Full text data of RPL23A
RPL23A
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L23a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L23a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62750
ID RL23A_HUMAN Reviewed; 156 AA.
AC P62750; B2R5B2; P29316; P39024; Q92774;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=60S ribosomal protein L23a;
GN Name=RPL23A;
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=Melanoma;
RA Jiang H., Lin J., Tao J., Fisher P.B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Reddy K.B., Lin C.W., Howe P.H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8662070; DOI=10.1007/s002510050095;
RA Fan W., Cai W., Parimoo S., Lennon G.G., Weissman S.M.;
RT "Identification of seven new human MHC class I region genes around the
RT HLA-F locus.";
RL Immunogenetics 44:97-103(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9417910; DOI=10.1006/geno.1997.5038;
RA Fan W., Christensen M., Eichler E., Zhang X., Lennon G.;
RT "Cloning, sequencing, gene organization, and localization of the human
RT ribosomal protein RPL23A gene.";
RL Genomics 46:234-239(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-156.
RC TISSUE=Liver;
RA Bonaldo M., Soares M.B.;
RT "Identification and localization of six liver expressed genes on human
RT chromosome 13.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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).
RN [15]
RP VARIANT THR-99.
RX PubMed=22431104; DOI=10.1002/humu.22081;
RA Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A.,
RA Davies S.M., Kattamis A., Doherty L., Landowski M., Buros C.,
RA Ghazvinian R., Sieff C.A., Newburger P.E., Niewiadomska E.,
RA Matysiak M., Glader B., Atsidaftos E., Lipton J.M., Gleizes P.E.,
RA Beggs A.H.;
RT "Frameshift mutation in p53 regulator RPL26 is associated with
RT multiple physical abnormalities and a specific pre-ribosomal RNA
RT processing defect in diamond-blackfan anemia.";
RL Hum. Mutat. 33:1037-1044(2012).
CC -!- FUNCTION: This protein binds to a specific region on the 26S rRNA
CC (By similarity).
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1 (By similarity).
CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR EMBL; U43701; AAB03210.1; -; mRNA.
DR EMBL; U02032; AAA03341.1; -; mRNA.
DR EMBL; U37230; AAB17510.1; -; mRNA.
DR EMBL; AF001689; AAC51934.1; -; Genomic_DNA.
DR EMBL; AK312123; BAG35059.1; -; mRNA.
DR EMBL; CH471159; EAW51132.1; -; Genomic_DNA.
DR EMBL; BC014459; AAH14459.1; -; mRNA.
DR EMBL; BC058041; AAH58041.1; -; mRNA.
DR EMBL; L13799; AAA35681.1; -; mRNA.
DR RefSeq; NP_000975.2; NM_000984.5.
DR UniGene; Hs.419463; -.
DR PDB; 3J3B; EM; 5.00 A; X=1-156.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62750; -.
DR SMR; P62750; 36-156.
DR IntAct; P62750; 22.
DR MINT; MINT-4999907; -.
DR STRING; 9606.ENSP00000389103; -.
DR PhosphoSite; P62750; -.
DR DMDM; 51338637; -.
DR SWISS-2DPAGE; P62750; -.
DR PaxDb; P62750; -.
DR PRIDE; P62750; -.
DR Ensembl; ENST00000422514; ENSP00000389103; ENSG00000198242.
DR GeneID; 6147; -.
DR KEGG; hsa:6147; -.
DR UCSC; uc002hci.3; human.
DR CTD; 6147; -.
DR GeneCards; GC17P027046; -.
DR H-InvDB; HIX0016623; -.
DR HGNC; HGNC:10317; RPL23A.
DR HPA; HPA051754; -.
DR MIM; 602326; gene.
DR neXtProt; NX_P62750; -.
DR PharmGKB; PA34691; -.
DR eggNOG; COG0089; -.
DR HOGENOM; HOG000231365; -.
DR HOVERGEN; HBG056619; -.
DR KO; K02893; -.
DR PhylomeDB; P62750; -.
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 ChiTaRS; RPL23A; human.
DR GeneWiki; RPL23A; -.
DR GenomeRNAi; 6147; -.
DR NextBio; 23883; -.
