ID IF2P_HUMAN Reviewed; 1220 AA. AC O60841; O95805; Q53RV7; Q53SI8; Q9UF81; Q9UMN7; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 24-NOV-2009, sequence version 4. DT 27-MAR-2024, entry version 215. DE RecName: Full=Eukaryotic translation initiation factor 5B; DE Short=eIF-5B; DE EC=3.6.5.3; DE AltName: Full=Translation initiation factor IF-2; GN Name=EIF5B; Synonyms=IF2, KIAA0741; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT THR-522. RC TISSUE=Cervix carcinoma; RX PubMed=10432305; DOI=10.1042/bj3420097; RA Wilson S.A., Sieiro-Vazquez C., Edwards N.J., Iourin O., Byles E.D., RA Kotsopoulou E., Adamson C.S., Kingsman S.M., Kingsman A.J., RA Martin-Rendon E.; RT "Cloning and characterization of hIF2, a human homologue of bacterial RT translation initiation factor 2 and its interaction with HIV-1 matrix."; RL Biochem. J. 342:97-103(1999). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF VAL-640; HIS-706 AND ASP-759, RP CHARACTERIZATION, AND VARIANT THR-522. RC TISSUE=Testis; RX PubMed=10200264; DOI=10.1073/pnas.96.8.4342; RA Lee J.H., Choi S.K., Roll-Mecak A., Burley S.K., Dever T.E.; RT "Universal conservation in translation initiation revealed by human and RT archaeal homologs of bacterial translation initiation factor IF2."; RL Proc. Natl. Acad. Sci. U.S.A. 96:4342-4347(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [5] RP PROTEIN SEQUENCE OF 9-33; 77-94; 106-122; 180-197; 206-224; 285-298; RP 425-436; 629-644; 653-683; 695-713; 749-757; 766-777; 882-902; 1000-1015; RP 1044-1055; 1096-1120 AND 1175-1185, PHOSPHORYLATION AT SER-190, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RA Bienvenut W.V., Waridel P., Quadroni M.; RL Submitted (MAR-2009) to UniProtKB. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 89-1220. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 833-1220. RX PubMed=11124703; RX DOI=10.1002/1097-0061(200101)18:1<69::aid-yea647>3.0.co;2-h; RA Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., RA Zimbello R., Lanfranchi G., Valle G.; RT "Characterization of 16 novel human genes showing high similarity to yeast RT sequences."; RL Yeast 18:69-80(2001). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10659855; DOI=10.1038/35002118; RA Pestova T.V., Lomakin I.B., Lee J.H., Choi S.K., Dever T.E., Hellen C.U.; RT "The joining of ribosomal subunits in eukaryotes requires eIF5B."; RL Nature 403:332-335(2000). RN [9] RP INTERACTION WITH EIF1AX. RX PubMed=12569173; DOI=10.1073/pnas.0437845100; RA Marintchev A., Kolupaeva V.G., Pestova T.V., Wagner G.; RT "Mapping the binding interface between human eukaryotic initiation factors RT 1A and 5B: a new interaction between old partners."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1535-1540(2003). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; SER-164 AND RP SER-214, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Prostate cancer; RX PubMed=17487921; DOI=10.1002/elps.200600782; RA Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.; RT "Toward a global characterization of the phosphoproteome in prostate cancer RT cells: identification of phosphoproteins in the LNCaP cell line."; RL Electrophoresis 28:2027-2034(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells RT and high confident phosphopeptide identification by cross-validation of RT MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=T-cell; RX PubMed=19367720; DOI=10.1021/pr800500r; RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.; RT "Phosphorylation analysis of primary human T lymphocytes using sequential RT IMAC and titanium oxide enrichment."; RL J. Proteome Res. 7:5167-5176(2008). