Tag Content
UniProt Accession
Theoretical PI
Molecular Weight
12510 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Gene Synonyms/Alias
Protein Name
Signal recognition particle 14 kDa protein 
Protein Synonyms/Alias
Mus musculus (Mouse) 
NCBI Taxonomy ID
Chromosome Location
View in Ensembl genome browser  
Function in Stage
Function in Cell Type
Probability (GAS) of Function in Spermatogenesis
The probability was calculated by GAS algorithm, ranging from 0 to 1. The closer it is to 1, the more possibly it functions in spermatogenesis.
Temporarily unavailable 
Abstract of related literatures
1. Using an enhancement of the polymerase chain reaction (PCR) technique, we have isolated a complementary DNA encoding SRP14 (14-kDa subunit), one of six proteins contained in the signal recognition particle (SRP). Several pools of degenerate oligonucleotides encoding different peptide sequences of SRP14 were used to generate amplified DNA by the PCR. A cross-hybridization procedure was developed to identify the authentic SRP14 cDNA clone among the amplified DNA products obtained by PCR. The basis of this approach is the assumption that a partial cDNA of SRP14 should be the only DNA product common to two amplification reactions primed with different degenerate oligonucleotide mixtures. The partial canine cDNA of SRP14 identified by this procedure served as a probe to isolate a complete cDNA clone of SRP14 from a mouse embryonic cDNA library in lambda phage gt10. PMID: [2557625] 

2. This study describes comprehensive polling of transcription start and termination sites and analysis of previously unidentified full-length complementary DNAs derived from the mouse genome. We identify the 5' and 3' boundaries of 181,047 transcripts with extensive variation in transcripts arising from alternative promoter usage, splicing, and polyadenylation. There are 16,247 new mouse protein-coding transcripts, including 5154 encoding previously unidentified proteins. Genomic mapping of the transcriptome reveals transcriptional forests, with overlapping transcription on both strands, separated by deserts in which few transcripts are observed. The data provide a comprehensive platform for the comparative analysis of mammalian transcriptional regulation in differentiation and development. PMID: [16141072] 

3. The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a random strategy to select clones from a large number of cDNA libraries from diverse tissues. Candidate clones were chosen based on 5'-EST sequences, and then fully sequenced to high accuracy and analyzed by algorithms developed for this project. Currently, more than 11,000 human and 10,000 mouse genes are represented in MGC by at least one clone with a full ORF. The random selection approach is now reaching a saturation point, and a transition to protocols targeted at the missing transcripts is now required to complete the mouse and human collections. Comparison of the sequence of the MGC clones to reference genome sequences reveals that most cDNA clones are of very high sequence quality, although it is likely that some cDNAs may carry missense variants as a consequence of experimental artifact, such as PCR, cloning, or reverse transcriptase errors. Recently, a rat cDNA component was added to the project, and ongoing frog (Xenopus) and zebrafish (Danio) cDNA projects were expanded to take advantage of the high-throughput MGC pipeline. PMID: [15489334] 

4. Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 microg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at -80 degrees C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies. PMID: [19367708] 

5. The mammalian signal recognition particle (SRP) is an 11S cytoplasmic ribonucleoprotein that plays an essential role in protein sorting. SRP recognizes the signal sequence of the nascent polypeptide chain emerging from the ribosome, and targets the ribosome-nascent chain-SRP complex to the rough endoplasmic reticulum. The SRP consists of six polypeptides (SRP9, SRP14, SRP19, SRP54, SRP68 and SRP72) and a single 300 nucleotide RNA molecule. SRP9 and SRP14 proteins form a heterodimer that binds to the Alu domain of SRP RNA which is responsible for translation arrest. We report the first crystal structure of a mammalian SRP protein, that of the mouse SRP9/14 heterodimer, determined at 2.5 A resolution. SRP9 and SRP14 are found to be structurally homologous, containing the same alpha-beta-beta-beta-alpha fold. This we designate the Alu binding module (Alu bm), an additional member of the family of small alpha/beta RNA binding domains. The heterodimer has pseudo 2-fold symmetry and is saddle like, comprising a strongly curved six-stranded amphipathic beta-sheet with the four helices packed on the convex side and the exposed concave surface being lined with positively charged residues. PMID: [9233785] 

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Signal-recognition-particle assembly has a crucial rolein targeting secretory proteins to the rough endoplasmic reticulummembrane. SRP9 together with SRP14 and the Alu portion of the SRPRNA, constitutes the elongation arrest domain of SRP. The complexof SRP9 and SRP14 is required for SRP RNA binding. 
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Subcellular Location
Tissue Specificity
Gene Ontology
GO IDGO termEvidence
GO:0005786 C:signal recognition particle, endoplasmic reticulum targeting IEA:UniProtKB-KW.
GO:0008312 F:7S RNA binding IEA:InterPro.
GO:0030942 F:endoplasmic reticulum signal peptide binding IEA:InterPro.
GO:0045900 P:negative regulation of translational elongation IEA:InterPro.
GO:0042493 P:response to drug IEA:Compara.
GO:0006614 P:SRP-dependent cotranslational protein targeting to membrane IEA:InterPro.
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IPR003210;    Signal_recog_particle_SRP14.
IPR009018;    Signal_recog_particle_SRP9/14.
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PF02290;    SRP14;    1.
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Created Date
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    110       Signal recognition particle 14 kDa
MOD_RES      45     45       Phosphoserine.
HELIX         6     19
STRAND       21     23
STRAND       26     33
STRAND       55     64
STRAND       66     72
HELIX        76     90
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Nucleotide Sequence
Length: 706 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 110 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
Gene Symbol Ref Databases
Other Protein-Protein interaction resources
String database  
View Microarray data