Version 5.4
Mus musculus Protein: Emg1
Summary
InnateDB Protein IDBP-187462.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Emg1
Protein Name EMG1 nucleolar protein homolog (S. cerevisiae)
Synonyms C2f; Grcc2f;
Species Mus musculus
Ensembl Protein ENSMUSP00000004379
InnateDB Gene IDBG-187460 (Emg1)
Protein Structure
UniProt Annotation
Function Involved in 40S ribosomal subunit biogenesis and 18S rRNA processing. Specifically catalyzes the N1-methylation of the pseudouridine corresponding to position 1248 in human 18S rRNA. Thus, appears to be the methyltransferase involved in the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3- carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus, nucleolus {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 1 experimentally validated interaction(s) in this database.
Experimentally validated
Total 1 [view]
Protein-Protein 1 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0008168 methyltransferase activity
GO:0019843 rRNA binding
GO:0070037 rRNA (pseudouridine) methyltransferase activity
Biological Process
GO:0001824 blastocyst development
GO:0017126 nucleologenesis
GO:0031167 rRNA methylation
Cellular Component
GO:0005575 cellular_component
GO:0005730 nucleolus
Protein Structure and Domains
PDB ID MGI:1315195
InterPro IPR005304 Ribosomal biogenesis, methyltransferase, EMG1/NEP1
PFAM PF03587
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt O35130
PhosphoSite PhosphoSite-O35130
TrEMBL Q542P8
UniProt Splice Variant
Entrez Gene 14791
UniGene Mm.6390
RefSeq NP_038564
MGI ID
MGI Symbol Emg1
OMIM
CCDS CCDS20524
HPRD
IMGT
EMBL AC002397 AK081757 BC002004 CH466523
GenPept AAC36006 AAH02004 BAC38322 EDK99747

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca