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Protein

Protein Gemin2

Gene

Gem2

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

The SMN complex plays an essential role in spliceosomal snRNP assembly in the cytoplasm, is required for pre-mRNA splicing in the nucleus and acts as a chaperone that discriminates target and non-target RNAs of Sm proteins.2 Publications

GO - Biological processi

  1. adult locomotory behavior Source: FlyBase
  2. flight behavior Source: FlyBase
  3. spliceosomal complex assembly Source: InterPro
  4. spliceosomal snRNP assembly Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Gemin2Imported
Gene namesi
Name:Gem2Imported
ORF Names:CG10419
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036850. Gem2.

Subcellular locationi

Cytoplasm 2 Publications
Note: Component of U bodies.2 Publications

GO - Cellular componenti

  1. cytoplasmic U snRNP body Source: FlyBase
  2. SmD-containing SMN-Sm protein complex Source: UniProtKB
  3. SMN-Gemin2 complex Source: UniProtKB
  4. spliceosomal complex Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 245245Protein Gemin2PRO_0000424375Add
BLAST

Proteomic databases

PRIDEiQ9VVX0.

Expressioni

Tissue specificityi

Expressed in nurse cells and oocytes.1 Publication

Gene expression databases

BgeeiQ9VVX0.

Interactioni

Subunit structurei

Part of the core SMN complex, which seems to be composed of Smn and Gem2 only. The SMN complex associates with the entire set of spliceosomal snRNP Sm proteins, SmB, SmD1, SmD2, SmD3, SmE, SmF and SmG, and with the snRNP-specific proteins snRNP-U1-70K, U2A, snf/U1A and U5-116KD.2 Publications

Protein-protein interaction databases

IntActiQ9VVX0. 3 interactions.
MINTiMINT-1625145.
STRINGi7227.FBpp0074799.

Structurei

Secondary structure

1
245
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi32 – 343Combined sources
Helixi35 – 4612Combined sources
Beta strandi56 – 583Combined sources
Helixi85 – 11127Combined sources
Helixi116 – 1183Combined sources
Helixi127 – 1359Combined sources
Helixi140 – 1434Combined sources
Helixi148 – 16013Combined sources
Beta strandi171 – 1744Combined sources
Helixi175 – 18713Combined sources
Helixi194 – 21219Combined sources
Helixi219 – 23416Combined sources
Helixi242 – 2443Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V98X-ray3.10A2/AF/AN/AV/Ad/Al/At/B2/BF/BN/BV/Bd/Bl/Bt/CF/CN/CV/Cd/Cl/Ct1-245[»]
SMRiQ9VVX0. Positions 30-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the gemin-2 family.Sequence Analysis

Phylogenomic databases

GeneTreeiENSGT00390000013814.
InParanoidiQ9VVX0.
KOiK13130.
OMAiCLGERLY.
OrthoDBiEOG7XH6RF.
PhylomeDBiQ9VVX0.

Family and domain databases

InterProiIPR007022. GEMIN2.
IPR017364. GEMIN2_metazoa.
[Graphical view]
PANTHERiPTHR12794. PTHR12794. 1 hit.
PIRSFiPIRSF038038. SMN_Gemin2. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9VVX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQHEPEDQTF QLQALEICEP DSSFDPQKPP ESGEEYLMHM FYERKRCPAV
60 70 80 90 100
VTKRSSKIRN NTGNTTLEML DNPELPPFKC LLPTPEWRDE QVKSFQAARS
110 120 130 140 150
QVLVLRKELA NNNYDQSGEP PLTSDQEKWK EFCRNQQPLL STLLHLTQND
160 170 180 190 200
LELLLEMLSK WLQDPNTTVD LLHDVWLARW LYATLVCLHL PLEPHVFSTL
210 220 230 240
RYIARTCIHL RNQLKEDEVQ RAAPYNLLLT LTVQVFAQND FKDYI
Length:245
Mass (Da):28,751
Last modified:April 30, 2000 - v1
Checksum:i1E9A700ADD97EDFF
GO

Sequence cautioni

The sequence AAL39848.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49187.1.
AE014296 Genomic DNA. Translation: AGB94727.1.
AY069703 mRNA. Translation: AAL39848.2. Different initiation.
RefSeqiNP_001262034.1. NM_001275105.1.
NP_649092.1. NM_140835.4.
UniGeneiDm.1995.

Genome annotation databases

EnsemblMetazoaiFBtr0075032; FBpp0074799; FBgn0036850.
FBtr0330093; FBpp0303126; FBgn0036850.
GeneIDi40087.
KEGGidme:Dmel_CG10419.
UCSCiCG10419-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014296 Genomic DNA. Translation: AAF49187.1.
AE014296 Genomic DNA. Translation: AGB94727.1.
AY069703 mRNA. Translation: AAL39848.2. Different initiation.
RefSeqiNP_001262034.1. NM_001275105.1.
NP_649092.1. NM_140835.4.
UniGeneiDm.1995.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4V98X-ray3.10A2/AF/AN/AV/Ad/Al/At/B2/BF/BN/BV/Bd/Bl/Bt/CF/CN/CV/Cd/Cl/Ct1-245[»]
SMRiQ9VVX0. Positions 30-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9VVX0. 3 interactions.
MINTiMINT-1625145.
STRINGi7227.FBpp0074799.

Proteomic databases

PRIDEiQ9VVX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0075032; FBpp0074799; FBgn0036850.
FBtr0330093; FBpp0303126; FBgn0036850.
GeneIDi40087.
KEGGidme:Dmel_CG10419.
UCSCiCG10419-RA. d. melanogaster.

Organism-specific databases

CTDi40087.
FlyBaseiFBgn0036850. Gem2.

Phylogenomic databases

GeneTreeiENSGT00390000013814.
InParanoidiQ9VVX0.
KOiK13130.
OMAiCLGERLY.
OrthoDBiEOG7XH6RF.
PhylomeDBiQ9VVX0.

Miscellaneous databases

GenomeRNAii40087.
NextBioi816928.

Gene expression databases

BgeeiQ9VVX0.

Family and domain databases

InterProiIPR007022. GEMIN2.
IPR017364. GEMIN2_metazoa.
[Graphical view]
PANTHERiPTHR12794. PTHR12794. 1 hit.
PIRSFiPIRSF038038. SMN_Gemin2. 1 hit.
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(1999) [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: BerkeleyImported.
  4. "Evolution of an RNP assembly system: a minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster."
    Kroiss M., Schultz J., Wiesner J., Chari A., Sickmann A., Fischer U.
    Proc. Natl. Acad. Sci. U.S.A. 105:10045-10050(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN THE SMN COMPLEX, INTERACTION WITH THE SPLICEOSOME USNRNP PROTEINS SNRNP-U1-70K, U2A, SNF/U1A AND U5-116KD, INTERACTION WITH THE SNRNP SM PROTEINS, SUBCELLULAR LOCATION.
  5. "Drosophila SMN complex proteins Gemin2, Gemin3, and Gemin5 are components of U bodies."
    Cauchi R.J., Sanchez-Pulido L., Liu J.L.
    Exp. Cell Res. 316:2354-2364(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  6. "Structural basis of assembly chaperone-mediated snRNP formation."
    Grimm C., Chari A., Pelz J.P., Kuper J., Kisker C., Diederichs K., Stark H., Schindelin H., Fischer U.
    Mol. Cell 49:692-703(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS), FUNCTION, SUBUNIT.

Entry informationi

Entry nameiGEMI2_DROME
AccessioniPrimary (citable) accession number: Q9VVX0
Secondary accession number(s): Q7K0M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 12, 2013
Last sequence update: April 30, 2000
Last modified: March 31, 2015
This is version 100 of the entry and version 1 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

External Data

Dasty 3

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 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.