Full text data of RPL22
RPL22
[Confidence: low (only semi-automatic identification from reviews)]
60S ribosomal protein L22 (EBER-associated protein; EAP; Epstein-Barr virus small RNA-associated protein; Heparin-binding protein HBp15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
60S ribosomal protein L22 (EBER-associated protein; EAP; Epstein-Barr virus small RNA-associated protein; Heparin-binding protein HBp15)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P35268
ID RL22_HUMAN Reviewed; 128 AA.
AC P35268; B2R495; Q6IBD1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=60S ribosomal protein L22;
DE AltName: Full=EBER-associated protein;
DE Short=EAP;
DE AltName: Full=Epstein-Barr virus small RNA-associated protein;
DE AltName: Full=Heparin-binding protein HBp15;
GN Name=RPL22;
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], AND PROTEIN SEQUENCE OF 2-46 AND 108-125.
RC TISSUE=Placenta;
RX PubMed=1846807;
RA Toczyski D.P.W., Steitz J.A.;
RT "EAP, a highly conserved cellular protein associated with Epstein-Barr
RT virus small RNAs (EBERs).";
RL EMBO J. 10:459-466(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=8135813; DOI=10.1006/bbrc.1994.1286;
RA Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D.,
RA Ozaki T., McKeehan W.L., Crabb J.W., Whitney R.G.;
RT "A novel heparin-binding protein, HBp15, is identified as mammalian
RT ribosomal protein L22.";
RL Biochem. Biophys. Res. Commun. 199:706-713(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 2-10; 53-65; 70-81 AND 102-113, CLEAVAGE OF
RP INITIATOR METHIONINE, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, and Eye;
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 [9]
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 [10]
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 -!- MISCELLANEOUS: Binds to Epstein-Barr virus small RNAs and to
CC heparin.
CC -!- SIMILARITY: Belongs to the ribosomal protein L22e 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; X59357; CAA42007.1; -; mRNA.
DR EMBL; D17652; BAA04545.1; -; mRNA.
DR EMBL; AK311749; BAG34692.1; -; mRNA.
DR EMBL; CR456873; CAG33154.1; -; mRNA.
DR EMBL; AL031847; CAI19448.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71518.1; -; Genomic_DNA.
DR EMBL; BC035566; AAH35566.1; -; mRNA.
DR EMBL; BC058887; AAH58887.1; -; mRNA.
DR EMBL; BC066314; AAH66314.1; -; mRNA.
DR PIR; JC2120; JC2120.
DR RefSeq; NP_000974.1; NM_000983.3.
DR UniGene; Hs.515329; -.
DR UniGene; Hs.554762; -.
DR PDB; 3J3B; EM; 5.00 A; U=1-128.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P35268; -.
DR SMR; P35268; 15-126.
DR IntAct; P35268; 30.
DR MINT; MINT-1149755; -.
DR STRING; 9606.ENSP00000346088; -.
DR PhosphoSite; P35268; -.
DR DMDM; 464628; -.
DR SWISS-2DPAGE; P35268; -.
DR PaxDb; P35268; -.
DR PeptideAtlas; P35268; -.
DR PRIDE; P35268; -.
DR Ensembl; ENST00000234875; ENSP00000346088; ENSG00000116251.
DR GeneID; 6146; -.
DR KEGG; hsa:6146; -.
DR UCSC; uc001amd.3; human.
DR CTD; 6146; -.
DR GeneCards; GC01M006179; -.
DR HGNC; HGNC:10315; RPL22.
DR MIM; 180474; gene.
DR neXtProt; NX_P35268; -.
DR PharmGKB; PA34688; -.
DR eggNOG; NOG260326; -.
DR HOGENOM; HOG000198396; -.
DR HOVERGEN; HBG004373; -.
DR InParanoid; P35268; -.
DR KO; K02891; -.
DR OMA; NNLGDNV; -.
DR PhylomeDB; P35268; -.
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; RPL22; -.
DR GenomeRNAi; 6146; -.
DR NextBio; 23879; -.
DR PRO; PR:P35268; -.
DR ArrayExpress; P35268; -.
DR Bgee; P35268; -.
DR CleanEx; HS_RPL22; -.
DR Genevestigator; P35268; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
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; IPR002671; Ribosomal_L22e.
DR PANTHER; PTHR10064; PTHR10064; 1.
DR Pfam; PF01776; Ribosomal_L22e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Heparin-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 128 60S ribosomal protein L22.
FT /FTId=PRO_0000215501.
FT COMPBIAS 120 128 Asp/Glu-rich (highly acidic).
SQ SEQUENCE 128 AA; 14787 MW; 0F3ED8BE70C9F962 CRC64;
MAPVKKLVVK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN GKAGNLGGGV
VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL RVVANSKESY ELRYFQINQD
EEEEEDED
//
ID RL22_HUMAN Reviewed; 128 AA.
AC P35268; B2R495; Q6IBD1;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 128.
DE RecName: Full=60S ribosomal protein L22;
DE AltName: Full=EBER-associated protein;
DE Short=EAP;
DE AltName: Full=Epstein-Barr virus small RNA-associated protein;
DE AltName: Full=Heparin-binding protein HBp15;
GN Name=RPL22;
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], AND PROTEIN SEQUENCE OF 2-46 AND 108-125.
RC TISSUE=Placenta;
RX PubMed=1846807;
RA Toczyski D.P.W., Steitz J.A.;
RT "EAP, a highly conserved cellular protein associated with Epstein-Barr
RT virus small RNAs (EBERs).";
RL EMBO J. 10:459-466(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Submandibular gland;
RX PubMed=8135813; DOI=10.1006/bbrc.1994.1286;
RA Fujita Y., Okamoto T., Noshiro M., Kato Y., Takada K., Sato J.D.,
RA Ozaki T., McKeehan W.L., Crabb J.W., Whitney R.G.;
RT "A novel heparin-binding protein, HBp15, is identified as mammalian
RT ribosomal protein L22.";
RL Biochem. Biophys. Res. Commun. 199:706-713(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 MRNA].
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 [5]
RP PROTEIN SEQUENCE OF 2-10; 53-65; 70-81 AND 102-113, CLEAVAGE OF
RP INITIATOR METHIONINE, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
RA Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
RA Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
RA Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
RA Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
RA Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
RA Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
RA Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
RA Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
RA Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
RA Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
RA Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
RA Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
RA Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
RA Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
RA Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [7]
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Cervix, and Eye;
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 [9]
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 [10]
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 -!- MISCELLANEOUS: Binds to Epstein-Barr virus small RNAs and to
CC heparin.
CC -!- SIMILARITY: Belongs to the ribosomal protein L22e 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; X59357; CAA42007.1; -; mRNA.
DR EMBL; D17652; BAA04545.1; -; mRNA.
DR EMBL; AK311749; BAG34692.1; -; mRNA.
DR EMBL; CR456873; CAG33154.1; -; mRNA.
DR EMBL; AL031847; CAI19448.1; -; Genomic_DNA.
DR EMBL; CH471130; EAW71518.1; -; Genomic_DNA.
DR EMBL; BC035566; AAH35566.1; -; mRNA.
DR EMBL; BC058887; AAH58887.1; -; mRNA.
DR EMBL; BC066314; AAH66314.1; -; mRNA.
DR PIR; JC2120; JC2120.
DR RefSeq; NP_000974.1; NM_000983.3.
DR UniGene; Hs.515329; -.
DR UniGene; Hs.554762; -.
DR PDB; 3J3B; EM; 5.00 A; U=1-128.
DR PDBsum; 3J3B; -.
DR ProteinModelPortal; P35268; -.
DR SMR; P35268; 15-126.
DR IntAct; P35268; 30.
DR MINT; MINT-1149755; -.
DR STRING; 9606.ENSP00000346088; -.
DR PhosphoSite; P35268; -.
DR DMDM; 464628; -.
