Full text data of RPL27A
RPL27A
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L27a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L27a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46776
ID RL27A_HUMAN Reviewed; 148 AA.
AC P46776; B2R4B3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=60S ribosomal protein L27a;
GN Name=RPL27A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10449908;
RA Kusuda J., Hirai M., Tanuma R., Hirata M., Hashimoto K.;
RT "Genomic structure and chromosome location of RPL27A/Rpl27a, the genes
RT encoding human and mouse ribosomal protein L27A.";
RL Cytogenet. Cell Genet. 85:248-251(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-106.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-55 AND LYS-110, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP HYDROXYLATION AT HIS-39 BY MINA.
RX PubMed=23103944; DOI=10.1038/nchembio.1093;
RA Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
RA Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
RA Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
RA Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
RA Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
RA Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
RA Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- INTERACTION:
CC P13984:GTF2F2; NbExp=2; IntAct=EBI-350581, EBI-1030560;
CC -!- PTM: Hydroxylated on His-39 by MINA.
CC -!- SIMILARITY: Belongs to the ribosomal protein L15P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U14968; AAA85656.1; -; mRNA.
DR EMBL; AB020236; BAA77361.1; -; Genomic_DNA.
DR EMBL; AK311767; BAG34710.1; -; mRNA.
DR EMBL; CH471064; EAW68619.1; -; Genomic_DNA.
DR EMBL; BC005326; AAH05326.1; -; mRNA.
DR EMBL; BC020169; AAH20169.1; -; mRNA.
DR EMBL; AB007178; BAA25837.1; -; Genomic_DNA.
DR PIR; S55914; S55914.
DR RefSeq; NP_000981.1; NM_000990.4.
DR UniGene; Hs.523463; -.
DR PDB; 3J3B; EM; 5.00 A; a=1-148.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P46776; -.
DR SMR; P46776; 2-148.
DR IntAct; P46776; 14.
DR MINT; MINT-1150308; -.
DR STRING; 9606.ENSP00000346015; -.
DR PhosphoSite; P46776; -.
DR DMDM; 1173017; -.
DR SWISS-2DPAGE; P46776; -.
DR PaxDb; P46776; -.
DR PRIDE; P46776; -.
DR Ensembl; ENST00000314138; ENSP00000346015; ENSG00000166441.
DR GeneID; 6157; -.
DR KEGG; hsa:6157; -.
DR UCSC; uc001mgs.4; human.
DR CTD; 6157; -.
DR GeneCards; GC11P008703; -.
DR HGNC; HGNC:10329; RPL27A.
DR MIM; 603637; gene.
DR neXtProt; NX_P46776; -.
DR PharmGKB; PA34708; -.
DR eggNOG; COG0200; -.
DR HOGENOM; HOG000231263; -.
DR HOVERGEN; HBG054587; -.
DR InParanoid; P46776; -.
DR KO; K02900; -.
DR OMA; DKAPVID; -.
DR OrthoDB; EOG78SQKP; -.
DR PhylomeDB; P46776; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPL27A; -.
DR GenomeRNAi; 6157; -.
DR NextBio; 23911; -.
DR PRO; PR:P46776; -.
DR ArrayExpress; P46776; -.
DR Bgee; P46776; -.
DR CleanEx; HS_RPL27A; -.
DR Genevestigator; P46776; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L18e; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydroxylation;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 148 60S ribosomal protein L27a.
FT /FTId=PRO_0000104879.
FT MOD_RES 39 39 (3S)-3-hydroxyhistidine.
FT MOD_RES 47 47 N6-acetyllysine.
FT MOD_RES 55 55 N6-acetyllysine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 110 110 N6-acetyllysine.
SQ SEQUENCE 148 AA; 16561 MW; CB5E09C91507798F CRC64;
MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGLHH HRINFDKYHP GYFGKVGMKH
YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGAAPI IDVVRSGYYK VLGKGKLPKQ
PVIVKAKFFS RRAEEKIKSV GGACVLVA
//
ID RL27A_HUMAN Reviewed; 148 AA.
AC P46776; B2R4B3;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 119.
