Version 5.4
Mus musculus Protein: Mettl11b
Summary
InnateDB Protein IDBP-535342.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol Mettl11b
Protein Name methyltransferase like 11B
Synonyms
Species Mus musculus
Ensembl Protein ENSMUSP00000124211
InnateDB Gene IDBG-202146 (Mettl11b)
Protein Structure
UniProt Annotation
Function Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]- Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. May activate NTMT1 by priming its substrates for trimethylation (By similarity). {ECO:0000250}.
Subcellular Localization Nucleus {ECO:0000250}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 0 experimentally validated interaction(s) in this database.
Gene Ontology

Molecular Function
Accession GO Term
GO:0003674 molecular_function
GO:0008168 methyltransferase activity
Biological Process
GO:0008150 biological_process
GO:0032259 methylation
Cellular Component
GO:0005575 cellular_component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:2685053
InterPro IPR008576 Protein of unknown function DUF858, methyltransferase-like
IPR029063 S-adenosyl-L-methionine-dependent methyltransferase-like
PFAM PF05891
PRINTS
PIRSF PIRSF016958
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt B2RXM4
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 240879
UniGene Mm.484621
RefSeq NP_001137428
MGI ID
MGI Symbol Mettl11b
OMIM
CCDS CCDS48420
HPRD
IMGT
EMBL BC157906 BC158115 BC172048 CH466520
GenPept AAI57907 AAI58116 AAI72048 EDL39274

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