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SRP54/YPR088C Single Page Format

This page provides an alternative format to the SGD Locus Summary Page. Note that additional information may be available on or linked from the standard format SGD Locus Summary page.

Contents

Names and Identifiers GO Annotations Pathways Summary Paragraph Mutant Phenotypes Interactions Homologs Protein Info (physical properties, transcript info) PDB Homologs (protein structure info) Motifs Genome-wide Expression (and other large-scale analyses) Locus History (misc. notes) Sequence Retrieval and Analysis Map and Displays Localization Community Annotation Literature Guide

Sequence Coordinates   ChrXVI: 713026 to 711401 CDS: 713026 - 711401 Click on map for expanded view SGD ORF map GBrowse

SGD Locus Page

Names and Identifiers [TOP] [NEXT]
Standard Name	Systematic Name	Alias	Feature Type	SGDID
SRP54	YPR088C	SRH1	ORF, Verified	S000006292
Description
Signal recognition particle (SRP) subunit (homolog of mammalian SRP54); contains the signal sequence-binding activity of SRP, interacts with the SRP RNA, and mediates binding of SRP to signal receptor; contains GTPase domain

GO Annotations [TOP] [NEXT]
Molecular Function Annotation(s) Reference(s) Evidence Assigned By 7S RNA binding Van Nues RW and Brown JD (2004) Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain. RNA 10(1):75-89        IDA : Inferred from Direct Assay Assigned on 2008-07-28 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR004125 , EBI:IPR006325 Assigned on 2009-06-17 UniProtKB GTP binding Amaya Y, et al. (1990) Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K subunit of mammalian signal recognition particle. J Biochem 107(3):457-63      ISA : Inferred from Sequence Alignment with EBI:P06625 , EBI:P61010 Assigned on 2008-07-01 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR000897 , EBI:IPR006325 , EBI:IPR013822 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0342 Assigned on 2007-05-23 UniProtKB GTPase activator activity GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0343 Assigned on 2007-05-23 UniProtKB RNA binding GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0694 Assigned on 2008-02-14 UniProtKB nucleoside-triphosphatase activity DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR003593 Assigned on 2007-05-23 UniProtKB nucleotide binding DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR003593 Assigned on 2007-05-23 UniProtKB GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0547 Assigned on 2007-05-23 UniProtKB signal sequence binding Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400      IPI : Inferred from Physical Interaction Assigned on 2003-05-27 SGD
Biological Process Annotation(s) Reference(s) Evidence Assigned By SRP-dependent cotranslational protein targeting to membrane Hann BC and Walter P (1991) The signal recognition particle in S. cerevisiae. Cell 67(1):131-44        IMP : Inferred from Mutant Phenotype Assigned on 2008-07-01 SGD DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR000897 , EBI:IPR004125 , EBI:IPR006325 , EBI:IPR013822 Assigned on 2007-05-23 UniProtKB SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition Amaya Y, et al. (1990) Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K subunit of mammalian signal recognition particle. J Biochem 107(3):457-63      ISA : Inferred from Sequence Alignment with EBI:P61010 Assigned on 2008-07-01 SGD Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400      IC : Inferred By Curator from signal recognition particle, endoplasmic reticulum targeting Assigned on 2005-01-28 SGD protein targeting to ER Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400      IPI : Inferred from Physical Interaction Assigned on 2002-06-20 SGD
Cellular Component Annotation(s) Reference(s) Evidence Assigned By cytoplasm GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0963 Assigned on 2008-02-14 UniProtKB GOA curators and UniProt curators (2007) Gene Ontology annotation based on Swiss-Prot Subcellular Location vocabulary mapping.      IEA : Inferred from Electronic Annotation with EBI:SL-0086 Assigned on 2008-02-13 UniProtKB ribonucleoprotein complex GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0687 Assigned on 2007-05-23 UniProtKB signal recognition particle DDB, et al. (2001) Gene Ontology annotation through association of InterPro records with GO terms.      IEA : Inferred from Electronic Annotation with EBI:IPR004125 , EBI:IPR006325 Assigned on 2009-06-17 UniProtKB signal recognition particle, endoplasmic reticulum targeting Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400      IDA : Inferred from Direct Assay Assigned on 2002-06-20 SGD GOA curators (2000) Gene Ontology annotation based on Swiss-Prot keyword mapping.      IEA : Inferred from Electronic Annotation with EBI:KW-0733 Assigned on 2008-02-14 UniProtKB

Pathways [TOP] [NEXT]
No pathways available

Summary Paragraph [TOP] [NEXT]

