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Search results 1 to 100 out of 133 for Srp19

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Hits by Pathway

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Hits by Category

Type Details Score
Gene
6728 | SRP19
Type: gene
Organism: human
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Gene
737811 | SRP19
Type: gene
Organism: chimpanzee
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Gene
606764 | SRP19
Type: gene
Organism: dog, domestic
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Gene
514960 | SRP19
Type: gene
Organism: cattle
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Gene
770061 | SRP19
Type: gene
Organism: chicken
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Gene
406652 | srp19
Type: gene
Organism: zebrafish
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Gene
693829 | SRP19
Type: gene
Organism: macaque, rhesus
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Gene
496535 | srp19
Type: gene
Organism: frog, western clawed
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Gene
291685 | Srp19
Type: gene
Organism: rat
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Protein Coding Gene
MGI:1913634 | Srp19
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9D7A6
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
Q9D104
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein Coding Gene
MGP_CAROLIEiJ_G0022086 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0024237 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0024203 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0024172 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0024203 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0023971 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1913634 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0024645 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0023446 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CBAJ_G0023939 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_DBA2J_G0024071 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_FVBNJ_G0024037 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_LPJ_G0024152 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NODShiLtJ_G0024065 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_NZOHlLtJ_G0024693 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PWKPhJ_G0023189 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_WSBEiJ_G0023509 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_PahariEiJ_G0018820 | -
Type: protein_coding_gene
Organism: Mus pahari
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Protein Coding Gene
MGP_SPRETEiJ_G0022998 | -
Type: protein_coding_gene
Organism: Mus spretus
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GXD Expression
GXD Expression
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640617
Pattern: Regionally restricted
Stage: TS17
Assay Id: MGI:5823727
Age: embryonic day 10.5
Image: Srp19_a8_E10.5b_RF_JL
Note: Staining is observed in the distal limb bud.
Specimen Label: Srp19_a8_E10.5b_RF_JL
Detected: true
Specimen Num: 1
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GXD Expression
GXD Expression
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640619
Pattern: Regionally restricted
Stage: TS19
Assay Id: MGI:5823727
Age: embryonic day 11.5
Image: Srp19_a8_E11.5a_RF_JL
Note: Domains of staining are similar to those seen at E10.5.
Specimen Label: Srp19_a8_E11.5a_RF_JL
Detected: true
Specimen Num: 2
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GXD Expression
GXD Expression
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640619
Pattern: Regionally restricted
Stage: TS19
Assay Id: MGI:5823727
Age: embryonic day 11.5
Image: Srp19_a8_E11.5b_RF_JL
Note: Domains of staining are similar to those seen at E10.5.
Specimen Label: Srp19_a8_E11.5b_RF_JL
Detected: true
Specimen Num: 3
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GXD Expression
GXD Expression
 
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640617
Pattern: Not Specified
Stage: TS17
Assay Id: MGI:5823727
Age: embryonic day 10.5
Image: Srp19_a8_E10.5a_JL
Specimen Label: Srp19_a8_E10.5a_JL
Detected: true
Specimen Num: 4
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GXD Expression
GXD Expression
 
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640617
Pattern: Not Specified
Stage: TS17
Assay Id: MGI:5823727
Age: embryonic day 10.5
Image: Srp19_a8_E10.5b_JL
Specimen Label: Srp19_a8_E10.5b_JL
Detected: true
Specimen Num: 5
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GXD Expression
GXD Expression
 
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640619
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:5823727
Age: embryonic day 11.5
Image: Srp19_a8_E11.5a_JL
Specimen Label: Srp19_a8_E11.5a_JL
Detected: true
Specimen Num: 6
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GXD Expression
GXD Expression
 
Probe: MGI:5811066
Assay Type: RNA in situ
Annotation Date: 2017-02-09
Strength: Present
Sex: Not Specified
Emaps: EMAPS:1640619
Pattern: Not Specified
Stage: TS19
Assay Id: MGI:5823727
Age: embryonic day 11.5
Image: Srp19_a8_E11.5b_JL
Specimen Label: Srp19_a8_E11.5b_JL
Detected: true
Specimen Num: 7
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Publication
26238476 | J:226028
First Author: Lewandowski JP
Year: 2015
Journal: Dev Biol
Title: Spatiotemporal regulation of GLI target genes in the mammalian limb bud.
Volume: 406
Issue: 1
Pages: 92-103
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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
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:73065
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2001
Title: Gene Ontology Annotation by the MGI Curatorial Staff
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Publication
- | J:265051
     
