Version 5.4
Homo sapiens Protein: URM1
Summary
InnateDB Protein IDBP-87988.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol URM1
Protein Name ubiquitin related modifier 1
Synonyms
Species Homo sapiens
Ensembl Protein ENSP00000361941
InnateDB Gene IDBG-87984 (URM1)
Protein Structure
UniProt Annotation
Function Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2- thiolation reaction by being thiocarboxylated (-COSH) at its C- terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as MOCS3, ATPBD3, CTU2, USP15 and CAS. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates. {ECO:0000255HAMAP- Rule:MF_03048, ECO:0000269PubMed:19017811, ECO:0000269PubMed:21209336}.
Subcellular Localization Cytoplasm.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 38 experimentally validated interaction(s) in this database.
Experimentally validated
Total 38 [view]
Protein-Protein 38 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
Biological Process
GO:0034227 tRNA thio-modification
Cellular Component
GO:0005737 cytoplasm
Protein Structure and Domains
PDB ID
InterPro IPR015221 Ubiquitin-related modifier 1
IPR016155 Molybdopterin synthase/thiamin biosynthesis sulphur carrier, beta-grasp
PFAM PF09138
PRINTS
PIRSF PIRSF037379
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-
TrEMBL
UniProt Splice Variant
Entrez Gene 81605
UniGene Hs.495229
RefSeq NP_001252511
HUGO HGNC:28378
OMIM 612693
CCDS CCDS59148
HPRD 12976
IMGT
EMBL
GenPept

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