|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 101 to 179 out of 179 for Nhp2

<< First    < Previous  |  Next >    Last >>
0.039s

Categories

Hits by Pathway

Hits by Category

Hits by Strain

Type Details Score
Allele
Nhp2<Gt(E043B06)Wrst> | MGI:3894219
 
Name: NHP2 ribonucleoprotein; gene trap E043B06, German Gene Trap Consortium
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(AE0770)Wtsi> | MGI:4338134
 
Name: NHP2 ribonucleoprotein; gene trap AE0770, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(AE0771)Wtsi> | MGI:4338135
 
Name: NHP2 ribonucleoprotein; gene trap AE0771, Wellcome Trust Sanger Institute
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<tm1a(KOMP)Wtsi> | MGI:4362251
Name: NHP2 ribonucleoprotein; targeted mutation 1a, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Conditional ready, Null/knockout, Reporter
•
•
•
•
•
Allele
Nhp2<tm1e(KOMP)Wtsi> | MGI:4364446
Name: NHP2 ribonucleoprotein; targeted mutation 1e, Wellcome Trust Sanger Institute
Allele Type: Targeted
Attribute String: Null/knockout, Reporter
•
•
•
•
•
Allele
Nhp2<Gt(EUCE0210a06)Hmgu> | MGI:4370056
 
Name: NHP2 ribonucleoprotein; gene trap EUCE0210a06, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(EUCE0057g08)Hmgu> | MGI:4372904
 
Name: NHP2 ribonucleoprotein; gene trap EUCE0057g08, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(EUCE00145c05)Hmgu> | MGI:4388059
 
Name: NHP2 ribonucleoprotein; gene trap EUCE00145c05, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(EUCE0084b10)Hmgu> | MGI:4392305
 
Name: NHP2 ribonucleoprotein; gene trap EUCE0084b10, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(EUCJ0010c03)Hmgu> | MGI:4869792
 
Name: NHP2 ribonucleoprotein; gene trap EUCJ0010c03, Helmholtz Zentrum Muenchen GmbH
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<em1Gpt> | MGI:7303025
Name: NHP2 ribonucleoprotein; endonuclease-mediated mutation 1, GemPharmatech Co., Ltd
Allele Type: Endonuclease-mediated
Attribute String: Conditional ready, No functional change
•
•
•
•
•
Strain
MGI:5557936 | C57BL/6NTac-Nhp2<tm1a(KOMP)Wtsi>/WtsiH
Attribute String: coisogenic, targeted mutation, mutant strain
•
•
•
•
•
Strain
MGI:6346735 | C57BL/6N-Nhp2<tm1a(KOMP)Wtsi>/Mmucd
Attribute String: mutant strain, coisogenic, targeted mutation
•
•
•
•
•
Strain
MGI:5608162 | C57BL/6N-Nhp2<tm1a(KOMP)Wtsi>/Wtsi
Attribute String: coisogenic, targeted mutation
•
•
•
•
•
Allele
Nhp2<Gt(IST13147F12)Tigm> | MGI:5153075
 
Name: NHP2 ribonucleoprotein; gene trap IST13147F12, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13356G1)Tigm> | MGI:5159116
 
Name: NHP2 ribonucleoprotein; gene trap IST13356G1, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13532H8)Tigm> | MGI:5174922
 
Name: NHP2 ribonucleoprotein; gene trap IST13532H8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13626D3)Tigm> | MGI:5177905
 
Name: NHP2 ribonucleoprotein; gene trap IST13626D3, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13753E7)Tigm> | MGI:5189173
 
Name: NHP2 ribonucleoprotein; gene trap IST13753E7, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13773C8)Tigm> | MGI:5193357
 
Name: NHP2 ribonucleoprotein; gene trap IST13773C8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13854F8)Tigm> | MGI:5196287
 
Name: NHP2 ribonucleoprotein; gene trap IST13854F8, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST13968C4)Tigm> | MGI:5200074
 
Name: NHP2 ribonucleoprotein; gene trap IST13968C4, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST14205G6)Tigm> | MGI:5213543
 