DR PRO; PR:P62750; -.
DR ArrayExpress; P62750; -.
DR Bgee; P62750; -.
DR CleanEx; HS_RPL23A; -.
DR Genevestigator; P62750; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IMP: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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR019985; Ribosomal_L23.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR TIGRFAMs; TIGR03636; L23_arch; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Methylation; Phosphoprotein;
KW Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 156 60S ribosomal protein L23a.
FT /FTId=PRO_0000129467.
FT MOD_RES 2 2 N,N,N-trimethylalanine (By similarity).
FT MOD_RES 45 45 Phosphothreonine.
FT VARIANT 99 99 I -> T (rare variant found in Diamond-
FT Blackfan anemia patients; unknown
FT pathological significance).
FT /FTId=VAR_069221.
FT CONFLICT 1 2 MA -> IP (in Ref. 2; AAA03341).
FT CONFLICT 78 78 K -> N (in Ref. 3; AAB17510).
FT CONFLICT 110 110 K -> S (in Ref. 3; AAB17510).
SQ SEQUENCE 156 AA; 17695 MW; 3980E77B47FAB70E CRC64;
MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
//
ID RL23A_HUMAN Reviewed; 156 AA.
AC P62750; B2R5B2; P29316; P39024; Q92774;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 109.
DE RecName: Full=60S ribosomal protein L23a;
GN Name=RPL23A;
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=Melanoma;
RA Jiang H., Lin J., Tao J., Fisher P.B.;
RL Submitted (JUL-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RA Reddy K.B., Lin C.W., Howe P.H.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8662070; DOI=10.1007/s002510050095;
RA Fan W., Cai W., Parimoo S., Lennon G.G., Weissman S.M.;
RT "Identification of seven new human MHC class I region genes around the
RT HLA-F locus.";
RL Immunogenetics 44:97-103(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9417910; DOI=10.1006/geno.1997.5038;
RA Fan W., Christensen M., Eichler E., Zhang X., Lennon G.;
RT "Cloning, sequencing, gene organization, and localization of the human
RT ribosomal protein RPL23A gene.";
RL Genomics 46:234-239(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adrenal gland;
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 [6]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-156.
RC TISSUE=Liver;
RA Bonaldo M., Soares M.B.;
RT "Identification and localization of six liver expressed genes on human
RT chromosome 13.";
RL Submitted (JUL-1993) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-45, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 80S RIBOSOME.
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).
RN [15]
RP VARIANT THR-99.
RX PubMed=22431104; DOI=10.1002/humu.22081;
RA Gazda H.T., Preti M., Sheen M.R., O'Donohue M.F., Vlachos A.,
RA Davies S.M., Kattamis A., Doherty L., Landowski M., Buros C.,
RA Ghazvinian R., Sieff C.A., Newburger P.E., Niewiadomska E.,
RA Matysiak M., Glader B., Atsidaftos E., Lipton J.M., Gleizes P.E.,
RA Beggs A.H.;
RT "Frameshift mutation in p53 regulator RPL26 is associated with
RT multiple physical abnormalities and a specific pre-ribosomal RNA
RT processing defect in diamond-blackfan anemia.";
RL Hum. Mutat. 33:1037-1044(2012).
CC -!- FUNCTION: This protein binds to a specific region on the 26S rRNA
CC (By similarity).
CC -!- PTM: N-terminus is methylated by METTL11A/NTM1 (By similarity).
CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family.
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DR EMBL; U43701; AAB03210.1; -; mRNA.
DR EMBL; U02032; AAA03341.1; -; mRNA.
DR EMBL; U37230; AAB17510.1; -; mRNA.
DR EMBL; AF001689; AAC51934.1; -; Genomic_DNA.
DR EMBL; AK312123; BAG35059.1; -; mRNA.
DR EMBL; CH471159; EAW51132.1; -; Genomic_DNA.
DR EMBL; BC014459; AAH14459.1; -; mRNA.
DR EMBL; BC058041; AAH58041.1; -; mRNA.
DR EMBL; L13799; AAA35681.1; -; mRNA.
DR RefSeq; NP_000975.2; NM_000984.5.
DR UniGene; Hs.419463; -.