First Author: MGI and IMPC
Year: 2018
Journal: Database Release
Title: MGI Load of Endonuclease-Mediated Alleles (CRISPR) from the International Mouse Phenotyping Consortium (IMPC)
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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
18799693 | J:142754
First Author: Hansen GM
Year: 2008
Journal: Genome Res
Title: Large-scale gene trapping in C57BL/6N mouse embryonic stem cells.
Volume: 18
Issue: 10
Pages: 1670-9
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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:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Publication
16141072 | J:99680
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
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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
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
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:164563
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Title: Human to Mouse ISO GO annotation transfer
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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: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: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: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: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: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: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: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: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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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: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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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
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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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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Publication
16469117 | -
First Author: Römisch K
Year: 2006
Journal: Arthritis Res Ther
Title: Human autoantibodies against the 54 kDa protein of the signal recognition particle block function at multiple stages.
Volume: 8
Issue: 2
Pages: R39
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Publication
17622352 | -
First Author: Reyes CL
Year: 2007
Journal: PLoS One
Title: X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.
Volume: 2
Issue: 7
Pages: e607
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Publication
17507650 | -
First Author: Bradshaw N
Year: 2007
Journal: Mol Biol Cell
Title: The signal recognition particle (SRP) RNA links conformational changes in the SRP to protein targeting.
Volume: 18
Issue: 7
Pages: 2728-34
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Publication
12364595 | -
First Author: Tozik I
Year: 2002
Journal: Nucleic Acids Res
Title: Reconstitution of the signal recognition particle of the halophilic archaeon Haloferax volcanii.
Volume: 30
Issue: 19
Pages: 4166-75
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Publication
12605305 | -
 
First Author: Koch HG
Year: 2003
Journal: Rev Physiol Biochem Pharmacol
Title: Signal recognition particle-dependent protein targeting, universal to all kingdoms of life.
Volume: 146
Pages: 55-94
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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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SO Term
SO:0000590 | SRP_RNA
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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
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
P16254
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: false
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Protein
A2AUM6
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: false
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Protein
P49962
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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Protein
Q5EAT0
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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Protein
A0A1L1SSI7
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
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Protein
Q3UIK3
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
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Protein
C3VDI1
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
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Protein
Q9CS54
Organism: Mus musculus/domesticus
Length: 197  
Fragment?: true
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Publication
9799502 | -
First Author: Jagath JR
Year: 1998
Journal: Biochemistry
Title: Interaction of guanine nucleotides with the signal recognition particle from Escherichia coli.
Volume: 37
Issue: 44
Pages: 15408-13
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Publication
10656787 | -
First Author: Jagath JR
Year: 2000
Journal: J Mol Biol
Title: Conformational changes in the bacterial SRP receptor FtsY upon binding of guanine nucleotides and SRP.
Volume: 295
Issue: 4
Pages: 745-53
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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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Protein Domain
IPR022941 | SRP54
Type: Family
Description: This entry represents the SRP54 subunit of the signal recognition particle protein translocation system.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 [].The bacterial homologues of the SRP54 protein and SRP RNA are Ffh and 4.5S RNA. They comprise a minimal bacterial SRP that can target ribosome-nascent chain complexes to the plasma membrane via interaction with FtsY, the bacterialhomologue of the SRP receptor [, ].
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Protein Domain
IPR009018 | Signal_recog_particle_SRP9/14
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 superfamily represents both the 9kDa SRP9 and the 14kDa SRP14 components. Both SRP9 and SRP14 have the same (beta)-α-β(3)-alpha fold. The heterodimer has pseudo two-fold symmetry and is saddle-like, consisting of a curved six-stranded β-sheet that has four helices packed on the convex side and an exposed concave surface lined with positively charged residues. The SRP9/SRP14 heterodimer is essential for SRP RNA binding, mediating the pausing of synthesis of ribosome associated nascent polypeptides that have been engaged by the targeting domain of SRP [].
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Protein Domain
IPR007222 | Sig_recog_particle_rcpt_asu_N
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 [].The SR receptor is a monomer consisting of the loosely membrane-associated SR-alpha homologue FtsY, while the eukaryotic SR receptor is a heterodimer of SR-alpha (70kDa) and SR-beta (25kDa), both of which contain a GTP-binding domain []. SR-alpha regulates the targeting of SRP-ribosome-nascent polypeptide complexes to the translocon []. SR-alpha binds to the SRP54 subunit of the SRP complex. The SR-beta subunit is a transmembrane GTPase that anchors the SR-alpha subunit (a peripheral membrane GTPase) to the ER membrane []. SR-beta interacts with the N-terminal SRX-domain of SR-alpha, which is not present in the bacterial FtsY homologue. SR-beta also functions in recruiting the SRP-nascent polypeptide to the protein-conducting channel. This entry represents the alpha subunit of the SR receptor.
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