Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
human |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
cattle |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chicken |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
zebrafish |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
frog, western clawed |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The signal recognition particle (SRP) is a large ribonucleoprotein complex that targets secretory and membrane proteins to the endoplasmic reticulum membrane [, ]. The mammalian SRP contains a 303-nucleotide SRP RNA and six proteins, named SRP9, SRP14, SRP19, SRP54, SRP68, and SRP72. Among them, the two largest, SRP68 and SRP72, form a stable SRP68/72 heterodimer of unknown structure, which is required for sorting secretory proteins []. SRP68 binds to SRP RNA directly, while SRP72 binds the SRP RNA largely via non-specific electrostatic interaction. The binding of SRP72 with SRP RNA enhances the affinity of SRP68 for the RNA. |
|
•
•
•
•
•
|
Gene |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
dog, domestic |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
587
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
334
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
625
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Menichelli E |
Year: |
2007 |
Journal: |
J Mol Biol |
Title: |
Protein-induced conformational changes of RNA during the assembly of human signal recognition particle. |
Volume: |
367 |
Issue: |
1 |
Pages: |
187-203 |
|
•
•
•
•
•
|
Publication |
First Author: |
Iakhiaeva E |
Year: |
2009 |
Journal: |
Protein Sci |
Title: |
Characterization of the SRP68/72 interface of human signal recognition particle by systematic site-directed mutagenesis. |
Volume: |
18 |
Issue: |
10 |
Pages: |
2183-95 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee JH |
Year: |
2021 |
Journal: |
Sci Adv |
Title: |
Receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER. |
Volume: |
7 |
Issue: |
21 |
|
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus caroli |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus pahari |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
Mus spretus |
|
•
•
•
•
•
|
Publication |
First Author: |
Vermeiren S |
Year: |
2023 |
Journal: |
iScience |
Title: |
Prdm12 represses the expression of the visceral neuron determinants Phox2a/b in developing somatosensory ganglia. |
Volume: |
26 |
Issue: |
12 |
Pages: |
108364 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2001 |
|
Title: |
Gene Ontology Annotation by the MGI Curatorial Staff |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Hansen J |
Year: |
2003 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
A large-scale, gene-driven mutagenesis approach for the functional analysis of the mouse genome. |
Volume: |
100 |
Issue: |
17 |
Pages: |
9918-22 |
|
•
•
•
•
•
|
Publication |
First Author: |
Stryke D |
Year: |
2003 |
Journal: |
Nucleic Acids Res |
Title: |
BayGenomics: a resource of insertional mutations in mouse embryonic stem cells. |
Volume: |
31 |
Issue: |
1 |
Pages: |
278-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Velocigene |
Year: |
2008 |
Journal: |
MGI Direct Data Submission |
Title: |
Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals) |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
International Mouse Strain Resource |
Year: |
2014 |
Journal: |
Database Download |
Title: |
MGI download of germline transmission data for alleles from IMSR strain data |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Wellcome Trust Sanger Institute |
Year: |
2009 |
Journal: |
MGI Direct Data Submission |
Title: |
Alleles produced for the KOMP project by the Wellcome Trust Sanger Institute |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
DDB, FB, MGI, GOA, ZFIN curators |
Year: |
2001 |
|
Title: |
Gene Ontology annotation through association of InterPro records with GO terms |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
GOA curators |
Year: |
2016 |
|
Title: |
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
UniProt-GOA |
Year: |
2012 |
|
Title: |
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2003 |
|
Title: |
MGI Sequence Curation Reference |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Kawai J |
Year: |
2001 |
Journal: |
Nature |
Title: |
Functional annotation of a full-length mouse cDNA collection. |
Volume: |
409 |
Issue: |
6821 |
Pages: |
685-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zambrowicz BP |
Year: |
2003 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Wnk1 kinase deficiency lowers blood pressure in mice: a gene-trap screen to identify potential targets for therapeutic intervention. |
Volume: |
100 |
Issue: |
24 |
Pages: |
14109-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics (MGI) and National Center for Biotechnology Information (NCBI) |
Year: |
2008 |
Journal: |
Database Download |
Title: |
Mouse Gene Trap Data Load from dbGSS |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Skarnes WC |
Year: |
2011 |
Journal: |
Nature |
Title: |
A conditional knockout resource for the genome-wide study of mouse gene function. |
Volume: |
474 |
Issue: |
7351 |
Pages: |
337-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
GemPharmatech |
Year: |
2020 |
|
Title: |
GemPharmatech Website. |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Okazaki Y |
Year: |
2002 |
Journal: |
Nature |
Title: |
Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs. |
Volume: |
420 |
Issue: |
6915 |
Pages: |
563-73 |
|
•
•
•
•
•
|
Publication |
First Author: |
The Gene Ontology Consortium |
Year: |
2010 |
|
Title: |
Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Diez-Roux G |
Year: |
2011 |
Journal: |
PLoS Biol |
Title: |
A high-resolution anatomical atlas of the transcriptome in the mouse embryo. |
Volume: |
9 |
Issue: |
1 |
Pages: |
e1000582 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2). |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Scientific Curators |
Year: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
MGI Genome Annotation Group and UniGene Staff |
Year: |
2015 |
Journal: |
Database Download |
Title: |
MGI-UniGene Interconnection Effort |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
Year: |
2010 |
|
Title: |
Annotation inferences using phylogenetic trees |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Database and National Center for Biotechnology Information |
Year: |
2000 |
Journal: |
Database Release |
Title: |
Entrez Gene Load |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
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 Scientific Curators |
Year: |
2005 |
|
Title: |
Obtaining and loading genome assembly coordinates from NCBI annotations |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Bairoch A |
Year: |
1999 |
Journal: |
Database Release |
Title: |
SWISS-PROT Annotated protein sequence database |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Allen Institute for Brain Science |
Year: |
2004 |
Journal: |
Allen Institute |
Title: |
Allen Brain Atlas: mouse riboprobes |
|
|
|
|
•
•
•
•
•
|
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 |
|
|
|
|
•
•
•
•
•
|
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 Gene 1.0 ST Array Platform |
|
|
|
|
•
•
•
•
•
|
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. |
|
|
|
|
•
•
•
•
•
|
UniProt Feature |
Begin: |
1 |
Description: |
Signal recognition particle subunit SRP68 |
Type: |
chain |
End: |
625 |
|
•
•
•
•
•
|
Publication |
First Author: |
Grotwinkel JT |
Year: |
2014 |
Journal: |
Science |
Title: |
SRP RNA remodeling by SRP68 explains its role in protein translocation. |
Volume: |
344 |
Issue: |
6179 |
Pages: |
101-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Iakhiaeva E |
Year: |
2006 |
Journal: |
Protein Sci |
Title: |
Protein SRP68 of human signal recognition particle: identification of the RNA and SRP72 binding domains. |
Volume: |
15 |
Issue: |
6 |
Pages: |
1290-302 |
|
•
•
•
•
•
|
Publication |
First Author: |
Grosshans H |
Year: |
2001 |
Journal: |
J Cell Biol |
Title: |
Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. |
Volume: |
153 |
Issue: |
4 |
Pages: |
745-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mason N |
Year: |
2000 |
Journal: |
EMBO J |
Title: |
Elongation arrest is a physiologically important function of signal recognition particle. |
Volume: |
19 |
Issue: |
15 |
Pages: |
4164-74 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
SRP72 is a core component of the signal recognition particle ribonucleoprotein complex that functions in targeting nascent secretory proteins to the endoplasmic reticulum membrane [, ]. SRP72 binds the 7S RNA only in presence of SRP68 []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
Signal recognition particles (SRPs) are ribonucleoprotein complexes that target particular nascent pre-secretory proteins to the endoplasmic reticulum. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER []. SRP68 is one of the two largest proteins found in SRPs (the other being SRP72), and it forms a heterodimer with SRP72. Heterodimer formation is essential for SRP function []. SRP68 binds to SRP RNA directly, while SRP72 binds the SRP RNA largely via nonspecific electrostatic interaction. The binding of SRP72 with SRP RNA enhances the affinity of SRP68 for the RNA. This entry describes the N-terminal RNA-binding domain (RBD) of SRP68, a tetratricopeptide-like module. Interactions between SRP68-RBD and SRP RNA (7SL RNA) are thought to facilitate a conformation of SRP RNA that is required for interactions with ribosomal RNA [, , ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Signal recognition particles (SRPs) are ribonucleoprotein complexes that target particular nascent pre-secretory proteins to the endoplasmic reticulum. The SRP complex targets the ribosome-nascent chain complex to the SRP receptor (SR), which is anchored in the ER, where SR compaction and GTPase rearrangement drive cotranslational protein translocation into the ER []. SRP68 is one of the two largest proteins found in SRPs (the other being SRP72), and it forms a heterodimer with SRP72. Heterodimer formation is essential for SRP function []. SRP68 binds to SRP RNA directly, while SRP72 binds the SRP RNA largely via nonspecific electrostatic interaction. The binding of SRP72 with SRP RNA enhances the affinity of SRP68 for the RNA. This entry describes the N-terminal RNA-binding domain (RBD) of SRP68, a tetratricopeptide-like module. Interactions between SRP68-RBD and SRP RNA (7SL RNA) are thought to facilitate a conformation of SRP RNA that is required for interactions with ribosomal RNA [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Becker MM |
Year: |
2017 |
Journal: |
Nucleic Acids Res |
Title: |
Structures of human SRP72 complexes provide insights into SRP RNA remodeling and ribosome interaction. |
Volume: |
