ID VE2_HPV16 Reviewed; 365 AA. AC P03120; Q71BI4; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 02-SEP-2026, entry version 180. DE RecName: Full=Regulatory protein E2 {ECO:0000255|HAMAP-Rule:MF_04001}; GN Name=E2 {ECO:0000255|HAMAP-Rule:MF_04001}; OS Human papillomavirus type 16. OC Viruses; Floreoviria; Shotokuvirae; Cossaviricota; Papovaviricetes; OC Zurhausenvirales; Papillomaviridae; Firstpapillomavirinae; OC Alphapapillomavirus; Alphapapillomavirus 9. OX NCBI_TaxID=333760; OH NCBI_TaxID=9606; Homo sapiens (Human). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2990099; DOI=10.1016/0042-6822(85)90214-4; RA Seedorf K., Krammer G., Durst M., Suhai S., Rowekamp W.G.; RT "Human papillomavirus type 16 DNA sequence."; RL Virology 145:181-185(1985). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Isolate European German 131; RA Terai M., Fu L., Ma Z., Burk R.D.; RT "Cloning and sequencing of non-European human papillomavirus (HPV) variant RT complete genomes from cervicovaginal cells by an overlapping PCR method."; RL Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION. RX PubMed=3033289; DOI=10.1128/jvi.61.5.1630-1638.1987; RA Phelps W.C., Howley P.M.; RT "Transcriptional trans-activation by the human papillomavirus type 16 E2 RT gene product."; RL J. Virol. 61:1630-1638(1987). RN [4] RP FUNCTION. RX PubMed=1326651; DOI=10.1128/jvi.66.10.5949-5958.1992; RA Del Vecchio A.M., Romanczuk H., Howley P.M., Baker C.C.; RT "Transient replication of human papillomavirus DNAs."; RL J. Virol. 66:5949-5958(1992). RN [5] RP PHOSPHORYLATION, SUBCELLULAR LOCATION, AND DIMERIZATION. RX PubMed=7645246; DOI=10.1006/viro.1995.1424; RA Sanders C.M., Stern P.L., Maitland N.J.; RT "Characterization of human papillomavirus type 16 E2 protein and subdomains RT expressed in insect cells."; RL Virology 211:418-433(1995). RN [6] RP FUNCTION, AND INTERACTION WITH L2. RX PubMed=15681049; DOI=10.1016/j.virusres.2004.07.004; RA Okoye A., Cordano P., Taylor E.R., Morgan I.M., Everett R., Campo M.S.; RT "Human papillomavirus 16 L2 inhibits the transcriptional activation RT function, but not the DNA replication function, of HPV-16 E2."; RL Virus Res. 108:1-14(2005). RN [7] RP INTERACTION WITH E7. RX PubMed=16439535; DOI=10.1128/jvi.80.4.1787-1797.2006; RA Gammoh N., Grm H.S., Massimi P., Banks L.; RT "Regulation of human papillomavirus type 16 E7 activity through direct RT protein interaction with the E2 transcriptional activator."; RL J. Virol. 80:1787-1797(2006). RN [8] RP FUNCTION, AND INTERACTION WITH HOST BRD4. RX PubMed=16611886; DOI=10.1128/jvi.80.9.4276-4285.2006; RA Schweiger M.R., You J., Howley P.M.; RT "Bromodomain protein 4 mediates the papillomavirus E2 transcriptional RT activation function."; RL J. Virol. 80:4276-4285(2006). RN [9] RP INTERACTION WITH HOST TAF1. RX PubMed=18580066; DOI=10.1159/000141706; RA Centeno F., Ramirez-Salazar E., Garcia-Villa E., Gariglio P., Garrido E.; RT "TAF1 interacts with and modulates human papillomavirus 16 E2-dependent RT transcriptional regulation."; RL Intervirology 51:137-143(2008). RN [10] RP SUMOYLATION, MUTAGENESIS OF LYS-292, AND SUBCELLULAR LOCATION. RX PubMed=18619639; DOI=10.1016/j.virol.2008.06.008; RA Wu Y.C., Roark A.A., Bian X.L., Wilson V.G.; RT "Modification of papillomavirus E2 proteins by the small ubiquitin-like RT modifier family members (SUMOs)."; RL Virology 378:329-338(2008). RN [11] RP PHOSPHORYLATION. RX PubMed=19781729; DOI=10.1016/j.virol.2009.08.046; RA Johansson C., Graham S.V., Dornan E.S., Morgan I.M.; RT "The human papillomavirus 16 E2 protein is stabilised in S phase."; RL Virology 394:194-199(2009). RN [12] RP INTERACTION WITH HOST TOPBP1. RX PubMed=22973044; DOI=10.1128/jvi.01002-12; RA Donaldson M.M., Mackintosh L.J., Bodily J.M., Dornan E.S., Laimins L.A., RA Morgan I.M.; RT "An interaction between human papillomavirus 16 E2 and TopBP1 is required RT for optimum viral DNA replication and episomal genome establishment."; RL J. Virol. 