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{{Infobox_gene}}
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'''40S ribosomal protein S27a''' is a [[protein]] that in humans is encoded by the ''RPS27A'' [[gene]].<ref name="pmid9582194">{{cite journal |vauthors=Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC | title = A map of 75 human ribosomal protein genes | journal = Genome Res | volume = 8 | issue = 5 | pages = 509–23 |date=Aug 1998 | pmid = 9582194 | pmc =  | doi =  10.1101/gr.8.5.509}}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RPS27A ribosomal protein S27a| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6233| accessdate = }}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_RPS27A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1aar.
| PDB = {{PDB2|1aar}}, {{PDB2|1cmx}}, {{PDB2|1d3z}}, {{PDB2|1f9j}}, {{PDB2|1fxt}}, {{PDB2|1g6j}}, {{PDB2|1gjz}}, {{PDB2|1nbf}}, {{PDB2|1ogw}}, {{PDB2|1otr}}, {{PDB2|1p3q}}, {{PDB2|1q0w}}, {{PDB2|1q5w}}, {{PDB2|1s1q}}, {{PDB2|1sif}}, {{PDB2|1tbe}}, {{PDB2|1ubi}}, {{PDB2|1ubq}}, {{PDB2|1ud7}}, {{PDB2|1uzx}}, {{PDB2|1v80}}, {{PDB2|1v81}}, {{PDB2|1wr1}}, {{PDB2|1wr6}}, {{PDB2|1wrd}}, {{PDB2|1xd3}}, {{PDB2|1xqq}}, {{PDB2|1yd8}}, {{PDB2|1yiw}}, {{PDB2|1yj1}}, {{PDB2|1yx5}}, {{PDB2|1yx6}}, {{PDB2|1zgu}}, {{PDB2|2ayo}}, {{PDB2|2bgf}}, {{PDB2|2c7m}}, {{PDB2|2c7n}}, {{PDB2|2d3g}}, {{PDB2|2den}}, {{PDB2|2dx5}}, {{PDB2|2fcm}}, {{PDB2|2fcn}}, {{PDB2|2fcq}}, {{PDB2|2fcs}}, {{PDB2|2fid}}, {{PDB2|2fif}}, {{PDB2|2fuh}}, {{PDB2|2g3q}}, {{PDB2|2g45}}, {{PDB2|2gbj}}, {{PDB2|2gbk}}, {{PDB2|2gbm}}, {{PDB2|2gbn}}, {{PDB2|2gbr}}, {{PDB2|2gmi}}, {{PDB2|2hd5}}, {{PDB2|2hth}}, {{PDB2|2ibi}}, {{PDB2|2j7q}}, {{PDB2|2nr2}}, {{PDB2|2o6v}}, {{PDB2|2oob}}
| Name = Ribosomal protein S27a
| HGNCid = 10417
| Symbol = RPS27A
| AltSymbols =; CEP80; HUBCEP80; UBA80; UBCEP1
| OMIM = 191343
| ECnumber = 
| Homologene = 37715
| MGIid = 1925544
| Function = {{GNF_GO|id=GO:0003735 |text = structural constituent of ribosome}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}} {{GNF_GO|id=GO:0005840 |text = ribosome}} {{GNF_GO|id=GO:0005843 |text = cytosolic small ribosomal subunit (sensu Eukaryota)}}
| Process = {{GNF_GO|id=GO:0006412 |text = translation}} {{GNF_GO|id=GO:0006464 |text = protein modification process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 6233
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_002945
    | Hs_RefseqmRNA = NM_002954
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr =
    | Hs_GenLoc_start =
    | Hs_GenLoc_end =
    | Hs_Uniprot =   
    | Mm_EntrezGene = 78294
    | Mm_Ensembl =   
    | Mm_RefseqmRNA = NM_001033865
    | Mm_RefseqProtein = NP_001029037
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Ribosomal protein S27a''', also known as '''RPS27A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RPS27A ribosomal protein S27a| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6233| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi.<ref name="entrez">{{cite web | title = Entrez Gene: RPS27A ribosomal protein S27a| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6233| accessdate = }}</ref>
| summary_text = [[Ubiquitin]], a highly conserved protein that has a major role in targeting cellular proteins for [[proteolysis|degradation]] by the 26S [[proteosome]], is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the [[N terminus]] and [[ribosomal protein]] S27a at the [[C terminus]]. When expressed in [[yeast]], the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the [[ribosome]] and belongs to the S27AE family of ribosomal proteins. It contains C4-type [[zinc finger]] domains and is located in the [[cytoplasm]]. [[Pseudogene]]s derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the [[ubiquitin-like protein]] fubi.<ref name="entrez"/>
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
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| citations =  
| citations =  
*{{cite journal  | author=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11-12 |pages= 933-47 |year= 1996 |pmid= 8722009 |doi=  }}
*{{cite journal  |vauthors=Wool IG, Chan YL, Glück A |title=Structure and evolution of mammalian ribosomal proteins. |journal=Biochem. Cell Biol. |volume=73 |issue= 11–12 |pages= 933–47 |year= 1996 |pmid= 8722009 |doi=10.1139/o95-101 }}
*{{cite journal  | author=Adams SM, Sharp MG, Walker RA, ''et al.'' |title=Differential expression of translation-associated genes in benign and malignant human breast tumours. |journal=Br. J. Cancer |volume=65 |issue= 1 |pages= 65-71 |year= 1992 |pmid= 1370760 |doi=  }}
