ZN777_HUMAN
ID ZN777_HUMAN Reviewed; 831 AA.
AC Q9ULD5; Q8N2R2; Q8N659;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 08-MAY-2019, sequence version 3.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Zinc finger protein 777 {ECO:0000305};
GN Name=ZNF777 {ECO:0000312|HGNC:HGNC:22213}; Synonyms=KIAA1285;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-749.
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 259-831, AND VARIANT THR-512.
RC TISSUE=Lung;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 318-831.
RC TISSUE=Embryo;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND SER-502, AND
RP IDENTIFICATION 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-604 AND SER-623, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION BY
RP MASS 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 [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25560148; DOI=10.1002/jcb.25046;
RA Yuki R., Aoyama K., Kubota S., Yamaguchi N., Kubota S., Hasegawa H.,
RA Morii M., Huang X., Liu K., Williams R., Fukuda M.N., Yamaguchi N.;
RT "Overexpression of zinc-finger protein 777 (ZNF777) inhibits proliferation
RT at low cell density through down-regulation of FAM129A.";
RL J. Cell. Biochem. 116:954-968(2015).
RN [9]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330 AND LYS-452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [10]
RP FUNCTION, AND SUBUNIT.
RX PubMed=31856708; DOI=10.1186/s12860-019-0243-y;
RA Al Chiblak M., Steinbeck F., Thiesen H.J., Lorenz P.;
RT "DUF3669, a 'domain of unknown function' within ZNF746 and ZNF777,
RT oligomerizes and contributes to transcriptional repression.";
RL BMC Mol. Cell Biol. 20:60-60(2019).
CC -!- FUNCTION: May be involved in transcriptional repression
CC (PubMed:31856708). Inhibits cell proliferation through CDKN1A/p21
CC induction by down-regulation of NIBAN1/FAM129A at low cell density
CC (PubMed:25560148). {ECO:0000269|PubMed:25560148,
CC ECO:0000269|PubMed:31856708}.
CC -!- SUBUNIT: Heterooligomer with ZNF746. {ECO:0000269|PubMed:31856708}.
CC -!- INTERACTION:
CC Q9ULD5; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-11975599, EBI-739624;
CC Q9ULD5; P49761: CLK3; NbExp=3; IntAct=EBI-11975599, EBI-745579;
CC Q9ULD5; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-11975599, EBI-10175124;
CC Q9ULD5; A1L4K1: FSD2; NbExp=3; IntAct=EBI-11975599, EBI-5661036;
CC Q9ULD5; Q14005-2: IL16; NbExp=6; IntAct=EBI-11975599, EBI-17178971;
CC Q9ULD5; Q2KHM9: KIAA0753; NbExp=3; IntAct=EBI-11975599, EBI-2805604;
CC Q9ULD5; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-11975599, EBI-10172052;
CC Q9ULD5; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-11975599, EBI-1105213;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25560148}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH23985.2; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA86599.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA86599.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Vector contamination at the C-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC11033.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC073314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB033111; BAA86599.1; ALT_SEQ; mRNA.
DR EMBL; BC023985; AAH23985.2; ALT_INIT; mRNA.
DR EMBL; AK074515; BAC11033.1; ALT_INIT; mRNA.
DR CCDS; CCDS43675.1; -.
DR RefSeq; NP_056509.2; NM_015694.2.
DR RefSeq; XP_011514357.1; XM_011516055.2.
DR AlphaFoldDB; Q9ULD5; -.
DR SMR; Q9ULD5; -.
DR BioGRID; 118035; 97.
DR IntAct; Q9ULD5; 19.
DR STRING; 9606.ENSP00000247930; -.
DR iPTMnet; Q9ULD5; -.
DR PhosphoSitePlus; Q9ULD5; -.
DR BioMuta; ZNF777; -.
DR DMDM; 152112417; -.
DR EPD; Q9ULD5; -.
DR jPOST; Q9ULD5; -.
DR MassIVE; Q9ULD5; -.
DR MaxQB; Q9ULD5; -.
DR PaxDb; Q9ULD5; -.
DR PeptideAtlas; Q9ULD5; -.
DR PRIDE; Q9ULD5; -.
DR Antibodypedia; 827; 78 antibodies from 17 providers.
DR DNASU; 27153; -.
DR Ensembl; ENST00000247930.5; ENSP00000247930.4; ENSG00000196453.8.
DR GeneID; 27153; -.
DR KEGG; hsa:27153; -.
DR MANE-Select; ENST00000247930.5; ENSP00000247930.4; NM_015694.3; NP_056509.2.
DR UCSC; uc003wfv.4; human.
DR CTD; 27153; -.