DE RecName: Full=60S ribosomal protein L27a;
GN Name=RPL27A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10449908;
RA Kusuda J., Hirai M., Tanuma R., Hirata M., Hashimoto K.;
RT "Genomic structure and chromosome location of RPL27A/Rpl27a, the genes
RT encoding human and mouse ribosomal protein L27A.";
RL Cytogenet. Cell Genet. 85:248-251(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 73-106.
RX PubMed=9582194;
RA Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
RA Hudson T.J., Tanaka T., Page D.C.;
RT "A map of 75 human ribosomal protein genes.";
RL Genome Res. 8:509-523(1998).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND MASS
RP SPECTROMETRY.
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47; LYS-55 AND LYS-110, AND
RP MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP HYDROXYLATION AT HIS-39 BY MINA.
RX PubMed=23103944; DOI=10.1038/nchembio.1093;
RA Ge W., Wolf A., Feng T., Ho C.H., Sekirnik R., Zayer A., Granatino N.,
RA Cockman M.E., Loenarz C., Loik N.D., Hardy A.P., Claridge T.D.,
RA Hamed R.B., Chowdhury R., Gong L., Robinson C.V., Trudgian D.C.,
RA Jiang M., Mackeen M.M., McCullagh J.S., Gordiyenko Y., Thalhammer A.,
RA Yamamoto A., Yang M., Liu-Yi P., Zhang Z., Schmidt-Zachmann M.,
RA Kessler B.M., Ratcliffe P.J., Preston G.M., Coleman M.L.,
RA Schofield C.J.;
RT "Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and
RT humans.";
RL Nat. Chem. Biol. 8:960-962(2012).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS).
RX PubMed=23636399; DOI=10.1038/nature12104;
RA Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
RA Wilson D.N., Beckmann R.;
RT "Structures of the human and Drosophila 80S ribosome.";
RL Nature 497:80-85(2013).
CC -!- INTERACTION:
CC P13984:GTF2F2; NbExp=2; IntAct=EBI-350581, EBI-1030560;
CC -!- PTM: Hydroxylated on His-39 by MINA.
CC -!- SIMILARITY: Belongs to the ribosomal protein L15P family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; U14968; AAA85656.1; -; mRNA.
DR EMBL; AB020236; BAA77361.1; -; Genomic_DNA.
DR EMBL; AK311767; BAG34710.1; -; mRNA.
DR EMBL; CH471064; EAW68619.1; -; Genomic_DNA.
DR EMBL; BC005326; AAH05326.1; -; mRNA.
DR EMBL; BC020169; AAH20169.1; -; mRNA.
DR EMBL; AB007178; BAA25837.1; -; Genomic_DNA.
DR PIR; S55914; S55914.
DR RefSeq; NP_000981.1; NM_000990.4.
DR UniGene; Hs.523463; -.
DR PDB; 3J3B; EM; 5.00 A; a=1-148.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P46776; -.
DR SMR; P46776; 2-148.
DR IntAct; P46776; 14.
DR MINT; MINT-1150308; -.
DR STRING; 9606.ENSP00000346015; -.
DR PhosphoSite; P46776; -.
DR DMDM; 1173017; -.
DR SWISS-2DPAGE; P46776; -.
DR PaxDb; P46776; -.
DR PRIDE; P46776; -.
DR Ensembl; ENST00000314138; ENSP00000346015; ENSG00000166441.
DR GeneID; 6157; -.
DR KEGG; hsa:6157; -.
DR UCSC; uc001mgs.4; human.
DR CTD; 6157; -.
DR GeneCards; GC11P008703; -.
DR HGNC; HGNC:10329; RPL27A.
DR MIM; 603637; gene.
DR neXtProt; NX_P46776; -.
DR PharmGKB; PA34708; -.
DR eggNOG; COG0200; -.
DR HOGENOM; HOG000231263; -.
DR HOVERGEN; HBG054587; -.
DR InParanoid; P46776; -.
DR KO; K02900; -.
DR OMA; DKAPVID; -.
DR OrthoDB; EOG78SQKP; -.
DR PhylomeDB; P46776; -.
DR Reactome; REACT_116125; Disease.
DR Reactome; REACT_17015; Metabolism of proteins.
DR Reactome; REACT_1762; 3' -UTR-mediated translational regulation.
DR Reactome; REACT_21257; Metabolism of RNA.
DR Reactome; REACT_71; Gene Expression.
DR GeneWiki; RPL27A; -.
