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Protein

Protein Smaug

Gene

smg

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

Functioni

Translation regulator that binds to the 3'-UTR of specific mRNAs such as nanos (nos) and prevents their translation. Prevents translation of unlocalized nos in the bulk cytoplasm via the recruitment of cup.4 Publications

GO - Molecular functioni

  • mRNA 3'-UTR binding Source: FlyBase
  • mRNA binding Source: FlyBase
  • myosin binding Source: FlyBase
  • translation repressor activity Source: UniProtKB
  • translation repressor activity, nucleic acid binding Source: FlyBase

GO - Biological processi

  • establishment of RNA localization Source: FlyBase
  • multicellular organism development Source: UniProtKB-KW
  • negative regulation of translation Source: FlyBase
  • nuclear-transcribed mRNA poly(A) tail shortening Source: FlyBase
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: FlyBase
  • regulation of mRNA stability Source: FlyBase
  • regulation of transcription, DNA-templated Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Repressor

Keywords - Biological processi

Translation regulation

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Protein Smaug
Gene namesi
Name:smg
ORF Names:CG5263
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0016070. smg.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic mRNA processing body Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi606 – 6061K → A: Reduced RNA-binding. Complete loss; when associated with R-609. 1 Publication
Mutagenesisi609 – 6091R → A: Reduced RNA-binding. Complete loss; when associated with A-606. 1 Publication
Mutagenesisi611 – 6111H → S or Q: Reduced RNA-binding. 1 Publication
Mutagenesisi612 – 6121K → Q: Loss of RNA-binding. 1 Publication
Mutagenesisi613 – 6131Y → F: Reduced RNA-binding. 1 Publication
Mutagenesisi632 – 6321F → L: No effect on RNA-binding; when associated with L-634. 1 Publication
Mutagenesisi634 – 6341Q → L: No effect on RNA-binding; when associated with L-632. 1 Publication
Mutagenesisi640 – 6401K → S: Reduced RNA-binding. 1 Publication
Mutagenesisi642 – 6421A → H or Q: Loss of RNA-binding. 1 Publication
Mutagenesisi658 – 6581N → D: No effect on RNA-binding; when associated with R-665; I-724 and R-749. 1 Publication
Mutagenesisi665 – 6651Q → R: No effect on RNA-binding; when associated with D-658; I-724 and R-749. 1 Publication
Mutagenesisi724 – 7241V → I: No effect on RNA-binding; when associated with D-658; R-665 and R-749. 1 Publication
Mutagenesisi739 – 7391R → S: No effect on RNA-binding.
Mutagenesisi749 – 7491H → R: No effect on RNA-binding; when associated with D-658; I-724 and R-665. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 999999Protein SmaugPRO_0000071972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei564 – 5641Phosphoserine1 Publication
Modified residuei575 – 5751Phosphoserine1 Publication
Modified residuei972 – 9721Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ23972.
PRIDEiQ23972.

PTM databases

iPTMnetiQ23972.

Expressioni

Tissue specificityi

At syncytial blastoderm, it is located throughout the bulk cytoplasm and pole plasm. By the time of cellularization, it concentrates at the posterior pole.3 Publications

Developmental stagei

Expressed maternally. The protein accumulates during the first 3 hours after fertilization, and then decreases rapidly.1 Publication

Gene expression databases

BgeeiQ23972.
GenevisibleiQ23972. DM.

Interactioni

Subunit structurei

Interacts with oskar (osk). Binds to the 3'-UTR of nos. Interacts with cup, which in turn recruits eIF4-E, leading to an indirect interaction between smg and eIF4-E that prevents mRNA translation. Forms a complex with aub, twin, AGO3, nos mRNA and piRNAs that targets the nos 3'-untranslated region, in early embryos.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
cupQ9VMA34EBI-108638,EBI-95398

GO - Molecular functioni

  • myosin binding Source: FlyBase

Protein-protein interaction databases

BioGridi64438. 7 interactions.
IntActiQ23972. 8 interactions.
MINTiMINT-851035.
STRINGi7227.FBpp0288542.

