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Q9VV74

- SMN_DROME

UniProt

Q9VV74 - SMN_DROME

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Protein

Survival motor neuron protein

Gene
Smn, CG16725
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 5 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. Required for normal expression of spliceosomal snRNAs and for U12 intron splicing. Required in cholinergic neurons, but not in motor neurons, to ensure correct splicing and proper levels of stas mRNA and normal neurotransmitter release by motor neurons (1 Publication and 1 Publication). However, Smn is required in motor neurons, but not in cholinergic neurons, for normal motor behavior but plays no role in synaptic transmission according to 1 Publication. In both muscle and neurons, required for the formation of a normal neuromuscular junction (NMJ) structure. Plays a neuron-specific role in long-term homeostatic compensation at the larval NMJ. In the thorax of adult flies, required for Act88F, an indirect flight muscle (IFM)-specific actin, expression and for proper IFM myofibril formation. In nurse cells, oocytes and follicle cells, required to maintain normal organization of nuclear compartments including chromosomes, nucleoli, Cajal bodies, histone locus bodies and heterochromatin. Required for the functional integrity of the cytoplasmic U snRNP body (U body) and P body. Required in dividing postembryonic neuroblasts (pNBs) for the correct basal localization of mira. The tight regulation of its expression is critical for stem cell division, proliferation and differentiation in male germline and developing central nervous system (CNS). Required for tracheal terminal cell lumen formation.12 Publications

GO - Molecular functioni

  1. alpha-actinin binding Source: FlyBase
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct
  4. RNA binding Source: InterPro

GO - Biological processi

  1. alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor clustering Source: UniProtKB
  2. basal protein localization Source: UniProtKB
  3. central nervous system development Source: UniProtKB
  4. chromosome organization Source: UniProtKB
  5. cytoplasmic mRNA processing body assembly Source: UniProtKB
  6. cytoplasmic U snRNP body assembly Source: UniProtKB
  7. embryo development Source: UniProtKB
  8. larval development Source: UniProtKB
  9. larval locomotory behavior Source: UniProtKB
  10. mRNA splicing, via spliceosome Source: UniProtKB
  11. neuromuscular junction development Source: UniProtKB
  12. neuromuscular synaptic transmission Source: UniProtKB
  13. oocyte morphogenesis Source: UniProtKB
  14. positive regulation of synaptic transmission, cholinergic Source: UniProtKB
  15. regulation of excitatory postsynaptic membrane potential Source: UniProtKB
  16. ribonucleoprotein complex assembly Source: FlyBase
  17. skeletal muscle thin filament assembly Source: FlyBase
  18. spliceosomal snRNP assembly Source: UniProtKB
  19. stem cell differentiation Source: UniProtKB
  20. stem cell division Source: UniProtKB
  21. stem cell proliferation Source: UniProtKB
  22. terminal button organization Source: UniProtKB
  23. terminal cell fate specification, open tracheal system Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

mRNA processing, mRNA splicing

Names & Taxonomyi

Protein namesi
Recommended name:
Survival motor neuron protein
Gene namesi
Name:Smn
ORF Names:CG16725
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803: Chromosome 3L

Organism-specific databases

FlyBaseiFBgn0036641. Smn.

Subcellular locationi

Cytoplasm. Nucleusgem. CytoplasmmyofibrilsarcomereI band. CytoplasmmyofibrilsarcomereZ line
Note: Component of U bodies. High expression detected in the cytoplasm of female germline stem cells and cystoblast which persists up to stage 10 egg chambers. Accumulates in the cytoplasm of dividing pNBs. Colocalizes with Actn at the Z-line of IFMs. Expression concentrates at the post-synaptic region of NMJs in larval brain.7 Publications

GO - Cellular componenti

  1. Cajal body Source: FlyBase
  2. cytoplasm Source: UniProtKB
  3. cytoplasmic U snRNP body Source: UniProtKB
  4. Gemini of coiled bodies Source: UniProtKB
  5. I band Source: FlyBase
  6. neuromuscular junction Source: FlyBase
  7. nucleus Source: FlyBase
  8. SmD-containing SMN-Sm protein complex Source: UniProtKB
  9. SMN-Gemin2 complex Source: UniProtKB
  10. spliceosomal complex Source: UniProtKB-KW
  11. Z disc Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Disruption phenotypei

Embryos lacking maternal and zygotic Smn die between 0 and 4 hours after egg laying. Zygotic mutants never initiate pupation but instead persist as third instar larvae, often surviving at this stage for several days. Mutant larvae exhibit reduced CNS, testes and muscle size, decreased locomotion and altered rhythmic motor activity. At the NMJ, mutant larvae show an overall decrease in the number of synaptic boutons, but an increase in enlarged ones, loss of large glutamate receptor clusters and an aberrant increase in evoked excitatory postsynaptic potential (eEPSP) amplitude and in miniature EPSP frequency. Mutant larvae also show defective mira subcellular localization in pNBs. Mutant larvae show a decrease of spliceosomal snRNA levels and splicing defects in U12 intron-containing genes (1 Publication). But appreciable splicing defects in U12 intron-containing genes are not observed in mutant larvae, although a decrease in spliceosomal snRNA levels is detected, in 1 Publication.8 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi20 – 201D → V: Does not affect homodimer formation. 1 Publication
Mutagenesisi70 – 701F → S: Does not affect homodimer formation. 1 Publication
Mutagenesisi201 – 2011S → F in allele Smn-B; homozygous lethal at late larval stages and abolishes homodimerization. 1 Publication
Mutagenesisi202 – 2021G → S in allele Smn-73Ao; homozygous lethal at late larval stages and abolishes homodimerization. 1 Publication
Mutagenesisi203 – 2031Y → C: Weakly inhibits homodimer formation. 1 Publication
Mutagenesisi205 – 2051T → I: Rescues larval viability and locomotion defects and only partially restores U5 and U12 snRNA levels in the null mutant. Weakly inhibits homodimer formation. Does not affect protein stability. 1 Publication
Mutagenesisi206 – 2061G → S: Inhibits homodimer formation. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 226226Survival motor neuron proteinPRO_0000424374Add
BLAST

Proteomic databases

PRIDEiQ9VV74.

Expressioni

Tissue specificityi

In late first instar larvae, expressed in pNBs. Expression increases as the pNBs enlarge, with the highest accumulation observed in dividing pNBs of second and third instar larvae. Enriched in type ID (thoracic and brain lobe), type IA and all the mira-expressing NBs of the brain lobes. In larvae, also expressed in muscle fibers. In larval and adult testis, expressed in germline stem cells and gonialblast, expression decreases as cells differentiate into cysts and spermatocytes. In adult fly thorax, expressed in the IFMs. In adult ovary, expressed in germline stem cells, cystoblasts, follicle cells, nurse cells and oocyte (at protein level). Also expressed in larval salivary glands.6 Publications

Developmental stagei

Expressed both maternally and zygotically. Expressed ubiquitously throughout development. Expression is high during embryogenesis but decreases 30-fold in adult flies (at protein level).5 Publications

Interactioni

Subunit structurei

Homodimer (via C-terminal region). 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. Associates weakly with Gem3. Interacts with SmB and SmD1; the interaction is favored by methylation of the Sm proteins. Interacts with Actn; the interaction occurs in thoracic tissues and in adult flies. Interacts with Rpp20, msk and snupn.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-185315,EBI-185315
Rpp20Q2MGL33EBI-185315,EBI-1151669
SNRPNP631622EBI-185315,EBI-712493From a different organism.

Protein-protein interaction databases

DIPiDIP-18223N.
IntActiQ9VV74. 8 interactions.
MINTiMINT-750365.
STRINGi7227.FBpp0075153.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 239

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1VU2X-ray3.101/E/M/U/c/k/s1-122[»]
1VU3X-ray3.10E/M/U/c/k/s1-122[»]
4F77X-ray3.101/E/M/U/c/k/s1-122[»]
ProteinModelPortaliQ9VV74.
SMRiQ9VV74. Positions 2-27, 68-121.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 12860TudorAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni159 – 22668Required for homodimerization1 PublicationAdd
BLAST

Sequence similaritiesi

Belongs to the SMN family.
Contains 1 Tudor domain.

Phylogenomic databases

eggNOGiNOG296671.
InParanoidiQ9VV74.
KOiK13129.
OMAiSAMLMSW.
OrthoDBiEOG7K6PVX.
PhylomeDBiQ9VV74.

Family and domain databases

InterProiIPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view]
PfamiPF06003. SMN. 1 hit.
[Graphical view]
SMARTiSM00333. TUDOR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VV74-1 [UniParc]FASTAAdd to Basket

« Hide

MSDETNAAVW DDSLLVKTYD ESVGLAREAL ARRLADSTNK REEENAAAAE    50
EEAGEISATG GATSPEPVSF KVGDYARATY VDGVDYEGAV VSINEEKGTC 100
VLRYLGYENE QEVLLVDLLP SWGKRVRREQ FLIAKKDEDE QLSRPKASAG 150
SHSKTPKSSR RSRISGGLVM PPMPPVPPMI VGQGDGAEQD FVAMLTAWYM 200
SGYYTGLYQG KKEASTTSGK KKTPKK 226
Length:226
Mass (Da):24,622
Last modified:May 1, 2000 - v1
Checksum:i9F00D85A3E9614C7
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF296281 mRNA. Translation: AAG17893.1.
AE014296 Genomic DNA. Translation: AAF49446.1.
AE014296 Genomic DNA. Translation: AGB94647.1.
AY058529 mRNA. Translation: AAL13758.1.
RefSeqiNP_001261954.1. NM_001275025.1.
NP_524112.1. NM_079388.4.
UniGeneiDm.2679.

Genome annotation databases

EnsemblMetazoaiFBtr0075395; FBpp0075153; FBgn0036641.
FBtr0329921; FBpp0302954; FBgn0036641.
GeneIDi39844.
KEGGidme:Dmel_CG16725.
UCSCiCG16725-RA. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF296281 mRNA. Translation: AAG17893.1 .
AE014296 Genomic DNA. Translation: AAF49446.1 .
AE014296 Genomic DNA. Translation: AGB94647.1 .
AY058529 mRNA. Translation: AAL13758.1 .
RefSeqi NP_001261954.1. NM_001275025.1.
NP_524112.1. NM_079388.4.
UniGenei Dm.2679.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1VU2 X-ray 3.10 1/E/M/U/c/k/s 1-122 [» ]
1VU3 X-ray 3.10 E/M/U/c/k/s 1-122 [» ]
4F77 X-ray 3.10 1/E/M/U/c/k/s 1-122 [» ]
ProteinModelPortali Q9VV74.
SMRi Q9VV74. Positions 2-27, 68-121.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-18223N.
IntActi Q9VV74. 8 interactions.
MINTi MINT-750365.
STRINGi 7227.FBpp0075153.

Proteomic databases

PRIDEi Q9VV74.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0075395 ; FBpp0075153 ; FBgn0036641 .
FBtr0329921 ; FBpp0302954 ; FBgn0036641 .
GeneIDi 39844.
KEGGi dme:Dmel_CG16725.
UCSCi CG16725-RA. d. melanogaster.

Organism-specific databases

CTDi 39844.
FlyBasei FBgn0036641. Smn.

Phylogenomic databases

eggNOGi NOG296671.
InParanoidi Q9VV74.
KOi K13129.
OMAi SAMLMSW.
OrthoDBi EOG7K6PVX.
PhylomeDBi Q9VV74.

Miscellaneous databases

GenomeRNAii 39844.
NextBioi 815685.

Family and domain databases

InterProi IPR010304. Survival_motor_neuron.
IPR002999. Tudor.
[Graphical view ]
Pfami PF06003. SMN. 1 hit.
[Graphical view ]
SMARTi SM00333. TUDOR. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Disruption of SMN function by ectopic expression of the human SMN gene in Drosophila."
    Miguel-Aliaga I., Chan Y.B., Davies K.E., van den Heuvel M.
    FEBS Lett. 486:99-102(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, DEVELOPMENTAL STAGE.
  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: Larva and Pupae.
  5. Cited for: FUNCTION, SUBUNIT, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-201 AND GLY-202.
  6. "Rpp20 interacts with SMN and is re-distributed into SMN granules in response to stress."
    Hua Y., Zhou J.
    Biochem. Biophys. Res. Commun. 314:268-276(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH RPP20.
  7. "The Sm-protein methyltransferase, dart5, is essential for germ-cell specification and maintenance."
    Gonsalvez G.B., Rajendra T.K., Tian L., Matera A.G.
    Curr. Biol. 16:1077-1089(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMB.
  8. Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  9. "A Drosophila melanogaster model of spinal muscular atrophy reveals a function for SMN in striated muscle."
    Rajendra T.K., Gonsalvez G.B., Walker M.P., Shpargel K.B., Salz H.K., Matera A.G.
    J. Cell Biol. 176:831-841(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, INTERACTION WITH ACTN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  10. "U bodies are cytoplasmic structures that contain uridine-rich small nuclear ribonucleoproteins and associate with P bodies."
    Liu J.L., Gall J.G.
    Proc. Natl. Acad. Sci. U.S.A. 104:11655-11659(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  11. Cited for: FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
  12. "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(2008) [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, INTERACTION WITH GEM3.
  13. "Sm protein methylation is dispensable for snRNP assembly in Drosophila melanogaster."
    Gonsalvez G.B., Praveen K., Hicks A.J., Tian L., Matera A.G.
    RNA 14:878-887(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SMD1.
  14. "The spinal muscular atrophy protein SMN affects Drosophila germline nuclear organization through the U body-P body pathway."
    Lee L., Davies S.E., Liu J.L.
    Dev. Biol. 332:142-155(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  15. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  16. "Survival motor neuron protein regulates stem cell division, proliferation, and differentiation in Drosophila."
    Grice S.J., Liu J.L.
    PLoS Genet. 7:E1002030-E1002030(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
  17. "Behavioral and electrophysiological outcomes of tissue-specific Smn knockdown in Drosophila melanogaster."
    Timmerman C., Sanyal S.
    Brain Res. 1489:66-80(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  18. "SMN is required for sensory-motor circuit function in Drosophila."
    Imlach W.L., Beck E.S., Choi B.J., Lotti F., Pellizzoni L., McCabe B.D.
    Cell 151:427-439(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  19. "An SMN-dependent U12 splicing event essential for motor circuit function."
    Lotti F., Imlach W.L., Saieva L., Beck E.S., Hao le T., Li D.K., Jiao W., Mentis G.Z., Beattie C.E., McCabe B.D., Pellizzoni L.
    Cell 151:440-454(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE.
  20. "A Drosophila model of spinal muscular atrophy uncouples snRNP biogenesis functions of survival motor neuron from locomotion and viability defects."
    Praveen K., Wen Y., Matera A.G.
    Cell Rep. 1:624-631(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, DISRUPTION PHENOTYPE, MUTAGENESIS OF ASP-20; PHE-70; TYR-203; THR-205 AND GLY-206.
  21. "Drosophila Zpr1 (Zinc finger protein 1) is required downstream of both EGFR and FGFR signaling in tracheal subcellular lumen formation."
    Ruiz O.E., Nikolova L.S., Metzstein M.M.
    PLoS ONE 7:E45649-E45649(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Identification and characterization of Drosophila Snurportin reveals a role for the import receptor Moleskin/Importin7 in snRNP biogenesis."
    Natalizio A.H., Matera A.G.
    Mol. Biol. Cell 24:2932-2942(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MSK AND SNUPN.
  23. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 1-122, FUNCTION, SUBUNIT.

Entry informationi

Entry nameiSMN_DROME
AccessioniPrimary (citable) accession number: Q9VV74
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 13, 2013
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 120 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