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Search results 1 to 100 out of 147 for Srp68

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Type Details Score
Gene
6730 | SRP68
Type: gene
Organism: human
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Gene
538777 | SRP68
Type: gene
Organism: cattle
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Gene
417363 | SRP68
Type: gene
Organism: chicken
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Gene
446119 | srp68
Type: gene
Organism: zebrafish
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Gene
705568 | SRP68
Type: gene
Organism: macaque, rhesus
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Gene
100158589 | srp68
Type: gene
Organism: frog, western clawed
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Protein Domain
IPR026258 | SRP68
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.
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Gene
363707 | Srp68
Type: gene
Organism: rat
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Gene
403952 | SRP68
Type: gene
Organism: dog, domestic
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Gene
738851 | SRP68
Type: gene
Organism: chimpanzee
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Protein Coding Gene
MGI:1917447 | Srp68
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
A2AAN2
Organism: Mus musculus/domesticus
Length: 587  
Fragment?: false
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Protein
Q8K258
Organism: Mus musculus/domesticus
Length: 334  
Fragment?: false
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Protein
Q8BMA6
Organism: Mus musculus/domesticus
Length: 625  
Fragment?: false
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Publication
17254600 | -
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
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Publication
34020957 | -
 
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
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Publication
19693936 | -
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
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Protein Coding Gene
MGP_CAROLIEiJ_G0017437 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0019421 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0019390 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0019360 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0019364 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0019170 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1917447 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0019814 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0018725 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0019142 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0019253 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0019245 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0019323 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0019278 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0019852 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0018489 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0018777 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0018566 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0018282 | -
Type: protein_coding_gene
Organism: Mus spretus
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Publication
38025786 | J:343072
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
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Publication
- | J:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
12904583 | J:85162
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
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Publication
12520002 | J:91812
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
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:204812
     
First Author: International Mouse Strain Resource
Year: 2014
Journal: Database Download
Title: MGI download of germline transmission data for alleles from IMSR strain data
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Publication
- | J:148605
     
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
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Publication
- | J:72247
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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Publication
- | J:342604
       
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
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
11217851 | J:65060
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
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Publication
14610273 | J:86696
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
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Publication
- | J:141210
     
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
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Publication
21677750 | J:173534
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
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
12466851 | J:80000
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
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Publication
- | J:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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Publication
21267068 | J:153498
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
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Publication
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
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).
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
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
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Publication
- | J:144086
     
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
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UniProt Feature
UniProt Feature
Begin: 1
Description: Signal recognition particle subunit SRP68
Type: chain
End: 625
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Publication
24700861 | -
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
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Publication
16672232 | -
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
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Publication
11352936 | -
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
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Publication
10921896 | -
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
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Protein Domain
IPR026270 | SRP72
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 [].
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Protein Domain
IPR038253 | SRP68_N_sf
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 [, , ].
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Protein Domain
IPR034652 | SRP68-RBD
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 [, , ].
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Publication
27899666 | -
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
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Publication
7518075 | J:18406
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
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Protein
Q9CS54
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
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Publication
7925282 | -
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
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Publication
15588816 | -
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
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Protein Domain
IPR002778 | Signal_recog_particle_SRP19
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 [].
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Protein Domain
IPR022938 | SRP19_arc-type
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.
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Protein Domain
IPR036521 | SRP19-like_sf
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
IPR039432 | SRP9_dom
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
IPR039914 | SRP9
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
IPR013699 | Signal_recog_part_SRP72_RNA-bd
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
7730321 | -
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
Q9D7A6
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
P16254
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: false
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Protein
Q9D104
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
Q9CRF7
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: true
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Protein
Q8BZ07
Organism: Mus musculus/domesticus
Length: 113  
Fragment?: false
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Protein
D6RHP8
Organism: Mus musculus/domesticus
Length: 40  
Fragment?: false
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Protein
Q3UXK5
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: false
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Protein
G5E8T3
Organism: Mus musculus/domesticus
Length: 120  
Fragment?: false
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Protein
A2AUM6
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
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Publication
17434535 | -
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
P49962
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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