86:12806-12815(2012). RN [13] RP PHOSPHORYLATION AT SER-243, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=25340539; DOI=10.1371/journal.pone.0110882; RA Chang S.W., Liu W.C., Liao K.Y., Tsao Y.P., Hsu P.H., Chen S.L.; RT "Phosphorylation of HPV-16 E2 at serine 243 enables binding to Brd4 and RT mitotic chromosomes."; RL PLoS ONE 9:E110882-E110882(2014). RN [14] RP INTERACTION WITH PROTEIN L1, AND SUBCELLULAR LOCATION. RX PubMed=25911730; DOI=10.1099/vir.0.000162; RA Siddiqa A., Leon K.C., James C.D., Bhatti M.F., Roberts S., Parish J.L.; RT "The human papillomavirus type 16 L1 protein directly interacts with E2 and RT enhances E2-dependent replication and transcription activation."; RL J. Gen. Virol. 96:2274-2285(2015). RN [15] RP FUNCTION. RX PubMed=26365679; DOI=10.1016/j.virusres.2015.09.008; RA Gauson E.J., Wang X., Dornan E.S., Herzyk P., Bristol M., Morgan I.M.; RT "Failure to interact with Brd4 alters the ability of HPV16 E2 to regulate RT host genome expression and cellular movement."; RL Virus Res. 211:1-8(2015). RN [16] RP ROLE AS ANTIGEN IN HEAD AND NECK SQUAMOUS CELL CARCINOMA. RX PubMed=33208941; DOI=10.1038/s41586-020-2931-3; RA Wieland A., Patel M.R., Cardenas M.A., Eberhardt C.S., Hudson W.H., RA Obeng R.C., Griffith C.C., Wang X., Chen Z.G., Kissick H.T., Saba N.F., RA Ahmed R.; RT "Defining HPV-specific B cell responses in patients with head and neck RT cancer."; RL Nature 597:274-278(2021). RN [17] RP ROLE AS ANTIGEN IN HEAD AND NECK SQUAMOUS CELL CARCINOMA. RX PubMed=34471285; DOI=10.1038/s41586-021-03862-z; RA Eberhardt C.S., Kissick H.T., Patel M.R., Cardenas M.A., Prokhnevska N., RA Obeng R.C., Nasti T.H., Griffith C.C., Im S.J., Wang X., Shin D.M., RA Carrington M., Chen Z.G., Sidney J., Sette A., Saba N.F., Wieland A., RA Ahmed R.; RT "Functional HPV-specific PD-1+ stem-like CD8 T cells in head and neck RT cancer."; RL Nature 597:279-284(2021). RN [18] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-201, AND TRANSACTIVATION DOMAIN. RX PubMed=10089541; DOI=10.1107/s0907444998010889; RA Burns J.E., Moroz O.V., Antson A.A., Sanders C.M., Wilson K.S., RA Maitland N.J.; RT "Expression, crystallization and preliminary X-ray analysis of the E2 RT transactivation domain from papillomavirus type 16."; RL Acta Crystallogr. D 54:1471-1474(1998). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 285-365, DIMERIZATION, AND RP DNA-BINDING DOMAIN. RX PubMed=9878365; DOI=10.1006/jmbi.1998.2260; RA Hegde R.S., Androphy E.J.; RT "Crystal structure of the E2 DNA-binding domain from human papillomavirus RT type 16: implications for its DNA binding-site selection mechanism."; RL J. Mol. Biol. 284:1479-1489(1998). RN [20] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-201. RX PubMed=10693813; DOI=10.1038/35001638; RA Antson A.A., Burns J.E., Moroz O.V., Scott D.J., Sanders C.M., RA Bronstein I.B., Dodson G.G., Wilson K.S., Maitland N.J.; RT "Structure of the intact transactivation domain of the human papillomavirus RT E2 protein."; RL Nature 403:805-809(2000). RN [21] RP STRUCTURE BY NMR OF 286-365. RX