ID ZN574_HUMAN Reviewed; 896 AA.
AC Q6ZN55; Q6IPE0; Q6ZN10; Q7L5Z5; Q8NCE3; Q9H6N0;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 2.
DT 27-MAR-2024, entry version 160.
DE RecName: Full=Zinc finger protein 574;
GN Name=ZNF574;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Cerebellum, Hepatoma, and Teratocarcinoma;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Mammary gland;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; THR-724 AND SER-728, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-164; SER-298; SER-717 AND
RP SER-728, AND IDENTIFICATION BY MASS 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-717 AND SER-728, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-113 AND SER-164, 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 [9]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-832, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- INTERACTION:
CC Q6ZN55-2; Q8NHQ1: CEP70; NbExp=3; IntAct=EBI-17189720, EBI-739624;
CC Q6ZN55-2; A2VCK2: DCDC2B; NbExp=3; IntAct=EBI-17189720, EBI-10173222;
CC Q6ZN55-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-17189720, EBI-5916454;
CC Q6ZN55-2; Q9UBR4-2: LHX3; NbExp=3; IntAct=EBI-17189720, EBI-12039345;
CC Q6ZN55-2; Q5JTD7: LRRC73; NbExp=3; IntAct=EBI-17189720, EBI-12003882;
CC Q6ZN55-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-17189720, EBI-16439278;
CC Q6ZN55-2; P78424: POU6F2; NbExp=3; IntAct=EBI-17189720, EBI-12029004;
CC Q6ZN55-2; Q12933: TRAF2; NbExp=3; IntAct=EBI-17189720, EBI-355744;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZN55-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZN55-2; Sequence=VSP_022878;
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {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; AK025712; BAB15225.1; -; mRNA.
DR EMBL; AK074788; BAC11210.1; -; mRNA.
DR EMBL; AK131369; BAD18520.1; -; mRNA.
DR EMBL; AK131418; BAD18565.1; -; mRNA.
DR EMBL; BC001184; AAH01184.2; -; mRNA.
DR EMBL; BC071962; AAH71962.1; -; mRNA.
DR CCDS; CCDS12596.1; -. [Q6ZN55-1]
DR RefSeq; NP_001317448.1; NM_001330519.1.
DR RefSeq; NP_073589.4; NM_022752.5. [Q6ZN55-1]
DR RefSeq; XP_005259216.1; XM_005259159.2. [Q6ZN55-1]
DR RefSeq; XP_011525530.1; XM_011527228.2. [Q6ZN55-1]
DR RefSeq; XP_011525531.1; XM_011527229.2. [Q6ZN55-1]
DR RefSeq; XP_011525532.1; XM_011527230.2. [Q6ZN55-1]
DR AlphaFoldDB; Q6ZN55; -.
DR SMR; Q6ZN55; -.
DR BioGRID; 122276; 288.
DR IntAct; Q6ZN55; 44.
DR MINT; Q6ZN55; -.
DR STRING; 9606.ENSP00000222339; -.
DR iPTMnet; Q6ZN55; -.
DR PhosphoSitePlus; Q6ZN55; -.
DR BioMuta; ZNF574; -.
DR DMDM; 125991263; -.
DR EPD; Q6ZN55; -.
DR jPOST; Q6ZN55; -.
DR MassIVE; Q6ZN55; -.
DR MaxQB; Q6ZN55; -.
DR PaxDb; 9606-ENSP00000469029; -.
DR PeptideAtlas; Q6ZN55; -.
DR ProteomicsDB; 67982; -. [Q6ZN55-1]
DR ProteomicsDB; 67983; -. [Q6ZN55-2]
DR Pumba; Q6ZN55; -.
DR Antibodypedia; 30883; 68 antibodies from 21 providers.
DR DNASU; 64763; -.
DR Ensembl; ENST00000359044.5; ENSP00000351939.3; ENSG00000105732.13. [Q6ZN55-1]
DR Ensembl; ENST00000600245.1; ENSP00000469029.1; ENSG00000105732.13. [Q6ZN55-1]
DR GeneID; 64763; -.
DR KEGG; hsa:64763; -.
DR MANE-Select; ENST00000359044.5; ENSP00000351939.3; NM_022752.6; NP_073589.4.
DR UCSC; uc002osk.6; human. [Q6ZN55-1]
DR AGR; HGNC:26166; -.
DR CTD; 64763; -.
DR DisGeNET; 64763; -.
DR GeneCards; ZNF574; -.
DR HGNC; HGNC:26166; ZNF574.
DR HPA; ENSG00000105732; Low tissue specificity.
DR neXtProt; NX_Q6ZN55; -.
DR OpenTargets; ENSG00000105732; -.
DR PharmGKB; PA134916492; -.
DR VEuPathDB; HostDB:ENSG00000105732; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000161799; -.
DR HOGENOM; CLU_002678_24_1_1; -.
DR InParanoid; Q6ZN55; -.
DR OMA; CAKPFNS; -.
DR OrthoDB; 5299235at2759; -.
DR PhylomeDB; Q6ZN55; -.
