Tag Content
SG ID
SG00016014 
UniProt Accession
Theoretical PI
10.25  
Molecular Weight
31231 Da  
Genbank Nucleotide ID
Genbank Protein ID
Gene Name
Rps2 
Gene Synonyms/Alias
Llrep3, Rps4 
Protein Name
40S ribosomal protein S2 
Protein Synonyms/Alias
40S ribosomal protein S4; Protein LLRep3; 
Organism
Mus musculus (Mouse) 
NCBI Taxonomy ID
10090 
Chromosome Location
chr:17;24855061-24858874;1
View in Ensembl genome browser  
Function in Stage
Uncertain 
Function in Cell Type
Uncertain 
Probability (GAS) of Function in Spermatogenesis
0.002166115 
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.
Description
Temporarily unavailable 
Abstract of related literatures
1. A mouse cDNA clone corresponding to an abundantly transcribed poly(A)+ mRNA was found to be represented by 200 copies in mammalian genomes. To understand the origin and nature of this sequence family, we studied two genomic members and two cDNA clones from mouse liver. The DNA sequence of the coding strand of a full-length cDNA clone was shown to have an open reading frame capable of encoding a 25-kilodalton polypeptide that has not been previously described. In vitro transcription-translation experiments verified the presence of an open reading frame encoding a protein of the predicted size. Restriction analysis of genomic DNA and DNA sequence analysis of genomic clones indicated that many of the 200 members of this family represent processed pseudogenes, with one or a small number of active structural genes. The vast majority of the genomic copies are heterogeneous in length, truncated at their 5' ends with respect to the mRNA, and do not appear to have intervening sequences. Two distinct genomic members of this family were sequenced and found to represent incomplete copies of the mRNA. Both are 5' truncated at slightly different points with respect to the mRNA. Both pseudogenes have multiple base changes, insertions, and deletions relative to the mRNA, and one of them encodes the poly(A) tail of the mRNA. The expression of this gene family is highest in rapidly dividing cells such as early mouse embryos and testis, but was seen in all tissues tested. This gene shows extremely high sequence conservation, extending to chicken, amphibian, and nematode genomes. Surprisingly, the gene appears to exist in only one copy in these organisms. PMID: [3405219] 

2. 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] 

3. External stimuli trigger internal signaling events within a cell that may represent either a temporary or permanent shift in the phosphorylation state of its proteome. Numerous reports have elucidated phosphorylation sites from a variety of biological samples and more recent studies have monitored the temporal dynamics of protein phosphorylation as a given system is perturbed. Understanding which proteins are phosphorylated as well as when they are phosphorylated may indicate novel functional roles within a system and allow new therapeutic avenues to be explored. To elucidate the dynamics of protein phosphorylation within differentiating murine P19 embryonal carcinoma cells, we induced P19 cells to differentiate using all-trans-retinoic acid and developed a strategy that combines isotopically labeled methyl esterification, immobilized metal affinity chromatography, mass spectrometric analysis, and a rigorous and unique data evaluation approach. We present the largest differential phosphoproteomic analysis using isotopically labeled methyl esterification to date, identifying a total of 472 phosphorylation sites on 151 proteins; 56 of these proteins had altered abundances following treatment with retinoic acid and approximately one-third of these have been previously associated with cellular differentiation. A series of bioinformatic tools were used to extract information from the data and explore the implications of our findings. This study represents the first global gel-free analysis that elucidates protein phosphorylation dynamics during cellular differentiation. PMID: [17622165] 

4. Metazoans employ reversible tyrosine phosphorylation to regulate innumerable biological processes. Thus, the large-scale identification of tyrosine phosphorylation sites from primary tissues is an essential step toward a molecular systems understanding of dynamic regulation in vivo. The relative paucity of phosphotyrosine has greatly limited its identification in large-scale phosphoproteomic experiments. However, using antiphosphotyrosine peptide immunoprecipitations, we report the largest study to date of tyrosine phosphorylation sites from primary tissue, identifying 414 unique tyrosine phosphorylation sites from murine brain. To measure the conservation of phosphorylated tyrosines and their surrounding residues, we constructed a computational pipeline and identified patterns of conservation within the signature of phosphotyrosine. PMID: [18034455] 

5. Protein phosphorylation is a complex network of signaling and regulatory events that affects virtually every cellular process. Our understanding of the nature of this network as a whole remains limited, largely because of an array of technical challenges in the isolation and high-throughput sequencing of phosphorylated species. In the present work, we demonstrate that a combination of tandem phosphopeptide enrichment methods, high performance MS, and optimized database search/data filtering strategies is a powerful tool for surveying the phosphoproteome. Using our integrated analytical platform, we report the identification of 5,635 nonredundant phosphorylation sites from 2,328 proteins from mouse liver. From this list of sites, we extracted both novel and known motifs for specific Ser/Thr kinases including a "dipolar" motif. We also found that C-terminal phosphorylation was more frequent than at any other location and that the distribution of potential kinases for these sites was unique. Finally, we identified double phosphorylation motifs that may be involved in ordered phosphorylation. PMID: [17242355] 

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Function
 
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Subcellular Location
 
Tissue Specificity
 
Gene Ontology
GO IDGO termEvidence
GO:0015935 C:small ribosomal subunit IEA:InterPro.
GO:0003723 F:RNA binding IEA:InterPro.
GO:0003735 F:structural constituent of ribosome IEA:InterPro.
GO:0006412 P:translation IEA:InterPro.
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Interpro
IPR014720;    dsRNA-bd-like.
IPR000851;    Ribosomal_S5.
IPR005324;    Ribosomal_S5_C.
IPR020568;    Ribosomal_S5_D2-typ_fold.
IPR014721;    Ribosomal_S5_D2-typ_fold_subgr.
IPR005711;    Ribosomal_S5_euk/arc.
IPR013810;    Ribosomal_S5_N.
IPR018192;    Ribosomal_S5_N_CS.
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Pfam
PF00333;    Ribosomal_S5;    1.
PF03719;    Ribosomal_S5_C;    1.
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SMART
PROSITE
PS00585;    RIBOSOMAL_S5;    1.
PS50881;    S5_DSRBD;    1.
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PRINTS
Created Date
18-Oct-2012 
Record Type
GAS predicted 
Sequence Annotation
INIT_MET      1      1       Removed (By similarity).
CHAIN         2    293       40S ribosomal protein S2.
                             /FTId=PRO_0000131674.
DOMAIN      102    165       S5 DRBM.
MOD_RES       2      2       N-acetylalanine (By similarity).
MOD_RES      77     77       Phosphoserine.
MOD_RES      82     82       Phosphotyrosine.
MOD_RES      85     85       Phosphoserine.
MOD_RES     133    133       Phosphotyrosine.
MOD_RES     263    263       N6-acetyllysine (By similarity).
MOD_RES     264    264       Phosphoserine.
MOD_RES     275    275       N6-acetyllysine (By similarity).
MOD_RES     278    278       Phosphothreonine (By similarity).
MOD_RES     281    281       Phosphoserine (By similarity).
MOD_RES     293    293       Phosphothreonine (By similarity).
CONFLICT    270    270       T -> S (in Ref. 1; AAA40074).
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Nucleotide Sequence
Length: 1728 bp   Go to nucleotide: FASTA
Protein Sequence
Length: 293 bp   Go to amino acid: FASTA
The verified Protein-Protein interaction information
UniProt
Gene Symbol Ref Databases
YwhabIntAct 
Other Protein-Protein interaction resources
String database  
View Microarray data
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