Structurei

Secondary structure

1
999
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi601 – 6077Combined sources
Helixi611 – 6177Combined sources
Helixi622 – 6254Combined sources
Helixi630 – 6356Combined sources
Helixi640 – 66829Combined sources
Helixi674 – 6829Combined sources
Turni683 – 6864Combined sources
Helixi698 – 7003Combined sources
Helixi702 – 71817Combined sources
Helixi723 – 7253Combined sources
Helixi727 – 74115Combined sources
Helixi744 – 7496Combined sources
Helixi750 – 76112Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OXJX-ray1.80A593-764[»]
ProteinModelPortaliQ23972.
SMRiQ23972. Positions 596-763.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ23972.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini600 – 65455SAMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni583 – 763181Interaction with cupAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi302 – 33837Ser-richAdd
BLAST
Compositional biasi871 – 976106Gln-richAdd
BLAST

Domaini

The SAM domain mediates the association with the 3'-UTR of specific mRNAs.

Sequence similaritiesi

Belongs to the SMAUG family.Curated

Phylogenomic databases

eggNOGiKOG3791. Eukaryota.
ENOG410XSUP. LUCA.
GeneTreeiENSGT00390000015877.
InParanoidiQ23972.
OMAiGSINPLC.
OrthoDBiEOG7TTQ74.
PhylomeDBiQ23972.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.170. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR015327. PHAT_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF09246. PHAT. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48371. SSF48371. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform A (identifier: Q23972-1) [UniParc]FASTAAdd to basket

Also known as: B, C, E

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MKYATGTDNA MTSGISGQTN NSNSASNEMQ PTTSTPTAAH KEATSTATTT
60 70 80 90 100
ATYANGNPNS NANPSQSQPS NALFCEQVTT VTNLFEKWND CERTVVMYAL
110 120 130 140 150
LKRLRYPSLK FLQYSIDSNL TQNLGTSQTN LSSVVIDINA NNPVYLQNLL
160 170 180 190 200
NAYKTFQPCD LLDAMSSSSS DKDSMPCYGS DFQITTSAQC DERKLYARKE
210 220 230 240 250
DILHEVLNML PLLKPGNEEA KLIYLTLIPV AVKDTMQQIV PTELVQQIFS
260 270 280 290 300
YLLIHPAITS EDRRSLNIWL RHLEDHIQAA AAGLTNRSYF LQPSPQLVAG
310 320 330 340 350
GSSTGSGSCS SSATSSSTAS CSSVASSSLC PASGSRSSRT NDWQTIAPPS
360 370 380 390 400
KQLQNKLAGD WRGNGGGSSS GSINPLCDNL NGITLNELAS SQNSLGLSLE
410 420 430 440 450
GSSSLVNGVV AGAGSMLGIA GGDDHDTSFS KNGTEILDFD PVTADMGEAC
460 470 480 490 500
SLASSSLCGR NGGNPVEDRS QPPPNLQQQL LQPPPYASIL MGNVGDQFGE
510 520 530 540 550
INRWSLDSKI AALKTRRSNS LTTQTISSCS SSSNSSVITV NDNCSNSTEN
560 570 580 590 600
LAQFANKPRS FSLSIEHQRG ALMNSGSDTR LDEFKPNYIK FHTRNVGMSG
610 620 630 640 650
IGLWLKSLRL HKYIELFKNM TYEEMLLITE DFLQSVGVTK GASHKLALCI
660 670 680 690 700
DKLKERANIL NRVEQELLSG QMELSTAVEE LTNIVLTPMK PLESPGPPEE
710 720 730 740 750
NIGLRFLKVI DIVTNTLQQD PYAVQDDETL GVLMWILDRS IHNEAFMNHA
760 770 780 790 800
SQLKDLKFKL SKMKISMVPK MHHVKPAGVG PNNGNINKPR WNGKTRKCDT
810 820 830 840 850
KNGSNDRINN RKNSNDMLNF SLNCLPHPLP HHSQQAPPPL PQFDYNGYGG
860 870 880 890 900
GPSHQPQYKS SSYPSFMGNP QQQPPPPPSS KSHHHPQQMQ QMLQQHNHFP
910 920 930 940 950
ALPQQTPPQS HRRSLNNLIL VAGGPQQPQQ LIFKPGQGVL TNNGSNDNLV
960 970 980 990
LERNQQSQQQ QQQRKLSGGV SSAEQQPKKT MAAVVMENLA KFDQHFTLF
Length:999
Mass (Da):109,065
Last modified:February 2, 2004 - v2
Checksum:i6EBB615435F07190
GO
Isoform D (identifier: Q23972-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     987-999: ENLAKFDQHFTLF → VSNPNQNQDQ...CRQMTEQAMN

