ZN521_MOUSE
ID ZN521_MOUSE Reviewed; 1311 AA.
AC Q6KAS7; Q8BIF5; Q8BV21; Q8CIQ2; Q8VDS6;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Zinc finger protein 521;
DE AltName: Full=Ecotropic viral integration site 3 protein;
GN Name=Znf521; Synonyms=Evi3, Zfp521;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INVOLVEMENT
RP IN B-CELL LEUKEMIA, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ;
RX PubMed=12393497; DOI=10.1182/blood-2002-08-2652;
RA Warming S., Liu P., Suzuki T., Akagi K., Lindtner S., Pavlakis G.N.,
RA Jenkins N.A., Copeland N.G.;
RT "Evi3, a common retroviral integration site in murine B-cell lymphoma,
RT encodes an EBFAZ-related Kruppel-like zinc finger protein.";
RL Blood 101:1934-1940(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 771-1311 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 983-1311 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP INVOLVEMENT IN B-CELL LEUKEMIA.
RX PubMed=15580294; DOI=10.1038/sj.onc.1208243;
RA Hentges K.E., Weiser K.C., Schountz T., Woodward L.S., Morse H.C.,
RA Justice M.J.;
RT "Evi3, a zinc-finger protein related to EBFAZ, regulates EBF activity in B-
RT cell leukemia.";
RL Oncogene 24:1220-1230(2005).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605 AND SER-608, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Transcription factor that can both act as an activator or a
CC repressor depending on the context. Involved in BMP signaling and in
CC the regulation of the immature compartment of the hematopoietic system.
CC Associates with SMADs in response to BMP2 leading to activate
CC transcription of BMP target genes. Acts as a transcriptional repressor
CC via its interaction with EBF1, a transcription factor involved
CC specification of B-cell lineage; this interaction preventing EBF1 to
CC bind DNA and activate target genes.
CC -!- SUBUNIT: Interacts with EBF1. Interacts with SMAD1 and SMAD4 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12393497}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6KAS7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6KAS7-2; Sequence=VSP_028553;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed in all B-cell stages.
CC {ECO:0000269|PubMed:12393497}.
CC -!- DOMAIN: Uses different DNA- and protein-binding zinc fingers to
CC regulate the distinct BMP-Smad and hematopoietic system. {ECO:0000250}.
CC -!- DISEASE: Note=Defects in Znf521 are a cause of B-cell lymphomas. The
CC Znf521 gene is a frequent target of retroviral integration in murine B-
CC cell lymphomas. Involved in most B-cell tumors in the AKXD-27 strain.
CC Viral insertion into the Znf521 gene in the AKXD-27 strain causes
CC Znf521 overexpression in B-cell tumors, resulting in the up-regulation
CC of EBF1 and the increased expression of a number of EBF1 target genes.
CC This in contrast to the role of Znf521 in other cells as a
CC transcriptional repressor of EBF1. Misexpression initiates
CC tumorigenesis by perturbing B-cell development via an interaction with
CC EBF1. {ECO:0000269|PubMed:12393497, ECO:0000269|PubMed:15580294}.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC36964.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD21380.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY147406; AAN39839.1; -; mRNA.
DR EMBL; AK131130; BAD21380.1; ALT_INIT; mRNA.
DR EMBL; BC021376; AAH21376.1; -; mRNA.
DR EMBL; AK077697; BAC36964.1; ALT_INIT; mRNA.
DR EMBL; AK081096; BAC38132.1; -; mRNA.
DR CCDS; CCDS37740.1; -. [Q6KAS7-1]
DR RefSeq; NP_663467.1; NM_145492.4. [Q6KAS7-1]
DR AlphaFoldDB; Q6KAS7; -.
DR BioGRID; 230369; 4.
DR IntAct; Q6KAS7; 1.
DR STRING; 10090.ENSMUSP00000025288; -.
DR GlyConnect; 2829; 5 N-Linked glycans (3 sites).
DR GlyGen; Q6KAS7; 3 sites, 5 N-linked glycans (3 sites).
DR iPTMnet; Q6KAS7; -.
DR PhosphoSitePlus; Q6KAS7; -.
DR MaxQB; Q6KAS7; -.
DR PaxDb; Q6KAS7; -.
DR PeptideAtlas; Q6KAS7; -.
DR PRIDE; Q6KAS7; -.
DR ProteomicsDB; 302085; -. [Q6KAS7-1]
DR ProteomicsDB; 302086; -. [Q6KAS7-2]
DR Antibodypedia; 7815; 204 antibodies from 23 providers.
DR DNASU; 225207; -.
DR Ensembl; ENSMUST00000025288; ENSMUSP00000025288; ENSMUSG00000024420. [Q6KAS7-1]
DR Ensembl; ENSMUST00000234410; ENSMUSP00000157321; ENSMUSG00000024420. [Q6KAS7-1]
DR GeneID; 225207; -.
DR KEGG; mmu:225207; -.
DR UCSC; uc008edc.1; mouse. [Q6KAS7-1]
DR CTD; 225207; -.
DR MGI; MGI:95459; Zfp521.
DR VEuPathDB; HostDB:ENSMUSG00000024420; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000159287; -.
DR HOGENOM; CLU_004018_0_0_1; -.
DR InParanoid; Q6KAS7; -.
DR OMA; LACMYCT; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q6KAS7; -.
DR TreeFam; TF331504; -.
DR BioGRID-ORCS; 225207; 6 hits in 76 CRISPR screens.
