Version 5.4
Homo sapiens Protein: POP4
Summary
InnateDB Protein IDBP-41734.6
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol POP4
Protein Name processing of precursor 4, ribonuclease P/MRP subunit (S. cerevisiae)
Synonyms RPP29;
Species Homo sapiens
Ensembl Protein ENSP00000221770
InnateDB Gene IDBG-41732 (POP4)
Protein Structure
UniProt Annotation
Function Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P.
Subcellular Localization Nucleus, nucleolus {ECO:0000269PubMed:10352175}.
Disease Associations
Tissue Specificity
Comments
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 10 experimentally validated interaction(s) in this database.
Experimentally validated
Total 10 [view]
Protein-Protein 8 [view]
Protein-DNA 0
Protein-RNA 2 [view]
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Gene Ontology

Molecular Function
Accession GO Term
GO:0003723 RNA binding
GO:0004540 ribonuclease activity
Biological Process
GO:0006364 rRNA processing
GO:0006379 mRNA cleavage
GO:0008033 tRNA processing
Cellular Component
GO:0000172 ribonuclease MRP complex
GO:0030677 ribonuclease P complex
Protein Structure and Domains
PDB ID
InterPro IPR002730 Ribonuclease P/MRP, subunit p29
IPR023534 Rof/RNase P-like
PFAM PF01868
PRINTS
PIRSF
SMART SM00538
TIGRFAMs
Post-translational Modifications
Modification
Cross-References
SwissProt
PhosphoSite PhosphoSite-O95707
TrEMBL
UniProt Splice Variant
Entrez Gene 10775
UniGene Hs.715732
RefSeq
HUGO HGNC:30081
OMIM 606114
CCDS
HPRD 09358
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