Note: No experimental confirmation available.
Show »
Length:1,109
Mass (Da):120,713
Checksum:i45DF745BB0DC2B82
GO

Sequence cautioni

The sequence AAA03462.1 differs from that shown.Absence of a large region from Gly-793 to the end of the coding region that changes the frame.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei987 – 99913ENLAK…HFTLF → VSNPNQNQDQHDQPQILINN NNNNSMLNNNLINQQQLQLL AAAAAAVGSGSCLCSNGGGG ACVHNICHQSSKNNNHGVDH CLSQSPLGSLGMSPHVTEYK MNDFKSLEQLETLCRQMTEQ AMN in isoform D. CuratedVSP_039395Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159852 mRNA. Translation: AAD54965.1.
AF132213 mRNA. Translation: AAF61321.1.
AE014296 Genomic DNA. Translation: AAF50333.3.
AE014296 Genomic DNA. Translation: AAF50334.3.
AE014296 Genomic DNA. Translation: ACL83279.1.
AE014296 Genomic DNA. Translation: ACL83280.1.
AE014296 Genomic DNA. Translation: AAN11981.1.
AY058607 mRNA. Translation: AAL13836.1.
U03277 Unassigned DNA. Translation: AAA03462.1. Sequence problems.
RefSeqiNP_001137924.1. NM_001144452.2. [Q23972-2]
NP_001137925.1. NM_001144453.2. [Q23972-1]
NP_523987.1. NM_079263.3. [Q23972-1]
NP_729441.1. NM_168309.3. [Q23972-1]
NP_729442.1. NM_168310.3. [Q23972-1]
UniGeneiDm.2553.

Genome annotation databases

EnsemblMetazoaiFBtr0076549; FBpp0076276; FBgn0016070. [Q23972-1]
FBtr0076550; FBpp0076277; FBgn0016070. [Q23972-1]
FBtr0076551; FBpp0076278; FBgn0016070. [Q23972-1]
FBtr0290104; FBpp0288543; FBgn0016070. [Q23972-1]
GeneIDi39034.
KEGGidme:Dmel_CG5263.
UCSCiCG5263-RA. d. melanogaster. [Q23972-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF159852 mRNA. Translation: AAD54965.1.
AF132213 mRNA. Translation: AAF61321.1.
AE014296 Genomic DNA. Translation: AAF50333.3.
AE014296 Genomic DNA. Translation: AAF50334.3.
AE014296 Genomic DNA. Translation: ACL83279.1.
AE014296 Genomic DNA. Translation: ACL83280.1.
AE014296 Genomic DNA. Translation: AAN11981.1.
AY058607 mRNA. Translation: AAL13836.1.
U03277 Unassigned DNA. Translation: AAA03462.1. Sequence problems.
RefSeqiNP_001137924.1. NM_001144452.2. [Q23972-2]
NP_001137925.1. NM_001144453.2. [Q23972-1]
NP_523987.1. NM_079263.3. [Q23972-1]
NP_729441.1. NM_168309.3. [Q23972-1]
NP_729442.1. NM_168310.3. [Q23972-1]
UniGeneiDm.2553.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1OXJX-ray1.80A593-764[»]
ProteinModelPortaliQ23972.
SMRiQ23972. Positions 596-763.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi64438. 7 interactions.
IntActiQ23972. 8 interactions.
MINTiMINT-851035.
STRINGi7227.FBpp0288542.

PTM databases

iPTMnetiQ23972.

Proteomic databases

PaxDbiQ23972.
PRIDEiQ23972.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0076549; FBpp0076276; FBgn0016070. [Q23972-1]
FBtr0076550; FBpp0076277; FBgn0016070. [Q23972-1]
FBtr0076551; FBpp0076278; FBgn0016070. [Q23972-1]
FBtr0290104; FBpp0288543; FBgn0016070. [Q23972-1]
GeneIDi39034.
KEGGidme:Dmel_CG5263.
UCSCiCG5263-RA. d. melanogaster. [Q23972-1]

Organism-specific databases

CTDi39034.
FlyBaseiFBgn0016070. smg.

