cha S.S., Oh B.H.
    EMBO J. 25:1353-1363(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 27-251 IN COMPLEX WITH MOUSE ELONGIN-B AND ELONGIN-C, INTERACTION WITH VAS, MUTAGENESIS OF TYR-131; GLY-147; ARG-148; GLU-187; ARG-204 AND TRP-219.
  8. "Structural basis for protein recognition by B30.2/SPRY domains."
    Woo J.S., Suh H.Y., Park S.Y., Oh B.H.
    Mol. Cell 24:967-976(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 27-232 IN COMPLEX WITH VAS FRAGMENT, MUTAGENESIS OF TRP-219.

Entry informationi

Entry nameiGUS_DROME
AccessioniPrimary (citable) accession number: A1Z6E0
Secondary accession number(s): A1Z6D7
, A1Z6D9, A1Z6E2, F2FB59, Q7JUY1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 2013
Last sequence update: March 16, 2016
Last modified: July 6, 2016
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.