*{{cite journal  | author=Adams SM |title=Differential expression of translation-associated genes in benign and malignant human breast tumours |journal=Br. J. Cancer |volume=65 |issue= 1 |pages= 65–71 |year= 1992 |pmid= 1370760 |doi=  10.1038/bjc.1992.12| pmc=1977345 |name-list-format=vanc| author2=Sharp MG  | author3=Walker RA  | display-authors=3  | last4=Brammar  | first4=WJ  | last5=Varley  | first5=JM  }}
*{{cite journal | author=Pancré V, Pierce RJ, Fournier F, ''et al.'' |title=Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL). |journal=Eur. J. Immunol. |volume=21 |issue= 11 |pages= 2735-41 |year= 1991 |pmid= 1657614 |doi=  }}
*{{cite journal  | author=Pancré V |title=Effect of ubiquitin on platelet functions: possible identity with platelet activity suppressive lymphokine (PASL) |journal=Eur. J. Immunol. |volume=21 |issue= 11 |pages= 2735–41 |year= 1991 |pmid= 1657614 |doi=10.1002/eji.1830211113 |name-list-format=vanc| author2=Pierce RJ | author3=Fournier F  | display-authors=3  | last4=Mehtali  | first4=Majid  | last5=Delanoye  | first5=Anne  | last6=Capron  | first6=André  | last7=Auriault  | first7=Claude }}
*{{cite journal  | author=Kanayama H, Tanaka K, Aki M, ''et al.'' |title=Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells. |journal=Cancer Res. |volume=51 |issue= 24 |pages= 6677-85 |year= 1992 |pmid= 1660345 |doi=  }}
*{{cite journal  | author=Kanayama H |title=Changes in expressions of proteasome and ubiquitin genes in human renal cancer cells |journal=Cancer Res. |volume=51 |issue= 24 |pages= 6677–85 |year= 1992 |pmid= 1660345 |doi=  |name-list-format=vanc| author2=Tanaka K  | author3=Aki M  | display-authors=3  | last4=Kagawa  | first4=S  | last5=Miyaji  | first5=H  | last6=Satoh  | first6=M  | last7=Okada  | first7=F  | last8=Sato  | first8=S  | last9=Shimbara  | first9=N }}
*{{cite journal | author=Monia BP, Ecker DJ, Jonnalagadda S, ''et al.'' |title=Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins. |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 4093-103 |year= 1989 |pmid= 2537304 |doi=  }}
*{{cite journal  | author=Monia BP |title=Gene synthesis, expression, and processing of human ubiquitin carboxyl extension proteins |journal=J. Biol. Chem. |volume=264 |issue= 7 |pages= 4093–103 |year= 1989 |pmid= 2537304 |doi=  |name-list-format=vanc| author2=Ecker DJ  | author3=Jonnalagadda S  | display-authors=3  | last4=Marsh  | first4=J | last5=Gotlib  | first5=L  | last6=Butt  | first6=TR  | last7=Crooke  | first7=ST }}
*{{cite journal  | author=Redman KL, Rechsteiner M |title=Identification of the long ubiquitin extension as ribosomal protein S27a. |journal=Nature |volume=338 |issue= 6214 |pages= 438-40 |year= 1989 |pmid= 2538756 |doi= 10.1038/338438a0 }}
*{{cite journal  |vauthors=Redman KL, Rechsteiner M |title=Identification of the long ubiquitin extension as ribosomal protein S27a |journal=Nature |volume=338 |issue= 6214 |pages= 438–40 |year= 1989 |pmid= 2538756 |doi= 10.1038/338438a0 }}
*{{cite journal | author=Lund PK, Moats-Staats BM, Simmons JG, ''et al.'' |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor. |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609-13 |year= 1985 |pmid= 2581967 |doi=  }}
*{{cite journal  | author=Lund PK |title=Nucleotide sequence analysis of a cDNA encoding human ubiquitin reveals that ubiquitin is synthesized as a precursor |journal=J. Biol. Chem. |volume=260 |issue= 12 |pages= 7609–13 |year= 1985 |pmid= 2581967 |doi=  |name-list-format=vanc| author2=Moats-Staats BM  | author3=Simmons JG  | display-authors=3  | last4=Hoyt  | first4=E  | last5=d'Ercole  | first5=AJ  | last6=Martin  | first6=F  | last7=Van Wyk  | first7=JJ  }}
*{{cite journal  | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal  |vauthors=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides |journal=Gene |volume=138 |issue= 1–2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=10.1016/0378-1119(94)90802-8  }}
*{{cite journal | author=Vladimirov SN, Ivanov AV, Karpova GG, ''et al.'' |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry. |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144-9 |year= 1996 |pmid= 8706699 |doi=  }}
*{{cite journal  | author=Vladimirov SN |title=Characterization of the human small-ribosomal-subunit proteins by N-terminal and internal sequencing, and mass spectrometry |journal=Eur. J. Biochem. |volume=239 |issue= 1 |pages= 144–9 |year= 1996 |pmid= 8706699 |doi=10.1111/j.1432-1033.1996.0144u.x |name-list-format=vanc| author2=Ivanov AV  | author3=Karpova GG  | display-authors=3  | last4=Musolyamov  | first4=Alekxander K.  | last5=Egorov  | first5=Tsezi A.  | last6=Thiede  | first6=Bernd | last7=Wittmann-Liebold  | first7=Brigitte  | last8=Otto  | first8=Albrecht  }}
*{{cite journal  | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal  | author=Suzuki Y |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library |journal=Gene |volume=200 |issue= 1–2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=10.1016/S0378-1119(97)00411-3  |name-list-format=vanc| author2=Yoshitomo-Nakagawa K  | author3=Maruyama K  | display-authors=3  | last4=Suyama  | first4=Akira  | last5=Sugano  | first5=Sumio  }}