PubMed=15702528; DOI=10.1023/b:jnmr.0000048942.96866.76; RA Nadra A.D., Eliseo T., Mok Y.K., Almeida C.L., Bycroft M., Paci M., RA de Prat-Gay G., Cicero D.O.; RT "Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional RT regulator with a dimeric beta-barrel fold."; RL J. Biomol. NMR 30:211-214(2004). RN [22] RP X-RAY CRYSTALLOGRAPHY (1.59 ANGSTROMS) OF 1-201, AND INTERACTION WITH HOST RP BRD4. RX PubMed=17189190; DOI=10.1016/j.molcel.2006.11.002; RA Abbate E.A., Voitenleitner C., Botchan M.R.; RT "Structure of the papillomavirus DNA-tethering complex E2:Brd4 and a RT peptide that ablates HPV chromosomal association."; RL Mol. Cell 24:877-889(2006). RN [23] RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 285-365. RX PubMed=17915949; DOI=10.1021/bi701104q; RA Dellarole M., Sanchez I.E., Freire E., de Prat-Gay G.; RT "Increased stability and DNA site discrimination of 'single chain' variants RT of the dimeric beta-barrel DNA binding domain of the human papillomavirus RT E2 transcriptional regulator."; RL Biochemistry 46:12441-12450(2007). RN [24] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 283-365. RX PubMed=21482558; DOI=10.1096/fj.10-176461; RA Bose K., Meinke G., Bohm A., Baleja J.D.; RT "Design and characterization of an enhanced repressor of human RT papillomavirus E2 protein."; RL FASEB J. 25:2354-2361(2011). CC -!- FUNCTION: Plays a role in the initiation of viral DNA replication. A CC dimer of E2 interacts with a dimer of E1 in order to improve CC specificity of E1 DNA binding activity. Once the complex recognizes and CC binds DNA at specific sites, the E2 dimer is removed from DNA. E2 also CC regulates viral transcription through binding to the E2RE response CC element (5'-ACCNNNNNNGGT-3') present in multiple copies in the CC regulatory regions of the viral genome. Activates or represses CC transcription depending on E2RE's position with regards to proximal CC promoter elements including the TATA-box. Repression occurs by CC sterically hindering the assembly of the transcription initiation CC complex. {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:1326651, CC ECO:0000269|PubMed:15681049, ECO:0000269|PubMed:16611886, CC ECO:0000269|PubMed:25340539, ECO:0000269|PubMed:26365679, CC ECO:0000269|PubMed:3033289}. CC -!- SUBUNIT: Binds DNA as homodimer. Interacts with protein E1; this CC interaction greatly increases E1 DNA-binding activity. Interacts with CC protein L1; this interaction enhances E2-dependent replication and CC transcription activation. Interacts with protein L2; this interaction CC inhibits E2 transcriptional activity but not DNA replication function CC E2. Interacts with protein E7; this interaction inhibits E7 oncogenic CC activity. Interacts with host TAF1; this interaction modulates E2- CC dependent transcriptional regulation. Interacts with host BRD4; this CC interaction mediates E2 transcriptional activation function. CC Additionally, the interaction with host BRD4 on mitotic chromosomes CC mediates tethering of the viral genome. Interacts with host TOPBP1; CC this interaction is required for optimal viral DNA replication. CC {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:15681049, CC ECO:0000269|PubMed:16439535, ECO:0000269|PubMed:16611886, CC ECO:0000269|PubMed:17189190, ECO:0000269|PubMed:18580066, CC ECO:0000269|PubMed:22973044, ECO:0000269|PubMed:25911730, CC ECO:0000269|PubMed:7645246, ECO:0000269|PubMed:9878365}. CC -!