Isolation and characterization of genomic and cDNA clones of human erythropoietin.

true 1986-07-21 2008-07-22 98 EPO_HUMAN Erythropoietin Epoetin Isolation and characterization of genomic and cDNA clones of human erythropoietin. Jacobs K. Shoemaker C. Rudersdorf R. Neill S.D. Kaufman R.J. Mufson A. Seehra J. Jones S.S. Hewick R. Fritsch E.F. Kawakita M. Shimizu T. Miyake T. doi:10.1038/313806a0 1985 Nature 313 806-810 NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] Cloning and expression of the human erythropoietin gene. Lin F.-K. Suggs S. Lin C.-H. Browne J.K. Smalling R. Egrie J.C. Chen K.K. Fox G.M. Martin F. Stabinsky Z. Badrawi S.M. Lai P.-H. Goldwasser E. 1985 Proc. Natl. Acad. Sci. U.S.A. 82 7580-7584 NUCLEOTIDE SEQUENCE [GENOMIC DNA] Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes. Gloeckner G. Scherer S. Schattevoy R. Boright A.P. Weber J. Tsui L.-C. Rosenthal A. 1998 Genome Res. 8 1060-1073 NUCLEOTIDE SEQUENCE [GENOMIC DNA] Erythropoietin gene sequence in the Quechua, a high altitude native population. Rupert J.L. Hochachka P.W. 1999-11 EMBL/GenBank/DDBJ NUCLEOTIDE SEQUENCE [GENOMIC DNA] The DNA sequence of human chromosome 7. Hillier L.W. Fulton R.S. Fulton L.A. Graves T.A. Pepin K.H. Wagner-McPherson C. Layman D. Maas J. Jaeger S. Walker R. Wylie K. Sekhon M. Becker M.C. O'Laughlin M.D. Schaller M.E. Fewell G.A. Delehaunty K.D. Miner T.L. Nash W.E. Cordes M. Du H. Sun H. Edwards J. Bradshaw-Cordum H. Ali J. Andrews S. Isak A. Vanbrunt A. Nguyen C. Du F. Lamar B. Courtney L. Kalicki J. Ozersky P. Bielicki L. Scott K. Holmes A. Harkins R. Harris A. Strong C.M. Hou S. Tomlinson C. Dauphin-Kohlberg S. Kozlowicz-Reilly A. Leonard S. Rohlfing T. Rock S.M. Tin-Wollam A.-M. Abbott A. Minx P. Maupin R. Strowmatt C. Latreille P. Miller N. Johnson D. Murray J. Woessner J.P. Wendl M.C. Yang S.-P. Schultz B.R. Wallis J.W. Spieth J. Bieri T.A. Nelson J.O. Berkowicz N. Wohldmann P.E. Cook L.L. Hickenbotham M.T. Eldred J. Williams D. Bedell J.A. Mardis E.R. Clifton S.W. Chissoe S.L. Marra M.A. Raymond C. Haugen E. Gillett W. Zhou Y. James R. Phelps K. Iadanoto S. Bubb K. Simms E. Levy R. Clendenning J. Kaul R. Kent W.J. Furey T.S. Baertsch R.A. Brent M.R. Keibler E. Flicek P. Bork P. Suyama M. Bailey J.A. Portnoy M.E. Torrents D. Chinwalla A.T. Gish W.R. Eddy S.R. McPherson J.D. Olson M.V. Eichler E.E. Green E.D. Waterston R.H. Wilson R.K. doi:10.1038/nature01782 2003 Nature 424 157-164 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). The MGC Project Team doi:10.1101/gr.2596504 2004 Genome Res. 14 2121-2127 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] Brain Gene expression of mutant erythropoietin in hepatocellular carcinoma. Funakoshi A. Muta H. Baba T. Shimizu S. doi:10.1006/bbrc.1993.2104 1993 Biochem. Biophys. Res. Commun. 195 717-722 NUCLEOTIDE SEQUENCE [MRNA] OF 58-193 VARIANTS HEPATOCELLULAR CARCINOMA 131-ASN-PHE-132 AND GLN-149 Structural characterization of human erythropoietin. Lai P.H. Everett R. Wang F.F. Arakawa T. Goldwasser E. 1986 J. Biol. Chem. 261 3116-3121 PROTEIN SEQUENCE OF 28-193 DISULFIDE BONDS Urine Isolation of human erythropoietin with monoclonal antibodies. Yanagawa S. Hirade K. Ohnota H. Sasaki R. Chiba H. Ueda M. Goto M. 1984 J. Biol. Chem. 259 2707-2710 PRELIMINARY PROTEIN SEQUENCE OF 28-57 Comparative study of the asparagine-linked sugar chains of human erythropoietins purified from urine and the culture medium of recombinant Chinese hamster ovary cells. Takeuchi M. Takasaki S. Miyazaki H. Kato T. Hoshi S. Kochibe N. Kobata A. 1988 J. Biol. Chem. 263 3657-3663 STRUCTURE OF CARBOHYDRATES Site-specific glycosylation of human recombinant erythropoietin: analysis of glycopeptides or peptides at each glycosylation site by fast atom bombardment mass spectrometry. Sasaki H. Ochi N. Dell A. Fukuda M. doi:10.1021/bi00423a017 1988 Biochemistry 27 8618-8626 STRUCTURE OF CARBOHYDRATES Structures and functional roles of the sugar chains of human erythropoietins. Takeuchi M. Kobata A. doi:10.1093/glycob/1.4.337 1991 Glycobiology 1 337-346 STRUCTURE OF CARBOHYDRATES Sugar profiling proves that human serum erythropoietin differs from recombinant human erythropoietin. Skibeli V. Nissen-Lie G. Torjesen P. doi:10.1182/blood.V98.13.3626 2001 Blood 98 3626-3634 STRUCTURE OF CARBOHYDRATES Efficiency of signalling through cytokine receptors depends critically on receptor orientation. Syed R.S. Reid S.W. Li C. Cheetham J.C. Aoki K.H. Liu B. Zhan H. Osslund T.D. Chirino A.J. Zhang J. Finer-Moore J. Elliott S. Sitney K. Katz B.A. Matthews D.J. Wendoloski J.J. Egrie J. Stroud R.M. doi:10.1038/26773 1998 Nature 395 511-516 X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) NMR structure of human erythropoietin and a comparison with its receptor bound conformation. Cheetham J.C. Smith D.M. Aoki K.H. Stevenson J.L. Hoeffel T.J. Syed R.S. Egrie J. Harvey T.S. doi:10.1038/2302 1998 Nat. Struct. Biol. 5 861-866 STRUCTURE BY NMR OF 28-193 EPO Erythropoietin is the principal hormone involved in the regulation of erythrocyte differentiation and the maintenance of a physiological level of circulating erythrocyte mass. Produced by kidney or liver of adult mammals and by liver of fetal or neonatal mammals. Used for the treatment of anemia. Available under the names Epogen (Amgen), Epogin (Chugai), Epomax (Elanex), Eprex (Janssen-Cilag), NeoRecormon or Recormon (Roche), Dynepo (Shire Pharmaceuticals) and Procrit (Ortho Biotech). Variations in the glycosylation pattern of EPO distinguishes these products. Epogen, Epogin, Eprex and Procrit are generically known as epoetin alfa, NeoRecormon and Recormon as epoetin beta, Dynepo as epoetin delta and Epomax as epoetin omega. Epoetin zeta is the name used for some 'biosimilars' forms of epoetin alfa and is available under the names Silapo (Stada) and Retacrit (Hospira). Darbepoetin alfa is a form created by 5 substitutions (Asn-57, Thr-59, Val-114, Asn-115 and Thr-117) that create 2 new N-glycosylation sites. It has a longer circulating half-life in vivo. It is available under the name Aranesp (Amgen). EPO is being much misused as a performance-enhancing drug in endurance athletes. Belongs to the EPO/TPO family. 1 27 Erythropoietin 28 193 Removed in mature form (Partial) 190 193 Removed in mature form (Partial) 193 193 N-linked (GlcNAc...) 51 51 N-linked (GlcNAc...) 65 65 N-linked (GlcNAc...) 110 110 O-linked (GalNAc...) 153 153 34 34 188 188 56 56 60 60 In an hepatocellular carcinoma. NF 131 132 In an hepatocellular carcinoma. Q 149 149 Q 40 40 AA sequence QQ 85 85 R 140 140 32 34 36 52 53 55 61 68 75 78 83 109 118 138 141 147 160 164 165 177 179 188 false 1 DOK2 R&D Systems' cytokine source book: Erythropoietin Wikipedia; Erythropoietin entry EMBL EMBL EMBL EMBL EMBL EMBL EMBL EMBL EMBL EMBL EMBL EMBL PIR A01855 RefSeq UniGene PDB A=28-193 PDB 2.80 C=28-193 PDB 1.90 A=28-193 PDBsum PDBsum PDBsum DIP IntAct GlycoSuiteDB Ensembl Homo sapiens GeneID KEGG H-InvDB HGNC EPO HPA MIM gene PharmGKB HOGENOM HOVERGEN DrugBank Darbepoetin alfa DrugBank Epoetin alfa LinkHub ArrayExpress CleanEx GermOnline Homo sapiens InterPro 4_helix_cytokine_core InterPro EPO_TPO InterPro Erythroptn Gene3D 4_helix_cytokine_core 1 PANTHER Erythroptn 1 Pfam EPO_TPO 1 PIRSF EPO 1 PRINTS ERYTHROPTN PROSITE EPO_TPO 1 ProtInc IntAct ProtInc UniProtKB UniProtKB UniProtKB UniProtKB UniProtKB ProtInc 1986-07-21 1 true 21307 MGVHECPAWL WLLLSLLSLP LGLPVLGAPP RLICDSRVLE RYLLEAKEAE NITTGCAEHC SLNENITVPD TKVNFYAWKR MEVGQQAVEV WQGLALLSEA VLRGQALLVN SSQPWEPLQL HVDKAVSGLR SLTTLLRALG AQKEAISPPD AASAAPLRTI TADTFRKLFR VYSNFLRGKL KLYTGEACRT GDR