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134; RP SER-135; SER-137; SER-164; SER-182; SER-183; SER-186; SER-190; THR-301; RP SER-547; SER-560; SER-588 AND SER-595, AND IDENTIFICATION BY MASS RP 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113 AND SER-164, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [17] RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=18572216; DOI=10.1016/j.virol.2008.05.019; RA de Breyne S., Bonderoff J.M., Chumakov K.M., Lloyd R.E., Hellen C.U.; RT "Cleavage of eukaryotic initiation factor eIF5B by enterovirus 3C RT proteases."; RL Virology 378:118-122(2008). RN [18] 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., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; TYR-134; SER-135; RP SER-137; SER-164; SER-182; SER-183; SER-186 AND SER-214, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113; SER-135; SER-137; RP SER-164; SER-182; SER-186; SER-190; SER-214; THR-301; SER-588; SER-589; RP SER-591 AND SER-595, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; TYR-134; RP SER-135; SER-137; SER-164; SER-171; SER-214 AND THR-498, AND IDENTIFICATION RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [22] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-107; SER-113; RP SER-135; SER-137; SER-164; SER-186; SER-214; SER-222; SER-438 AND SER-1168, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [23] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-107; SER-113; SER-135; RP SER-137; SER-164; SER-182; SER-190 AND SER-214, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [24] RP INTERACTION WITH EIF5 AND EIF1AX. RX PubMed=30211544; DOI=10.1021/acs.biochem.8b00839; RA Lin K.Y., Nag N., Pestova T.V., Marintchev A.; RT "Human eIF5 and eIF1A compete for binding to eIF5B."; RL Biochemistry 57:5910-5920(2018). RN [25] {ECO:0000312|PDB:7TQL} RP STRUCTURE BY ELECTRON MICROSCOPY (3.40 ANGSTROMS) OF 602-1219 IN COMPLEX RP WITH A GTP ANALOG, FUNCTION, CATALYTIC ACTIVITY, PROBABLE ACTIVE SITE, RP MUTAGENESIS OF HIS-706; ARG-1105; ARG-1174; 1188-ARG-GLN-1189; ARG-1199 AND RP 1218-GLU-ILE-1219, AND INTERACTION WITH EIF1AX. RX PubMed=35732735; DOI=10.1038/s41586-022-04858-z; RA Lapointe C.P., Grosely R., Sokabe M., Alvarado C., Wang J., Montabana E., RA Villa N., Shin B.S., Dever T.E., Fraser C.S., Fernandez I.S., Puglisi J.D.; RT "eIF5B and eIF1A reorient initiator tRNA to allow ribosomal subunit RT joining."; RL Nature 607:185-190(2022). RN [26] RP VARIANT [LARGE SCALE ANALYSIS] THR-522, AND IDENTIFICATION BY MASS RP 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., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). CC -!- FUNCTION: Plays a role in translation initiation (PubMed:10659855, CC PubMed:35732735). Ribosome-dependent GTPase that promotes the joining CC of the 60S ribosomal subunit to the pre-initiation complex to form the CC 80S initiation complex with the initiator methionine-tRNA in the P-site CC base paired to the start codon (PubMed:10659855, PubMed:35732735). CC Together with eIF1A (EIF1AX), actively orients the initiator CC methionine-tRNA in a conformation that allows 60S ribosomal subunit CC joining to form the 80S initiation complex (PubMed:12569173, CC PubMed:35732735). Is released after formation of the 80S initiation CC complex (PubMed:35732735). Its GTPase activity is not essential for CC ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A CC (EIF1AX) ejection quickly followed by EIF5B release to form elongation- CC competent ribosomes (PubMed:10659855, PubMed:35732735). In contrast to CC its procaryotic homolog, does not promote recruitment of Met-rRNA to CC the small ribosomal subunit (PubMed:10659855). CC {ECO:0000269|PubMed:10659855, ECO:0000269|PubMed:12569173, CC ECO:0000269|PubMed:35732735}. CC -!- CATALYTIC ACTIVITY: CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.3; CC Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; CC Evidence={ECO:0000269|PubMed:10659855, ECO:0000305|PubMed:35732735}; CC -!- COFACTOR: CC Name=a monovalent cation; Xref=ChEBI:CHEBI:60242; CC Evidence={ECO:0000250|UniProtKB:G0S8G9}; CC Note=Binds 1 monovalent cation per monomer in the active site. CC Structural cofactor that stabilizes the GTP-bound 'on' state. May also CC act as a transition state stabilizer of the hydrolysis reaction. CC {ECO:0000250|UniProtKB:G0S8G9}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=1 pmol/min/ug enzyme {ECO:0000269|PubMed:10659855}; CC Note=Obtained in the presence of 40S and 60S ribosomal subunits. 60S CC ribosomal subunit is necessary for enzyme activation, while 40S CC ribosomal subunit is not.; CC -!- SUBUNIT: Interacts through its C-terminal domain (CTD) with the CTD of CC eIF1A (EIF1AX) or with the CTD of EIF5 (mutually exclusive) through a CC common binding site (PubMed:30211544). Interacts with eIF1A (EIF1AX) CC from the location of the start codon by the 43S complex until the CC formation of the 80S complex (PubMed:12569173, PubMed:35732735). CC Interacts with ANXA5 in a calcium and phospholipid-dependent manner (By CC similarity). {ECO:0000250|UniProtKB:B2GUV7, CC ECO:0000269|PubMed:35732735}. CC -!- INTERACTION: CC O60841; O14602: EIF1AY; NbExp=2; IntAct=EBI-928530, EBI-286439; CC O60841; P14921: ETS1; NbExp=2; IntAct=EBI-928530, EBI-913209; CC O60841; P28799: GRN; NbExp=3; IntAct=EBI-928530, EBI-747754; CC O60841; O43933: PEX1; NbExp=3; IntAct=EBI-928530, EBI-988601; CC O60841; O76024: WFS1; NbExp=3; IntAct=EBI-928530, EBI-720609; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q05D44}. CC -!- PTM: (Microbial infection) Cleaved and inactivated by the protease 3C CC of poliovirus, Coxsackievirus B3 and Human rhinovirus 14, allowing the CC virus to shutoff the host cell translation. CC {ECO:0000269|PubMed:18572216}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA34461.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; 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; AJ006776; CAB44357.1; -; mRNA. DR EMBL; AF078035; AAD16006.1; -; mRNA. DR EMBL; AC018690; AAY24313.1; -; Genomic_DNA. DR EMBL; AC079447; AAX93258.1; -; Genomic_DNA. DR EMBL; AB018284; BAA34461.2; ALT_INIT; mRNA. DR EMBL; AL133563; CAB63717.1; -; mRNA. DR EMBL; AJ006412; CAA07018.1; -; mRNA. DR CCDS; CCDS42721.1; -. DR PIR; T43483; T43483. DR RefSeq; NP_056988.3; NM_015904.3. DR PDB; 7TQL; EM; 3.40 A; 1=602-1219. DR PDBsum; 7TQL; -. DR AlphaFoldDB; O60841; -. DR EMDB; EMD-26067; -. DR SMR; O60841; -. DR BioGRID; 115024; 177. DR IntAct; O60841; 52. DR MINT; O60841; -. DR STRING; 9606.ENSP00000289371; -. DR ChEMBL; CHEMBL4105852; -. DR GlyGen; O60841; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O60841; -. DR MetOSite; O60841; -. DR PhosphoSitePlus; O60841; -. DR SwissPalm; O60841; -. DR BioMuta; EIF5B; -. DR EPD; O60841; -. DR jPOST; O60841; -. DR MassIVE; O60841; -. DR MaxQB; O60841; -. DR PaxDb; 9606-ENSP00000289371; -. DR PeptideAtlas; O60841; -. DR ProteomicsDB; 49628; -. DR Pumba; O60841; -. DR Antibodypedia; 32818; 202 antibodies from 27 providers. DR DNASU; 9669; -. DR Ensembl; ENST00000289371.11; ENSP00000289371.5; ENSG00000158417.11. DR GeneID; 9669; -. DR KEGG; hsa:9669; -. DR MANE-Select; ENST00000289371.11; ENSP00000289371.5; NM_015904.4; NP_056988.3. DR UCSC; uc002tab.4; human. DR AGR; HGNC:30793; -. DR CTD; 9669; -. DR DisGeNET; 9669; -. DR GeneCards; EIF5B; -. DR HGNC; HGNC:30793; EIF5B. DR HPA; ENSG00000158417; Low tissue specificity. DR MIM; 606086; gene. DR neXtProt; NX_O60841; -. DR OpenTargets; ENSG00000158417; -. DR PharmGKB; PA134864457; -. DR VEuPathDB; HostDB:ENSG00000158417; -. DR eggNOG; KOG1144; Eukaryota. DR GeneTree; ENSGT00940000162583; -. DR HOGENOM; CLU_002656_0_1_1; -. DR InParanoid; O60841; -. DR OMA; EFAVMLC; -. DR OrthoDB; 169393at2759; -. DR PhylomeDB; O60841; -. DR TreeFam; TF101535; -. DR BRENDA; 3.6.5.3; 2681. DR PathwayCommons; O60841; -. DR Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit. DR SignaLink; O60841; -. DR SIGNOR; O60841; -. DR BioGRID-ORCS; 9669; 442 hits in 1150 CRISPR screens. DR ChiTaRS; EIF5B; human. DR GeneWiki; EIF5B; -. DR GenomeRNAi; 9669; -. DR Pharos; O60841; Tchem. DR PRO; PR:O60841; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; O60841; Protein. DR Bgee; ENSG00000158417; Expressed in tendon of biceps brachii and 209 other cell types or tissues. DR ExpressionAtlas; O60841; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0045202; C:synapse; IEA:Ensembl. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0003743; F:translation initiation factor activity; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IDA:UniProtKB. DR GO; GO:0006446; P:regulation of translational initiation; IDA:UniProtKB. DR GO; GO:0042255; P:ribosome assembly; IDA:UniProtKB. DR GO; GO:0006413; P:translational initiation; IBA:GO_Central. DR CDD; cd03703; aeIF5B_II; 1. DR CDD; cd16266; IF2_aeIF5B_IV; 1. DR CDD; cd01887; IF2_eIF5B; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.30.10; Translation factors; 2. DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1. DR InterPro; IPR029459; EFTU-type. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; T_Tr_GTP-bd_dom. DR InterPro; IPR015760; TIF_IF2. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR036925; TIF_IF2_dom3_sf. DR InterPro; IPR009000; Transl_B-barrel_sf. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR43381:SF4; EUKARYOTIC TRANSLATION INITIATION FACTOR 5B; 1. DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1. DR Pfam; PF00009; GTP_EFTU; 1. DR Pfam; PF14578; GTP_EFTU_D4; 1. DR Pfam; PF11987; IF-2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF50447; Translation proteins; 1. DR PROSITE; PS51722; G_TR_2; 1. DR Genevisible; O60841; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding; Hydrolase; KW Initiation factor; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Protein biosynthesis; Reference proteome. FT CHAIN 1..1220 FT /note="Eukaryotic translation initiation factor 5B" FT /id="PRO_0000137294" FT DOMAIN 629..846 FT /note="tr-type G" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 1..417 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 430..608 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 638..645 FT /note="G1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 663..667 FT /note="G2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 702..705 FT /note="G3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 756..759 FT /note="G4" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT REGION 824..826 FT /note="G5" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01059" FT COMPBIAS 1..21 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 32..56 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 78..149 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 156..199 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..284 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 300..339 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..417 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 436..459 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 488..512 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 513..529 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 530..569 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 570..608 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 706 FT /evidence="ECO:0000305|PubMed:35732735" FT BINDING 640..646 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:35732735, FT ECO:0007744|PDB:7TQL" FT BINDING 663..665 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:35732735, FT ECO:0007744|PDB:7TQL" FT BINDING 756..757 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:35732735, FT ECO:0007744|PDB:7TQL" FT BINDING 759..760 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:35732735, FT ECO:0007744|PDB:7TQL" FT BINDING 825..826 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000305|PubMed:35732735, FT ECO:0007744|PDB:7TQL" FT SITE 478..479 FT /note="(Microbial infection) Cleavage; by viral protease 3C FT of poliovirus, Coxsackievirus B3 and Human rhinovirus 14" FT /evidence="ECO:0000269|PubMed:18572216" FT MOD_RES 66 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 107 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 113 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 134 FT /note="Phosphotyrosine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692" FT MOD_RES 135 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 137 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 164 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18318008, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 171 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 182 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:24275569" FT MOD_RES 183 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT MOD_RES 186 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 190 FT /note="Phosphoserine" FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569" FT MOD_RES 214 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:17487921, ECO:0007744|PubMed:17924679, FT ECO:0007744|PubMed:19367720, ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 222 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 301 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 438 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 498 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 547 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 557 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:B2GUV7" FT MOD_RES 560 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 588 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 589 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 591 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231" FT MOD_RES 595 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231" FT MOD_RES 1168 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VARIANT 337 FT /note="S -> G (in dbSNP:rs10642)" FT /id="VAR_055954" FT VARIANT 360 FT /note="R -> G (in dbSNP:rs3205296)" FT /id="VAR_055955" FT VARIANT 522 FT /note="K -> T (in dbSNP:rs7558074)" FT /evidence="ECO:0000269|PubMed:10200264, FT ECO:0000269|PubMed:10432305, ECO:0007744|PubMed:21269460" FT /id="VAR_060587" FT MUTAGEN 640 FT /note="V->G: Loss of activity in vivo. Retains full FT activity in vitro." FT /evidence="ECO:0000269|PubMed:10200264" FT MUTAGEN 706 FT /note="H->E: Loss of activity; both in vivo and in vitro. FT Loss of EIF5B release from the 80S initiation complex, FT certainly due to loss of ability to hydrolyze GTP." FT /evidence="ECO:0000269|PubMed:10200264, FT ECO:0000269|PubMed:35732735" FT MUTAGEN 706 FT /note="H->Q: Loss of activity in vivo. Partial activity in FT vitro." FT /evidence="ECO:0000269|PubMed:10200264" FT MUTAGEN 759 FT /note="D->N: Loss of activity; both in vivo and in vitro." FT /evidence="ECO:0000269|PubMed:10200264" FT MUTAGEN 1105 FT /note="R->A: Disruption of contacts with the Met-tRNA FT acceptor stem; when associated with A-1174." FT /evidence="ECO:0000269|PubMed:35732735" FT MUTAGEN 1174 FT /note="R->A: Disruption of contacts with the Met-tRNA FT acceptor stem; when associated with A-1105." FT /evidence="ECO:0000269|PubMed:35732735" FT MUTAGEN 1188..1189 FT /note="RQ->ER: Disruption of contacts with eIF1A (EIF1AX); FT when associated with E-1199 and 1218-R-R-1219." FT /evidence="ECO:0000269|PubMed:35732735" FT MUTAGEN 1199 FT /note="R->E: Disruption of contacts with eIF1A (EIF1AX); FT when associated with 1188-E-E-1189 and 1218-R-R-1219." FT /evidence="ECO:0000269|PubMed:35732735" FT MUTAGEN 1218..1219 FT /note="EI->RR: Disruption of contacts with eIF1A (EIF1AX); FT when associated with 1188-E-R-1189 and E-1199." FT /evidence="ECO:0000269|PubMed:35732735" FT CONFLICT 64 FT /note="E -> G (in Ref. 3; BAA34461)" FT /evidence="ECO:0000305" FT CONFLICT 92 FT /note="T -> I (in Ref. 1; CAB44357)" FT /evidence="ECO:0000305" FT CONFLICT 180 FT /note="I -> M (in Ref. 2; AAD16006)" FT /evidence="ECO:0000305" FT CONFLICT 256 FT /note="K -> R (in Ref. 2; AAD16006)" FT /evidence="ECO:0000305" FT CONFLICT 549 FT /note="E -> V (in Ref. 2; AAD16006)" FT /evidence="ECO:0000305" FT CONFLICT 669 FT /note="G -> W (in Ref. 2; AAD16006)" FT /evidence="ECO:0000305" FT CONFLICT 894 FT /note="E -> K (in Ref. 1; CAB44357)" FT /evidence="ECO:0000305" FT HELIX 603..622 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 633..637 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 639..646 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 647..652 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 661..664 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 676..685 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 699..702 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 708..711 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 721..726 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 729..731 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 735..746 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 751..755 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 757..759 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 772..777 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 781..799 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 800..802 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 808..811 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 814..816 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 818..822 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 824..827 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 831..844 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 857..866 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 867..869 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 870..879 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 887..890 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 897..900 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 903..906 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 913..915 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 920..923 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 927..934 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 943..949 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 952..954 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 961..963 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 981..987 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 988..1001 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1005..1013 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 1015..1025 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 1029..1031 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1033..1038 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 1043..1051 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1055..1061 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 1062..1081 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1086..1088 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1092..1096 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1105..1117 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1125..1135 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1138..1143 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1157..1161 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 1173..1175 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1182..1184 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 1188..1195 FT /evidence="ECO:0007829|PDB:7TQL" FT STRAND 1199..1202 FT /evidence="ECO:0007829|PDB:7TQL" FT HELIX 1209..1214 FT /evidence="ECO:0007829|PDB:7TQL" FT TURN 1215..1218 FT /evidence="ECO:0007829|PDB:7TQL" SQ SEQUENCE 1220 AA; 138827 MW; 454C29FB90AA768E CRC64; MGKKQKNKSE DSTKDDIDLD ALAAEIEGAG AAKEQEPQKS KGKKKKEKKK QDFDEDDILK ELEELSLEAQ GIKADRETVA VKPTENNEEE FTSKDKKKKG QKGKKQSFDD NDSEELEDKD SKSKKTAKPK VEMYSGSDDD DDFNKLPKKA KGKAQKSNKK WDGSEEDEDN SKKIKERSRI NSSGESGDES DEFLQSRKGQ KKNQKNKPGP NIESGNEDDD ASFKIKTVAQ KKAEKKERER KKRDEEKAKL RKLKEKEELE TGKKDQSKQK ESQRKFEEET VKSKVTVDTG VIPASEEKAE TPTAAEDDNE GDKKKKDKKK KKGEKEEKEK EKKKGPSKAT VKAMQEALAK LKEEEERQKR EEEERIKRLE ELEAKRKEEE RLEQEKRERK KQKEKERKER LKKEGKLLTK SQREARARAE ATLKLLQAQG VEVPSKDSLP KKRPIYEDKK RKKIPQQLES KEVSESMELC AAVEVMEQGV PEKEETPPPV EPEEEEDTED AGLDDWEAMA SDEETEKVEG NKVHIEVKEN PEEEEEEEEE EEEDEESEEE EEEEGESEGS EGDEEDEKVS DEKDSGKTLD KKPSKEMSSD SEYDSDDDRT KEERAYDKAK RRIEKRRLEH SKNVNTEKLR APIICVLGHV DTGKTKILDK LRHTHVQDGE AGGITQQIGA TNVPLEAINE QTKMIKNFDR ENVRIPGMLI IDTPGHESFS NLRNRGSSLC DIAILVVDIM HGLEPQTIES INLLKSKKCP FIVALNKIDR LYDWKKSPDS DVAATLKKQK KNTKDEFEER AKAIIVEFAQ QGLNAALFYE NKDPRTFVSL VPTSAHTGDG MGSLIYLLVE LTQTMLSKRL AHCEELRAQV MEVKALPGMG TTIDVILING RLKEGDTIIV PGVEGPIVTQ IRGLLLPPPM KELRVKNQYE KHKEVEAAQG VKILGKDLEK TLAGLPLLVA YKEDEIPVLK DELIHELKQT LNAIKLEEKG VYVQASTLGS LEALLEFLKT SEVPYAGINI GPVHKKDVMK ASVMLEHDPQ YAVILAFDVR IERDAQEMAD SLGVRIFSAE IIYHLFDAFT KYRQDYKKQK QEEFKHIAVF PCKIKILPQY IFNSRDPIVM GVTVEAGQVK QGTPMCVPSK NFVDIGIVTS IEINHKQVDV AKKGQEVCVK IEPIPGESPK MFGRHFEATD ILVSKISRQS IDALKDWFRD EMQKSDWQLI VELKKVFEII //