- INTERACTION: CC P03120; P03114: E1; NbExp=3; IntAct=EBI-1779322, EBI-7387308; CC P03120; O60885: BRD4; Xeno; NbExp=4; IntAct=EBI-1779322, EBI-723869; CC P03120; O60885-1: BRD4; Xeno; NbExp=2; IntAct=EBI-1779322, EBI-9345088; CC P03120; Q9H0C5: BTBD1; Xeno; NbExp=3; IntAct=EBI-1779322, EBI-935503; CC P03120; P17676: CEBPB; Xeno; NbExp=2; IntAct=EBI-1779322, EBI-969696; CC P03120; P79101: CPSF3; Xeno; NbExp=2; IntAct=EBI-1779322, EBI-7894416; CC P03120; O19137: CPSF4; Xeno; NbExp=3; IntAct=EBI-1779322, EBI-7894441; CC P03120; P31274: HOXC9; Xeno; NbExp=3; IntAct=EBI-1779322, EBI-1779423; CC P03120; P22736: NR4A1; Xeno; NbExp=3; IntAct=EBI-1779322, EBI-721550; CC P03120; P03132: Rep68; Xeno; NbExp=2; IntAct=EBI-1779322, EBI-7387242; CC P03120; Q92547: TOPBP1; Xeno; NbExp=2; IntAct=EBI-1779322, EBI-308302; CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04001, CC ECO:0000269|PubMed:18619639, ECO:0000269|PubMed:25340539, CC ECO:0000269|PubMed:25911730, ECO:0000269|PubMed:7645246}. CC -!- PTM: Phosphorylated. Phosphorylation at Ser-243 mediates binding to CC host Brd4 and is required for host chromosome binding. CC {ECO:0000255|HAMAP-Rule:MF_04001, ECO:0000269|PubMed:25340539, CC ECO:0000269|PubMed:7645246}. CC -!- PTM: Sumoylation plays a regulatory role in E2 transcriptional CC activity. {ECO:0000255|HAMAP-Rule:MF_04001, CC ECO:0000269|PubMed:18619639}. CC -!- MISCELLANEOUS: HPV16, in comparison to HPV types 6 and 11, is more CC often associated with malignant genital cancers in humans. CC -!- MISCELLANEOUS: Part of the antigens expressed and presented within HPV- CC positive head and neck tumors. {ECO:0000269|PubMed:33208941, CC ECO:0000269|PubMed:34471285}. CC -!- SIMILARITY: Belongs to the papillomaviridae E2 protein family. CC {ECO:0000255|HAMAP-Rule:MF_04001}. 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; K02718; AAA46941.1; -; Genomic_DNA. DR EMBL; AF536179; AAQ10715.1; -; Genomic_DNA. DR PIR; A03669; W2WLHS. DR RefSeq; NP_041328.1; NC_001526.4. DR PDB; 1BY9; X-ray; 2.20 A; A=285-365. DR PDB; 1DTO; X-ray; 1.90 A; A=1-201. DR PDB; 1R8P; NMR; -; A/B=286-365. DR PDB; 1ZZF; NMR; -; A/B=286-365. DR PDB; 2NNU; X-ray; 1.59 A; A=1-201. DR PDB; 2Q79; X-ray; 1.80 A; A=285-365. DR PDB; 3MI7; X-ray; 2.20 A; X=283-365. DR AlphaFoldDB; P03120; -. DR BMRB; P03120; -. DR MDRepo; P03120; -. DR SASBDB; P03120; -. DR SMR; P03120; -. DR BioGRID; 4263559; 2257. DR DIP; DIP-44574N; -. DR IntAct; P03120; 64. DR MINT; P03120; -. DR BindingDB; P03120; -. DR ChEMBL; CHEMBL4656; -. DR DrugCentral; P03120; -. DR iPTMnet; P03120; -. DR DNASU; 1489080; -. DR GeneID; 1489080; -. DR KEGG; vg:1489080; -. DR OrthoDB; 15886at10239; -. DR EvolutionaryTrace; P03120; -. DR PRO; PR:P03120; -. DR Proteomes; UP000009251; Segment. DR GO; GO:0042025; C:host cell nucleus; EXP:UniProtKB. DR GO; GO:0044163; C:host cytoskeleton; IDA:CACAO. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:UniProtKB-UniRule. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006351; P:DNA-templated transcription; IEA:UniProtKB-UniRule. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule. DR FunFam; 1.10.287.30:FF:000001; Regulatory protein E2; 1. DR FunFam; 2.170.200.10:FF:000001; Regulatory protein E2; 1. DR FunFam; 3.30.70.330:FF:000918; Regulatory protein E2; 1. DR Gene3D; 3.30.70.330; -; 1. DR Gene3D; 1.10.287.30; E2 (early) protein, N terminal domain, subdomain 1; 1. DR Gene3D; 2.170.200.10; Papillomavirus E2 early protein domain; 1. DR HAMAP; MF_04001; PPV_E2; 1. DR InterPro; IPR035975; E2/EBNA1_C_sf. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf. DR InterPro; IPR000427; Papillomavirus_E2_C. DR InterPro; IPR001866; PPV_E2_N. DR InterPro; IPR033668; Reg_prot_E2. DR InterPro; IPR036050; Regulatory_protein_E2_N. DR InterPro; IPR042503; Regulatory_protein_E2_N_1. DR InterPro; IPR042504; Regulatory_protein_E2_N_2. DR Pfam; PF00511; PPV_E2_C; 1. DR Pfam; PF00508; PPV_E2_N; 1. DR SUPFAM; SSF51332; E2 regulatory, transactivation domain; 1. DR SUPFAM; SSF54957; Viral DNA-binding domain; 1. DR PDBsum; 1BY9; -. DR PDBsum; 1DTO; -. DR PDBsum; 1R8P; -. DR PDBsum; 1ZZF; -. DR PDBsum; 2NNU; -. DR PDBsum; 2Q79; -. DR PDBsum; 3MI7; -. PE 1: Evidence at protein level; KW 3D-structure; Activator; DNA replication; DNA-binding; Early protein; KW Host nucleus; Isopeptide bond; Phosphoprotein; Reference proteome; KW Repressor; Transcription; Transcription regulation; Ubl conjugation. FT CHAIN 1..365 FT /note="Regulatory protein E2" FT /id="PRO_0000133195" FT REGION 1..200 FT /note="Transactivation domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001, FT ECO:0000269|PubMed:10089541" FT REGION 285..365 FT /note="DNA-binding domain" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001, FT ECO:0000269|PubMed:9878365" FT MOD_RES 243 FT /note="Phosphoserine; by host" FT /evidence="ECO:0000269|PubMed:25340539" FT CROSSLNK 292 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_04001, FT ECO:0000269|PubMed:18619639" FT MUTAGEN 292 FT /note="K->R: Complete loss of sumoylation." FT /evidence="ECO:0000269|PubMed:18619639" FT CONFLICT 77 FT /note="L -> P (in Ref. 2; AAQ10715)" FT /evidence="ECO:0000305" FT CONFLICT 210 FT /note="I -> T (in Ref. 2; AAQ10715)" FT /evidence="ECO:0000305" FT CONFLICT 219 FT /note="P -> S (in Ref. 2; AAQ10715)" FT /evidence="ECO:0000305" FT CONFLICT 310 FT /note="T -> K (in Ref. 2; AAQ10715)" FT /evidence="ECO:0000305" FT HELIX 1..21 FT /evidence="ECO:0007829|PDB:2NNU" FT HELIX 26..48 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 52..54 FT /evidence="ECO:0007829|PDB:2NNU" FT HELIX 59..61 FT /evidence="ECO:0007829|PDB:1DTO" FT HELIX 62..83 FT /evidence="ECO:0007829|PDB:2NNU" FT TURN 86..89 FT /evidence="ECO:0007829|PDB:2NNU" FT TURN 94..97 FT /evidence="ECO:0007829|PDB:2NNU" FT HELIX 99..103 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 104..106 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 110..121 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 127..141 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 144..148 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 154..161 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 164..170 FT /evidence="ECO:0007829|PDB:2NNU" FT HELIX 171..178 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 184..190 FT /evidence="ECO:0007829|PDB:2NNU" FT STRAND 287..293 FT /evidence="ECO:0007829|PDB:2Q79" FT HELIX 295..305 FT /evidence="ECO:0007829|PDB:2Q79" FT HELIX 306..311 FT /evidence="ECO:0007829|PDB:2Q79" FT STRAND 313..315 FT /evidence="ECO:0007829|PDB:2Q79" FT HELIX 316..318 FT /evidence="ECO:0007829|PDB:2Q79" FT STRAND 331..336 FT /evidence="ECO:0007829|PDB:2Q79" FT HELIX 340..349 FT /evidence="ECO:0007829|PDB:2Q79" FT STRAND 356..362 FT /evidence="ECO:0007829|PDB:2Q79" SQ SEQUENCE 365 AA; 41825 MW; 27581F82B246E112 CRC64; METLCQRLNV CQDKILTHYE NDSTDLRDHI DYWKHMRLEC AIYYKAREMG FKHINHQVVP TLAVSKNKAL QAIELQLTLE TIYNSQYSNE KWTLQDVSLE VYLTAPTGCI KKHGYTVEVQ FDGDICNTMH YTNWTHIYIC EEASVTVVEG QVDYYGLYYV HEGIRTYFVQ FKDDAEKYSK NKVWEVHAGG QVILCPTSVF SSNEVSSPEI IRQHLANHPA ATHTKAVALG TEETQTTIQR PRSEPDTGNP CHTTKLLHRD SVDSAPILTA FNSSHKGRIN CNSNTTPIVH LKGDANTLKC LRYRFKKHCT LYTAVSSTWH WTGHNVKHKS AIVTLTYDSE WQRDQFLSQV KIPKTITVST GFMSI //