DR TreeFam; TF350791; -.
DR PathwayCommons; Q6ZN55; -.
DR SignaLink; Q6ZN55; -.
DR BioGRID-ORCS; 64763; 548 hits in 1181 CRISPR screens.
DR ChiTaRS; ZNF574; human.
DR GenomeRNAi; 64763; -.
DR Pharos; Q6ZN55; Tdark.
DR PRO; PR:Q6ZN55; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q6ZN55; Protein.
DR Bgee; ENSG00000105732; Expressed in cerebellar vermis and 201 other cell types or tissues.
DR ExpressionAtlas; Q6ZN55; baseline and differential.
DR Genevisible; Q6ZN55; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0001228; F:DNA-binding transcription activator 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:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 3.30.160.60; Classic Zinc Finger; 13.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR PANTHER; PTHR24381:SF393; CHROMATIN-LINKED ADAPTOR FOR MSL PROTEINS, ISOFORM B-RELATED; 1.
DR PANTHER; PTHR24381; ZINC FINGER PROTEIN; 1.
DR Pfam; PF00096; zf-C2H2; 6.
DR Pfam; PF13912; zf-C2H2_6; 2.
DR Pfam; PF12874; zf-met; 1.
DR SMART; SM00355; ZnF_C2H2; 20.
DR SUPFAM; SSF57667; beta-beta-alpha zinc fingers; 11.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 18.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 19.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Methylation; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..896
FT /note="Zinc finger protein 574"
FT /id="PRO_0000274861"
FT ZN_FING 16..38
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 76..98
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 126..148
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 214..236
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 309..331
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 336..358
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 364..386
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 392..413
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 466..489
FT /note="C2H2-type 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 495..517
FT /note="C2H2-type 10; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 523..545
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 551..573
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 579..601
FT /note="C2H2-type 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 607..630
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 636..659
FT /note="C2H2-type 15; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 667..689
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 738..760
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 766..788
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 794..816
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 822..844
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 239..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 717
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 724
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231"
FT MOD_RES 832
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT VAR_SEQ 1
FT /note="M -> MPRATWANSKERSWAESERGPRDTGNGGSKAERHIQEIETGRGGDRA
FT KAHRRQRMRLRGTERASLGPGRRLGDSRGTDMPGARAQGLAAA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_022878"
FT VARIANT 332
FT /note="R -> Q (in dbSNP:rs3745226)"
FT /id="VAR_030351"
FT VARIANT 711
FT /note="T -> S (in dbSNP:rs35898322)"
FT /id="VAR_052870"
FT VARIANT 785
FT /note="R -> Q (in dbSNP:rs3745228)"
FT /id="VAR_030352"
FT CONFLICT 513
FT /note="H -> R (in Ref. 1; BAD18565)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="E -> G (in Ref. 1; BAC11210)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 896 AA; 98900 MW; F1E3EBCC47427654 CRC64;
MTEESEETVL YIEHRYVCSE CNQLYGSLEE VLMHQNSHVP QQHFELVGVA DPGVTVATDT
ASGTGLYQTL VQESQYQCLE CGQLLMSPSQ LLEHQELHLK MMAPQEAVPA EPSPKAPPLS
SSTIHYECVD CKALFASQEL WLNHRQTHLR ATPTKAPAPV VLGSPVVLGP PVGQARVAVE
HSYRKAEEGG EGATVPSAAA TTTEVVTEVE LLLYKCSECS QLFQLPADFL EHQATHFPAP
VPESQEPALQ QEVQASSPAE VPVSQPDPLP ASDHSYELRN GEAIGRDRRG RRARRNNSGE
AGGAATQELF CSACDQLFLS PHQLQQHLRS HREGVFKCPL CSRVFPSPSS LDQHLGDHSS
ESHFLCVDCG LAFGTEALLL AHRRAHTPNP LHSCPCGKTF VNLTKFLYHR RTHGVGGVPL
PTTPVPPEEP VIGFPEPAPA ETGEPEAPEP PVSEETSAGP AAPGTYRCLL CSREFGKALQ
LTRHQRFVHR LERRHKCSIC GKMFKKKSHV RNHLRTHTGE RPFPCPDCSK PFNSPANLAR
HRLTHTGERP YRCGDCGKAF TQSSTLRQHR LVHAQHFPYR CQECGVRFHR PYRLLMHRYH
HTGEYPYKCR ECPRSFLLRR LLEVHQLVVH AGRQPHRCPS CGAAFPSSLR LREHRCAAAA
AQAPRRFECG TCGKKVGSAA RLQAHEAAHA AAGPGEVLAK EPPAPRAPRA TRAPVASPAA
LGSTATASPA APARRRGLEC SECKKLFSTE TSLQVHRRIH TGERPYPCPD CGKAFRQSTH
LKDHRRLHTG ERPFACEVCG KAFAISMRLA EHRRIHTGER PYSCPDCGKS YRSFSNLWKH
RKTHQQQHQA AVRQQLAEAE AAVGLAVMET AVEALPLVEA IEIYPLAEAE GVQISG
//