45 |
Issue: |
1 |
Pages: |
470-481 |
|
•
•
•
•
•
|
Publication |
First Author: |
Althoff S |
Year: |
1994 |
Journal: |
Nucleic Acids Res |
Title: |
Molecular evolution of SRP cycle components: functional implications. |
Volume: |
22 |
Issue: |
11 |
Pages: |
1933-47 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
197
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Brown JD |
Year: |
1994 |
Journal: |
EMBO J |
Title: |
Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. |
Volume: |
13 |
Issue: |
18 |
Pages: |
4390-400 |
|
•
•
•
•
•
|
Publication |
First Author: |
Iakhiaeva E |
Year: |
2005 |
Journal: |
J Mol Biol |
Title: |
Identification of an RNA-binding domain in human SRP72. |
Volume: |
345 |
Issue: |
4 |
Pages: |
659-66 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interactionof SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 [].This entry represents the SRP19 subunit. The SRP19 protein is unstructured but forms a compact core domain and two extended RNA-binding loops upon binding the signal recognition particle (SRP) RNA []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 [].This entry represents the SRP19 subunit in Archaea and Fungi. In Fungi it is known as SEC65 subunit. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA.This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 [].This entry represents the SRP19 subunit. The SRP19 protein is unstructured but forms a compact core domain and two extended RNA-binding loops upon binding the signal recognition particle (SRP) RNA []. |
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Protein Domain |
Type: |
Domain |
Description: |
This domain can be found in human SRP9 protein and its homologues, such as the Srp21 protein from budding yeasts []. These proteins are part of the signal recognition particle (SRP) [].The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 []. |
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Protein Domain |
Type: |
Family |
Description: |
This entry represents proteins contain an SRP9 domain, such as human signal recognition particle 9kDa protein (SRP9), a component of the signal recognition particle (SRP) [],The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 []. |
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Protein Domain |
Type: |
Domain |
Description: |
The signal recognition particle (SRP) is a multimeric protein, which along with its conjugate receptor (SR), is involved in targeting secretory proteins to the rough endoplasmic reticulum (RER) membrane in eukaryotes, or to the plasma membrane in prokaryotes [, ]. SRP recognises the signal sequence of the nascent polypeptide on the ribosome. In eukaryotes this retards its elongation until SRP docks the ribosome-polypeptide complex to the RER membrane via the SR receptor []. Eukaryotic SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide 7S RNA molecule. The RNA component catalyses the interaction of SRP with its SR receptor []. In higher eukaryotes, the SRP complex consists of the Alu domain and the S domain linked by the SRP RNA. The Alu domain consists of a heterodimer of SRP9 and SRP14 bound to the 5' and 3' terminal sequences of SRP RNA. This domain is necessary for retarding the elongation of the nascent polypeptide chain, which gives SRP time to dock the ribosome-polypeptide complex to the RER membrane. In archaea, the SRP complex contains 7S RNA like its eukaryotic counterpart, yet only includes two of the six protein subunits found in the eukarytic complex: SRP19 and SRP54 [].This entry represents the RNA binding domain of the SRP72 subunit. This domain is responsible for the binding of SRP72 to the 7S SRP RNA []. |
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Publication |
First Author: |
Hsu K |
Year: |
1995 |
Journal: |
J Biol Chem |
Title: |
Human signal recognition particle (SRP) Alu-associated protein also binds Alu interspersed repeat sequence RNAs. Characterization of human SRP9. |
Volume: |
270 |
Issue: |
17 |
Pages: |
10179-86 |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
144
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
110
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
144
|
Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
135
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Fragment?: |
true |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
113
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Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
40
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
78
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Fragment?: |
false |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
120
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Fragment?: |
false |
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•
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
97
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Fragment?: |
false |
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Publication |
First Author: |
Maity TS |
Year: |
2007 |
Journal: |
J Mol Biol |
Title: |
A threefold RNA-protein interface in the signal recognition particle gates native complex assembly. |
Volume: |
369 |
Issue: |
2 |
Pages: |
512-24 |
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Protein |
Organism: |
Mus musculus/domesticus |
Length: |
86
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Fragment?: |
false |
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