Full text data of RPL28
RPL28
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
60S ribosomal protein L28
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L28
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P46779
ID RL28_HUMAN Reviewed; 137 AA.
AC P46779; B2R4A6; B4DEP9; C9JB50; E9PB24; G5E9L2; Q6IAY0; Q96FX1;
read moreAC Q9BWQ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=60S ribosomal protein L28;
GN Name=RPL28;
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).
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Hippocampus;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=B-cell, Kidney, Prostatic adenocarcinoma, 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 [7]
RP PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma, and Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Lilla S., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT SER-2.
RX PubMed=12962325; DOI=10.1023/A:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, 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 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 P43146:DCC; NbExp=3; IntAct=EBI-366357, EBI-1222919;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P46779-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46779-2; Sequence=VSP_043026;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P46779-3; Sequence=VSP_046173;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P46779-4; Sequence=VSP_047026;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC Name=5;
CC IsoId=P46779-5; Sequence=VSP_047027;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ribosomal protein L28e family.
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DR EMBL; U14969; AAA85657.1; -; mRNA.
DR EMBL; CR457024; CAG33305.1; -; mRNA.
DR EMBL; AK311760; BAG34703.1; -; mRNA.
DR EMBL; AK293736; BAG57160.1; -; mRNA.
DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72374.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72375.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72376.1; -; Genomic_DNA.
DR EMBL; BC010173; AAH10173.1; -; mRNA.
DR EMBL; BC010182; AAH10182.1; -; mRNA.
DR EMBL; BC011582; AAH11582.1; -; mRNA.
DR EMBL; BG777550; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S55915; S55915.
DR RefSeq; NP_000982.2; NM_000991.4.
DR RefSeq; NP_001129606.1; NM_001136134.1.
DR RefSeq; NP_001129607.1; NM_001136135.1.
DR RefSeq; NP_001129608.1; NM_001136136.1.
DR RefSeq; NP_001129609.1; NM_001136137.1.
DR UniGene; Hs.652114; -.
DR PDB; 3J3B; EM; 5.00 A; r=1-137.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P46779; -.
DR SMR; P46779; 1-137.
DR IntAct; P46779; 23.
DR MINT; MINT-5004261; -.
DR STRING; 9606.ENSP00000401450; -.
DR PhosphoSite; P46779; -.
DR DMDM; 22002069; -.
DR PaxDb; P46779; -.
DR PeptideAtlas; P46779; -.
DR PRIDE; P46779; -.
DR DNASU; 6158; -.
DR Ensembl; ENST00000344063; ENSP00000342787; ENSG00000108107.
DR Ensembl; ENST00000428193; ENSP00000391665; ENSG00000108107.
DR Ensembl; ENST00000431533; ENSP00000400596; ENSG00000108107.
DR Ensembl; ENST00000458349; ENSP00000401450; ENSG00000108107.
DR Ensembl; ENST00000558815; ENSP00000452909; ENSG00000108107.
DR Ensembl; ENST00000559463; ENSP00000453319; ENSG00000108107.
DR Ensembl; ENST00000560583; ENSP00000453029; ENSG00000108107.
DR GeneID; 6158; -.
DR KEGG; hsa:6158; -.
DR UCSC; uc010yfy.1; human.
DR CTD; 6158; -.
DR GeneCards; GC19P055897; -.
DR HGNC; HGNC:10330; RPL28.
DR HPA; HPA050459; -.
DR MIM; 603638; gene.
DR neXtProt; NX_P46779; -.
DR PharmGKB; PA34710; -.
DR eggNOG; NOG148062; -.
DR HOGENOM; HOG000200513; -.
DR HOVERGEN; HBG000701; -.
DR InParanoid; P46779; -.
DR KO; K02903; -.
DR OMA; PAKNTVR; -.
DR OrthoDB; EOG74N5JT; -.
DR PhylomeDB; P46779; -.
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; RPL28; human.
DR GeneWiki; 60S_ribosomal_protein_L28; -.
DR GenomeRNAi; 6158; -.
DR NextBio; 23915; -.
DR PMAP-CutDB; P46779; -.
DR PRO; PR:P46779; -.
DR ArrayExpress; P46779; -.
DR Bgee; P46779; -.
DR CleanEx; HS_RPL28; -.
DR Genevestigator; P46779; -.
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 InterPro; IPR002672; Ribosomal_L28e.
DR PANTHER; PTHR10544; PTHR10544; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 137 60S ribosomal protein L28.
FT /FTId=PRO_0000122389.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 115 115 Phosphoserine.
FT VAR_SEQ 69 137 GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMA
FT AIRRASAILRSQKPVMVKRKRTRPTKSS -> E (in
FT isoform 4).
FT /FTId=VSP_047026.
FT VAR_SEQ 70 137 QRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAA
FT IRRASAILRSQKPVMVKRKRTRPTKSS -> EFCLVWARER
FT PLSRVWEL (in isoform 5).
FT /FTId=VSP_047027.
FT VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> VSWGLGIR
FT LGETGQCCGEGPPTTGCNMGWRGMDSCFQPTPHTQHWPRGR
FT LVECMG (in isoform 2).
FT /FTId=VSP_043026.
FT VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> DMLASTGS
FT GLCCSVAVQPWASSSTSLCLRTLICNMRVDRPYYSGLMRRL
FT NVQNLLDCAHKS (in isoform 3).
FT /FTId=VSP_046173.
FT VARIANT 66 66 R -> L (in dbSNP:rs13502).
FT /FTId=VAR_034460.
FT CONFLICT 84 84 K -> R (in Ref. 6; AAH10182).
FT CONFLICT 120 120 S -> T (in Ref. 1; AAA85657).
SQ SEQUENCE 137 AA; 15748 MW; 44DCDE45473D7C7B CRC64;
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV
VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS
QKPVMVKRKR TRPTKSS
//
ID RL28_HUMAN Reviewed; 137 AA.
AC P46779; B2R4A6; B4DEP9; C9JB50; E9PB24; G5E9L2; Q6IAY0; Q96FX1;
read moreAC Q9BWQ0;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=60S ribosomal protein L28;
GN Name=RPL28;
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).
RC TISSUE=Colon;
RX PubMed=7772601; DOI=10.1016/0167-4781(95)00045-I;
RA Frigerio J.-M., Dagorn J.-C., Iovanna J.L.;
RT "Cloning, sequencing and expression of the L5, L21, L27a, L28, S5, S9,
RT S10 and S29 human ribosomal protein mRNAs.";
RL Biochim. Biophys. Acta 1262:64-68(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, and Hippocampus;
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=B-cell, Kidney, Prostatic adenocarcinoma, 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 [7]
RP PROTEIN SEQUENCE OF 2-11; 23-33; 40-58; 72-79 AND 120-127, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Hepatoma, and Ovarian carcinoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A., Lilla S., Lempens A.,
RA Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [8]
RP MASS SPECTROMETRY, AND PROBABLE ACETYLATION AT SER-2.
RX PubMed=12962325; DOI=10.1023/A:1025068419698;
RA Odintsova T.I., Muller E.C., Ivanov A.V., Egorov T.A., Bienert R.,
RA Vladimirov S.N., Kostka S., Otto A., Wittmann-Liebold B.,
RA Karpova G.G.;
RT "Characterization and analysis of posttranslational modifications of
RT the human large cytoplasmic ribosomal subunit proteins by mass
RT spectrometry and Edman sequencing.";
RL J. Protein Chem. 22:249-258(2003).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115, 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 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 P43146:DCC; NbExp=3; IntAct=EBI-366357, EBI-1222919;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P46779-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P46779-2; Sequence=VSP_043026;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=P46779-3; Sequence=VSP_046173;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=P46779-4; Sequence=VSP_047026;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC Name=5;
CC IsoId=P46779-5; Sequence=VSP_047027;
CC Note=No experimental confirmation available. Gene prediction
CC based on EST data;
CC -!- SIMILARITY: Belongs to the ribosomal protein L28e family.
CC -----------------------------------------------------------------------
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DR EMBL; U14969; AAA85657.1; -; mRNA.
DR EMBL; CR457024; CAG33305.1; -; mRNA.
DR EMBL; AK311760; BAG34703.1; -; mRNA.
DR EMBL; AK293736; BAG57160.1; -; mRNA.
DR EMBL; AC020922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72374.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72375.1; -; Genomic_DNA.
DR EMBL; CH471135; EAW72376.1; -; Genomic_DNA.
DR EMBL; BC010173; AAH10173.1; -; mRNA.
DR EMBL; BC010182; AAH10182.1; -; mRNA.
DR EMBL; BC011582; AAH11582.1; -; mRNA.
DR EMBL; BG777550; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S55915; S55915.
DR RefSeq; NP_000982.2; NM_000991.4.
DR RefSeq; NP_001129606.1; NM_001136134.1.
DR RefSeq; NP_001129607.1; NM_001136135.1.
DR RefSeq; NP_001129608.1; NM_001136136.1.
DR RefSeq; NP_001129609.1; NM_001136137.1.
DR UniGene; Hs.652114; -.
DR PDB; 3J3B; EM; 5.00 A; r=1-137.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P46779; -.
DR SMR; P46779; 1-137.
DR IntAct; P46779; 23.
DR MINT; MINT-5004261; -.
DR STRING; 9606.ENSP00000401450; -.
DR PhosphoSite; P46779; -.
DR DMDM; 22002069; -.
DR PaxDb; P46779; -.
DR PeptideAtlas; P46779; -.
DR PRIDE; P46779; -.
DR DNASU; 6158; -.
DR Ensembl; ENST00000344063; ENSP00000342787; ENSG00000108107.
DR Ensembl; ENST00000428193; ENSP00000391665; ENSG00000108107.
DR Ensembl; ENST00000431533; ENSP00000400596; ENSG00000108107.
DR Ensembl; ENST00000458349; ENSP00000401450; ENSG00000108107.
DR Ensembl; ENST00000558815; ENSP00000452909; ENSG00000108107.
DR Ensembl; ENST00000559463; ENSP00000453319; ENSG00000108107.
DR Ensembl; ENST00000560583; ENSP00000453029; ENSG00000108107.
DR GeneID; 6158; -.
DR KEGG; hsa:6158; -.
DR UCSC; uc010yfy.1; human.
DR CTD; 6158; -.
DR GeneCards; GC19P055897; -.
DR HGNC; HGNC:10330; RPL28.
DR HPA; HPA050459; -.
DR MIM; 603638; gene.
DR neXtProt; NX_P46779; -.
DR PharmGKB; PA34710; -.
DR eggNOG; NOG148062; -.
DR HOGENOM; HOG000200513; -.
DR HOVERGEN; HBG000701; -.
DR InParanoid; P46779; -.
DR KO; K02903; -.
DR OMA; PAKNTVR; -.
DR OrthoDB; EOG74N5JT; -.
DR PhylomeDB; P46779; -.
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; RPL28; human.
DR GeneWiki; 60S_ribosomal_protein_L28; -.
DR GenomeRNAi; 6158; -.
DR NextBio; 23915; -.
DR PMAP-CutDB; P46779; -.
DR PRO; PR:P46779; -.
DR ArrayExpress; P46779; -.
DR Bgee; P46779; -.
DR CleanEx; HS_RPL28; -.
DR Genevestigator; P46779; -.
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 InterPro; IPR002672; Ribosomal_L28e.
DR PANTHER; PTHR10544; PTHR10544; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Phosphoprotein; Polymorphism;
KW Reference proteome; Ribonucleoprotein; Ribosomal protein.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 137 60S ribosomal protein L28.
FT /FTId=PRO_0000122389.
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 115 115 Phosphoserine.
FT VAR_SEQ 69 137 GQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMA
FT AIRRASAILRSQKPVMVKRKRTRPTKSS -> E (in
FT isoform 4).
FT /FTId=VSP_047026.
FT VAR_SEQ 70 137 QRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAA
FT IRRASAILRSQKPVMVKRKRTRPTKSS -> EFCLVWARER
FT PLSRVWEL (in isoform 5).
FT /FTId=VSP_047027.
FT VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> VSWGLGIR
FT LGETGQCCGEGPPTTGCNMGWRGMDSCFQPTPHTQHWPRGR
FT LVECMG (in isoform 2).
FT /FTId=VSP_043026.
FT VAR_SEQ 109 137 AAIRRASAILRSQKPVMVKRKRTRPTKSS -> DMLASTGS
FT GLCCSVAVQPWASSSTSLCLRTLICNMRVDRPYYSGLMRRL
FT NVQNLLDCAHKS (in isoform 3).
FT /FTId=VSP_046173.
FT VARIANT 66 66 R -> L (in dbSNP:rs13502).
FT /FTId=VAR_034460.
FT CONFLICT 84 84 K -> R (in Ref. 6; AAH10182).
FT CONFLICT 120 120 S -> T (in Ref. 1; AAA85657).