Phylogenomic databases

eggNOGiKOG3791. Eukaryota.
ENOG410XSUP. LUCA.
GeneTreeiENSGT00390000015877.
InParanoidiQ23972.
OMAiGSINPLC.
OrthoDBiEOG7TTQ74.
PhylomeDBiQ23972.

Miscellaneous databases

EvolutionaryTraceiQ23972.
GenomeRNAii39034.
PROiQ23972.

Gene expression databases

BgeeiQ23972.
GenevisibleiQ23972. DM.

Family and domain databases

Gene3Di1.10.150.50. 1 hit.
1.25.40.170. 1 hit.
InterProiIPR016024. ARM-type_fold.
IPR015327. PHAT_dom.
IPR001660. SAM.
IPR013761. SAM/pointed.
[Graphical view]
PfamiPF09246. PHAT. 1 hit.
PF00536. SAM_1. 1 hit.
[Graphical view]
SMARTiSM00454. SAM. 1 hit.
[Graphical view]
SUPFAMiSSF47769. SSF47769. 1 hit.
SSF48371. SSF48371. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Smaug, a novel RNA-binding protein that operates a translational switch in Drosophila."
    Dahanukar A., Walker J.A., Wharton R.P.
    Mol. Cell 4:209-218(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), FUNCTION, SUBCELLULAR LOCATION, RNA-BINDING, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INTERACTION WITH OSK.
    Strain: Iso-1.
  2. "Smaug, a novel and conserved protein, contributes to repression of nanos mRNA translation in vitro."
    Smibert C.A., Lie Y.S., Shillinglaw W., Henzel W.J., Macdonald P.M.
    RNA 5:1535-1547(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), PROTEIN SEQUENCE OF 95-102; 272-287; 461-469; 570-580; 740-754; 776-788; 935-953; 966-977 AND 980-991, FUNCTION, RNA-BINDING, TISSUE SPECIFICITY.
    Tissue: Embryo.
  3. "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.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
    Strain: Berkeley.
    Tissue: Embryo.
  6. Edgar B.
    Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE OF 573-792 (ISOFORMS A/D).
    Strain: Sevelin.
    Tissue: Embryo.
  7. "smaug protein represses translation of unlocalized nanos mRNA in the Drosophila embryo."
    Smibert C.A., Wilson J.E., Kerr K., Macdonald P.M.
    Genes Dev. 10:2600-2609(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Overlapping but distinct RNA elements control repression and activation of nanos translation."
    Crucs S., Chatterjee S., Gavis E.R.
    Mol. Cell 5:457-467(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING.
  9. "The RNA-binding SAM domain of Smaug defines a new family of post-transcriptional regulators."
    Aviv T., Lin Z., Lau S., Rendl L.M., Sicheri F., Smibert C.A.
    Nat. Struct. Biol. 10:614-621(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-606; ARG-609; HIS-611; LYS-612; TYR-613 AND ALA-642.
  10. "Drosophila Cup is an eIF4E-binding protein that functions in Smaug-mediated translational repression."
    Nelson M.R., Leidal A.M., Smibert C.A.
    EMBO J. 23:150-159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CUP.
  11. "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-564; SER-575 AND SER-972, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  12. "Maternal mRNA deadenylation and decay by the piRNA pathway in the early Drosophila embryo."
    Rouget C., Papin C., Boureux A., Meunier A.C., Franco B., Robine N., Lai E.C., Pelisson A., Simonelig M.
    Nature 467:1128-1132(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AUB, TWIN AND AGO3, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 596-764, MUTAGENESIS OF PHE-632; GLN-634; LYS-640; ASN-658; GLN-665; VAL-724 AND HIS-749.

Entry informationi

Entry nameiSMG_DROME
AccessioniPrimary (citable) accession number: Q23972
Secondary accession number(s): A4V1P7
, B7Z0F4, B7Z0F5, Q9V3T0, Q9VSS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 2, 2004
Last sequence update: February 2, 2004
Last modified: July 6, 2016
This is version 135 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, Direct protein sequencing, 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.