*{{cite journal  | author=Kenmochi N, Kawaguchi T, Rozen S, ''et al.'' |title=A map of 75 human ribosomal protein genes. |journal=Genome Res. |volume=8 |issue= 5 |pages= 509-23 |year= 1998 |pmid= 9582194 |doi= }}
*{{cite journal  |vauthors=Kirschner LS, Stratakis CA |title=Structure of the human ubiquitin fusion gene Uba80 (RPS27a) and one of its pseudogenes |journal=Biochem. Biophys. Res. Commun. |volume=270 |issue= 3 |pages= 1106–10 |year= 2000 |pmid= 10772958 |doi= 10.1006/bbrc.2000.2568 }}
*{{cite journal | author=Kirschner LS, Stratakis CA |title=Structure of the human ubiquitin fusion gene Uba80 (RPS27a) and one of its pseudogenes. |journal=Biochem. Biophys. Res. Commun. |volume=270 |issue= 3 |pages= 1106-10 |year= 2000 |pmid= 10772958 |doi= 10.1006/bbrc.2000.2568 }}
*{{cite journal  | author=Petersen BO |title=Cell cycle– and cell growth–regulated proteolysis of mammalian CDC6 is dependent on APC–CDH1 |journal=Genes Dev. |volume=14 |issue= 18 |pages= 2330–43 |year= 2000 |pmid= 10995389 |doi=10.1101/gad.832500  | pmc=316932  |name-list-format=vanc| author2=Wagener C  | author3=Marinoni F  | display-authors=3  | last4=Kramer  | first4=ER  | last5=Melixetian  | first5=M  | last6=Lazzerini Denchi  | first6=E  | last7=Gieffers  | first7=C  | last8=Matteucci  | first8=C  | last9=Peters  | first9=JM  }}
*{{cite journal  | author=Petersen BO, Wagener C, Marinoni F, ''et al.'' |title=Cell cycle- and cell growth-regulated proteolysis of mammalian CDC6 is dependent on APC-CDH1. |journal=Genes Dev. |volume=14 |issue= 18 |pages= 2330-43 |year= 2000 |pmid= 10995389 |doi= }}
*{{cite journal  |vauthors=Bolton D, Evans PA, Stott K, Broadhurst RW |title=Structure and properties of a dimeric N-terminal fragment of human ubiquitin |journal=J. Mol. Biol. |volume=314 |issue= 4 |pages= 773–87 |year= 2002 |pmid= 11733996 |doi= 10.1006/jmbi.2001.5181 }}
*{{cite journal  | author=Bolton D, Evans PA, Stott K, Broadhurst RW |title=Structure and properties of a dimeric N-terminal fragment of human ubiquitin. |journal=J. Mol. Biol. |volume=314 |issue= 4 |pages= 773-87 |year= 2002 |pmid= 11733996 |doi= 10.1006/jmbi.2001.5181 }}
*{{cite journal  | author=Yoshihama M |title=The Human Ribosomal Protein Genes: Sequencing and Comparative Analysis of 73 Genes |journal=Genome Res. |volume=12 |issue= 3 |pages= 379–90 |year= 2002 |pmid= 11875025 |doi= 10.1101/gr.214202  | pmc=155282  |name-list-format=vanc| author2=Uechi T  | author3=Asakawa S  | display-authors=3  | last4=Kawasaki  | first4=K  | last5=Kato  | first5=S  | last6=Higa  | first6=S  | last7=Maeda  | first7=N  | last8=Minoshima  | first8=S  | last9=Tanaka  | first9=T }}
*{{cite journal | author=Yoshihama M, Uechi T, Asakawa S, ''et al.'' |title=The human ribosomal protein genes: sequencing and comparative analysis of 73 genes. |journal=Genome Res. |volume=12 |issue= 3 |pages= 379-90 |year= 2002 |pmid= 11875025 |doi= 10.1101/gr.214202 }}
*{{cite journal  | author=Strausberg RL |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  |vauthors=Cohen BD, Bariteau JT, Magenis LM, Dias JA |title=Regulation of follitropin receptor cell surface residency by the ubiquitin-proteasome pathway |journal=Endocrinology |volume=144 |issue= 10 |pages= 4393–402 |year= 2003 |pmid= 12960054 |doi= 10.1210/en.2002-0063 }}
*{{cite journal  | author=Cohen BD, Bariteau JT, Magenis LM, Dias JA |title=Regulation of follitropin receptor cell surface residency by the ubiquitin-proteasome pathway. |journal=Endocrinology |volume=144 |issue= 10 |pages= 4393-402 |year= 2003 |pmid= 12960054 |doi= 10.1210/en.2002-0063 }}
*{{cite journal  | author=Ota T |title=Complete sequencing and characterization of 21,243 full-length human cDNAs |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285  |name-list-format=vanc| author2=Suzuki Y  | author3=Nishikawa T  | display-authors=3  | last4=Otsuki  | first4=Tetsuji  | last5=Sugiyama  | first5=Tomoyasu  | last6=Irie  | first6=Ryotaro  | last7=Wakamatsu  | first7=Ai  | last8=Hayashi  | first8=Koji  | last9=Sato  | first9=Hiroyuki }}
*{{cite journal  | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  |vauthors=Li H, Seth A |title=An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein |journal=Oncogene |volume=23 |issue= 10 |pages= 1801–8 |year= 2004 |pmid= 14755250 |doi= 10.1038/sj.onc.1207319 }}
*{{cite journal  | author=Li H, Seth A |title=An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein. |journal=Oncogene |volume=23 |issue= 10 |pages= 1801-8 |year= 2004 |pmid= 14755250 |doi= 10.1038/sj.onc.1207319 }}
}}
}}
{{refend}}
{{refend}}