Name: NHP2 ribonucleoprotein; gene trap IST14205G6, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Allele
Nhp2<Gt(IST14525B5)Tigm> | MGI:5237588
 
Name: NHP2 ribonucleoprotein; gene trap IST14525B5, Texas A&M Institute for Genomic Medicine
Allele Type: Gene trapped
•
•
•
•
•
Genotype
Genotype
Symbol: Nhp2/Nhp2
Background: C57BL/6N-Nhp2/Wtsi
Zygosity: hm
Has Mutant Allele: true
•
•
•
•
•
Genotype
Genotype
Symbol: Nhp2/Nhp2<+>
Background: C57BL/6N-Nhp2/Wtsi
Zygosity: ht
Has Mutant Allele: true
•
•
•
•
•
Protein Coding Gene
MGI:893586 | Snu13
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Allele
Tg(Nhp2-EGFP)HS231Gsat | MGI:4847259
Name: transgene insertion HS231, GENSAT Project at Rockefeller University
Allele Type: Transgenic
Attribute String: Reporter
•
•
•
•
•
Strain
MGI:5003724 | STOCK Tg(Nhp2-EGFP)HS231Gsat/Mmucd
Attribute String: mutant stock, transgenic
•
•
•
•
•
Publication
18473479 | -
First Author: Reichow SL
Year: 2008
Journal: Biochemistry
Title: Nop10 is a conserved H/ACA snoRNP molecular adaptor.
Volume: 47
Issue: 23
Pages: 6148-56
•
•
•
•
•
Protein Domain
IPR023532 | Nop10_arc-typ
Type: Family
Description: Nop10 is a component of the small nucleolar ribonucleoprotein particles containing H/ACA-type snoRNAs (H/ACA snoRNPs). H/ACA snoRNPs are primarily responsible for catalysing the isomerisation of uridine to pseudouridine (Psi) in ribosomal and other cellular RNAs. The protein component of the H/ACA snoRNP consists of Cbf5, Gar1, Nhp2 and Nop10. The complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind. Nop10 has an essential role in the assembly and activity of these particles and binds directly to the Cbf5 to form the minimal active enzyme in archaea. The complex interacts with snoRNAs, Nop10 acting as a molecular adaptor for guiding snoRNP assembly [].
•
•
•
•
•
Publication
33852194 | J:307419
First Author: Ryu H
Year: 2021
Journal: EMBO Rep
Title: The deubiquitinase USP36 promotes snoRNP group SUMOylation and is essential for ribosome biogenesis.
Volume: 22
Issue: 6
Pages: e50684
•
•
•
•
•
Protein Domain
IPR036756 | H/ACA_rnp_Nop10_sf
Type: Homologous_superfamily
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].In eukaryotes Nop10 is a nucleolar protein that is specifically associated with H/ACA snoRNAs. It is essential for normal 18S rRNA production and rRNA pseudouridylation by the ribonucleoprotein particles containing H/ACA snoRNAs (H/ACA snoRNPs). Nop10 is probably necessary for the stability of these RNPs []. The Nop10 domain structure has a rubredoxin-like fold.
•
•
•
•
•
Protein Domain
IPR007264 | H/ACA_rnp_Nop10
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].In eukaryotes Nop10 is a nucleolar protein that is specifically associated with H/ACA snoRNAs. It is essential for normal 18S rRNA production and rRNA pseudouridylation by the ribonucleoprotein particles containing H/ACA snoRNAs (H/ACA snoRNPs). Nop10 is probably necessary for the stability of these RNPs [].
•
•
•
•
•
Protein
Q9CQS2
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: false
•
•
•
•
•
Publication
9843512 | -
First Author: Henras A
Year: 1998
Journal: EMBO J
Title: Nhp2p and Nop10p are essential for the function of H/ACA snoRNPs.
Volume: 17
Issue: 23
Pages: 7078-90
•
•
•
•
•
Publication
16647858 | -
First Author: Meier UT
Year: 2006
Journal: Trends Biochem Sci
Title: How a single protein complex accommodates many different H/ACA RNAs.
Volume: 31
Issue: 6
Pages: 311-5
•
•
•
•
•
Publication
10871366 | -
First Author: Watanabe Y
Year: 2000
Journal: Nucleic Acids Res
Title: Evolutionary appearance of genes encoding proteins associated with box H/ACA snoRNAs: cbf5p in Euglena gracilis, an early diverging eukaryote, and candidate Gar1p and Nop10p homologs in archaebacteria.
