Full text data of RPL12
RPL12
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L12
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L12
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P30050
ID RL12_HUMAN Reviewed; 165 AA.
AC P30050; Q5VVV2; Q6PB27;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=60S ribosomal protein L12;
GN Name=RPL12;
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] (ISOFORM 1).
RX PubMed=8441690; DOI=10.1093/nar/21.3.749;
RA Chu W., Presky D.H., Swerlisk R.A., Burns D.K.;
RT "The primary structure of human ribosomal protein L12.";
RL Nucleic Acids Res. 21:749-749(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary;
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 SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-83, AND MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
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 [13]
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).
CC -!- FUNCTION: Binds directly to 26S ribosomal RNA (By similarity).
CC -!- INTERACTION:
CC P27824:CANX; NbExp=3; IntAct=EBI-352743, EBI-355947;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30050-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30050-2; Sequence=VSP_034695;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family.
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DR EMBL; L06505; AAA36157.1; -; mRNA.
DR EMBL; AL445222; CAH72929.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87669.1; -; Genomic_DNA.
DR EMBL; BC050644; AAH50644.1; -; mRNA.
DR EMBL; BC059950; AAH59950.1; -; mRNA.
DR EMBL; BC094831; AAH94831.1; -; mRNA.
DR EMBL; BC105603; AAI05604.1; -; mRNA.
DR PIR; S35531; S35531.
DR RefSeq; NP_000967.1; NM_000976.3.
DR RefSeq; XP_005252188.1; XM_005252131.1.
DR UniGene; Hs.408054; -.
DR PDB; 3J3B; EM; 5.00 A; K=1-165.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P30050; -.
DR SMR; P30050; 1-163.
DR IntAct; P30050; 29.
DR MINT; MINT-2802291; -.
DR STRING; 9606.ENSP00000354739; -.
DR PhosphoSite; P30050; -.
DR DMDM; 266921; -.
DR SWISS-2DPAGE; P30050; -.
DR PaxDb; P30050; -.
DR PRIDE; P30050; -.
DR DNASU; 6136; -.
DR Ensembl; ENST00000361436; ENSP00000354739; ENSG00000197958.
DR Ensembl; ENST00000536368; ENSP00000441179; ENSG00000197958.
DR GeneID; 6136; -.
DR KEGG; hsa:6136; -.
DR UCSC; uc004bqy.2; human.
DR CTD; 6136; -.
DR GeneCards; GC09M130209; -.
DR H-InvDB; HIX0170298; -.
DR HGNC; HGNC:10302; RPL12.
DR HPA; HPA003403; -.
DR MIM; 180475; gene.
DR neXtProt; NX_P30050; -.
DR PharmGKB; PA34665; -.
DR eggNOG; COG0080; -.
DR HOVERGEN; HBG007231; -.
DR InParanoid; P30050; -.
DR KO; K02870; -.
DR OMA; GCTIDGR; -.
DR OrthoDB; EOG7JMGG9; -.
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; RPL12; human.
DR GeneWiki; RPL12; -.
DR GenomeRNAi; 6136; -.
DR NextBio; 23835; -.
DR PRO; PR:P30050; -.
DR Bgee; P30050; -.
DR CleanEx; HS_RPL12; -.
DR Genevestigator; P30050; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1; -.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1 165 60S ribosomal protein L12.
FT /FTId=PRO_0000104456.
FT MOD_RES 38 38 Phosphoserine.
FT MOD_RES 54 54 N6-acetyllysine.
FT MOD_RES 83 83 N6-acetyllysine.
FT VAR_SEQ 38 70 Missing (in isoform 2).
FT /FTId=VSP_034695.
SQ SEQUENCE 165 AA; 17819 MW; 7EFD783A8ED350F9 CRC64;
MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT GDWKGLRITV
KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH SGNITFDEIV NIARQMRHRS
LARELSGTIK EILGTAQSVG CNVDGRHPHD IIDDINSGAV ECPAS
//
ID RL12_HUMAN Reviewed; 165 AA.
AC P30050; Q5VVV2; Q6PB27;
DT 01-APR-1993, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-APR-1993, sequence version 1.
DT 22-JAN-2014, entry version 133.
DE RecName: Full=60S ribosomal protein L12;
GN Name=RPL12;
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] (ISOFORM 1).
