Full text data of RPL18A
RPL18A
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L18a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L18a
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q02543
ID RL18A_HUMAN Reviewed; 176 AA.
AC Q02543;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=60S ribosomal protein L18a;
GN Name=RPL18A;
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].
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zenz K.I.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 INTERACTION WITH IPO9.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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 -!- SUBUNIT: Binds IPO9 with high affinity.
CC -!- SIMILARITY: Belongs to the ribosomal protein L18Ae family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56788.1; Type=Frameshift; Positions=65;
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; L05093; AAC18781.1; -; mRNA.
DR EMBL; X80822; CAA56788.1; ALT_FRAME; mRNA.
DR EMBL; AC005796; AAC62828.1; -; Genomic_DNA.
DR EMBL; BC007512; AAH07512.1; -; mRNA.
DR EMBL; BC066319; AAH66319.1; -; mRNA.
DR EMBL; BC071920; AAH71920.1; -; mRNA.
DR PIR; S47353; S47353.
DR RefSeq; NP_000971.1; NM_000980.3.
DR UniGene; Hs.337766; -.
DR PDB; 3J3B; EM; 5.00 A; S=1-176.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; Q02543; -.
DR SMR; Q02543; 2-176.
DR IntAct; Q02543; 18.
DR MINT; MINT-5000271; -.
DR STRING; 9606.ENSP00000222247; -.
DR PhosphoSite; Q02543; -.
DR DMDM; 730538; -.
DR SWISS-2DPAGE; Q02543; -.
DR PaxDb; Q02543; -.
DR PeptideAtlas; Q02543; -.
DR PRIDE; Q02543; -.
DR DNASU; 6142; -.
DR Ensembl; ENST00000222247; ENSP00000222247; ENSG00000105640.
DR GeneID; 6142; -.
DR KEGG; hsa:6142; -.
DR UCSC; uc002nhp.3; human.
DR CTD; 6142; -.
DR GeneCards; GC19P017970; -.
DR HGNC; HGNC:10311; RPL18A.
DR HPA; HPA055259; -.
DR MIM; 604178; gene.
DR neXtProt; NX_Q02543; -.
DR PharmGKB; PA34680; -.
DR eggNOG; COG2157; -.
DR HOGENOM; HOG000211377; -.
DR HOVERGEN; HBG066281; -.
DR InParanoid; Q02543; -.
DR KO; K02882; -.
DR OMA; VNVIHEK; -.
DR OrthoDB; EOG7TMZT2; -.
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; RPL18A; -.
DR GenomeRNAi; 6142; -.
DR NextBio; 23861; -.
DR PRO; PR:Q02543; -.
DR ArrayExpress; Q02543; -.
DR Bgee; Q02543; -.
DR CleanEx; HS_RPL18A; -.
DR Genevestigator; Q02543; -.
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 HAMAP; MF_00273; Ribosomal_L18Ae; 1; -.
DR InterPro; IPR021138; Ribosomal_L18a/L20.
DR InterPro; IPR023573; Ribosomal_L18a/LX.
DR Pfam; PF01775; Ribosomal_L18ae; 1.
DR PIRSF; PIRSF002190; Ribosomal_L18a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 176 60S ribosomal protein L18a.
FT /FTId=PRO_0000213925.
FT MOD_RES 63 63 Phosphotyrosine.
FT MOD_RES 71 71 Phosphoserine.
FT CONFLICT 83 83 R -> S (in Ref. 2; CAA56788).
FT CONFLICT 134 134 A -> V (in Ref. 2; CAA56788).
SQ SEQUENCE 176 AA; 20762 MW; 5E501C6D835BE580 CRC64;
MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ LKKMKKSSGE
IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL TTAGAVTQCY RDMGARHRAR
AHSIQIMKVE EIAASKCRRP AVKQFHDSKI KFPLPHRVLR RQHKPRFTTK RPNTFF
//
ID RL18A_HUMAN Reviewed; 176 AA.
AC Q02543;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-FEB-1995, sequence version 2.
DT 22-JAN-2014, entry version 131.
DE RecName: Full=60S ribosomal protein L18a;
GN Name=RPL18A;
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].
RA Bhat K.S.;
RL Submitted (NOV-1992) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Zenz K.I.;
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Muscle;
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 INTERACTION WITH IPO9.
RX PubMed=11823430; DOI=10.1093/emboj/21.3.377;
RA Jaekel S., Mingot J.-M., Schwarzmaier P., Hartmann E., Goerlich D.;
RT "Importins fulfill a dual function as nuclear import receptors and
RT cytoplasmic chaperones for exposed basic domains.";
RL EMBO J. 21:377-386(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-63, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASS
RP SPECTROMETRY.
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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 -!- SUBUNIT: Binds IPO9 with high affinity.
CC -!- SIMILARITY: Belongs to the ribosomal protein L18Ae family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56788.1; Type=Frameshift; Positions=65;
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; L05093; AAC18781.1; -; mRNA.
DR EMBL; X80822; CAA56788.1; ALT_FRAME; mRNA.
DR EMBL; AC005796; AAC62828.1; -; Genomic_DNA.
DR EMBL; BC007512; AAH07512.1; -; mRNA.
DR EMBL; BC066319; AAH66319.1; -; mRNA.
DR EMBL; BC071920; AAH71920.1; -; mRNA.
DR PIR; S47353; S47353.
DR RefSeq; NP_000971.1; NM_000980.3.
DR UniGene; Hs.337766; -.
DR PDB; 3J3B; EM; 5.00 A; S=1-176.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; Q02543; -.
DR SMR; Q02543; 2-176.
DR IntAct; Q02543; 18.
DR MINT; MINT-5000271; -.
DR STRING; 9606.ENSP00000222247; -.
DR PhosphoSite; Q02543; -.
DR DMDM; 730538; -.
DR SWISS-2DPAGE; Q02543; -.
DR PaxDb; Q02543; -.
DR PeptideAtlas; Q02543; -.
DR PRIDE; Q02543; -.
DR DNASU; 6142; -.
DR Ensembl; ENST00000222247; ENSP00000222247; ENSG00000105640.
DR GeneID; 6142; -.
DR KEGG; hsa:6142; -.
DR UCSC; uc002nhp.3; human.
DR CTD; 6142; -.
DR GeneCards; GC19P017970; -.
DR HGNC; HGNC:10311; RPL18A.
DR HPA; HPA055259; -.
DR MIM; 604178; gene.
DR neXtProt; NX_Q02543; -.
DR PharmGKB; PA34680; -.
DR eggNOG; COG2157; -.
DR HOGENOM; HOG000211377; -.
DR HOVERGEN; HBG066281; -.
DR InParanoid; Q02543; -.
DR KO; K02882; -.
DR OMA; VNVIHEK; -.
DR OrthoDB; EOG7TMZT2; -.
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; RPL18A; -.
DR GenomeRNAi; 6142; -.
DR NextBio; 23861; -.
DR PRO; PR:Q02543; -.
DR ArrayExpress; Q02543; -.
DR Bgee; Q02543; -.
DR CleanEx; HS_RPL18A; -.
DR Genevestigator; Q02543; -.
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 HAMAP; MF_00273; Ribosomal_L18Ae; 1; -.
DR InterPro; IPR021138; Ribosomal_L18a/L20.
DR InterPro; IPR023573; Ribosomal_L18a/LX.
DR Pfam; PF01775; Ribosomal_L18ae; 1.
DR PIRSF; PIRSF002190; Ribosomal_L18a; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Phosphoprotein; Reference proteome;
KW Ribonucleoprotein; Ribosomal protein.
FT CHAIN 1 176 60S ribosomal protein L18a.
FT /FTId=PRO_0000213925.
FT MOD_RES 63 63 Phosphotyrosine.
FT MOD_RES 71 71 Phosphoserine.
FT CONFLICT 83 83 R -> S (in Ref. 2; CAA56788).
FT CONFLICT 134 134 A -> V (in Ref. 2; CAA56788).
SQ SEQUENCE 176 AA; 20762 MW; 5E501C6D835BE580 CRC64;
MKASGTLREY KVVGRCLPTP KCHTPPLYRM RIFAPNHVVA KSRFWYFVSQ LKKMKKSSGE
IVYCGQVFEK SPLRVKNFGI WLRYDSRSGT HNMYREYRDL TTAGAVTQCY RDMGARHRAR
AHSIQIMKVE EIAASKCRRP AVKQFHDSKI KFPLPHRVLR RQHKPRFTTK RPNTFF
//
MIM
604178
*RECORD*
*FIELD* NO
604178
*FIELD* TI
*604178 RIBOSOMAL PROTEIN L18A; RPL18A
*FIELD* TX
CLONING
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466). Adams et al. (1992)
isolated an RPL18A cDNA as a human brain EST. The complete coding
sequence of the human RPL18A gene has been deposited in GenBank (GENBANK
L05093). The deduced RPL18A protein has 176 amino acids.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL18A gene to 19p.
*FIELD* RF
1. Adams, M. D.; Dubnick, M.; Kerlavage, A. R.; Moreno, R.; Kelley,
J. M.; Utterback, T. R.; Nagle, J. W.; Fields, C.; Venter, J. C.:
Sequence identification of 2,375 human brain genes. Nature 355:
632-634, 1992. Note: Comment: Nature 357: 367-368, 1992.
2. 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* CD
Patti M. Sherman: 9/21/1999
*FIELD* ED
mgross: 02/06/2003
psherman: 12/7/1999
mgross: 9/23/1999
psherman: 9/21/1999
*RECORD*
*FIELD* NO
604178
*FIELD* TI
*604178 RIBOSOMAL PROTEIN L18A; RPL18A
*FIELD* TX
CLONING
The mammalian ribosome is composed of 4 RNA species (see 180450) and
read moreapproximately 80 different proteins (see 180466). Adams et al. (1992)
isolated an RPL18A cDNA as a human brain EST. The complete coding
sequence of the human RPL18A gene has been deposited in GenBank (GENBANK
L05093). The deduced RPL18A protein has 176 amino acids.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL18A gene to 19p.
*FIELD* RF
1. Adams, M. D.; Dubnick, M.; Kerlavage, A. R.; Moreno, R.; Kelley,
J. M.; Utterback, T. R.; Nagle, J. W.; Fields, C.; Venter, J. C.:
Sequence identification of 2,375 human brain genes. Nature 355:
632-634, 1992. Note: Comment: Nature 357: 367-368, 1992.
2. 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* CD
Patti M. Sherman: 9/21/1999
*FIELD* ED
mgross: 02/06/2003
psherman: 12/7/1999
mgross: 9/23/1999
psherman: 9/21/1999