Volume: 28
Issue: 12
Pages: 2342-52
•
•
•
•
•
Publication
17631273 | -
First Author: Dobbyn HC
Year: 2007
Journal: Biochem Biophys Res Commun
Title: Analysis of pre-mRNA and pre-rRNA processing factor Snu13p structure and mutants.
Volume: 360
Issue: 4
Pages: 857-62
•
•
•
•
•
Publication
19917616 | -
First Author: Hamma T
Year: 2010
Journal: J Biol Chem
Title: The box H/ACA ribonucleoprotein complex: interplay of RNA and protein structures in post-transcriptional RNA modification.
Volume: 285
Issue: 2
Pages: 805-9
•
•
•
•
•
Publication
14730029 | -
First Author: Dobbyn HC
Year: 2004
Journal: RNA
Title: Analysis of Snu13p mutations reveals differential interactions with the U4 snRNA and U3 snoRNA.
Volume: 10
Issue: 2
Pages: 308-20
•
•
•
•
•
Publication
12215523 | -
First Author: Galardi S
Year: 2002
Journal: Mol Cell Biol
Title: Purified box C/D snoRNPs are able to reproduce site-specific 2'-O-methylation of target RNA in vitro.
Volume: 22
Issue: 19
Pages: 6663-8
•
•
•
•
•
Publication
15044956 | -
First Author: Wang C
Year: 2004
Journal: EMBO J
Title: Architecture and assembly of mammalian H/ACA small nucleolar and telomerase ribonucleoproteins.
Volume: 23
Issue: 8
Pages: 1857-67
•
•
•
•
•
Protein Domain
IPR002415 | H/ACA_rnp_Nhp2-like
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].This entry represents H/ACA ribonucleoprotein complex subunit NHP2 and similar proteins from eukaryotes, including NHP2-like protein 1 from mammals (SNU13 homologue) and 13 kDa ribonucleoprotein-associated protein (SNU13) from yeast.Nhp2 is part of a complex which catalyses pseudouridylation of rRNA and is required for rRNA biogenesis. This involves the isomerisation of uridine such that the ribose is subsequently attached to C5, instead of the normal N1. Pseudouridine ("psi") residues may serve to stabilise the conformation of rRNAs. Nph2 associates non-specifically with RNA secondary structures instead of directly binding to an specific RNA motif. This protein seem to have evolved from the archaeal ribosomal L7Ae protein family []. Human SNU13 homologue is involved in pre-mRNA splicing as component of the spliceosome []. The protein undergoes a conformational change upon RNA-binding [].SNU13 from Saccharomyces cerevisiae (Baker's yeast) is also a component of the spliceosome and rRNA processing machinery, required for splicing of pre-mRNA and essential for the accumulation and stability of U4 snRNA, U6 snRNA, and box C/D snoRNAs [, , ].
•
•
•
•
•
Protein
F6SL78
Organism: Mus musculus/domesticus
Length: 79  
Fragment?: true
•
•
•
•
•
Publication
17612558 | -
First Author: Leulliot N
Year: 2007
Journal: J Mol Biol
Title: The box H/ACA RNP assembly factor Naf1p contains a domain homologous to Gar1p mediating its interaction with Cbf5p.
Volume: 371
Issue: 5
Pages: 1338-53
•
•
•
•
•
Publication
22085966 | -
First Author: Walbott H
Year: 2011
Journal: Genes Dev
Title: The H/ACA RNP assembly factor SHQ1 functions as an RNA mimic.
Volume: 25
Issue: 22
Pages: 2398-408
•
•
•
•
•
Publication
22117216 | -
First Author: Li S
Year: 2011
Journal: EMBO J
Title: Structure of the Shq1-Cbf5-Nop10-Gar1 complex and implications for H/ACA RNP biogenesis and dyskeratosis congenita.
Volume: 30
Issue: 24
Pages: 5010-20
•
•
•
•
•
Protein Domain
IPR039742 | Shq1
Type: Family
Description: The box H/ACA ribonucleoproteins (RNPs) are protein-RNA complexes responsible for pseudouridylation, the most abundant post-transcriptional modification of cellular RNAs []. Each distinct H/ACA RNA assembles with a common set of four proteins, Cbf5 (NAP57 in rodents and dyskerin in humans), Nop10, Nhp2 (L7Ae in archaea) and Gar1 []. Shq1 is an essential assembly factor for H/ACA ribonucleoproteins (RNPs) required for ribosome biogenesis, pre-mRNA splicing, and telomere maintenance []. It interacts with Cbf5 and may function as an assembly chaperone that protects the Cbf5 protein complexes from non-specific RNA binding and aggregation before assembly of H/ACA RNA [].
