Full text data of RPL23
RPL23
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L23 (60S ribosomal protein L17)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L23 (60S ribosomal protein L17)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P62829
ID RL23_HUMAN Reviewed; 140 AA.
AC P62829; P23131; P24048; Q29246; Q3SWV7; Q6P5S1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=60S ribosomal protein L23;
DE AltName: Full=60S ribosomal protein L17;
GN Name=RPL23;
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].
RX PubMed=1861993; DOI=10.1093/nar/19.14.4001;
RA Herault Y., Michel D., Chatelain G., Brun G.;
RT "cDNA and predicted amino acid sequences of the human ribosomal
RT protein genes rpS12 and rpL17.";
RL Nucleic Acids Res. 19:4001-4001(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1874450; DOI=10.1016/0378-1119(91)90091-O;
RA Berchtold M.W., Berger M.C.;
RT "Isolation and analysis of a human cDNA highly homologous to the yeast
RT gene encoding L17A ribosomal protein.";
RL Gene 102:283-288(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Uterus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [7]
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 [8]
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 Q00987:MDM2; NbExp=3; IntAct=EBI-353303, EBI-389668;
CC -!- SIMILARITY: Belongs to the ribosomal protein L14P 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; X52839; CAA37023.1; -; mRNA.
DR EMBL; X55954; CAA39417.1; -; mRNA.
DR EMBL; AB061827; BAB79465.1; -; Genomic_DNA.
DR EMBL; BC010114; AAH10114.1; -; mRNA.
DR EMBL; BC062716; AAH62716.1; -; mRNA.
DR EMBL; BC104651; AAI04652.1; -; mRNA.
DR EMBL; BC106061; AAI06062.1; -; mRNA.
DR PIR; S18815; R5HU23.
DR RefSeq; NP_000969.1; NM_000978.3.
DR UniGene; Hs.406300; -.
DR PDB; 3J3B; EM; 5.00 A; V=1-140.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62829; -.
DR SMR; P62829; 8-140.
DR IntAct; P62829; 30.
DR MINT; MINT-5001181; -.
DR STRING; 9606.ENSP00000377865; -.
DR PhosphoSite; P62829; -.
DR DMDM; 51338639; -.
DR SWISS-2DPAGE; P62829; -.
DR PaxDb; P62829; -.
DR PRIDE; P62829; -.
DR Ensembl; ENST00000394332; ENSP00000377865; ENSG00000125691.
DR Ensembl; ENST00000479035; ENSP00000420311; ENSG00000125691.
DR GeneID; 9349; -.
DR KEGG; hsa:9349; -.
DR UCSC; uc002hqx.1; human.
DR CTD; 9349; -.
DR GeneCards; GC17M037005; -.
DR HGNC; HGNC:10316; RPL23.
DR HPA; HPA003373; -.
DR MIM; 603662; gene.
DR neXtProt; NX_P62829; -.
DR PharmGKB; PA34690; -.
DR eggNOG; COG0093; -.
DR HOGENOM; HOG000183703; -.
DR HOVERGEN; HBG000282; -.
DR InParanoid; P62829; -.
DR KO; K02894; -.
DR OMA; ELRKKTM; -.
DR OrthoDB; EOG7ZD1X5; -.
DR PhylomeDB; P62829; -.
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; RpL23; human.
DR GeneWiki; RPL23; -.
DR GenomeRNAi; 9349; -.
DR NextBio; 35009; -.
DR PRO; PR:P62829; -.
DR ArrayExpress; P62829; -.
DR Bgee; P62829; -.
DR CleanEx; HS_RPL23; -.
DR Genevestigator; P62829; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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:0006610; P:ribosomal protein import into nucleus; NAS:UniProtKB.
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; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1; -.
DR InterPro; IPR019972; Ribosomal_L14_CS.
DR InterPro; IPR023571; Ribosomal_L14_dom.
DR InterPro; IPR000218; Ribosomal_L14b/L23e.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 140 60S ribosomal protein L23.
FT /FTId=PRO_0000128612.
FT MOD_RES 17 17 Phosphoserine.
FT MOD_RES 38 38 Phosphotyrosine.
FT CONFLICT 77 77 H -> R (in Ref. 4; AAH62716).
SQ SEQUENCE 140 AA; 14865 MW; 807E14139B2EB0B5 CRC64;
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN RLPAAGVGDM
VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED NAGVIVNNKG EMKGSAITGP
VAKECADLWP RIASNAGSIA
//
ID RL23_HUMAN Reviewed; 140 AA.
AC P62829; P23131; P24048; Q29246; Q3SWV7; Q6P5S1;
DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-AUG-2004, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=60S ribosomal protein L23;
DE AltName: Full=60S ribosomal protein L17;
GN Name=RPL23;
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].
RX PubMed=1861993; DOI=10.1093/nar/19.14.4001;
RA Herault Y., Michel D., Chatelain G., Brun G.;
RT "cDNA and predicted amino acid sequences of the human ribosomal
RT protein genes rpS12 and rpL17.";
RL Nucleic Acids Res. 19:4001-4001(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=1874450; DOI=10.1016/0378-1119(91)90091-O;
RA Berchtold M.W., Berger M.C.;
RT "Isolation and analysis of a human cDNA highly homologous to the yeast
RT gene encoding L17A ribosomal protein.";
RL Gene 102:283-288(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11875025; DOI=10.1101/gr.214202;
RA Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
RA Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
RT "The human ribosomal protein genes: sequencing and comparative
RT analysis of 73 genes.";
RL Genome Res. 12:379-390(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Kidney, and Uterus;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-38, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-17, 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 [7]
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 [8]
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 Q00987:MDM2; NbExp=3; IntAct=EBI-353303, EBI-389668;
CC -!- SIMILARITY: Belongs to the ribosomal protein L14P 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; X52839; CAA37023.1; -; mRNA.
DR EMBL; X55954; CAA39417.1; -; mRNA.
DR EMBL; AB061827; BAB79465.1; -; Genomic_DNA.
DR EMBL; BC010114; AAH10114.1; -; mRNA.
DR EMBL; BC062716; AAH62716.1; -; mRNA.
DR EMBL; BC104651; AAI04652.1; -; mRNA.
DR EMBL; BC106061; AAI06062.1; -; mRNA.
DR PIR; S18815; R5HU23.
DR RefSeq; NP_000969.1; NM_000978.3.
DR UniGene; Hs.406300; -.
DR PDB; 3J3B; EM; 5.00 A; V=1-140.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P62829; -.
DR SMR; P62829; 8-140.
DR IntAct; P62829; 30.
DR MINT; MINT-5001181; -.
DR STRING; 9606.ENSP00000377865; -.
DR PhosphoSite; P62829; -.
DR DMDM; 51338639; -.
DR SWISS-2DPAGE; P62829; -.
DR PaxDb; P62829; -.
DR PRIDE; P62829; -.
DR Ensembl; ENST00000394332; ENSP00000377865; ENSG00000125691.
DR Ensembl; ENST00000479035; ENSP00000420311; ENSG00000125691.
DR GeneID; 9349; -.
DR KEGG; hsa:9349; -.
DR UCSC; uc002hqx.1; human.
DR CTD; 9349; -.
DR GeneCards; GC17M037005; -.
DR HGNC; HGNC:10316; RPL23.
DR HPA; HPA003373; -.
DR MIM; 603662; gene.
DR neXtProt; NX_P62829; -.
DR PharmGKB; PA34690; -.
DR eggNOG; COG0093; -.
DR HOGENOM; HOG000183703; -.
DR HOVERGEN; HBG000282; -.
DR InParanoid; P62829; -.
DR KO; K02894; -.
DR OMA; ELRKKTM; -.
DR OrthoDB; EOG7ZD1X5; -.
DR PhylomeDB; P62829; -.
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; RpL23; human.
DR GeneWiki; RPL23; -.
DR GenomeRNAi; 9349; -.
DR NextBio; 35009; -.
DR PRO; PR:P62829; -.
DR ArrayExpress; P62829; -.
DR Bgee; P62829; -.
DR CleanEx; HS_RPL23; -.
DR Genevestigator; P62829; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:Ensembl.
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:0006610; P:ribosomal protein import into nucleus; NAS:UniProtKB.
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; 2.40.150.20; -; 1.
DR HAMAP; MF_01367; Ribosomal_L14; 1; -.
DR InterPro; IPR019972; Ribosomal_L14_CS.
DR InterPro; IPR023571; Ribosomal_L14_dom.
DR InterPro; IPR000218; Ribosomal_L14b/L23e.
DR PANTHER; PTHR11761; PTHR11761; 1.
DR Pfam; PF00238; Ribosomal_L14; 1.
DR SUPFAM; SSF50193; SSF50193; 1.
DR PROSITE; PS00049; RIBOSOMAL_L14; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 140 60S ribosomal protein L23.
FT /FTId=PRO_0000128612.
FT MOD_RES 17 17 Phosphoserine.
FT MOD_RES 38 38 Phosphotyrosine.
FT CONFLICT 77 77 H -> R (in Ref. 4; AAH62716).
SQ SEQUENCE 140 AA; 14865 MW; 807E14139B2EB0B5 CRC64;
MSKRGRGGSS GAKFRISLGL PVGAVINCAD NTGAKNLYII SVKGIKGRLN RLPAAGVGDM
VMATVKKGKP ELRKKVHPAV VIRQRKSYRR KDGVFLYFED NAGVIVNNKG EMKGSAITGP
VAKECADLWP RIASNAGSIA
//
MIM
603662
*RECORD*
*FIELD* NO
603662
*FIELD* TI
*603662 RIBOSOMAL PROTEIN L23; RPL23
*FIELD* TX
DESCRIPTION
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins, including RPL23 (Kenmochi et al.,
1998).
CLONING
By differential screening of a human lymphocyte cDNA library with probes
derived from actively dividing or quiescent quail neuroretina cells,
Herault et al. (1991) isolated cDNAs encoding ribosomal protein L23
(RPL23), which they called rpL17. The deduced 140-amino acid human RPL23
protein is 78% identical to yeast ribosomal protein L17.