SQ SEQUENCE 137 AA; 15748 MW; 44DCDE45473D7C7B CRC64;
MSAHLQWMVV RNCSSFLIKR NKQTYSTEPN NLKARNSFRY NGLIHRKTVG VEPAADGKGV
VVVIKRRSGQ RKPATSYVRT TINKNARATL SSIRHMIRKN KYRPDLRMAA IRRASAILRS
QKPVMVKRKR TRPTKSS
//
MIM
603638
*RECORD*
*FIELD* NO
603638
*FIELD* TI
*603638 RIBOSOMAL PROTEIN L28; RPL28
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins, including RPL28.
CLONING
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29;
603633), L5 (RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637),
and L28 (RPL28). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 137-amino acid human RPL28
differs from rat Rpl28 by 6 amino acids. Northern blot analysis
suggested variable expression of RPL28 in colorectal cancers compared to
adjacent normal tissues, although no correlation between the level of
expression and the severity of the disease was found.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL28 gene to 19q13.4 (GenBank GENBANK
AB007179).
Goldammer et al. (2002) created a comparative radiation hybrid map of
bovine chromosome 18 and the homologous chromosomes in human (16q and
19q) and mouse (8 and 7). The RPL28 gene was one the most telomeric
genes on human 19q and bovine chromosome 18.
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
3. Goldammer, T.; Kata, S. R.; Brunner, R. M.; Dorroch, U.; Sanftleben,
H.; Schwerin, M.; Womack, J. E.: A comparative radiation hybrid map
of bovine chromosome 18 and homologous chromosomes in human and mice. Proc.
Nat. Acad. Sci. 99: 2106-2111, 2002.
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
Victor A. McKusick - updated: 3/5/2002
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
mgross: 03/11/2002
terry: 3/5/2002
carol: 3/19/1999
*RECORD*
*FIELD* NO
603638
*FIELD* TI
*603638 RIBOSOMAL PROTEIN L28; RPL28
*FIELD* TX
DESCRIPTION
The mammalian ribosome is a macromolecular assembly of 4 RNA species
read more(see 180450) and approximately 80 different proteins, including RPL28.
CLONING
By searching sequence databases with the partial sequences of randomly
selected cDNAs from a human colorectal cDNA library, Frigerio et al.
(1995) identified cDNAs encoding homologs of rat ribosomal proteins S5
(RPS5; 603630), S9 (RPS9; 603631), S10 (RPS10; 603632), S29 (RPS29;
603633), L5 (RPL5; 603634), L21 (RPL21; 603636), L27a (RPL27A; 603637),
and L28 (RPL28). Frigerio et al. (1995) completed the cDNA sequences of
these human ribosomal proteins. The deduced 137-amino acid human RPL28
differs from rat Rpl28 by 6 amino acids. Northern blot analysis
suggested variable expression of RPL28 in colorectal cancers compared to
adjacent normal tissues, although no correlation between the level of
expression and the severity of the disease was found.
MAPPING
By somatic cell hybrid and radiation hybrid mapping analyses, Kenmochi
et al. (1998) mapped the human RPL28 gene to 19q13.4 (GenBank GENBANK
AB007179).
Goldammer et al. (2002) created a comparative radiation hybrid map of
bovine chromosome 18 and the homologous chromosomes in human (16q and
19q) and mouse (8 and 7). The RPL28 gene was one the most telomeric
genes on human 19q and bovine chromosome 18.
*FIELD* RF
1. Frigerio, J.-M.; Berthezene, P.; Garrido, P.; Ortiz, E.; Barthellemy,
S.; Vasseur, S.; Sastre, B.; Seleznieff, I.; Dagorn, J. C.; Iovanna,
J. L.: Analysis of 2166 clones from a human colorectal cancer cDNA
library by partial sequencing. Hum. Molec. Genet. 4: 37-43, 1995.
2. Frigerio, J.-M.; Dagorn, J.-C.; Iovanna, J. L.: Cloning, sequencing
and expression of the L5, L21, L27a, L28, S5, S9, S10 and S29 human
ribosomal protein mRNAs. Biochim. Biophys. Acta 1262: 64-68, 1995.
3. Goldammer, T.; Kata, S. R.; Brunner, R. M.; Dorroch, U.; Sanftleben,
H.; Schwerin, M.; Womack, J. E.: A comparative radiation hybrid map
of bovine chromosome 18 and homologous chromosomes in human and mice. Proc.
Nat. Acad. Sci. 99: 2106-2111, 2002.
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
Victor A. McKusick - updated: 3/5/2002
*FIELD* CD
Patti M. Sherman: 3/12/1999
*FIELD* ED
mgross: 03/11/2002
terry: 3/5/2002
carol: 3/19/1999