•
•
•
•
•
Protein Domain
IPR038664 | Gar1/Naf1_Cbf5-bd_sf
Type: Homologous_superfamily
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].Naf1 is an RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex, disappearing during maturation of the complex and being replaced by Gar1 to yield mature H/ACA snoRNPs complex. The core domain of Naf1 is homologous to the core domain of Gar1, suggesting that they share a common Cbf5 binding surface [].
•
•
•
•
•
Protein Domain
IPR007504 | H/ACA_rnp_Gar1/Naf1
Type: Family
Description: H/ACA ribonucleoprotein particles (RNPs) are a family of RNA pseudouridine synthases that specify modification sites through guide RNAs. The function of these H/ACA RNPs is essential for biogenesis of the ribosome, splicing of precursor mRNAs (pre-mRNAs), maintenance of telomeres and probably for additional cellular processes []. All H/ACA RNPs contain a specific RNA component (snoRNA or scaRNA) and at least four proteins common to all such particles: Cbf5, Gar1, Nhp2 and Nop10. These proteins are highly conserved from yeast to mammals and homologues are also present in archaea []. The H/ACA protein complex contains a stable core composed of Cbf5 and Nop10, to which Gar1 and Nhp2 subsequently bind [].Naf1 is an RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex, disappearing during maturation of the complex and being replaced by Gar1 to yield mature H/ACA snoRNPs complex. The core domain of Naf1 is homologous to the core domain of Gar1, suggesting that they share a common Cbf5 binding surface [].
•
•
•
•
•
Protein
Q9CY66
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
•
•
•
•
•
Protein
Q3UMQ8
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
•
•
•
•
•
Protein
D3YZ09
Organism: Mus musculus/domesticus
Length: 198  
Fragment?: true
•
•
•
•
•
Protein
Q3TKG5
Organism: Mus musculus/domesticus
Length: 231  
Fragment?: false
•
•
•
•
•
Protein
E9QJT2
Organism: Mus musculus/domesticus
Length: 597  
Fragment?: false
•
•
•
•
•
Publication
17412961 | -
First Author: Liu S
Year: 2007
Journal: Science
Title: Binding of the human Prp31 Nop domain to a composite RNA-protein platform in U4 snRNP.
Volume: 316
Issue: 5821
Pages: 115-20
•
•
•
•
•
Publication
28781166 | -
First Author: Bertram K
Year: 2017
Journal: Cell
Title: Cryo-EM Structure of a Pre-catalytic Human Spliceosome Primed for Activation.
Volume: 170
Issue: 4
Pages: 701-713.e11
•
•
•
•
•
Protein
Q7TMX5
Organism: Mus musculus/domesticus
Length: 569  
Fragment?: false
•
•
•
•
•
Protein
Q9D0T1
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
•
•
•
•
•
Publication
1756182 | -
First Author: Colombo P
Year: 1991
Journal: Biochim Biophys Acta
Title: The organization and expression of the human L7a ribosomal protein gene.
Volume: 1129
Issue: 1
Pages: 93-5
•
•
•
•
•
Publication
2183194 | -
First Author: Arevalo SG
Year: 1990
Journal: Nucleic Acids Res
Title: Ribosomal protein L4 of Saccharomyces cerevisiae: the gene and its protein.
Volume: 18
Issue: 6
Pages: 1447-9
•
•
•
•
•
Publication
2063628 | -
First Author: Kolodrubetz D
Year: 1991
Journal: Yeast
Title: Sequence and genetic analysis of NHP2: a moderately abundant high mobility group-like nuclear protein with an essential function in Saccharomyces cerevisiae.
Volume: 7
Issue: 2
Pages: 79-90
•
•
•
•
•
Protein Domain
IPR018492 | Ribosomal_L7Ae/L8/Nhp2