Berchtold and Berger (1991) isolated a human brain RPL23 cDNA using PCR.
Northern blot analysis detected a 600-bp RPL23 transcript in all human
tissues examined.
GENE FUNCTION
Impeding ribosomal biogenesis generates ribosomal stress that activates
p53 (TP53; 191170) to stop cell growth. Dai et al. (2006) stated that
the ribosomal proteins L5 (RPL5; 603634), L11 (RPL11; 604175), and L23
interact with MDM2 (164785) and inhibit MDM2-mediated p53 ubiquitination
and degradation in response to ribosomal stress. They found that L5 and
L23 inhibited ubiquitination of both p53 and MDM2 in human cell lines.
In contrast, L11 inhibited proteasome-mediated degradation of
ubiquitinated MDM2, but not p53, resulting in stabilization of p53.
MAPPING
Kenmochi et al. (1998) mapped the RPL23 gene to 17q using somatic cell
hybrid and radiation hybrid mapping analyses.
Berchtold and Berger (1991) reported that the human genome contains at
least 5 copies of the RPL23 gene, some of which might be pseudogenes.
*FIELD* RF
1. Berchtold, M. W.; Berger, M. C.: Isolation and analysis of a human
cDNA highly homologous to the yeast gene encoding L17A ribosomal protein. Gene 102:
283-288, 1991.
2. Dai, M.-S.; Shi, D.; Jin, Y.; Sun, X.-X.; Zhang, Y.; Grossman,
S. R.; Lu, H.: Regulation of the MDM2-p53 pathway by ribosomal protein
L11 involves a post-ubiquitination mechanism. J. Biol. Chem. 281:
24304-24313, 2006.
3. Herault, Y.; Michel, D.; Chatelain, G.; Brun, G.: cDNA and predicted
amino acid sequences of the human ribosomal protein genes rpS12 and
rpL17. Nucleic Acids Res. 19: 4001 only, 1991.
4. 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.
*FIELD* CN
Patricia A. Hartz - updated: 1/20/2010
*FIELD* CD
Patti M. Sherman: 3/22/1999
*FIELD* ED
mgross: 01/21/2010
terry: 1/20/2010
carol: 3/31/1999
*RECORD*
*FIELD* NO
603662
*FIELD* TI
*603662 RIBOSOMAL PROTEIN L23; RPL23
*FIELD* TX
DESCRIPTION
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins, including RPL23 (Kenmochi et al.,
1998).
CLONING
By differential screening of a human lymphocyte cDNA library with probes
derived from actively dividing or quiescent quail neuroretina cells,
Herault et al. (1991) isolated cDNAs encoding ribosomal protein L23
(RPL23), which they called rpL17. The deduced 140-amino acid human RPL23
protein is 78% identical to yeast ribosomal protein L17.
Berchtold and Berger (1991) isolated a human brain RPL23 cDNA using PCR.
Northern blot analysis detected a 600-bp RPL23 transcript in all human
tissues examined.
GENE FUNCTION
Impeding ribosomal biogenesis generates ribosomal stress that activates
p53 (TP53; 191170) to stop cell growth. Dai et al. (2006) stated that
the ribosomal proteins L5 (RPL5; 603634), L11 (RPL11; 604175), and L23
interact with MDM2 (164785) and inhibit MDM2-mediated p53 ubiquitination
and degradation in response to ribosomal stress. They found that L5 and
L23 inhibited ubiquitination of both p53 and MDM2 in human cell lines.
In contrast, L11 inhibited proteasome-mediated degradation of
ubiquitinated MDM2, but not p53, resulting in stabilization of p53.
MAPPING
Kenmochi et al. (1998) mapped the RPL23 gene to 17q using somatic cell
hybrid and radiation hybrid mapping analyses.
Berchtold and Berger (1991) reported that the human genome contains at
least 5 copies of the RPL23 gene, some of which might be pseudogenes.
*FIELD* RF
1. Berchtold, M. W.; Berger, M. C.: Isolation and analysis of a human
cDNA highly homologous to the yeast gene encoding L17A ribosomal protein. Gene 102:
283-288, 1991.
2. Dai, M.-S.; Shi, D.; Jin, Y.; Sun, X.-X.; Zhang, Y.; Grossman,
S. R.; Lu, H.: Regulation of the MDM2-p53 pathway by ribosomal protein
L11 involves a post-ubiquitination mechanism. J. Biol. Chem. 281:
24304-24313, 2006.
3. Herault, Y.; Michel, D.; Chatelain, G.; Brun, G.: cDNA and predicted
amino acid sequences of the human ribosomal protein genes rpS12 and
rpL17. Nucleic Acids Res. 19: 4001 only, 1991.
4. 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.
*FIELD* CN
Patricia A. Hartz - updated: 1/20/2010
*FIELD* CD
Patti M. Sherman: 3/22/1999
*FIELD* ED
mgross: 01/21/2010
terry: 1/20/2010
carol: 3/31/1999