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Protein

Small ubiquitin-related modifier

Gene

smt3

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

Functioni

GO - Biological processi

  • anterior/posterior pattern specification Source: FlyBase
  • cellular protein modification process Source: FlyBase
  • cellular response to transforming growth factor beta stimulus Source: FlyBase
  • central nervous system projection neuron axonogenesis Source: FlyBase
  • dendritic spine morphogenesis Source: FlyBase
  • dorsal appendage formation Source: FlyBase
  • lipid homeostasis Source: FlyBase
  • mitotic spindle organization Source: FlyBase
  • phagocytosis Source: FlyBase
  • positive regulation of MAP kinase activity Source: FlyBase
  • positive regulation of MyD88-dependent toll-like receptor signaling pathway Source: FlyBase
  • positive regulation of protein localization to plasma membrane Source: FlyBase
  • positive regulation of Ras protein signal transduction Source: FlyBase
  • protein desumoylation Source: FlyBase
  • protein import into nucleus Source: FlyBase
  • protein sumoylation Source: FlyBase
  • pupariation Source: FlyBase
  • regulation of glucose metabolic process Source: FlyBase
  • syncytial blastoderm mitotic cell cycle Source: FlyBase
  • tricarboxylic acid cycle Source: FlyBase
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathwayUniRule annotation

Enzyme and pathway databases

ReactomeiR-DME-3065679. SUMO is proteolytically processed.
R-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-3232118. SUMOylation of transcription factors.
R-DME-4551638. SUMOylation of chromatin organization proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.
R-DME-4615885. SUMOylation of DNA replication proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifierUniRule annotation
Short name:
SUMOUniRule annotation
Gene namesi
Name:smt3Imported
Synonyms:Smt3Imported
ORF Names:CG4494Imported, Dmel_CG4494Imported
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0264922. smt3.

Subcellular locationi

  • Nucleus UniRule annotation

GO - Cellular componenti

  • condensed chromosome outer kinetochore Source: FlyBase
  • condensed nuclear chromosome Source: FlyBase
  • condensed nuclear chromosome, centromeric region Source: FlyBase
  • midbody Source: FlyBase
  • nucleolus Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

NucleusUniRule annotation

Interactioni

Protein-protein interaction databases

MINTiMINT-866614.
STRINGi7227.FBpp0078984.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1FNMR-A1-88[»]
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini11 – 8878Ubiquitin-likeInterPro annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.UniRule annotation
Contains 1 ubiquitin-like domain.UniRule annotation

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
KOiK12160.
OMAiNAYCDRV.
OrthoDBiEOG76X62R.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O97102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEKKGGET EHINLKVLGQ DNAVVQFKIK KHTPLRKLMN AYCDRAGLSM
60 70 80 90
QVVRFRFDGQ PINENDTPTS LEMEEGDTIE VYQQQTGGAP
Length:90
Mass (Da):10,124
Last modified:May 1, 1999 - v1
Checksum:iE49DA04C24A13CA5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053083 mRNA. Translation: AAD19219.1.
AF218862 mRNA. Translation: AAF31702.1.
AE014134 Genomic DNA. Translation: AAF52470.1.
AY061090 mRNA. Translation: AAL28638.1.
AE014134 Genomic DNA. Translation: ALI30198.1.
RefSeqiNP_001303312.1. NM_001316383.1.
NP_477411.1. NM_058063.4.
UniGeneiDm.6873.

Genome annotation databases

EnsemblMetazoaiFBtr0079356; FBpp0078984; FBgn0264922.
FBtr0346716; FBpp0312327; FBgn0264922.
GeneIDi33981.
KEGGidme:Dmel_CG4494.
UCSCiCG4494-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053083 mRNA. Translation: AAD19219.1.
AF218862 mRNA. Translation: AAF31702.1.
AE014134 Genomic DNA. Translation: AAF52470.1.
AY061090 mRNA. Translation: AAL28638.1.
AE014134 Genomic DNA. Translation: ALI30198.1.
RefSeqiNP_001303312.1. NM_001316383.1.
NP_477411.1. NM_058063.4.
UniGeneiDm.6873.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K1FNMR-A1-88[»]
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-866614.
STRINGi7227.FBpp0078984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0079356; FBpp0078984; FBgn0264922.
FBtr0346716; FBpp0312327; FBgn0264922.
GeneIDi33981.
KEGGidme:Dmel_CG4494.
UCSCiCG4494-RA. d. melanogaster.

Organism-specific databases

CTDi33981.
FlyBaseiFBgn0264922. smt3.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
KOiK12160.
OMAiNAYCDRV.
OrthoDBiEOG76X62R.

Enzyme and pathway databases

ReactomeiR-DME-3065679. SUMO is proteolytically processed.
R-DME-3108214. SUMOylation of DNA damage response and repair proteins.
R-DME-3232118. SUMOylation of transcription factors.
R-DME-4551638. SUMOylation of chromatin organization proteins.
R-DME-4570464. SUMOylation of RNA binding proteins.
R-DME-4615885. SUMOylation of DNA replication proteins.

Miscellaneous databases

ChiTaRSismt3. fly.
GenomeRNAii33981.
NextBioi786256.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of the SMT3 cDNA and gene encoding ubiquitin-like protein from Drosophila melanogaster."
    Huang H.W., Tsoi S.C., Sun Y.H., Li S.S.
    Biochem. Mol. Biol. Int. 46:775-785(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  2. Li S.S.-L., Huang H.W.
    Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  3. "A functional interaction between dorsal and components of the Smt3 conjugation machinery."
    Bhaskar V., Valentine S.A., Courey A.J.
    J. Biol. Chem. 275:4033-4040(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
  4. "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.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BerkeleyImported.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  7. Cited for: GENOME REANNOTATION.
    Strain: BerkeleyImported.
  8. "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-RESEARCH0084(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  9. "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.
  10. "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.
  11. O'Boyle S.T.
    Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  12. "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 (SEP-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
  13. "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.
  14. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: BerkeleyImported.
  15. "NMR-derived solution structure of SUMO from Drosophila melanogaster (dSmt3)."
    Kumar D., Misra J.R., Misra A.K., Chugh J., Sharma S., Hosur R.V.
    Proteins 0:0-0(2009)
    Cited for: STRUCTURE BY NMR OF 1-88.
  16. Millard Andrew
    Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.

Entry informationi

Entry nameiO97102_DROME
AccessioniPrimary (citable) accession number: O97102
Entry historyi
Integrated into UniProtKB/TrEMBL: May 1, 1999
Last sequence update: May 1, 1999
Last modified: May 11, 2016
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, 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.