ID UBIQ_HUMAN Reviewed; 76 AA. AC P62988; P02248; P02249; P02250; Q29120; Q6LBL4; Q6LDU5; Q91887; AC Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8; Q9UPK7; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 13-AUG-1987, sequence version 1. DT 23-OCT-2007, entry version 56. DE Ubiquitin. GN Name=RPS27A; Synonyms=UBA80, UBCEP1; GN and GN Name=UBA52; Synonyms=UBCEP2; GN and GN Name=UBB; GN and GN Name=UBC; 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. RX MEDLINE=85230546; PubMed=2988935; RA Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., RA Vuust J.; RT "The human ubiquitin multigene family: some genes contain multiple RT directly repeated ubiquitin coding sequences."; RL EMBO J. 4:755-759(1985). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=87326412; PubMed=2820408; DOI=10.1016/0006-291X(87)90970-3; RA Einspanier R., Sharma H.S., Scheit K.H.; RT "Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in RT human ovarian granulosa cells."; RL Biochem. Biophys. Res. Commun. 147:581-587(1987). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB). RC TISSUE=Lymphocyte; RX MEDLINE=87146371; PubMed=3029682; DOI=10.1093/nar/15.2.443; RA Baker R.T., Board P.G.; RT "The human ubiquitin gene family: structure of a gene and pseudogenes RT from the Ub B subfamily."; RL Nucleic Acids Res. 15:443-463(1987). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (UBA52). RX MEDLINE=91212181; PubMed=1850507; DOI=10.1093/nar/19.5.1035; RA Baker R.T., Board P.G.; RT "The human ubiquitin-52 amino acid fusion protein gene shares several RT structural features with mammalian ribosomal protein genes."; RL Nucleic Acids Res. 19:1035-1040(1991). RN [5] RP NUCLEOTIDE SEQUENCE (UBA52). RA Wang H., Zhang Y., Okamoto T.; RT "Human ubiquitin A-52 residue ribosomal protein fusion product 1 RT (UBA52) in salivary epithelial cells."; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (RPS27A). RX MEDLINE=92037818; PubMed=1657614; RA Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A., RA Capron A., Auriault C.; RT "Effect of ubiquitin on platelet functions: possible identity with RT platelet activity suppressive lymphokine (PASL)."; RL Eur. J. Immunol. 21:2735-2741(1991). RN [7] RP NUCLEOTIDE SEQUENCE (RPS27A). RX MEDLINE=92126503; PubMed=1370760; RA Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.; RT "Differential expression of translation-associated genes in benign and RT malignant human breast tumours."; RL Br. J. Cancer 65:65-71(1992). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBC). RX MEDLINE=97074669; PubMed=8917096; DOI=10.1016/0378-1119(96)00145-X; RA Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E., RA Yamauchi M., Tsuji H.; RT "Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 RT cells."; RL Gene 175:179-185(1996). RN [9] RP NUCLEOTIDE SEQUENCE [MRNA] (UBC). RX PubMed=9644242; RA Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.; RT "Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay RT involving its in vitro translation product."; RL J. Biochem. 124:35-39(1998). RN [10] RP NUCLEOTIDE SEQUENCE (UBC). RX MEDLINE=98186276; PubMed=9504932; RA Nenoi M., Mita K., Ichimura S., Kawano A.; RT "Higher frequency of concerted evolutionary events in rodents than in RT man at the polyubiquitin gene VNTR locus."; RL Genetics 148:867-876(1998). RN [11] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (UBB AND UBC). RX PubMed=14745543; DOI=10.1007/s00239-003-2532-4; RA Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.; RT "Lineage-specific homogenization of the polyubiquitin gene among human RT and great apes."; RL J. Mol. Evol. 57:737-744(2003). RN [12] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (UBA52). 