SUMMARY PARAGRAPH for SRP54/YPR088C for SRP54 The signal recognition particle (SRP) is an abundant and conserved ribonucleoprotein necessary for targeting proteins to the endoplasmic reticulum membrane (1). SRP in eukaryotes contains six subunits and a 7S RNA molecule; in S. cerevisiae the subunits are encoded by SRP14, SRP21, SRP68, SRP72, SEC65, and SRP54, and the RNA (termed scR1) is encoded by SCR1 (1, 2). With the exception of Srp54p, the proteins and RNA assemble into a core complex in the nucleus; this particle is exported to the cytoplasm where Srp54p joins to form the complete complex (3). Sec65p is required for association of Srp54p with the SRP particle (4). Loss of any of the SRP components causes a slow growth phenotype and loss of SRP-mediated translocation, but not cell death, indicating that the signal recognition particle is not essential in yeast and SRP-independent translocation can occur (1, 2). The first step of SRP-mediated cotranslational targeting is interaction between SRP and the ribosome nascent chain complex (RNC), which is comprised of the translating ribosome and the emerging nascent protein. SRP interacts with the RNC through the N-terminal hydrophobic signal sequence of the nascent protein. SRP then directs the RNC to the ER membrane via interaction between SRP and a signal receptor complex (SR), encoded by SRP101 and SRP102. Finally, the RNC is transferred to the translocon, a protein-conducting membrane channel, and SRP and the SR dissociate. GTP binding by both SRP (via the Srp54p subunit) and the SR is critical for their interaction, and GTP hydrolysis facilitates their dissociation (reviewed in 5, and see 5 for more details). Biochemical analyses of the mammalian protein indicate that Srp54p contains the following domains: an N-terminal four-helix bundle (N domain), a central GTP binding consensus sequence (G domain), and a C-terminal methionine-rich domain (M domain). The N and G domains are involved in the GTP-dependent interaction with SR, while the M domain binds the 7S RNA and mediates the binding of SRP to the signal peptide (6, 7, reviewed in 5). Last Updated: 2008-08-11

Basic References [TOP]

BASIC INFORMATION REFERENCES forSRP54/YPR088C for SRP54 1) Hann BC and Walter P (1991) The signal recognition particle in S. cerevisiae. Cell 67(1):131-44        2) Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400      3) Ciufo LF and Brown JD (2000) Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway. Curr Biol 10(20):1256-64        4) Stirling CJ and Hewitt EW (1992) The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19. Nature 356(6369):534-7      5) Wild K, et al. (2004) SRP meets the ribosome. Nat Struct Mol Biol 11(11):1049-53        6) Zopf D, et al. (1990) The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 9(13):4511-7          7) Hann BC, et al. (1989) Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth. J Cell Biol 109(6 Pt 2):3223-30      8) Ogg SC, et al. (1998) A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit. J Cell Biol 142(2):341-54

Mutant Phenotypes [TOP] [NEXT]
Phenotype page for SRP54/YPR088C

Interactions: genetic, physical, and other gene-gene links. [TOP] [NEXT]
Interaction page for SRP54/YPR088C

Homologs [TOP] [NEXT]
Comparison Resources PSI-BLAST Results Ashbya Homologs (AGD) BLASTN vs. fungi BLASTP at NCBI BLASTP vs. fungi Candida Homologs (CGD) Candida Homologs (CandidaDB) Fungal Alignment Fungal Orthogroups Repository Ortholog Search (P-POD) PhylomeDB Synteny Viewer Yeast Gene Order Browser (YGOB) eukarYotic OrtholoGY (YOGY)

Physical Properties and Transcript Information: predicted from sequence [TOP] [NEXT]

Protein Sequence Calculations from Predicted Full length Translation N-term MVLADLG C-term AKQFGMG Length(aa) 541 MW(Da) 59,624 pI 9.04 Amino Acid Composition (full length) GCG tools: PepPlot, Helical Wheel, PepStruct Transcript Translation Calculations Codon Bias 0.196   Codon Adaptation Index 0.178   Frequency of Optimal Codons 0.528   Hydropathicity of Protein -0.343   Aromaticity Score 0.052

10 20 30 40 50 | | | | | MVLADLGKRINSAVNNAISNTQDDFTTSVDVMLKGIVTALLESDVNIALV SKLRNNIRSQLLSENRSEKSTTNAQTKKLIQKTVFDELCKLVTCEGSEEK AFVPKKRKTNIIMFVGLQGSGKTTSCTKLAVYYSKRGFKVGLVCADTFRA GAFDQLKQNAIRARIPFYGSYTETDPAKVAEEGINKFKKEKFDIIIVDTS GRHHQEEELFQEMIEISNVIKPNQTIMVLDASIGQAAEQQSKAFKESSDF GAIILTKMDGHARGGGAISAVAATNTPIIFIGTGEHIHDLEKFSPKSFIS KLLGIGDIESLFEQLQTVSNKEDAKATMENIQKGKFTLLDFKKQMQTIMK MGPLSNIAQMIPGMSNMMNQVGEEETSQKMKKMVYVLDSMTKEELESDGR MFIEEPTRMVRVAKGSGTSVFEVEMILMQQQMMARMAQTATQQQPGAPGA NARMPGMPNMPGMPNMPGMPNMPGMPKVTPQMMQQAQQKLKQNPGLMQNM MNMFGGGMGGGMGGGMPDMNEMMKMMQDPQMQQMAKQFGMG*

Protein Structures from PDB: proteins of known structure with sequence similarity to SRP54/YPR088C, based on Smith-Waterman analysis. [TOP] [NEXT]

PDB protein structure(s) homologous to SRP54 Homolog Source (per PDB) Protein Alignment: SRP54 vs. Homolog External Links P-Value %Identical %Similar Alignment 2j37 ( Chain: W) Model of mammalian srp bound to 80s rncs PDB_Info PDB_Structure Homo sapiens | Canis sp. | Triticum sp. | Triticum sp | Haloarcula marismortui 1.7e-92 48 29 View alignment SCOP MMDB CATH 3dm5 ( Chain: B, A) Structures of srp54 and srp19, the two proteins assembling the ribonucleic core of the signal recognition particle from the archaeon pyrococcus furiosus. PDB_Info PDB_Structure Pyrococcus furiosus Chain B = 2.3e-65 42 32 View alignment SCOP MMDB CATH Chain A = 2.3e-65 42 32 View alignment 2v3c ( Chain: D, C) Crystal structure of the srp54-srp19-7s.s srp rna complex of m. jannaschii PDB_Info PDB_Structure Methanocaldococcus jannaschii Chain D = 1.4e-60 43 32 View alignment SCOP MMDB CATH Chain C = 1.4e-60 43 32 View alignment 1qzw ( Chain: C, G, E, A) Crystal structure of the complete core of archaeal srp and implications for inter-domain communication PDB_Info PDB_Structure Sulfolobus solfataricus Chain C = 3.1e-59 42 29 View alignment SCOP MMDB CATH Chain G = 3.1e-59 42 29 View alignment Chain E = 3.1e-59 42 29 View alignment Chain A = 3.1e-59 42 29 View alignment 1qzx ( Chain: A, B) Crystal structure of the complete core of archaeal srp and implications for inter-domain communication PDB_Info PDB_Structure Sulfolobus solfataricus Chain A = 3.1e-59 42 29 View alignment SCOP MMDB CATH Chain B = 3.1e-59 42 29 View alignment 2iy3 ( Chain: A) Structure of the e. coli signal recognition particle bound to a translating ribosome PDB_Info PDB_Structure Thermus aquaticus, sulfolobus solfataricus | Escherichia coli 8.3e-43 35 32 View alignment SCOP MMDB CATH 1j8m ( Chain: F) Signal recognition particle conserved gtpase domain from a. ambivalens PDB_Info PDB_Structure Acidianus ambivalens 5.0e-41 45 29 View alignment SCOP MMDB CATH 1j8y ( Chain: F) Signal recognition particle conserved gtpase domain from a. ambivalens t112a mutant PDB_Info PDB_Structure Acidianus ambivalens 1.1e-40 45 29 View alignment SCOP MMDB CATH 2ffh ( Chain: C, A, B) The signal sequence binding protein ffh from thermus aquaticus PDB_Info PDB_Structure Thermus aquaticus Chain C = 2.1e-38 34 32 View alignment SCOP MMDB CATH Chain A = 2.1e-38 34 32 View alignment Chain B = 2.1e-38 34 32 View alignment 2j28 ( Chain: 9) Model of e. coli srp bound to 70s rncs PDB_Info PDB_Structure Escherichia coli 4.6e-38 31 34 View alignment SCOP MMDB CATH 3e70 ( Chain: C) Structures and conformations in solution of the signal recognition particle receptor from the archaeon pyrococcus furiosus PDB_Info PDB_Structure Pyrococcus furiosus 7.1e-29 36 35 View alignment SCOP MMDB CATH 3dmd ( Chain: B, C, A) Structures and conformations in solution of the signal recognition particle receptor from the archaeon pyrococcus furiosus PDB_Info PDB_Structure Pyrococcus furiosus Chain B = 7.1e-29 36 35 View alignment SCOP MMDB CATH Chain C = 7.1e-29 36 35 View alignment Chain A = 7.1e-29 36 35 View alignment 3dm9 ( Chain: B) Structures and conformations in solution of the signal recognition particle receptor from the archaeon pyrococcus furiosus PDB_Info PDB_Structure Pyrococcus furiosus 7.1e-29 36 35 View alignment SCOP MMDB CATH 1rj9 ( Chain: B, A) Structure of the heterodimer of the conserved gtpase domains of the signal recognition particle (ffh) and its receptor (ftsy) PDB_Info PDB_Structure Thermus aquaticus Chain B = 2.6e-27 36 31 View alignment SCOP MMDB CATH Chain A = 3.3e-23 32 33 View alignment 2j45 ( Chain: A, B) Water structure of t. aquaticus ffh ng domain at 1.1a resolution PDB_Info PDB_Structure Thermus aquaticus Chain A = 1.0e-26 35 32 View alignment SCOP MMDB CATH Chain B = 1.0e-26 35 32 View alignment 2c03 ( Chain: B, A) Gdp complex of srp gtpase ffh ng domain PDB_Info PDB_Structure Thermus aquaticus Chain B = 1.0e-26 35 32 View alignment SCOP MMDB CATH Chain A = 1.0e-26 35 32 View alignment 2j46 ( Chain: B, A) Water structure of t. aquaticus ffh ng domain at 1.1a resolution PDB_Info PDB_Structure Thermus aquaticus Chain B = 1.0e-26 35 32 View alignment SCOP MMDB CATH Chain A = 1.0e-26 35 32 View alignment 1o87 ( Chain: B, A) A new mggdp complex of the ffh ng domain PDB_Info PDB_Structure Thermus aquaticus Chain B = 1.0e-26 35 32 View alignment SCOP MMDB CATH Chain A = 1.0e-26 35 32 View alignment 2c04 ( Chain: A, B) Gmppcp complex of srp gtpase ffh ng domain at ultra-high resolution PDB_Info PDB_Structure Thermus aquaticus Chain A = 1.0e-26 35 32 View alignment SCOP MMDB CATH Chain B = 1.0e-26 35 32 View alignment 1ry1 ( Chain: U, W) Structure of the signal recognition particle interacting with the elongation-arrested ribosome PDB_Info PDB_Structure Homo sapiens | Thermus aquaticus | Mus musculus | Tursiops truncatus Chain U = 1.8e-26 36 31 View alignment SCOP MMDB CATH Chain W = 1.2e-11 43 37 View alignment 1jpn ( Chain: A, B) Gmppnp complex of srp gtpase ng domain PDB_Info PDB_Structure Thermus aquaticus Chain A = 1.8e-26 36 31 View alignment SCOP MMDB CATH Chain B = 1.8e-26 36 31 View alignment 1jpj ( Chain: A) Gmppnp complex of srp gtpase ng domain PDB_Info PDB_Structure Thermus aquaticus 1.8e-26 36 31 View alignment SCOP MMDB CATH 1ffh ( Chain: A) N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus PDB_Info PDB_Structure Thermus aquaticus 6.0e-26 35 32 View alignment SCOP MMDB CATH 1ls1 ( Chain: A) T. aquaticus ffh ng domain at 1.1a resolution PDB_Info PDB_Structure Thermus aquaticus 6.0e-26 35 32 View alignment SCOP MMDB CATH 1ng1 ( Chain: A) N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus PDB_Info PDB_Structure Thermus aquaticus 2.0e-25 35 32 View alignment SCOP MMDB CATH 2j7p ( Chain: A, B, E, D) Gmppnp-stabilized ng domain complex of the srp gtpases ffh and ftsy PDB_Info PDB_Structure Thermus aquaticus Chain A = 2.0e-25 35 32 View alignment SCOP MMDB CATH Chain B = 2.0e-25 35 32 View alignment Chain E = 5.9e-24 33 32 View alignment Chain D = 5.9e-24 33 32 View alignment 3ng1 ( Chain: B, A) N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus PDB_Info PDB_Structure Thermus aquaticus Chain B = 2.0e-25 35 32 View alignment SCOP MMDB CATH Chain A = 2.0e-25 35 32 View alignment 2cnw ( Chain: C, B, A, F, E, D) Gdpalf4 complex of the srp gtpases ffh and ftsy PDB_Info PDB_Structure Thermus aquaticus Chain C = 2.0e-25 35 32 View alignment SCOP MMDB CATH Chain B = 2.0e-25 35 32 View alignment Chain A = 2.0e-25 35 32 View alignment Chain F = 6.0e-24 33 32 View alignment Chain E = 6.0e-24 33 32 View alignment Chain D = 6.0e-24 33 32 View alignment 1okk ( Chain: A, D) Homo-heterodimeric complex of the srp gtpases PDB_Info PDB_Structure Thermus aquaticus Chain A = 2.0e-25 35 32 View alignment SCOP MMDB CATH Chain D = 6.5e-24 33 32 View alignment 2ng1 ( Chain: A) N and gtpase domains of the signal sequence recognition protein ffh from thermus aquaticus PDB_Info PDB_Structure Thermus aquaticus 2.0e-25 35 32 View alignment SCOP MMDB CATH 2iyl ( Chain: D) Structure of an ftsy:gdp complex PDB_Info PDB_Structure Thermus aquaticus 6.0e-24 33 32 View alignment SCOP MMDB CATH 2q9c ( Chain: A, B) Structure of ftsy:gmppnp with mgcl complex PDB_Info PDB_Structure Thermus aquaticus Chain A = 6.5e-24 33 32 View alignment SCOP MMDB CATH Chain B = 6.5e-24 33 32 View alignment 2q9a ( Chain: A, B) Structure of apo ftsy PDB_Info PDB_Structure Thermus aquaticus Chain A = 6.5e-24 33 32 View alignment SCOP MMDB CATH Chain B = 6.5e-24 33 32 View alignment 2q9b ( Chain: A, B) Structure of ftsy:gmppnp complex PDB_Info PDB_Structure Thermus aquaticus Chain A = 6.5e-24 33 32 View alignment SCOP MMDB CATH Chain B = 6.5e-24 33 32 View alignment 1vma ( Chain: A, B) Crystal structure of cell division protein ftsy (tm0570) from thermotoga maritima at 1.60 a resolution PDB_Info PDB_Structure Thermotoga maritima Chain A = 1.6e-23 40 31 View alignment SCOP MMDB CATH Chain B = 1.6e-23 40 31 View alignment 1zu5 ( Chain: A, B) Crystal structure of ftsy from mycoplasma mycoides- space group h32 PDB_Info PDB_Structure Mycoplasma mycoides Chain A = 3.1e-23 30 38 View alignment SCOP MMDB CATH Chain B = 3.1e-23 30 38 View alignment 1zu4 ( Chain: A) Crystal structure of ftsy from mycoplasma mycoides- space group p21212 PDB_Info PDB_Structure Mycoplasma mycoides 3.1e-23 30 38 View alignment SCOP MMDB CATH 3b9q ( Chain: A) The crystal structure of cpftsy from arabidopsis thaliana PDB_Info PDB_Structure Arabidopsis thaliana 6.1e-23 33 32 View alignment SCOP MMDB CATH 2og2 ( Chain: A) Crystal structure of chloroplast ftsy from arabidopsis thaliana PDB_Info PDB_Structure Arabidopsis thaliana 7.8e-23 33 32 View alignment SCOP MMDB CATH 2qy9 ( Chain: A) Structure of the ng+1 construct of the e. coli srp receptor ftsy PDB_Info PDB_Structure Escherichia coli 1.2e-21 34 31 View alignment SCOP MMDB CATH 1fts ( Chain: A) Signal recognition particle receptor from e. coli PDB_Info PDB_Structure Escherichia coli 1.3e-21 34 31 View alignment SCOP MMDB CATH 1mfq ( Chain: C) Crystal structure analysis of a ternary s-domain complex of human signal recognition particle PDB_Info PDB_Structure Homo sapiens 3.3e-12 43 38 View alignment SCOP MMDB CATH 2go5 ( Chain: W) Structure of signal recognition particle receptor (sr) in complex with signal recognition particle (srp) and ribosome nascent chain complex PDB_Info PDB_Structure Canis sp. | Triticum sp. | Homo sapiens | Mus musculus 1.2e-11 43 37 View alignment SCOP MMDB CATH 1qb2 ( Chain: A, B) Crystal structure of the conserved subdomain of human protein srp54m at 2.1a resolution: evidence for the mechanism of signal peptide binding PDB_Info PDB_Structure Homo sapiens Chain A = 1.2e-11 43 37 View alignment SCOP MMDB CATH Chain B = 1.2e-11 43 37 View alignment 2px0 ( Chain: H, C, A, G, F, E, D, B) Crystal structure of flhf complexed with gmppnp/mg(2+) PDB_Info PDB_Structure Bacillus subtilis Chain H = 6.2e-08 27 32 View alignment SCOP MMDB CATH Chain C = 6.2e-08 27 32 View alignment Chain A = 6.2e-08 27 32 View alignment Chain G = 6.2e-08 27 32 View alignment Chain F = 6.2e-08 27 32 View alignment Chain E = 6.2e-08 27 32 View alignment Chain D = 6.2e-08 27 32 View alignment Chain B = 6.2e-08 27 32 View alignment 2px3 ( Chain: A) Crystal structure of flhf complexed with gtp/mg(2+) PDB_Info PDB_Structure Bacillus subtilis 6.2e-08 27 32 View alignment SCOP MMDB CATH 2jqe ( Chain: A) Soution structure of af54 m-domain PDB_Info PDB_Structure Archaeoglobus fulgidus 1.0e-07 37 30 View alignment SCOP MMDB CATH 1wgw ( Chain: A) Solution structure of the n-terminal domain of mouse putative signal recoginition particle 54 (srp54) PDB_Info PDB_Structure Mus musculus 5.0e-05 40 31 View alignment SCOP MMDB CATH 1hq1 ( Chain: A) Structural and energetic analysis of rna recognition by a universally conserved protein from the signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.001999 29 34 View alignment SCOP MMDB CATH 2pxb ( Chain: A) Variant 2 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxp ( Chain: A) Variant 13 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxv ( Chain: A) Variant 6 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxt ( Chain: A) Variant 15 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxd ( Chain: A) Variant 1 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxf ( Chain: A) Variant 5 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxk ( Chain: A) Variant 8 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxq ( Chain: A) Variant 14 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxu ( Chain: A) Variant 16 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxl ( Chain: A) Variant 9 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH 2pxe ( Chain: A) Variant 4 of ribonucleoprotein core of the e. coli signal recognition particle PDB_Info PDB_Structure Escherichia coli 0.002200 29 34 View alignment SCOP MMDB CATH

Genome-wide Expression and Other Large-Scale Analyses [TOP] [NEXT]
Functional Analysis Expression Connection Summary Cell cycle and metabolic oscillation Cell cycle transcript profile Cyclebase Genevestigator GermOnline SPELL Microarray Search YGAC Triples Yeast Microarray Global Viewer YeastFunc	You can also search multiple datasets simultaneously using Expression Connection for expression studies or Function Junction for other large scale analyses.

Locus History (misc. notes) [TOP] [NEXT]

Nomenclature History

Standard Name	Reference
SRP54	SGD (2007) Information without a citation in SGD

Sequence Retrieval [TOP] [NEXT]
Sequence Type	Output Format
Genomic DNA	GCG | FASTA | NoHeader
Genomic DNA with 1 kb up and downstream	GCG | FASTA | NoHeader
DNA coding sequence (without introns, without flanking regions)	GCG | FASTA | NoHeader
Protein Translation of ORF	GCG | FASTA | NoHeader
6-Frame Translation(with Restriction Map)	GCG
Restriction Fragment Sizes	GCG
Sequence Analysis Tools BLASTP BLASTN Design Primers FASTA aa FASTA nt Restriction Fragment Map Restriction Fragment Sizes Six-Frame Translation

Sequence from other databases
Sequence ID	Source
YPR088C	SGD Systematic Sequence
856203	NCBI: Gene ID
NP_015413.1	NCBI: RefSeq protein version ID
NP_015413.1	NCBI: RefSeq protein version ID
6325345	NCBI: NCBI protein GI

Map and Displays [TOP] [NEXT]
Physical, Genetic Maps:	Chromosomal Feature Map	GBrowse	Combined Physical and Genetic Map	Genetic Distance vs. Physical Distance Ratios
Similarity Viewers:	Synteny Viewer	Genomic Stripe View	SAGE Results Map

Localization [TOP] [NEXT]
Localization Resources YGAC Triples YeastGFP DB (UCSF) at SGD

Community Annotation [TOP] [NEXT]
No community annotation available.

Literature Guide: papers categorized by topic. [TOP]
Topics	Reference	Other Genes Addressed
31 curated references; 0 references not yet curated
Reviews	Fonzi WA (2009) The protein secretory pathway of Candida albicans. Mycoses	|BTT1 |EGD1 |EGD2 |GEA1 |GEA2 |GSG1 |NCE101 |NCE102 |SCR1 |SEC14 |SEC3 |SEC4 |SEC61 |SEC65 |MORE
Mutants/Phenotypes Strains/Constructs	Breslow DK, et al. (2008) A comprehensive strategy enabling high-resolution functional analysis of the yeast genome. Nat Methods 5(8):711-8	|AAR2 |ABD1 |ABF1 |ACC1 |ACP1 |ADE13 |AFG2 |ALA1 |ALG1 |ALG13 |ALG14 |ALG2 |ALG7 |ALR1 |MORE
Other Features	Grallath S, et al. (2007) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 8(11):1086	|BTT1 |EGD1 |EGD2 |RPL25 |SSB1 |SSB2 |SSZ1
Cellular Location Protein Physical Properties Protein Processing/Modification/Regulation Protein-protein Interactions Strains/Constructs	Raue U, et al. (2007) Association of protein biogenesis factors at the yeast ribosomal tunnel exit is affected by the translational status and nascent polypeptide sequence. J Biol Chem 282(11):7809-16	|ARD1 |ASC1 |MAP1 |MAP2 |NAT1 |RPL19A |RPL19B |RPL39 |RPS17A |RPS17B |RPS9A |RPS9B |SSB1 |SSB2 |MORE
Evolution Fungal Related Genes/Proteins	De Hertogh B, et al. (2006) Emergence of species-specific transporters during evolution of the hemiascomycete phylum. Genetics 172(2):771-81	|AAC1 |AAC3 |ACS2 |ADP1 |ADY2 |AGC1 |AGP1 |AGP2 |AGP3 |ALP1 |ALR1 |ALR2 |ANT1 |AQR1 |MORE
Other Features	Grallath S, et al. (2006) L25 functions as a conserved ribosomal docking site shared by nascent chain-associated complex and signal-recognition particle. EMBO Rep 7(1):78-84	|BTT1 |EGD1 |EGD2 |RPL25 |SSB1 |SSB2 |SSZ1
Reviews	Pool MR (2005) Signal recognition particles in chloroplasts, bacteria, yeast and mammals (review). Mol Membr Biol 22(1-2):3-15	|SCR1 |SEC65 |SRP101 |SRP14 |SRP21 |SRP68 |SRP72
Fungal Related Genes/Proteins	Sims AH, et al. (2005) Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo. Appl Environ Microbiol 71(5):2737-47	|BCH2 |EPT1 |INO1 |KAR2 |NCE102 |RPT3 |SEC27 |SEC63 |SEC65 |SEC72 |SHR3 |SLC1 |UBA1
Function/Process Protein-Nucleic Acid Interactions	Van Nues RW and Brown JD (2004) Saccharomyces SRP RNA secondary structures: a conserved S-domain and extended Alu-domain. RNA 10(1):75-89	|SCR1 |SEC65
Reviews	Wild K, et al. (2004) SRP meets the ribosome. Nat Struct Mol Biol 11(11):1049-53
Reviews	Dani HM, et al. (2003) Advances in the structure and functions of signal recognition particle in protein targeting. J Biol Regul Homeost Agents 17(4):303-7	|SRP14
Function/Process Protein-protein Interactions	Helmers J, et al. (2003) The beta-subunit of the protein-conducting channel of the endoplasmic reticulum functions as the guanine nucleotide exchange factor for the beta-subunit of the signal recognition particle receptor. J Biol Chem 278(26):23686-90	|SBH1 |SBH2 |SEC61 |SEC7
Function/Process Mutants/Phenotypes Strains/Constructs	Willer M, et al. (2003) An in vitro assay using overexpressed yeast SRP demonstrates that cotranslational translocation is dependent upon the J-domain of Sec63p. Biochemistry 42(23):7171-7	|SCR1 |SEC63 |SEC65 |SRP14 |SRP21 |SRP68 |SRP72
Non-Fungal Related Genes/Proteins	Kuglstatter A, et al. (2002) Induced structural changes of 7SL RNA during the assembly of human signal recognition particle. Nat Struct Biol 9(10):740-4
Cellular Location Function/Process	Grosshans H, et al. (2001) Biogenesis of the signal recognition particle (SRP) involves import of SRP proteins into the nucleolus, assembly with the SRP-RNA, and Xpo1p-mediated export. J Cell Biol 153(4):745-62	|CRM1 |DIS3 |KAP123 |MEX67 |MTR10 |NSP1 |NUP159 |NUP85 |PSE1 |RNA1 |RRP4 |SCR1 |SEC65 |SRM1 |MORE
Cellular Location Function/Process Protein Processing/Modification/Regulation Techniques and Reagents	Ciufo LF and Brown JD (2000) Nuclear export of yeast signal recognition particle lacking Srp54p by the Xpo1p/Crm1p NES-dependent pathway. Curr Biol 10(20):1256-64	|CRM1 |SCR1 |SEC65 |SRP14 |SRP21 |SRP68 |SRP72 |YRB2
Non-Fungal Related Genes/Proteins	Clemons WM Jr, et al. (1999) Crystal structure of the conserved subdomain of human protein SRP54M at 2.1 A resolution: evidence for the mechanism of signal peptide binding. J Mol Biol 292(3):697-705
Techniques and Reagents	Arnold CE, et al. (1998) Leader peptide efficiency correlates with signal recognition particle dependence in Saccharomyces cerevisiae. Biotechnol Bioeng 59(3):286-93
Function/Process Genetic Interactions Mutants/Phenotypes	Ogg SC, et al. (1998) A functional GTPase domain, but not its transmembrane domain, is required for function of the SRP receptor beta-subunit. J Cell Biol 142(2):341-54	|KAR2 |SRP101 |SRP102
Mutants/Phenotypes Substrates/Ligands/Cofactors	Rothe C and Lehle L (1998) Sorting of invertase signal peptide mutants in yeast dependent and independent on the signal-recognition particle. Eur J Biochem 252(1):16-24
Non-Fungal Related Genes/Proteins	Lee IH and Ogrydziak DM (1997) Yarrowia lipolytica SRP54 homolog and translocation of Kar2p. Yeast 13(6):499-513	|KAR2
Non-Fungal Related Genes/Proteins	Thompson SA, et al. (1995) Nucleotide sequence of the Aspergillus niger srpA gene. Gene 167(1-2):337-8
Mutants/Phenotypes Other Features	Arnold CE and Wittrup KD (1994) The stress response to loss of signal recognition particle function in Saccharomyces cerevisiae. J Biol Chem 269(48):30412-8	|HSP104 |HSP82 |KAR2 |SSA1 |SSA2 |SSA3 |SSA4 |YDJ1
Mutants/Phenotypes Protein-protein Interactions Strains/Constructs	Brown JD, et al. (1994) Subunits of the Saccharomyces cerevisiae signal recognition particle required for its functional expression. EMBO J 13(18):4390-400	|SCR1 |SEC65 |SRP14 |SRP21 |SRP68 |SRP72
Genetic Interactions Protein-protein Interactions Strains/Constructs	Hann BC, et al. (1992) SEC65 gene product is a subunit of the yeast signal recognition particle required for its integrity. Nature 356(6369):532-3	|SEC65
Genetic Interactions Strains/Constructs	Stirling CJ and Hewitt EW (1992) The S. cerevisiae SEC65 gene encodes a component of yeast signal recognition particle with homology to human SRP19. Nature 356(6369):534-7	|SEC65
Function/Process Mutants/Phenotypes Strains/Constructs	Amaya Y and Nakano A (1991) SRH1 protein, the yeast homologue of the 54 kDa subunit of signal recognition particle, is involved in ER translocation of secretory proteins. FEBS Lett 283(2):325-8
Mutants/Phenotypes Protein-Nucleic Acid Interactions Strains/Constructs	Hann BC and Walter P (1991) The signal recognition particle in S. cerevisiae. Cell 67(1):131-44	|SCR1
DNA/RNA Sequence Features Non-Fungal Related Genes/Proteins Protein Sequence Features	Amaya Y, et al. (1990) Isolation of a yeast gene, SRH1, that encodes a homologue of the 54K subunit of mammalian signal recognition particle. J Biochem 107(3):457-63	|SUA7
Non-Fungal Related Genes/Proteins	Zopf D, et al. (1990) The methionine-rich domain of the 54 kd protein subunit of the signal recognition particle contains an RNA binding site and can be crosslinked to a signal sequence. EMBO J 9(13):4511-7	|SCR1 |SEC65
DNA/RNA Sequence Features Function/Process Fungal Related Genes/Proteins Non-Fungal Related Genes/Proteins Protein Sequence Features	Hann BC, et al. (1989) Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth. J Cell Biol 109(6 Pt 2):3223-30

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