DR GenomeRNAi; 6157; -.
DR NextBio; 23911; -.
DR PRO; PR:P46776; -.
DR ArrayExpress; P46776; -.
DR Bgee; P46776; -.
DR CleanEx; HS_RPL27A; -.
DR Genevestigator; P46776; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
DR GO; GO:0006414; P:translational elongation; TAS:Reactome.
DR GO; GO:0006413; P:translational initiation; TAS:Reactome.
DR GO; GO:0006415; P:translational termination; TAS:Reactome.
DR GO; GO:0019083; P:viral transcription; TAS:Reactome.
DR InterPro; IPR001196; Ribosomal_L15_CS.
DR InterPro; IPR021131; Ribosomal_L18e/L15P.
DR Pfam; PF00828; Ribosomal_L18e; 1.
DR SUPFAM; SSF52080; SSF52080; 1.
DR PROSITE; PS00475; RIBOSOMAL_L15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Hydroxylation;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 148 60S ribosomal protein L27a.
FT /FTId=PRO_0000104879.
FT MOD_RES 39 39 (3S)-3-hydroxyhistidine.
FT MOD_RES 47 47 N6-acetyllysine.
FT MOD_RES 55 55 N6-acetyllysine.
FT MOD_RES 68 68 Phosphoserine.
FT MOD_RES 110 110 N6-acetyllysine.
SQ SEQUENCE 148 AA; 16561 MW; CB5E09C91507798F CRC64;
MPSRLRKTRK LRGHVSHGHG RIGKHRKHPG GRGNAGGLHH HRINFDKYHP GYFGKVGMKH
YHLKRNQSFC PTVNLDKLWT LVSEQTRVNA AKNKTGAAPI IDVVRSGYYK VLGKGKLPKQ
PVIVKAKFFS RRAEEKIKSV GGACVLVA
//
MIM
603637
*RECORD*
*FIELD* NO
603637
*FIELD* TI
*603637 RIBOSOMAL PROTEIN L27a; RPL27A
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29;
603633), L5 (RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 148-amino acid human RPL27A
differs from rat Rpl27a by 3 amino acids. Northern blot analysis
suggested variable expression of RPL27A in colorectal cancers compared
to adjacent normal tissues, although no correlation between the level of
expression and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL27A gene to 11p15. By FISH, Kusuda et
al. (1999) mapped the mouse Rpl27a gene to chromosome 7E2-F1, a region
that shows homology of synteny to human 11p15.
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
3. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
4. Kusuda, J.; Hirai, M.; Tanuma, R.; Hirata, M.; Hashimoto, K.:
Genomic structure and chromosome location of RPL27A/Rpl27a, the genes
encoding human and mouse ribosomal protein L27A. Cytogenet. Cell
Genet. 85: 248-251, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 10/01/1999
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
carol: 10/01/1999
carol: 3/19/1999
*RECORD*
*FIELD* NO
603637
*FIELD* TI
*603637 RIBOSOMAL PROTEIN L27a; RPL27A
*FIELD* TX
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins.
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29;
603633), L5 (RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A), and L28
(RPL28; 603638). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 148-amino acid human RPL27A
differs from rat Rpl27a by 3 amino acids. Northern blot analysis
suggested variable expression of RPL27A in colorectal cancers compared
to adjacent normal tissues, although no correlation between the level of
expression and the severity of the disease was found.
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL27A gene to 11p15. By FISH, Kusuda et
al. (1999) mapped the mouse Rpl27a gene to chromosome 7E2-F1, a region
that shows homology of synteny to human 11p15.
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
3. Kenmochi, N.; Kawaguchi, T.; Rozen, S.; Davis, E.; Goodman, N.;
Hudson, T. J.; Tanaka, T.; Page, D. C.: A map of 75 human ribosomal
protein genes. Genome Res. 8: 509-523, 1998.
4. Kusuda, J.; Hirai, M.; Tanuma, R.; Hirata, M.; Hashimoto, K.:
Genomic structure and chromosome location of RPL27A/Rpl27a, the genes
encoding human and mouse ribosomal protein L27A. Cytogenet. Cell
Genet. 85: 248-251, 1999.
*FIELD* CN
Carol A. Bocchini - updated: 10/01/1999
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
carol: 10/01/1999
carol: 3/19/1999