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 [13] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (RPS27A; UBB AND UBC). RC TISSUE=Brain, Liver, Lung, and Placenta; 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 [14] RP NUCLEOTIDE SEQUENCE [MRNA] OF 5-76 (RPS27A). RX MEDLINE=85207809; PubMed=2581967; RA Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J., RA Martin F., van Wyk J.J.; RT "Nucleotide sequence analysis of a cDNA encoding human ubiquitin RT reveals that ubiquitin is synthesized as a precursor."; RL J. Biol. Chem. 260:7609-7613(1985). RN [15] RP PROTEIN SEQUENCE OF 1-74. RX MEDLINE=75156547; PubMed=124018; DOI=10.1038/255423a0; RA Schlesinger D.H., Goldstein G.; RT "Hybrid troponin reconstituted from vertebrate and arthropod RT subunits."; RL Nature 255:423-424(1975). RN [16] RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 RP AND LYS-48, AND MASS SPECTROMETRY. RX PubMed=16443603; DOI=10.1074/jbc.M512786200; RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.; RT "Alzheimer disease-specific conformation of hyperphosphorylated paired RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and RT Lys-6 ubiquitin conjugation."; RL J. Biol. Chem. 281:10825-10838(2006). RN [17] RP UBIQUITINATION AT LYS-27. RX PubMed=15466860; DOI=10.1074/jbc.M402916200; RA Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.; RT "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B RT contributes to neuritogenesis."; RL J. Biol. Chem. 279:53533-53543(2004). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND MASS RP SPECTROMETRY. RC TISSUE=Epithelium; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling networks."; RL Cell 127:635-648(2006). RN [19] RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND RP MASS SPECTROMETRY. RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018; RA Huang F., Kirkpatrick D., Jiang X., Gygi S., Sorkin A.; RT "Differential regulation of EGF receptor internalization and RT degradation by multiubiquitination within the kinase domain."; RL Mol. Cell 21:737-748(2006). RN [20] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS RP SPECTROMETRY. RX PubMed=17323924; DOI=10.1021/bi061994u; RA Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.; RT "Mass spectrometric characterization of the affinity-purified human RT 26S proteasome complex."; RL Biochemistry 46:3553-3565(2007). RN [21] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48, AND MASS RP SPECTROMETRY. RC TISSUE=Lung adenocarcinoma; RX PubMed=17203973; DOI=10.1021/pr060438j; RA Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., RA Haines D.S., Figeys D.; RT "The proteomic reactor facilitates the analysis of affinity-purified RT proteins by mass spectrometry: application for identifying RT ubiquitinated proteins in human cells."; RL J. Proteome Res. 6:298-305(2007). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=87311725; PubMed=3041007; DOI=10.1016/0022-2836(87)90679-6; RA Vijay-Kumar S., Bugg C.E., Cook W.J.; RT "Structure of ubiquitin refined at 1.8-A resolution."; RL J. Mol. Biol. 194:531-544(1987). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=94220022; PubMed=8166633; RA Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.; RT "Synthetic, structural and biological studies of the ubiquitin system: RT the total chemical synthesis of ubiquitin."; RL Biochem. J. 299:151-158(1994). RN [24] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS). RX MEDLINE=94149762; PubMed=8107144; DOI=10.1006/jmbi.1994.1169; RA Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.; RT "Structure of tetraubiquitin shows how multiubiquitin chains can be RT formed."; RL J. Mol. Biol. 236:601-609(1994). RN [25] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=11173499; DOI=10.1107/S090744490001800X; RA Phillips C.L., Thrower J., Pickart C.M., Hill C.P.; RT "Structure of a new crystal form of tetraubiquitin."; RL Acta Crystallogr. D 57:341-344(2001). RN [26] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7. RX PubMed=12507430; DOI=10.1016/S0092-8674(02)01199-6; RA Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., RA Shi Y.; RT "Crystal structure of a UBP-family deubiquitinating enzyme in RT isolation and in complex with ubiquitin aldehyde."; RL Cell 111:1041-1054(2002). CC -!- FUNCTION: Protein modifier which can be covalently attached to CC target lysines either as a monomer or as a lysine-linked polymer. CC Attachment to proteins as a Lys-48-linked polymer usually leads to CC their degradation by proteasome. Attachment to proteins as a CC monomer or as an alternatively linked polymer does not lead to CC proteasomal degradation and may be required for numerous CC fonctions, including maintenance of chromatin structure, CC regulation of gene expression, stress response, ribosome CC biogenesis and DNA repair. CC -!- INTERACTION: CC Q53FG0:-; NbExp=2; IntAct=EBI-413034, EBI-913954; CC Q99741:CDC6; NbExp=1; IntAct=EBI-413034, EBI-374862; CC P28562:DUSP1; NbExp=1; IntAct=EBI-413034, EBI-975493; CC Q9UJY5:GGA1; NbExp=1; IntAct=EBI-413034, EBI-447141; CC Q60592:Mast2 (xeno); NbExp=2; IntAct=EBI-413034, EBI-493888; CC P33993:MCM7; NbExp=1; IntAct=EBI-413034, EBI-355924; CC Q5TEM5:MYO6; NbExp=1; IntAct=EBI-413034, EBI-914259; CC Q13415:ORC1L; NbExp=1; IntAct=EBI-413034, EBI-374847; CC Q8IYW5:RNF168; NbExp=1; IntAct=EBI-413034, EBI-914207; CC O14048:ubx2 (xeno); NbExp=1; IntAct=EBI-413034, EBI-1005194; CC Q9UT81:ubx3 (xeno); NbExp=1; IntAct=EBI-413034, EBI-1005297; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. CC -!- PTM: Several types of polymeric chains can be formed, depending on CC the lysine used for the assembly. CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin CC precursor with exact head to tail repeats, the number of repeats CC differ between species and strains. In some species there is a CC final amino-acid after the last repeat, here in human a Val. Some CC ubiquitin genes contain a single copy of ubiquitin fused to a CC ribosomal protein (either L40 or S27a). CC -!- SIMILARITY: Belongs to the ubiquitin family. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M26880; AAA36789.1; ALT_TERM; mRNA. DR EMBL; M17597; AAA36787.1; ALT_TERM; mRNA. DR EMBL; X04803; CAA28495.1; ALT_TERM; Genomic_DNA. DR EMBL; X56997; CAA40312.1; ALT_TERM; Genomic_DNA. DR EMBL; X56998; CAA40313.1; ALT_TERM; mRNA. DR EMBL; X56999; CAA40314.1; ALT_TERM; mRNA. DR EMBL; AF348700; AAK31162.1; ALT_SEQ; mRNA. DR EMBL; X63237; CAA44911.1; ALT_TERM; mRNA. DR EMBL; S79522; AAB21188.1; ALT_TERM; mRNA. DR EMBL; D63791; BAA09860.1; ALT_TERM; Genomic_DNA. DR EMBL; AB009010; BAA23632.1; ALT_TERM; mRNA. DR EMBL; AB003730; BAA23486.1; ALT_TERM; Genomic_DNA. DR EMBL; AB089613; BAC56951.1; ALT_TERM; Genomic_DNA. DR EMBL; AB089617; BAC56955.1; ALT_TERM; Genomic_DNA. DR EMBL; AC005253; AAC25582.1; ALT_TERM; Genomic_DNA. DR EMBL; BC000379; AAH00379.1; ALT_TERM; mRNA. DR EMBL; BC009301; AAH09301.1; ALT_TERM; mRNA. DR EMBL; BC015127; AAH15127.1; ALT_TERM; mRNA. DR EMBL; BC026301; AAH26301.1; ALT_TERM; mRNA. DR EMBL; BC031027; AAH31027.1; ALT_TERM; mRNA. DR EMBL; BC039193; AAH39193.1; ALT_TERM; mRNA. DR EMBL; BC046123; AAH46123.1; ALT_TERM; mRNA. DR EMBL; BC066293; AAH66293.1; ALT_TERM; mRNA. DR EMBL; M10939; AAA36788.1; ALT_TERM; mRNA. DR PIR; A02574; UQHU. DR PIR; A22005; UQHUC. DR PIR; A26437; UQHUB. DR PIR; A29526; A29526. DR PIR; S34428; UQHUR. DR RefSeq; NP_061828.1; -. DR UniGene; Hs.311640; -. DR UniGene; Hs.356190; -. DR UniGene; Hs.520348; -. DR UniGene; Hs.5308; -. DR UniGene; Hs.546292; -. DR UniGene; Hs.673132; -. DR PDB; 1C3T; NMR; A=1-76. DR PDB; 1D3Z; NMR; A=1-76. DR PDB; 1F9J; X-ray; A/B=1-76. DR PDB; 1FXT; NMR; B=1-76. DR PDB; 1G6J; NMR; A=1-76. DR PDB; 1GJZ; NMR; A/B=1-51. DR PDB; 1NBF; X-ray; C/D=1-75. DR PDB; 1OGW; X-ray; A=-. DR PDB; 1Q5W; NMR; B=1-76. DR PDB; 1S1Q; X-ray; B/D=1-76. DR PDB; 1SIF; X-ray; A=2-76. DR PDB; 1TBE; X-ray; A/B=1-76. DR PDB; 1UBI; X-ray; @=1-76. DR PDB; 1UBQ; X-ray; @=1-76. DR PDB; 1XD3; X-ray; B/D=1-75. DR PDB; 1YX5; NMR; B=1-76. DR PDB; 1YX6; NMR; B=1-76. DR PDB; 1ZGU; NMR; B=1-76. DR PDB; 2AYO; X-ray; B=1-75. DR PDB; 2FUH; NMR; B=-. DR PDB; 2G45; X-ray; B/E=1-76. DR PDB; 2GBK; X-ray; C/D=10-76. DR PDB; 2GBM; X-ray; A=1-76. DR PDB; 2GBN; X-ray; A=1-76. DR PDB; 2HTH; X-ray; A=1-76. DR PDB; 2IBI; X-ray; B=1-75. DR IntAct; P62988; -. DR SWISS-2DPAGE; P62988; HUMAN. DR Aarhus/Ghent-2DPAGE; 13; IEF. DR DOSAC-COBS-2DPAGE; P62988; HUMAN. DR HSC-2DPAGE; P62988; HUMAN. DR Siena-2DPAGE; P62988; -. DR Ensembl; ENSG00000143947; Homo sapiens. DR Ensembl; ENSG00000150991; Homo sapiens. DR Ensembl; ENSG00000170315; Homo sapiens. DR Ensembl; ENSG00000196084; Homo sapiens. DR HGNC; HGNC:10417; RPS27A. DR HGNC; HGNC:12458; UBA52. DR HGNC; HGNC:12463; UBB. DR HGNC; HGNC:12468; UBC. DR HPA; CAB000362; -. DR HPA; CAB005419; -. DR MIM; 191321; gene. DR MIM; 191339; gene. DR MIM; 191340; gene. DR MIM; 191343; gene. DR PharmGKB; PA34821; -. DR Reactome; REACT_11045; Signaling by Wnt. DR Reactome; REACT_152; Cell Cycle, Mitotic. DR Reactome; REACT_1538; Cell Cycle Checkpoints. DR Reactome; REACT_383; DNA Replication. DR Reactome; REACT_6185; HIV Infection. DR Reactome; REACT_6850; Cdc20:Phospho-APC/C mediated degradation of Cyclin A. DR Reactome; REACT_8017; APC-Cdc20 mediated degradation of Nek2A. DR Reactome; REACT_9035; APC/C:Cdh1-mediated degradation of Skp2. DR LinkHub; P62988; -. DR ArrayExpress; P62988; -. DR GermOnline; ENSG00000143947; Homo sapiens. DR GermOnline; ENSG00000150991; Homo sapiens. DR GermOnline; ENSG00000170315; Homo sapiens. DR GermOnline; ENSG00000196084; Homo sapiens. DR GO; GO:0005634; C:nucleus; IC:UniProtKB. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0030528; F:transcription regulator activity; IDA:UniProtKB. DR GO; GO:0007411; P:axon guidance; TAS:UniProtKB. DR GO; GO:0007049; P:cell cycle; TAS:UniProtKB. DR GO; GO:0030433; P:ER-associated protein catabolic process; TAS:UniProtKB. DR GO; GO:0042062; P:long-term strengthening of neuromuscular ju...; TAS:UniProtKB. DR GO; GO:0045941; P:positive regulation of transcription; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IDA:UniProtKB. DR GO; GO:0048167; P:regulation of synaptic plasticity; TAS:UniProtKB. DR InterPro; IPR000626; Ubiquitin. DR Pfam; PF00240; ubiquitin; 1. DR PRINTS; PR00348; UBIQUITIN. DR SMART; SM00213; UBQ; 1. DR PROSITE; PS00299; UBIQUITIN_1; 1. DR PROSITE; PS50053; UBIQUITIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; Nucleus; KW Phosphorylation; Ubl conjugation. FT CHAIN 1 76 Ubiquitin. FT /FTId=PRO_0000114800. FT BINDING 54 54 Activating enzyme. FT BINDING 72 72 Activating enzyme. FT SITE 68 68 Essential for function. FT MOD_RES 57 57 Phosphoserine (By similarity). FT MOD_RES 65 65 Phosphoserine. FT CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin) FT (Probable). FT CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in ubiquitin). FT CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys) FT (interchain with K-? in acceptor FT proteins). FT STRAND 2 7 FT STRAND 12 16 FT HELIX 23 34 FT HELIX 38 40 FT STRAND 41 45 FT TURN 56 60 FT STRAND 66 71 SQ SEQUENCE 76 AA; 8565 MW; C42A35397FFD9B52 CRC64; MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGG //