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Database: UniProt
Entry: P62750
LinkDB: P62750
Original site: P62750 
ID   RL23A_HUMAN             Reviewed;         156 AA.
AC   P62750; B2R5B2; P29316; P39024; Q92774;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   19-MAR-2014, entry version 111.
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 IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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   -!- PTM: Citrullinated by PADI4 (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   BioGrid; 112067; 172.
DR   IntAct; P62750; 23.
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   TreeFam; TF314116; -.
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:0070062; C:extracellular vesicular exosome; IDA:UniProt.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0031932; C:TORC2 complex; IEA:Ensembl.
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   HAMAP; MF_01369_A; Ribosomal_L23_A; 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; Citrullination; Complete proteome; Methylation;
KW   Phosphoprotein; 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      41     41       Citrulline (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      2      2       A -> 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
//
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