DR PDB; 3J3B; EM; 5.00 A; X=1-156.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62750; -.
DR SMR; P62750; 36-156.
DR IntAct; P62750; 22.
DR MINT; MINT-4999907; -.
DR STRING; 9606.ENSP00000389103; -.
DR PhosphoSite; P62750; -.
DR DMDM; 51338637; -.
DR SWISS-2DPAGE; P62750; -.
DR PaxDb; P62750; -.
DR PRIDE; P62750; -.
DR Ensembl; ENST00000422514; ENSP00000389103; ENSG00000198242.
DR GeneID; 6147; -.
DR KEGG; hsa:6147; -.
DR UCSC; uc002hci.3; human.
DR CTD; 6147; -.
DR GeneCards; GC17P027046; -.
DR H-InvDB; HIX0016623; -.
DR HGNC; HGNC:10317; RPL23A.
DR HPA; HPA051754; -.
DR MIM; 602326; gene.
DR neXtProt; NX_P62750; -.
DR PharmGKB; PA34691; -.
DR eggNOG; COG0089; -.
DR HOGENOM; HOG000231365; -.
DR HOVERGEN; HBG056619; -.
DR KO; K02893; -.
DR PhylomeDB; P62750; -.
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 ChiTaRS; RPL23A; human.
DR GeneWiki; RPL23A; -.
DR GenomeRNAi; 6147; -.
DR NextBio; 23883; -.
DR PRO; PR:P62750; -.
DR ArrayExpress; P62750; -.
DR Bgee; P62750; -.
DR CleanEx; HS_RPL23A; -.
DR Genevestigator; P62750; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0008283; P:cell proliferation; IMP: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 Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR019985; Ribosomal_L23.
DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom.
DR InterPro; IPR001014; Ribosomal_L23/L25_CS.
DR InterPro; IPR005633; Ribosomal_L23/L25_N.
DR InterPro; IPR013025; Ribosomal_L25/23.
DR Pfam; PF00276; Ribosomal_L23; 1.
DR Pfam; PF03939; Ribosomal_L23eN; 1.
DR SUPFAM; SSF54189; SSF54189; 1.
DR TIGRFAMs; TIGR03636; L23_arch; 1.
DR PROSITE; PS00050; RIBOSOMAL_L23; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Methylation; Phosphoprotein;
KW Polymorphism; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding; rRNA-binding.
FT INIT_MET 1 1 Removed (By similarity).
FT CHAIN 2 156 60S ribosomal protein L23a.
FT /FTId=PRO_0000129467.
FT MOD_RES 2 2 N,N,N-trimethylalanine (By similarity).
FT MOD_RES 45 45 Phosphothreonine.
FT VARIANT 99 99 I -> T (rare variant found in Diamond-
FT Blackfan anemia patients; unknown
FT pathological significance).
FT /FTId=VAR_069221.
FT CONFLICT 1 2 MA -> IP (in Ref. 2; AAA03341).
FT CONFLICT 78 78 K -> N (in Ref. 3; AAB17510).
FT CONFLICT 110 110 K -> S (in Ref. 3; AAB17510).
SQ SEQUENCE 156 AA; 17695 MW; 3980E77B47FAB70E CRC64;
MAPKAKKEAP APPKAEAKAK ALKAKKAVLK GVHSHKKKKI RTSPTFRRPK TLRLRRQPKY
PRKSAPRRNK LDHYAIIKFP LTTESAMKKI EDNNTLVFIV DVKANKHQIK QAVKKLYDID
VAKVNTLIRP DGEKKAYVRL APDYDALDVA NKIGII
//
MIM
602326
*RECORD*
*FIELD* NO
602326
*FIELD* TI
*602326 RIBOSOMAL PROTEIN L23A; RPL23A
*FIELD* TX
See RPL19 (180466) for further discussion of this gene family.
read more
CLONING
Fan et al. (1997) cloned, sequenced, and mapped the gene for human
ribosomal protein RPL23A. A 0.6-kb transcript was found in all tissues
examined. In adult tissues, the RPL23A transcript was more abundant in
pancreas, skeletal muscle, and heart, while much less abundant in
kidney, brain, placenta, lung, and liver. The open reading frame encodes
a polypeptide of 156 amino acids, which is identical with the rat RPL23A
protein. In the 5-prime flanking region of the gene, a canonical TATA
sequence and a defined CAAT box were found for the first time in a
mammalian ribosomal protein gene.
