Version 5.4
Mus musculus Protein: AA960436
Summary
InnateDB Protein IDBP-183667.7
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol AA960436
Protein Name expressed sequence AA960436
Synonyms AA960436;
Species Mus musculus
Ensembl Protein ENSMUSP00000034245
InnateDB Gene IDBG-183665 (AA960436)
Protein Structure
UniProt Annotation
Function Phosphodiesterase responsible for the U6 snRNA 3' end processing. Acts as an exoribonuclease (RNase) responsible for trimming the poly(U) tract of the last nucleotides in the pre-U6 snRNA molecule, leading to the formation of mature U6 snRNA 3' end-terminated with a 2',3'-cyclic phosphate. {ECO:0000255HAMAP- Rule:MF_03040}.
Subcellular Localization Nucleus {ECO:0000255HAMAP-Rule:MF_03040}.
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.
They are also associated with 4 interaction(s) predicted by orthology.
Predicted by orthology
Total 4 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0000175 3'-5'-exoribonuclease activity
GO:0003824 catalytic activity
GO:0004518 nuclease activity
Biological Process
GO:0006397 mRNA processing
GO:0008380 RNA splicing
GO:0034477 U6 snRNA 3'-end processing
GO:0090503 RNA phosphodiester bond hydrolysis, exonucleolytic
Cellular Component
GO:0005634 nucleus
Protein Structure and Domains
PDB ID MGI:2142454
InterPro IPR009097 RNA ligase/cyclic nucleotide phosphodiesterase
IPR027521 U6 snRNA phosphodiesterase Usb1
PFAM PF09749
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt Q91W78
PhosphoSite PhosphoSite-Q91W78
TrEMBL D3Z5I2
UniProt Splice Variant
Entrez Gene 101985
UniGene Mm.394399
RefSeq NP_598715
MGI ID
MGI Symbol Usb1
OMIM
CCDS CCDS22560
HPRD
IMGT
EMBL AC165414 AK135527 AK160901 AK168683 BC016418
GenPept AAH16418 BAE22567 BAE36080 BAE40531

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