pop5 POP5 homolog, ribonuclease P/MRP subunit [Danio rerio (zebrafish)] - Gene

Summary

Official Symbol: pop5provided by ZNC
Official Full Name: POP5 homolog, ribonuclease P/MRP subunitprovided by ZNC
Primary source: ZFIN:ZDB-GENE-050320-123
See related: Ensembl:ENSDARG00000053452 AllianceGenome:ZFIN:ZDB-GENE-050320-123
Gene type: protein coding
RefSeq status: PROVISIONAL
Organism: Danio rerio
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes; Danionidae; Danioninae; Danio
Also known as: fc69d03; wu:fc69d03; wu:fy24c05; zgc:110616
Summary: Predicted to enable ribonuclease P RNA binding activity. Predicted to contribute to ribonuclease P activity. Predicted to be involved in rRNA processing and tRNA 5'-leader removal. Predicted to be located in nucleolus. Predicted to be part of nucleolar ribonuclease P complex and ribonuclease MRP complex. Orthologous to human POP5 (POP5 homolog, ribonuclease P/MRP subunit). [provided by Alliance of Genome Resources, Nov 2024]
Orthologs: human mouse all
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Genomic context

Location:: chromosome: 8

Exon count:: 5

Annotation release	Status	Assembly	Chr	Location
RS_2024_08	current	GRCz11 (GCF_000002035.6)	8	NC_007119.7 (41274208..41279294, complement)
105	previous assembly	GRCz10 (GCF_000002035.5)	8	NC_007119.6 (41266575..41271661, complement)

Chromosome 8 - NC_007119.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
Description: Sequencing the Zebrafish transcriptome from a range of tissues and developmental stages
BioProject: PRJEB1986
Analysis date: Fri Dec 8 19:48:10 2017

Bibliography

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GeneRIFs: Gene References Into Functions

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General gene information

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Gene Ontology Provided by ZFIN

Function	Evidence Code	Pubs
enables ribonuclease P RNA binding	IEA Inferred from Electronic Annotation more info
enables ribonuclease P RNA binding	ISS Inferred from Sequence or Structural Similarity more info
contributes_to ribonuclease P activity	ISS Inferred from Sequence or Structural Similarity more info

Process	Evidence Code	Pubs
involved_in rRNA processing	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within rRNA processing	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within tRNA 5'-leader removal	IEA Inferred from Electronic Annotation more info
involved_in tRNA 5'-leader removal	ISS Inferred from Sequence or Structural Similarity more info
involved_in tRNA processing	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within tRNA processing	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
part_of multimeric ribonuclease P complex	ISS Inferred from Sequence or Structural Similarity more info
part_of nucleolar ribonuclease P complex	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleolus	ISS Inferred from Sequence or Structural Similarity more info
located_in nucleus	IEA Inferred from Electronic Annotation more info
part_of ribonuclease MRP complex	IBA Inferred from Biological aspect of Ancestor more info
part_of ribonuclease P complex	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: ribonuclease P/MRP protein subunit POP5

Names: processing of precursor 5, ribonuclease P/MRP subunit

NP_001013566.1

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.