Version 5.4
Homo sapiens Protein: RPP30
Summary
InnateDB Protein IDBP-82159.5
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol RPP30
Protein Name ribonuclease P/MRP 30kDa subunit
Synonyms TSG15;
Species Homo sapiens
Ensembl Protein ENSP00000360768
InnateDB Gene IDBG-82153 (RPP30)
Protein Structure
UniProt Annotation
Function Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization Nucleus, nucleolus {ECO:0000305}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 21 experimentally validated interaction(s) in this database.
Experimentally validated
Total 21 [view]
Protein-Protein 21 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003824 catalytic activity
GO:0004526 ribonuclease P activity
GO:0004540 ribonuclease activity
GO:0044822 poly(A) RNA binding
Biological Process
GO:0008033 tRNA processing
GO:0090501 RNA phosphodiester bond hydrolysis
GO:0090502 RNA phosphodiester bond hydrolysis, endonucleolytic
Cellular Component
GO:0005634 nucleus
GO:0005655 nucleolar ribonuclease P complex
Protein Structure and Domains
PDB ID
InterPro IPR002738 RNase P subunit p30
IPR016195 Polymerase/histidinol phosphatase-like
PFAM PF01876
PRINTS
PIRSF
SMART
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt P78346
PhosphoSite PhosphoSite-P78346
TrEMBL
UniProt Splice Variant
Entrez Gene 10556
UniGene Hs.613824
RefSeq NP_006404
HUGO HGNC:17688
OMIM 606115
CCDS CCDS7411
HPRD 09359
IMGT
EMBL AK225532 AK312900 AL590622 BC006991 CH471066 U77665
GenPept AAC51143 AAH06991 BAG35746 CAC70100 EAW50117

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