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{{PDB Gallery|geneid=6233}}
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[[Category:Ribosomal proteins]]

Latest revision as of 08:58, 11 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

40S ribosomal protein S27a is a protein that in humans is encoded by the RPS27A gene.[1][2]

Ubiquitin, a highly conserved protein that has a major role in targeting cellular proteins for degradation by the 26S proteosome, is synthesized as a precursor protein consisting of either polyubiquitin chains or a single ubiquitin fused to an unrelated protein. This gene encodes a fusion protein consisting of ubiquitin at the N terminus and ribosomal protein S27a at the C terminus. When expressed in yeast, the protein is post-translationally processed, generating free ubiquitin monomer and ribosomal protein S27a. Ribosomal protein S27a is a component of the 40S subunit of the ribosome and belongs to the S27AE family of ribosomal proteins. It contains C4-type zinc finger domains and is located in the cytoplasm. Pseudogenes derived from this gene are present in the genome. As with ribosomal protein S27a, ribosomal protein L40 is also synthesized as a fusion protein with ubiquitin; similarly, ribosomal protein S30 is synthesized as a fusion protein with the ubiquitin-like protein fubi.[2]

References

  1. ↑ Kenmochi N, Kawaguchi T, Rozen S, Davis E, Goodman N, Hudson TJ, Tanaka T, Page DC (Aug 1998). "A map of 75 human ribosomal protein genes". Genome Res. 8 (5): 509–23. doi:10.1101/gr.8.5.509. PMID 9582194.
  2. ↑ 2.0 2.1 "Entrez Gene: RPS27A ribosomal protein S27a".

Further reading


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