GENE STRUCTURE
Fan et al. (1997) demonstrated that the 4.0-kb RPL23A gene contains 5
exons and 4 introns.
GENE FUNCTION
Using protein crosslinking, Pool et al. (2002) detected distinct modes
in the binding of the signal recognition particle (SRP) to the ribosome.
During signal peptide recognition, SRP54 (604857) is positioned at the
exit site close to ribosomal proteins L23a and L35. When SRP54 contacts
the signal recognition particle receptor (182180), SRP54 is rearranged
such that it is no longer close to L23a. This repositioning may allow
the translocon to dock with the ribosome, leading to insertion of the
signal peptide into the translocation channel.
MAPPING
By fluorescence in situ hybridization, Fan et al. (1997) mapped RPL23A
to 17q11.
*FIELD* RF
1. Fan, W.; Christensen, M.; Eichler, E.; Zhang, X.; Lennon, G.:
Cloning, sequencing, gene organization, and localization of the human
ribosomal protein RPL23A gene. Genomics 46: 234-239, 1997.
2. Pool, M. R.; Stumm, J.; Fulga, T. A.; Sinning, I.; Dobberstein,
B.: Distinct modes of signal recognition particle interaction with
the ribosome. Science 297: 1345-1348, 2002.
*FIELD* CN
Ada Hamosh - updated: 10/18/2002
*FIELD* CD
Victor A. McKusick: 2/9/1998
*FIELD* ED
alopez: 10/23/2002
terry: 10/18/2002
mark: 2/9/1998
*RECORD*
*FIELD* NO
602326
*FIELD* TI
*602326 RIBOSOMAL PROTEIN L23A; RPL23A
*FIELD* TX
See RPL19 (180466) for further discussion of this gene family.
read more
CLONING
Fan et al. (1997) cloned, sequenced, and mapped the gene for human
ribosomal protein RPL23A. A 0.6-kb transcript was found in all tissues
examined. In adult tissues, the RPL23A transcript was more abundant in
pancreas, skeletal muscle, and heart, while much less abundant in
kidney, brain, placenta, lung, and liver. The open reading frame encodes
a polypeptide of 156 amino acids, which is identical with the rat RPL23A
protein. In the 5-prime flanking region of the gene, a canonical TATA
sequence and a defined CAAT box were found for the first time in a
mammalian ribosomal protein gene.
GENE STRUCTURE
Fan et al. (1997) demonstrated that the 4.0-kb RPL23A gene contains 5
exons and 4 introns.
GENE FUNCTION
Using protein crosslinking, Pool et al. (2002) detected distinct modes
in the binding of the signal recognition particle (SRP) to the ribosome.
During signal peptide recognition, SRP54 (604857) is positioned at the
exit site close to ribosomal proteins L23a and L35. When SRP54 contacts
the signal recognition particle receptor (182180), SRP54 is rearranged
such that it is no longer close to L23a. This repositioning may allow
the translocon to dock with the ribosome, leading to insertion of the
signal peptide into the translocation channel.
MAPPING
By fluorescence in situ hybridization, Fan et al. (1997) mapped RPL23A
to 17q11.
*FIELD* RF
1. Fan, W.; Christensen, M.; Eichler, E.; Zhang, X.; Lennon, G.:
Cloning, sequencing, gene organization, and localization of the human
ribosomal protein RPL23A gene. Genomics 46: 234-239, 1997.
2. Pool, M. R.; Stumm, J.; Fulga, T. A.; Sinning, I.; Dobberstein,
B.: Distinct modes of signal recognition particle interaction with
the ribosome. Science 297: 1345-1348, 2002.
*FIELD* CN
Ada Hamosh - updated: 10/18/2002
*FIELD* CD
Victor A. McKusick: 2/9/1998
*FIELD* ED
alopez: 10/23/2002
terry: 10/18/2002
mark: 2/9/1998