RX PubMed=8441690; DOI=10.1093/nar/21.3.749;
RA Chu W., Presky D.H., Swerlisk R.A., Burns D.K.;
RT "The primary structure of human ribosomal protein L12.";
RL Nucleic Acids Res. 21:749-749(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Ovary;
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 SER-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein
RT phosphorylation analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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].
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-54 AND LYS-83, AND MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, 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 [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38, AND MASS
RP SPECTROMETRY.
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 [13]
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).
CC -!- FUNCTION: Binds directly to 26S ribosomal RNA (By similarity).
CC -!- INTERACTION:
CC P27824:CANX; NbExp=3; IntAct=EBI-352743, EBI-355947;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P30050-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P30050-2; Sequence=VSP_034695;
CC Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family.
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DR EMBL; L06505; AAA36157.1; -; mRNA.
DR EMBL; AL445222; CAH72929.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87669.1; -; Genomic_DNA.
DR EMBL; BC050644; AAH50644.1; -; mRNA.
DR EMBL; BC059950; AAH59950.1; -; mRNA.
DR EMBL; BC094831; AAH94831.1; -; mRNA.
DR EMBL; BC105603; AAI05604.1; -; mRNA.
DR PIR; S35531; S35531.
DR RefSeq; NP_000967.1; NM_000976.3.
DR RefSeq; XP_005252188.1; XM_005252131.1.
DR UniGene; Hs.408054; -.
DR PDB; 3J3B; EM; 5.00 A; K=1-165.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P30050; -.
DR SMR; P30050; 1-163.
DR IntAct; P30050; 29.
DR MINT; MINT-2802291; -.
DR STRING; 9606.ENSP00000354739; -.
DR PhosphoSite; P30050; -.
DR DMDM; 266921; -.
DR SWISS-2DPAGE; P30050; -.
DR PaxDb; P30050; -.
DR PRIDE; P30050; -.
DR DNASU; 6136; -.
DR Ensembl; ENST00000361436; ENSP00000354739; ENSG00000197958.
DR Ensembl; ENST00000536368; ENSP00000441179; ENSG00000197958.
DR GeneID; 6136; -.
DR KEGG; hsa:6136; -.
DR UCSC; uc004bqy.2; human.
DR CTD; 6136; -.
DR GeneCards; GC09M130209; -.
DR H-InvDB; HIX0170298; -.
DR HGNC; HGNC:10302; RPL12.
DR HPA; HPA003403; -.
DR MIM; 180475; gene.
DR neXtProt; NX_P30050; -.
DR PharmGKB; PA34665; -.
DR eggNOG; COG0080; -.
DR HOVERGEN; HBG007231; -.
DR InParanoid; P30050; -.
DR KO; K02870; -.
DR OMA; GCTIDGR; -.
DR OrthoDB; EOG7JMGG9; -.
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; RPL12; human.
DR GeneWiki; RPL12; -.
DR GenomeRNAi; 6136; -.
DR NextBio; 23835; -.
DR PRO; PR:P30050; -.
DR Bgee; P30050; -.
DR CleanEx; HS_RPL12; -.
DR Genevestigator; P30050; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.10.250; -; 1.
DR Gene3D; 3.30.1550.10; -; 1.
DR HAMAP; MF_00736; Ribosomal_L11; 1; -.
DR InterPro; IPR000911; Ribosomal_L11/L12.
DR InterPro; IPR020783; Ribosomal_L11_C.
DR InterPro; IPR020785; Ribosomal_L11_CS.
DR InterPro; IPR020784; Ribosomal_L11_N.
DR PANTHER; PTHR11661; PTHR11661; 1.
DR Pfam; PF00298; Ribosomal_L11; 1.
DR Pfam; PF03946; Ribosomal_L11_N; 1.
DR SMART; SM00649; RL11; 1.
DR SUPFAM; SSF46906; SSF46906; 1.
DR SUPFAM; SSF54747; SSF54747; 1.
DR PROSITE; PS00359; RIBOSOMAL_L11; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Phosphoprotein; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT CHAIN 1 165 60S ribosomal protein L12.
FT /FTId=PRO_0000104456.
FT MOD_RES 38 38 Phosphoserine.
FT MOD_RES 54 54 N6-acetyllysine.
FT MOD_RES 83 83 N6-acetyllysine.
FT VAR_SEQ 38 70 Missing (in isoform 2).
FT /FTId=VSP_034695.
SQ SEQUENCE 165 AA; 17819 MW; 7EFD783A8ED350F9 CRC64;
MPPKFDPNEI KVVYLRCTGG EVGATSALAP KIGPLGLSPK KVGDDIAKAT GDWKGLRITV
KLTIQNRQAQ IEVVPSASAL IIKALKEPPR DRKKQKNIKH SGNITFDEIV NIARQMRHRS
LARELSGTIK EILGTAQSVG CNVDGRHPHD IIDDINSGAV ECPAS
//
MIM
180475
*RECORD*
*FIELD* NO
180475
*FIELD* TI
*180475 RIBOSOMAL PROTEIN L12; RPL12
*FIELD* TX
CLONING
Biogenesis of the mammalian ribosome, the site of protein synthesis,
read moreinvolves coordinated expression of 4 ribosomal RNA molecules and
approximately 75 ribosomal proteins. Chu et al. (1993) isolated a cDNA
clone encoding human ribosomal protein L12 from a dermal microvascular
endothelial cell cDNA library. The protein contains 165 amino acids and
exhibits 99.4% sequence identity with rat ribosomal protein L12.
Northern blot analysis detected an mRNA transcript of 800 bases.
Cuccurese et al. (2005) identified an RPL12 splice variant in a human
lung carcinoma cell line that was induced following inhibition of
nonsense-mediated mRNA decay. The variant retains part of intron 1,
resulting in a premature termination codon. Northern blot analysis
showed that the variant is 0.8 kb, while the major species is 0.63 kb.
Intron 1 is highly conserved in human, mouse, and bovine RPL12 genes.
MAPPING
Hartz (2007) mapped the RPL12 gene to chromosome 9q33.3 based on an
alignment of the RPL12 sequence (GenBank GENBANK AB209471) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Chu, W.; Presky, D. H.; Swerlick, R. A.; Burns, D. K.: The primary
structure of human ribosomal protein L12. Nucleic Acids Res. 21:
749 only, 1993.
2. Cuccurese, M.; Russo, G.; Russo, A.; Pietropaolo, C.: Alternative
splicing and nonsense-mediated mRNA decay regulate mammalian ribosomal
gene expression. Nucleic Acids Res. 33: 5965-5977, 2005.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/1/2007.
*FIELD* CN
Patricia A. Hartz - updated: 5/8/2007
*FIELD* CD
Victor A. McKusick: 9/17/1993
*FIELD* ED
mgross: 06/01/2007
mgross: 6/1/2007
terry: 5/8/2007
carol: 9/17/1993
*RECORD*
*FIELD* NO
180475
*FIELD* TI
*180475 RIBOSOMAL PROTEIN L12; RPL12
*FIELD* TX
CLONING
Biogenesis of the mammalian ribosome, the site of protein synthesis,
read moreinvolves coordinated expression of 4 ribosomal RNA molecules and
approximately 75 ribosomal proteins. Chu et al. (1993) isolated a cDNA
clone encoding human ribosomal protein L12 from a dermal microvascular
endothelial cell cDNA library. The protein contains 165 amino acids and
exhibits 99.4% sequence identity with rat ribosomal protein L12.
Northern blot analysis detected an mRNA transcript of 800 bases.
Cuccurese et al. (2005) identified an RPL12 splice variant in a human
lung carcinoma cell line that was induced following inhibition of
nonsense-mediated mRNA decay. The variant retains part of intron 1,
resulting in a premature termination codon. Northern blot analysis
showed that the variant is 0.8 kb, while the major species is 0.63 kb.
Intron 1 is highly conserved in human, mouse, and bovine RPL12 genes.
MAPPING
Hartz (2007) mapped the RPL12 gene to chromosome 9q33.3 based on an
alignment of the RPL12 sequence (GenBank GENBANK AB209471) with the
genomic sequence (build 36.1).
*FIELD* RF
1. Chu, W.; Presky, D. H.; Swerlick, R. A.; Burns, D. K.: The primary
structure of human ribosomal protein L12. Nucleic Acids Res. 21:
749 only, 1993.
2. Cuccurese, M.; Russo, G.; Russo, A.; Pietropaolo, C.: Alternative
splicing and nonsense-mediated mRNA decay regulate mammalian ribosomal
gene expression. Nucleic Acids Res. 33: 5965-5977, 2005.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 6/1/2007.
*FIELD* CN
Patricia A. Hartz - updated: 5/8/2007
*FIELD* CD
Victor A. McKusick: 9/17/1993
*FIELD* ED
mgross: 06/01/2007
mgross: 6/1/2007
terry: 5/8/2007
carol: 9/17/1993