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].The genomic structure and sequence of the human ribosomal protein L7a has been determined and shown to resemble other mammalian ribosomal protein genes []. The sequence of a gene for ribosomal protein L4 of yeast has also been determined; its single open reading frame is highly similarto mammalian ribosomal protein L7a [, ]. Several other ribosomal proteins have been found to share sequence similarity with L7a, including Saccharomyces cerevisiae NHP2 [], Bacillus subtilis hypothetical protein ylxQ, Haloarcula marismortui Hs6, and Methanocaldococcus jannaschii (Methanococcus jannaschii) MJ1203.
•
•
•
•
•
Protein Domain
IPR000948 | Ribosomal_L7Ae_prok
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].The sequence of the acidic ribosomal protein S6 from Haloarcula marismortui has been determined []. The protein consists of 116 amino acid residues, and has a molecular mass of 12,251kDa. Sequence comparison with ribosomal proteins of other organisms has revealed that H. marismortui protein S6 is similar to mammalian protein L7a [], yeast L4 [], yeast NHP2 [], Bacillus subtilis hypothetical protein ylxQ and Methanocaldococcus jannaschii (Methanococcus jannaschii).
•
•
•
•
•
Protein Domain
IPR004037 | Ribosomal_L7Ae_CS
Type: Conserved_site
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate the rRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].The genomic structure and sequence of the human ribosomal protein L7a has been determined and shown to resemble other mammalian ribosomal protein genes []. The sequence of a gene for ribosomal protein L4 of yeast has also been determined; its single open reading frame is highly similarto mammalian ribosomal protein L7a [, ]. Several other ribosomal proteins have been found to share sequence similarity with L7a, including Saccharomyces cerevisiae NHP2 [], Bacillus subtilis hypothetical protein ylxQ, Haloarcula marismortui Hs6, and Methanocaldococcus jannaschii (Methanococcus jannaschii) MJ1203.
•
•
•
•
•
Protein
P12970
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
•
•
•
•
•
Protein
Q58ET1
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
•
•
•
•
•
Protein
Q80UT7
Organism: Mus musculus/domesticus
Length: 270  
Fragment?: true
•
•
•
•
•
Protein
Q5EBG5
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
•
•
•
•
•
Protein
Q6P1A9
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
•
•
•
•
•
Protein
Q8CDE3
Organism: Mus musculus/domesticus
Length: 206  
Fragment?: false
•
•
•
•
•
Publication
2046660 | -
First Author: Yon J
Year: 1991
Journal: Mol Gen Genet
Title: The organization and expression of the Saccharomyces cerevisiae L4 ribosomal protein genes and their identification as the homologues of the mammalian ribosomal protein gene L7a.
Volume: 227
Issue: 1
Pages: 72-80
•
•
•
•
•
Protein Domain
IPR001921 | Ribosomal_L7A/L8
Type: Family
Description: Ribosomes are the particles that catalyse mRNA-directed protein synthesis in all organisms. The codons of the mRNA are exposed on the ribosome to allow tRNA binding. This leads to the incorporation of amino acids into the growing polypeptide chain in accordance with the genetic information. Incoming amino acid monomers enter the ribosomal A site in the form of aminoacyl-tRNAs complexed with elongation factor Tu (EF-Tu) and GTP. The growing polypeptide chain, situated in the P site as peptidyl-tRNA, is then transferred to aminoacyl-tRNA and the new peptidyl-tRNA, extended by one residue, is translocated to the P site with the aid the elongation factor G (EF-G) and GTP as the deacylated tRNA is released from the ribosome through one or more exit sites [, ]. About 2/3 of the mass of the ribosome consists of RNA and 1/3 of protein. The proteins are named in accordance with the subunit of the ribosome which they belong to - the small (S1 to S31) and the large (L1 to L44). Usually they decorate therRNA cores of the subunits. Many ribosomal proteins, particularly those of the large subunit, are composed of a globular, surfaced-exposed domain with long finger-like projections that extend into the rRNA core to stabilise its structure. Most of the proteins interact with multiple RNA elements, often from different domains. In the large subunit, about 1/3 of the 23S rRNA nucleotides are at least in van der Waal's contact with protein, and L22 interacts with all six domains of the 23S rRNA. Proteins S4 and S7, which initiate assembly of the 16S rRNA, are located at junctions of five and four RNA helices, respectively. In this way proteins serve to organise and stabilise the rRNA tertiary structure. While the crucial activities of decoding and peptide transfer are RNA based, proteins play an active role in functions that may have evolved to streamline the process of protein synthesis. In addition to their function in the ribosome, many ribosomal proteins have some function 'outside' the ribosome [, ].The genomic structure and sequence of the human ribosomal protein L7a has been determined []. The gene contains 8 exons and 7 introns, encompassing 3179 bp. The human gene resembles other mammalian ribosomal protein genes in so far as it contains a short first exon, a short 5' untranslated leader and its transcriptional start sites at C residues embedded in a poly-pyrimidine tract [].The sequence of a gene for ribosomal protein L4 of Saccharomyces cerevisiae (Baker's yeast) has also been determined, which, unlike most of its other ribosomal protein genes, has no intron []. The single open reading frame is highly similar to mammalian ribosomal protein L7a.There appear to be two genes for L4, both ofwhich are active []. Yeast cells containing a disruption of the L4-1 gene form smaller colonies than either wild-type or disrupted L4-2 strains. Disruption of both L4 genes is lethal, probably resulting from an inability of the organism to produce functional ribosomes [].Several other ribosomal proteins have been found to share sequence similarity with L7a, including yeast NHP2 [], Bacillus subtilis hypothetical protein ylxQ, Haloarcula marismortui (Halobacterium marismortui) Hs6, and Methanocaldococcus jannaschii MJ1203.This InterPro entry focus on regions that characterise the ribosomal L7A proteins but distinguish them from the rest of the HMG-like family.
•
•
•
•
•
Publication
3315748 | -
First Author: Kimura J
Year: 1987
Journal: FEBS Lett
Title: Primary structures of three highly acidic ribosomal proteins S6, S12 and S15 from the archaebacterium Halobacterium marismortui.
Volume: 224
Issue: 1
Pages: 65-70
•
•
•
•
•
Publication
11297922 | -
First Author: Ramakrishnan V
Year: 2001
Journal: Curr Opin Struct Biol
Title: Atomic structures at last: the ribosome in 2000.
Volume: 11
Issue: 2
Pages: 144-54
•
•
•
•
•
Publication
11290319 | -
First Author: Maguire BA
Year: 2001
Journal: Cell
Title: The ribosome in focus.
Volume: 104
Issue: 6
Pages: 813-6
•
•
•
•
•
Publication
11114498 | -
First Author: Chandra Sanyal S
Year: 2000
Journal: Curr Opin Struct Biol
Title: The end of the beginning: structural studies of ribosomal proteins.
Volume: 10
Issue: 6
Pages: 633-6
•
•
•
•
•
Publication
- | J:100256
     
First Author: The Gene Expression Nervous System Atlas (GENSAT) Project, The Rockefeller University (New York, NY)
Year: 2005
Journal: Database Download
Title: MGI download of GENSAT transgene data
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom