RPP25 ribonuclease P and MRP subunit p25 [Homo sapiens (human)] - Gene

Summary

Official Symbol: RPP25provided by HGNC
Official Full Name: ribonuclease P and MRP subunit p25provided by HGNC
Primary source: HGNC:HGNC:30361
See related: Ensembl:ENSG00000178718 MIM:619235; AllianceGenome:HGNC:30361
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Homo sapiens
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Summary: Enables ribonuclease P RNA binding activity. Contributes to ribonuclease P activity. Involved in tRNA 5'-leader removal. Located in centriolar satellite and nucleoplasm. Part of multimeric ribonuclease P complex and ribonuclease MRP complex. Biomarker of autistic disorder. [provided by Alliance of Genome Resources, Apr 2022]
Orthologs: mouse all
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Genomic context

Location:: 15q24.2

Exon count:: 1

Annotation release	Status	Assembly	Chr	Location
RS_2023_03	current	GRCh38.p14 (GCF_000001405.40)	15	NC_000015.10 (74954418..74956772, complement)
RS_2023_03	current	T2T-CHM13v2.0 (GCF_009914755.1)	15	NC_060939.1 (72824301..72826655, complement)
105.20220307	previous assembly	GRCh37.p13 (GCF_000001405.25)	15	NC_000015.9 (75246759..75249113, complement)

Chromosome 15 - NC_000015.10 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Crystal structure of human RPP20-RPP25 proteins in complex with the P3 domain of lncRNA RMRP.
Title: Crystal structure of human RPP20-RPP25 proteins in complex with the P3 domain of lncRNA RMRP.
LINC00319 promotes migration, invasion and epithelial-mesenchymal transition process in cervical cancer by regulating miR-3127-5p/RPP25 axis.
Title: LINC00319 promotes migration, invasion and epithelial-mesenchymal transition process in cervical cancer by regulating miR-3127-5p/RPP25 axis.
Study showed the crystal structure of Rpp20/Rpp25 complex, and confirmed that Rpp20 and Rpp25 exhibit similar molecular structures to one another, to their yeast homologs (Pop7 andPop6, respectively), and to archaeal Alba proteins. These proteins do not seem to undergo significant conformational change upon RNA binding, suggesting that they interact with their cognate RNAs via a pre-formed binding surface.
Title: Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.
Rpp25 is a major target of autoantibodies to the Th/To autoantigen complex
Title: Rpp25 is a major target of autoantibodies to the Th/To complex as measured by a novel chemiluminescent assay.
Taken together, these findings suggest a potential role for the RPP25 gene transcript in the neurobiology of developmental brain disorders.
Title: RPP25 is developmentally regulated in prefrontal cortex and expressed at decreased levels in autism spectrum disorder.
analyses of interactions with deletion mutant proteins indicate that the Alba-type core domain of both Rpp20 and Rpp25 contains most of the determinants for mutual association and P3 RNA recognition.
Title: Heterodimerization of the human RNase P/MRP subunits Rpp20 and Rpp25 is a prerequisite for interaction with the P3 arm of RNase MRP RNA.

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Phenotypes

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Find tests for this gene in the NIH Genetic Testing Registry (GTR)

Review eQTL and phenotype association data in this region using PheGenI

Variation

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See variants in ClinVar

See studies and variants in dbVar

See Variation Viewer (GRCh37.p13)

See Variation Viewer (GRCh38)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

D15S1180 (e-PCR)
- UniSTS:58179

D15S1353 (e-PCR)
- UniSTS:44495

Gene Ontology Provided by GOA

Function	Evidence Code	Pubs
enables RNA binding	HDA more info	PubMed
enables RNA binding	IBA Inferred from Biological aspect of Ancestor more info	PubMed
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables ribonuclease P RNA binding	IDA Inferred from Direct Assay more info	PubMed
contributes_to ribonuclease P activity	IDA Inferred from Direct Assay more info	PubMed

Process	Evidence Code	Pubs
involved_in RNA phosphodiester bond hydrolysis, endonucleolytic	IEA Inferred from Electronic Annotation more info
involved_in rRNA processing	IEA Inferred from Electronic Annotation more info
involved_in tRNA 5'-leader removal	IBA Inferred from Biological aspect of Ancestor more info	PubMed
involved_in tRNA 5'-leader removal	IDA Inferred from Direct Assay more info	PubMed

Component	Evidence Code	Pubs
located_in centriolar satellite	IDA Inferred from Direct Assay more info
part_of multimeric ribonuclease P complex	IDA Inferred from Direct Assay more info	PubMed
located_in nucleolus	IEA Inferred from Electronic Annotation more info
located_in nucleoplasm	IDA Inferred from Direct Assay more info
located_in nucleoplasm	TAS Traceable Author Statement more info
part_of ribonuclease MRP complex	IBA Inferred from Biological aspect of Ancestor more info	PubMed
part_of ribonuclease MRP complex	IDA Inferred from Direct Assay more info	PubMed

General protein information

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Preferred Names: ribonuclease P protein subunit p25

Names: RNase P protein subunit p25; ribonuclease P 25kDa subunit; ribonuclease P/MRP 25kDa subunit; ribonuclease P/MRP subunit p25

NP_060263.2

EC 3.1.26.5

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.