DR SWISS-2DPAGE; P35268; -.
DR PaxDb; P35268; -.
DR PeptideAtlas; P35268; -.
DR PRIDE; P35268; -.
DR Ensembl; ENST00000234875; ENSP00000346088; ENSG00000116251.
DR GeneID; 6146; -.
DR KEGG; hsa:6146; -.
DR UCSC; uc001amd.3; human.
DR CTD; 6146; -.
DR GeneCards; GC01M006179; -.
DR HGNC; HGNC:10315; RPL22.
DR MIM; 180474; gene.
DR neXtProt; NX_P35268; -.
DR PharmGKB; PA34688; -.
DR eggNOG; NOG260326; -.
DR HOGENOM; HOG000198396; -.
DR HOVERGEN; HBG004373; -.
DR InParanoid; P35268; -.
DR KO; K02891; -.
DR OMA; NNLGDNV; -.
DR PhylomeDB; P35268; -.
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; RPL22; -.
DR GenomeRNAi; 6146; -.
DR NextBio; 23879; -.
DR PRO; PR:P35268; -.
DR ArrayExpress; P35268; -.
DR Bgee; P35268; -.
DR CleanEx; HS_RPL22; -.
DR Genevestigator; P35268; -.
DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; TAS:ProtInc.
DR GO; GO:0003735; F:structural constituent of ribosome; NAS:UniProtKB.
DR GO; GO:0046632; P:alpha-beta T cell differentiation; IEA:Ensembl.
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; IPR002671; Ribosomal_L22e.
DR PANTHER; PTHR10064; PTHR10064; 1.
DR Pfam; PF01776; Ribosomal_L22e; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Complete proteome; Direct protein sequencing;
KW Heparin-binding; Reference proteome; Ribonucleoprotein;
KW Ribosomal protein; RNA-binding.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 128 60S ribosomal protein L22.
FT /FTId=PRO_0000215501.
FT COMPBIAS 120 128 Asp/Glu-rich (highly acidic).
SQ SEQUENCE 128 AA; 14787 MW; 0F3ED8BE70C9F962 CRC64;
MAPVKKLVVK GGKKKKQVLK FTLDCTHPVE DGIMDAANFE QFLQERIKVN GKAGNLGGGV
VTIERSKSKI TVTSEVPFSK RYLKYLTKKY LKKNNLRDWL RVVANSKESY ELRYFQINQD
EEEEEDED
//
MIM
180474
*RECORD*
*FIELD* NO
180474
*FIELD* TI
*180474 RIBOSOMAL PROTEIN L22; RPL22
;;EPSTEIN-BARR ASSOCIATED PROTEIN; EAP
*FIELD* TX
read moreA reciprocal translocation between the long arms of chromosomes 3 and
21, at bands 3q26 and 21q22, occurs as an acquired clonal chromosomal
abnormality in malignant cells from patients with therapy-related
myelodysplastic syndrome or acute myeloid leukemia, as well as in some
patients with chronic myeloid leukemia in blast crisis. Nucifora et al.
(1993) showed that the gene on chromosome 21 is AML1 (151385), which is
fused to the ETO gene (133435) in 8;21 translocations. Nucifora et al.
(1993) isolated a fusion cDNA clone from a t(3;21) library derived from
a patient with therapy-related myelodysplastic syndrome; this clone
contained sequences from AML1 and from EAP, which they localized to 3q26
from the location of the breakpoint on chromosome 3. EAP is a highly
expressed small nuclear protein of 128 residues associated with
Epstein-Barr virus small RNA. The fusion clone contained the DNA-binding
5-prime part of AML1 that is fused to ETO in the t(8;21) and, in
addition, at least 1 other exon. The translocation replaced the last 9
codons of AML1 with the last 96 codons of EAP. The fusion does not
maintain the correct reading frame of EAP and may not lead to a
functional chimeric protein. EAP has been identified as the ribosomal
protein L22.
Nucifora and Rowley (1995) reviewed the involvement of the AML1 gene in
the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia.
Three loci closely situated to each other on 3q26 are involved in
fusions with AML1 in the 3;21 translocations: EVI1 (165215), EAP, and
MDS1 (600049). They pointed out that the order of the genes on 3q26 is
TEL--EAP--MDS1--EVI1 and provided a diagram (their Figure 5) of the 3q26
region containing these genes and of the various chimeric junctions they
had isolated from t(3;21) patients.
*FIELD* RF
1. Nucifora, G.; Begy, C. R.; Erickson, R.; Drabkin, H. A.; Rowley,
J. D.: The 3;21 translocation in myelodysplasia results in a fusion
transcript between the AML1 gene and the gene for EAP, a highly conserved
protein associated with the Epstein-Barr virus small RNA EBER 1. Proc.
Nat. Acad. Sci. 90: 7784-7788, 1993.
2. Nucifora, G.; Rowley, J. D.: AML1 and the 8;21 and 3;21 translocations
in acute and chronic myeloid leukemia. Blood 86: 1-14, 1995.
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
dkim: 12/10/1998
mark: 3/15/1996
carol: 9/15/1993
*RECORD*
*FIELD* NO
180474
*FIELD* TI
*180474 RIBOSOMAL PROTEIN L22; RPL22
;;EPSTEIN-BARR ASSOCIATED PROTEIN; EAP
*FIELD* TX
read moreA reciprocal translocation between the long arms of chromosomes 3 and
21, at bands 3q26 and 21q22, occurs as an acquired clonal chromosomal
abnormality in malignant cells from patients with therapy-related
myelodysplastic syndrome or acute myeloid leukemia, as well as in some
patients with chronic myeloid leukemia in blast crisis. Nucifora et al.
(1993) showed that the gene on chromosome 21 is AML1 (151385), which is
fused to the ETO gene (133435) in 8;21 translocations. Nucifora et al.
(1993) isolated a fusion cDNA clone from a t(3;21) library derived from
a patient with therapy-related myelodysplastic syndrome; this clone
contained sequences from AML1 and from EAP, which they localized to 3q26
from the location of the breakpoint on chromosome 3. EAP is a highly
expressed small nuclear protein of 128 residues associated with
Epstein-Barr virus small RNA. The fusion clone contained the DNA-binding
5-prime part of AML1 that is fused to ETO in the t(8;21) and, in
addition, at least 1 other exon. The translocation replaced the last 9
codons of AML1 with the last 96 codons of EAP. The fusion does not
maintain the correct reading frame of EAP and may not lead to a
functional chimeric protein. EAP has been identified as the ribosomal
protein L22.
Nucifora and Rowley (1995) reviewed the involvement of the AML1 gene in
the 8;21 and 3;21 translocations in acute and chronic myeloid leukemia.
Three loci closely situated to each other on 3q26 are involved in
fusions with AML1 in the 3;21 translocations: EVI1 (165215), EAP, and
MDS1 (600049). They pointed out that the order of the genes on 3q26 is
TEL--EAP--MDS1--EVI1 and provided a diagram (their Figure 5) of the 3q26
region containing these genes and of the various chimeric junctions they
had isolated from t(3;21) patients.
*FIELD* RF
1. Nucifora, G.; Begy, C. R.; Erickson, R.; Drabkin, H. A.; Rowley,
J. D.: The 3;21 translocation in myelodysplasia results in a fusion
transcript between the AML1 gene and the gene for EAP, a highly conserved
protein associated with the Epstein-Barr virus small RNA EBER 1. Proc.
Nat. Acad. Sci. 90: 7784-7788, 1993.
2. Nucifora, G.; Rowley, J. D.: AML1 and the 8;21 and 3;21 translocations
in acute and chronic myeloid leukemia. Blood 86: 1-14, 1995.
*FIELD* CD
Victor A. McKusick: 9/15/1993
*FIELD* ED
dkim: 12/10/1998
mark: 3/15/1996
carol: 9/15/1993