| Type |
Details |
Score |
| Publication |
| First Author: |
Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI) |
| Year: |
2010 |
| Journal: |
Database Download |
| Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Group |
| Year: |
2003 |
| Journal: |
Database Procedure |
| Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bairoch A |
| Year: |
1999 |
| Journal: |
Database Release |
| Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2005 |
|
| Title: |
Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics |
| Year: |
2010 |
| Journal: |
Database Release |
| Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2005 |
|
| Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mouse Genome Informatics Scientific Curators |
| Year: |
2009 |
| Journal: |
Database Download |
| Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform |
|
|
|
|
•
•
•
•
•
|
| UniProt Feature |
| Begin: |
1 |
| Description: |
Ribonuclease P/MRP protein subunit POP5 |
| Type: |
chain |
| End: |
169 |
|
•
•
•
•
•
|
| Gene |
| Type: |
gene |
| Organism: |
frog, African clawed |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry represents the Pop5 from eukaryotes and related proteins from archaea. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mattijssen S |
| Year: |
2010 |
| Journal: |
Wiley Interdiscip Rev RNA |
| Title: |
RNase MRP and disease. |
| Volume: |
1 |
| Issue: |
1 |
| Pages: |
102-16 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Walker SC |
| Year: |
2005 |
| Journal: |
Biochem Soc Trans |
| Title: |
Probing the structure of Saccharomyces cerevisiae RNase MRP. |
| Volume: |
33 |
| Issue: |
Pt 3 |
| Pages: |
479-81 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Marvin MC |
| Year: |
2011 |
| Journal: |
RNA |
| Title: |
Accumulation of noncoding RNA due to an RNase P defect in Saccharomyces cerevisiae. |
| Volume: |
17 |
| Issue: |
8 |
| Pages: |
1441-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Esakova O |
| Year: |
2010 |
| Journal: |
RNA |
| Title: |
Of proteins and RNA: the RNase P/MRP family. |
| Volume: |
16 |
| Issue: |
9 |
| Pages: |
1725-47 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bussey H |
| Year: |
1995 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The nucleotide sequence of chromosome I from Saccharomyces cerevisiae. |
| Volume: |
92 |
| Issue: |
9 |
| Pages: |
3809-13 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jarrous N |
| Year: |
1999 |
| Journal: |
RNA |
| Title: |
Rpp14 and Rpp29, two protein subunits of human ribonuclease P. |
| Volume: |
5 |
| Issue: |
2 |
| Pages: |
153-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gopalan V |
| Year: |
2018 |
| Journal: |
RNA |
| Title: |
Chance and necessity in the evolution of RNase P. |
| Volume: |
24 |
| Issue: |
1 |
| Pages: |
1-5 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
This superfamily contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2+-dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) [].Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].Proteins in this entry include Rnp2 (also known as Pop5) from archaea and Pop5/Rpp14 from humans. In eukaryotes Pop5 is a subunit of both the Rnp and MRP complexes. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].The structure of Rnp2 (ribonuclease P protein component 2) has a ferrodoxin-like fold composed of an α-β sandwich with antiparallel β-sheet and contains an extra C-terminal helix. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
150
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
51
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jarrous N |
| Year: |
2001 |
| Journal: |
RNA |
| Title: |
Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P. |
| Volume: |
7 |
| Issue: |
8 |
| Pages: |
1153-64 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cai T |
| Year: |
1999 |
| Journal: |
Mol Cell Biol |
| Title: |
Mutagenesis of SNM1, which encodes a protein component of the yeast RNase MRP, reveals a role for this ribonucleoprotein endoribonuclease in plasmid segregation. |
| Volume: |
19 |
| Issue: |
11 |
| Pages: |
7857-69 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Houser-Scott F |
| Year: |
2002 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P. |
| Volume: |
99 |
| Issue: |
5 |
| Pages: |
2684-9 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) [, ]. Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].This entry includes Rpp21 from animals, Snm1/Rpr2 from yeasts and RNP4 from archaea [, ]. Snm1 is a subunit of RNase MRP (mitochondrial RNA processing), a ribonucleoprotein endoribonuclease that has roles in both mitochondrial DNA replication and nuclear 5.8S rRNA processing. Snm1 is an RNA binding protein that binds the MRP RNA specifically []. This subunit possibly binds the precursor tRNA []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry contains ribonuclease P (Rnp) proteins from eukaryotes and archaea. Rnp is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) [, ]. Archaeal and eukaryotic RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis []. Human RNase P is composed of a singular protein Pop1 and three subcomplexes, the Rpp20-Rpp25 heterodimer, Pop5-Rpp14-(Rpp30)2-Rpp40 heteropentamer, and Rpp21-Rpp29-Rpp38 heterotrimer. Although both Pop5 and Rpp14 have similar protein structure, they share a very limited sequence similarity. Moreover, the C-terminal fragments after the conserved beta sheets in Pop5 and Rpp14 exhibit distinct structural features that mediate interactions with Pop1 and Rpp40, respectively [].In the hyperthermophilic archaeon Pyrococcus horikoshii OT3, RNase P is composed of the RNase P RNA (pRNA) and five proteins (PhoPop5, PhoRpp38, PhoRpp21, PhoRpp29, and PhoRpp30) [, ].Proteins in this entry include Rnp2 (also known as Pop5) from archaea and Pop5/Rpp14 from humans []. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
122
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lan P |
| Year: |
2018 |
| Journal: |
Science |
| Title: |