DR GeneCards; ZNF777; -.
DR HGNC; HGNC:22213; ZNF777.
DR HPA; ENSG00000196453; Low tissue specificity.
DR MIM; 619298; gene.
DR neXtProt; NX_Q9ULD5; -.
DR OpenTargets; ENSG00000196453; -.
DR PharmGKB; PA162410383; -.
DR VEuPathDB; HostDB:ENSG00000196453; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000155153; -.
DR HOGENOM; CLU_002678_76_2_1; -.
DR InParanoid; Q9ULD5; -.
DR OMA; ERGPAFN; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9ULD5; -.
DR TreeFam; TF337777; -.
DR PathwayCommons; Q9ULD5; -.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR SignaLink; Q9ULD5; -.
DR BioGRID-ORCS; 27153; 20 hits in 1098 CRISPR screens.
DR GenomeRNAi; 27153; -.
DR Pharos; Q9ULD5; Tdark.
DR PRO; PR:Q9ULD5; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9ULD5; protein.
DR Bgee; ENSG00000196453; Expressed in endothelial cell and 149 other tissues.
DR Genevisible; Q9ULD5; HS.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd07765; KRAB_A-box; 1.
DR InterPro; IPR001909; KRAB.
DR InterPro; IPR036051; KRAB_dom_sf.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01352; KRAB; 1.
DR Pfam; PF00096; zf-C2H2; 8.
DR SMART; SM00349; KRAB; 1.
DR SMART; SM00355; ZnF_C2H2; 9.
DR SUPFAM; SSF109640; SSF109640; 1.
DR SUPFAM; SSF57667; SSF57667; 5.
DR PROSITE; PS50805; KRAB; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 9.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 9.
PE 1: Evidence at protein level;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation;
KW Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..831
FT /note="Zinc finger protein 777"
FT /id="PRO_0000293692"
FT DOMAIN 285..356
FT /note="KRAB"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00119"
FT ZN_FING 546..568
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 574..596
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..658
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..716
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 722..744
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 750..772
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 778..800
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 806..828
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 1..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..634
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 157
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 604
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 330
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 452
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 70
FT /note="R -> W (in dbSNP:rs3735318)"
FT /id="VAR_057451"
FT VARIANT 115
FT /note="V -> A (in dbSNP:rs3735319)"
FT /id="VAR_057452"
FT VARIANT 512
FT /note="A -> T (in dbSNP:rs17852167)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_061965"
FT CONFLICT 446
FT /note="T -> TA (in Ref. 4; BAC11033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 831 AA; 93762 MW; 6AE3346E1A4EDF80 CRC64;
MENQRSSPLS FPSVPQEETL RQAPAGLPRE TLFQSRVLPP KEIPSLSPTI PRQGSLPQTS
SAPKQETSGR MPHVLQKGPS LLCSAASEQE TSLQGPLASQ EGTQYPPPAA AEQEVSLLSH
SPHHQEAPVH SPEAPEKDPL TLSPTVPETD MDPLLQSPVS QKDTPFQISS AVQKEQPLPT
AEITRLAVWA AVQAVERKLE AQAMRLLTLE GRTGTNEKKI ADCEKTAVEF ANHLESKWVV
LGTLLQEYGL LQRRLENMEN LLKNRNFWIL RLPPGSNGEV PKVPVTFDDV AVHFSEQEWG
NLSEWQKELY KNVMRGNYES LVSMDYAISK PDLMSQMERG ERPTMQEQED SEEGETPTDP
SAAHDGIVIK IEVQTNDEGS ESLETPEPLM GQVEEHGFQD SELGDPCGEQ PDLDMQEPEN
TLEESTEGSS EFSELKQMLV QQRNCTEGIV IKTEEQDEEE EEEEEDELPQ HLQSLGQLSG
RYEASMYQTP LPGEMSPEGE ESPPPLQLGN PAVKRLAPSV HGERHLSENR GASSQQQRNR
RGERPFTCME CGKSFRLKIN LIIHQRNHIK EGPYECAECE ISFRHKQQLT LHQRIHRVRG
GCVSPERGPT FNPKHALKPR PKSPSSGSGG GGPKPYKCPE CDSSFSHKSS LTKHQITHTG
ERPYTCPECK KSFRLHISLV IHQRVHAGKH EVSFICSLCG KSFSRPSHLL RHQRTHTGER
PFKCPECEKS FSEKSKLTNH CRVHSRERPH ACPECGKSFI RKHHLLEHRR IHTGERPYHC
AECGKRFTQK HHLLEHQRAH TGERPYPCTH CAKCFRYKQS LKYHLRTHTG E
