Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Ribosome maturation protein SDO1

Gene

SDO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the biogenesis of the 60S ribosomal subunit and translational activation of ribosomes. Together with the EF-2-like GTPase RIA1, may trigger the GTP-dependent release of TIF6 from 60S pre-ribosomes in the cytoplasm, thereby activating ribosomes for translation competence by allowing 80S ribosome assembly and facilitating TIF6 recycling to the nucleus, where it is required for 60S rRNA processing and nuclear export.2 Publications

GO - Molecular functioni

  • guanyl-nucleotide exchange factor activity Source: SGD

GO - Biological processi

  • mature ribosome assembly Source: SGD
  • positive regulation of GTPase activity Source: GOC
Complete GO annotation...

Keywords - Biological processi

Ribosome biogenesis

Enzyme and pathway databases

BioCyciYEAST:G3O-32183-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ribosome maturation protein SDO1
Gene namesi
Name:SDO1
Ordered Locus Names:YLR022C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XII

Organism-specific databases

EuPathDBiFungiDB:YLR022C.
SGDiS000004012. SDO1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311C → W: Impairs protein folding and stability. Loss of function. 1 Publication
Mutagenesisi34 – 341N → I: Impairs protein folding and stability. Loss of function. 1 Publication
Mutagenesisi71 – 711L → P: Impairs protein folding and stability. Loss of function. 1 Publication

Chemistry

ChEMBLiCHEMBL1741198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 250250Ribosome maturation protein SDO1PRO_0000123764Add
BLAST

Proteomic databases

MaxQBiQ07953.
PeptideAtlasiQ07953.

Interactioni

Subunit structurei

Associates with the 60S ribosomal subunit.

Protein-protein interaction databases

BioGridi31296. 120 interactions.
IntActiQ07953. 16 interactions.
MINTiMINT-2492507.

Structurei

3D structure databases

ProteinModelPortaliQ07953.
SMRiQ07953. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SDO1/SBDS family.Curated

Phylogenomic databases

GeneTreeiENSGT00390000008135.
HOGENOMiHOG000216685.
InParanoidiQ07953.
KOiK14574.
OMAiCTGLIDP.
OrthoDBiEOG7XSTS6.

Family and domain databases

Gene3Di3.30.1250.10. 1 hit.
InterProiIPR018978. Ribosome_mat_SBDS_C.
IPR018023. Ribosome_mat_SBDS_CS.
IPR019783. Ribosome_mat_SBDS_N.
IPR002140. Sdo1/SBDS.
[Graphical view]
PANTHERiPTHR10927:SF1. PTHR10927:SF1. 1 hit.
PfamiPF01172. SBDS. 1 hit.
PF09377. SBDS_C. 1 hit.
[Graphical view]
SUPFAMiSSF89895. SSF89895. 1 hit.
TIGRFAMsiTIGR00291. RNA_SBDS. 1 hit.
PROSITEiPS01267. UPF0023. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q07953-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPINQPSGQI KLTNVSLVRL KKARKRFEVA CYQNKVQDYR KGIEKDLDEV
60 70 80 90 100
LQIHQVFMNV SKGLVANKED LQKCFGTTNV DDVIEEIMHK GEIQLSEKER
110 120 130 140 150
QLMLNKVNNE MLTIVSAKCI NPVSKKRYPP TMIHKALQEL KFSPVINKPA
160 170 180 190 200
KLQALEAIKL LVSKQIIPIV RAKMKVKVAI SEPSRQPELI EKISKLIASS
210 220 230 240 250
PGESTKPELD PWTCTGLIDP VNYRDLMTLC DKKGTVQVLD MAVIDNTTHN
Length:250
Mass (Da):28,283
Last modified:November 1, 1996 - v1
Checksum:iEFC799ADEFF73E0E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73194 Genomic DNA. Translation: CAA97545.1.
BK006945 Genomic DNA. Translation: DAA09340.1.
PIRiS64849.
RefSeqiNP_013122.1. NM_001181909.1.

Genome annotation databases

EnsemblFungiiYLR022C; YLR022C; YLR022C.
GeneIDi850709.
KEGGisce:YLR022C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z73194 Genomic DNA. Translation: CAA97545.1.
BK006945 Genomic DNA. Translation: DAA09340.1.
PIRiS64849.
RefSeqiNP_013122.1. NM_001181909.1.

3D structure databases

ProteinModelPortaliQ07953.
SMRiQ07953. Positions 1-245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31296. 120 interactions.
IntActiQ07953. 16 interactions.
MINTiMINT-2492507.

Chemistry

ChEMBLiCHEMBL1741198.

Proteomic databases

MaxQBiQ07953.
PeptideAtlasiQ07953.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYLR022C; YLR022C; YLR022C.
GeneIDi850709.
KEGGisce:YLR022C.

Organism-specific databases

EuPathDBiFungiDB:YLR022C.
SGDiS000004012. SDO1.

Phylogenomic databases

GeneTreeiENSGT00390000008135.
HOGENOMiHOG000216685.
InParanoidiQ07953.
KOiK14574.
OMAiCTGLIDP.
OrthoDBiEOG7XSTS6.

Enzyme and pathway databases

BioCyciYEAST:G3O-32183-MONOMER.

Miscellaneous databases

NextBioi966763.
PROiQ07953.

Family and domain databases

Gene3Di3.30.1250.10. 1 hit.
InterProiIPR018978. Ribosome_mat_SBDS_C.
IPR018023. Ribosome_mat_SBDS_CS.
IPR019783. Ribosome_mat_SBDS_N.
IPR002140. Sdo1/SBDS.
[Graphical view]
PANTHERiPTHR10927:SF1. PTHR10927:SF1. 1 hit.
PfamiPF01172. SBDS. 1 hit.
PF09377. SBDS_C. 1 hit.
[Graphical view]
SUPFAMiSSF89895. SSF89895. 1 hit.
TIGRFAMsiTIGR00291. RNA_SBDS. 1 hit.
PROSITEiPS01267. UPF0023. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
    Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
    , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
    Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  2. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  5. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  6. Cited for: ASSOCIATION WITH 60S RIBOSOMAL SUBUNITS.
  7. "Structural and mutational analysis of the SBDS protein family. Insight into the leukemia-associated Shwachman-Diamond Syndrome."
    Shammas C., Menne T.F., Hilcenko C., Michell S.R., Goyenechea B., Boocock G.R.B., Durie P.R., Rommens J.M., Warren A.J.
    J. Biol. Chem. 280:19221-19229(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-31; ASN-34 AND LEU-71.
  8. "The Shwachman-Bodian-Diamond syndrome protein mediates translational activation of ribosomes in yeast."
    Menne T.F., Goyenechea B., Sanchez-Puig N., Wong C.C., Tonkin L.M., Ancliff P.J., Brost R.L., Costanzo M., Boone C., Warren A.J.
    Nat. Genet. 39:486-495(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. "Distinct ribosome maturation defects in yeast models of Diamond-Blackfan anemia and Shwachman-Diamond syndrome."
    Moore J.B. IV, Farrar J.E., Arceci R.J., Liu J.M., Ellis S.R.
    Haematologica 95:57-64(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSDO1_YEAST
AccessioniPrimary (citable) accession number: Q07953
Secondary accession number(s): D6VY24
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: May 11, 2016
This is version 123 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 5060 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XII
    Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

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.