Structural insight into precursor tRNA processing by yeast ribonuclease P. |
| Volume: |
362 |
| Issue: |
6415 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Terada A |
| Year: |
2006 |
| Journal: |
J Biochem |
| Title: |
Characterization of the archaeal ribonuclease P proteins from Pyrococcus horikoshii OT3. |
| Volume: |
140 |
| Issue: |
2 |
| Pages: |
293-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kimura M |
| Year: |
2017 |
| Journal: |
Biosci Biotechnol Biochem |
| Title: |
Structural basis for activation of an archaeal ribonuclease P RNA by protein cofactors. |
| Volume: |
81 |
| Issue: |
9 |
| Pages: |
1670-1680 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Pop8 is a component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. It is also a component of Ribonuclease MRP, which cleaves pre-rRNA sequences []. Ribonuclease P consists of an RNA moiety and at least 9 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RPP1 and RPR2. Ribonuclease MRP complex consists of an RNA moiety and at least 10 protein subunits including POP1, POP3, POP4, POP5, POP6, POP7, POP8, RMP1, RPP1 and SNM1, many of which are shared with the Ribonuclease P complex. This protein is found at the nucleus. Pop8 interacts with Pop5 and RPP1 to form the Pop5-Pop8-(RPP1)2 heterotetramer, which is part of thearm module of the p[protein hook []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chamberlain JR |
| Year: |
1998 |
| Journal: |
Genes Dev |
| Title: |
Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. |
| Volume: |
12 |
| Issue: |
11 |
| Pages: |
1678-90 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Homologous_superfamily |
| Description: |
Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].This entry includes p29 subunit (also known as Rpp29 or Pop4) of the Ribonuclease P complex []. Its homologues from eukaryotes are also a subunit of the RNase MRP complex. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured β-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex []. Rpp29 () catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Boomershine WP |
| Year: |
2003 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P. |
| Volume: |
100 |
| Issue: |
26 |
| Pages: |
15398-403 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sidote DJ |
| Year: |
2004 |
| Journal: |
Biochemistry |
| Title: |
Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus. |
| Volume: |
43 |
| Issue: |
44 |
| Pages: |
14128-38 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry represents the p29 subunit (also known as Rpp29 or Pop4) of the related ribonucleoproteins ribonuclease (RNase) P and RNase MRP from eukaryotes []. Rpp29 has a conserved C-terminal domain with an Sm-like fold []. Rpp29 () catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
221
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
van Eenennaam H |
| Year: |
1999 |
| Journal: |
Nucleic Acids Res |
| Title: |
hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes. |
| Volume: |
27 |
| Issue: |
12 |
| Pages: |
2465-72 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Ribonuclease P (Rnp) is a ubiquitous ribozyme that catalyzes a Mg2 -dependent hydrolysis to remove the 5'-leader sequence of precursor tRNA (pre-tRNA) in all three domains of life []. In bacteria, the catalytic RNA (typically ~120kDa) is aided by a small protein cofactor (~14kDa) []. Archaeal and eukaryote RNase P consist of a single RNA and archaeal RNase P has four or five proteins, while eukaryotic RNase P consists of 9 or 10 proteins. Eukaryotic and archaeal RNase P RNAs cooperatively function with protein subunits in catalysis [].Eukaryotic nuclear RNase P shares most of its protein components with another essential RNP enzyme, nucleolar RNase MRP []. RNase MRP (mitochondrial RNA processing) is an rRNA processing enzyme that cleaves various RNAs, including ribosomal, messenger, and mitochondrial RNAs. It can cleave a specific site within precursor rRNA to generate the mature 5'-end of 5.8S rRNA []. Despite its name, the vast majority of RNase MRP is localized in the nucleolus []. RNase MRP has been shown to cleave primers for mitochondrial DNA replication and CLB2 mRNA. In yeast, RNase MRP possesses one putatively catalytic RNA and at least 9 protein subunits (Pop1, Pop3-Pop8, Rpp1, Snm1 and Rmp1) []. Human RNase MRP complex consists of 267 nucleotides and supports the interaction with and among at least seven protein components: hPop1, hPop5, Rpp20, Rpp25, Rpp30, Rpp38, and Rpp40) and three additional proteins, hPop4, Rpp21 and Rpp14, have been reported to be associated with at least a subset of RNase MRP complexes [].This entry includes p29 subunit (also known as Rpp29 or Pop4) of the Ribonuclease P complex []. Its homologues from eukaryotes are also a subunit of the RNase MRP complex. The structure of the RNase P subunit, Rpp29, from Methanobacterium thermoautotrophicum has been determined. Mth Rpp29 is a member of the oligonucleotide/oligosaccharide binding fold family. It contains a structured β-barrel core and unstructured N- and C-terminal extensions bearing several highly conserved amino acid residues that could be involved in RNA contacts in the protein-RNA complex []. Rpp29 () catalyses the endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. It interacts with the Rpp25 and Pop5 subunits. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Carninci P |
| Year: |
2005 |
| Journal: |
Science |
| Title: |
The transcriptional landscape of the mammalian genome. |
| Volume: |
309 |
| Issue: |
5740 |
| Pages: |
1559-63 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gerhard DS |
| Year: |
2004 |
| Journal: |
Genome Res |
| Title: |
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |
| Volume: |
14 |
| Issue: |
10B |
| Pages: |
2121-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Huttlin EL |
| Year: |
2010 |
| Journal: |
Cell |
| Title: |
A tissue-specific atlas of mouse protein phosphorylation and expression. |
| Volume: |
143 |
| Issue: |
7 |
| Pages: |
1174-89 |
|
•
•
•
•
•
|