DR ChiTaRS; Zfp521; mouse.
DR PRO; PR:Q6KAS7; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; Q6KAS7; protein.
DR Bgee; ENSMUSG00000024420; Expressed in secondary palatal shelf and 232 other tissues.
DR ExpressionAtlas; Q6KAS7; baseline and differential.
DR Genevisible; Q6KAS7; MM.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0048663; P:neuron fate commitment; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF00096; zf-C2H2; 3.
DR SMART; SM00355; ZnF_C2H2; 30.
DR SUPFAM; SSF57667; SSF57667; 10.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 27.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 24.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Developmental protein; Differentiation;
KW DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..1311
FT /note="Zinc finger protein 521"
FT /id="PRO_0000306872"
FT ZN_FING 47..67
FT /note="C2H2-type 1; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 118..140
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 146..168
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 174..196
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 202..224
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 246..269
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 281..304
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 310..332
FT /note="C2H2-type 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 405..429
FT /note="C2H2-type 9; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 437..460
FT /note="C2H2-type 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 477..500
FT /note="C2H2-type 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 513..536
FT /note="C2H2-type 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 560..585
FT /note="C2H2-type 13; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 634..656
FT /note="C2H2-type 14"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 664..686
FT /note="C2H2-type 15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 694..717
FT /note="C2H2-type 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 722..745
FT /note="C2H2-type 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 752..775
FT /note="C2H2-type 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 783..805
FT /note="C2H2-type 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 809..832
FT /note="C2H2-type 20"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 886..908
FT /note="C2H2-type 21; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 930..952
FT /note="C2H2-type 22"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 959..981
FT /note="C2H2-type 23"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1020..1042
FT /note="C2H2-type 24"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1065..1083
FT /note="C2H2-type 25; degenerate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1138..1161
FT /note="C2H2-type 26"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1195..1217
FT /note="C2H2-type 27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1225..1247
FT /note="C2H2-type 28"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1256..1279
FT /note="C2H2-type 29"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1286..1309
FT /note="C2H2-type 30"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 81..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 863..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1105..1136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 546
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96K83"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 608
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 1146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q96K83"
FT VAR_SEQ 1191..1192
FT /note="EK -> G (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_028553"
FT CONFLICT 595
FT /note="I -> T (in Ref. 1; AAN39839)"
FT /evidence="ECO:0000305"
FT CONFLICT 771
FT /note="V -> L (in Ref. 4; BAC38132)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="M -> T (in Ref. 1; AAN39839)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1311 AA; 147666 MW; C8D922B5335C099A CRC64;
MSRRKQAKPR SLKDPNCKLE DKIEDGEAVD CKKRPEDGEE LEEDAVHSCD SCLQVFESLS
DITEHKIHQC QLTDGVDVED DPSCSWPASS PSSKDQTSPS HGEGCDFGEE EGGPGLPYPC
QFCDKSFSRL SYLKHHEQSH SDKLPFKCTY CSRLFKHKRS RDRHIKLHTG DKKYHCSECD
AAFSRSDHLK IHLKTHTSNK PYKCAVCRRG FLSSSSLHGH MQVHERNKDG SQSGSRMEDW
KMKDTQKCSQ CEEGFDFPED LQKHIAECHP ECSPNEDRAA LQCMYCHELF VEETSLMNHI
EQVHGGEKKN SCSICSESFL TVEELYSHMD SHQQPESCNH SNSPSLVTVG YTSVSSTTPD
SNLSVDSSTM VEAAPPIPKS RGRKRAAQQT SDMTGPSSKQ AKVTYSCIYC NKQLFSSLAV
LQIHLKTMHL DKPEQAHICQ YCLEVLPSLY NLNEHLKQVH EAQDPGLIVS AMPAIVYQCN
FCSEVVNDLN TLQEHIRCSH GFANPAAKDS NAFFCPHCYM GFLTDSSLEE HIRQVHCDLS
GSRFGSPVLG TPKEPVVEVY SCSYCTNSPI FNSVLKLNKH IKENHKNIPL ALNYIHNGKK
SRALSPLSPV AIEQTTLKMM QTVGGGPARA SGEYICNQCG AKYTSLDSFQ THLKTHLDTV
LPKLTCPQCN KEFPNQESLL KHVTIHFMIT STYYICESCD KQFTSVDDLQ KHLLDMHTFV
FFRCTLCQEV FDSKVSIQLH LAVKHSNEKK VYRCTSCNWD FRNETDLQLH VKHNHLENQG
KVHKCIFCGE SFGTEVELQC HITTHSKKYN CRFCSKAFHA VILLEKHLRE KHCVFETKTP
NCGTNGASEQ VQKEEAELQT LLTNSQESHN SHDGSEEDVD SSEPMYGCDI CGAAYTMETL
LQNHQLRDHN IRPGESAIVK KKAELIKGNY KCNVCSRTFF SENGLREHMQ THLGPVKHYM
CPICGERFPS LLTLTEHKVT HSKSLDTGNC RICKMPLQSE EEFLEHCQMH PDLRNSLTGF
RCVVCMQTVT STLELKIHGT FHMQKTGNGS SVQTTGRGQH VQKLYKCASC LKEFRSKQDL
VKLDINGLPY GLCAGCVNLS KSSSPGLSLP PGASRPGLGQ NESLSAMEGK GKAGGLKTRC
SSCNVKFESE SELQNHIQTV HRELVPDANS TQLKTPQVSP MPRISPSQSD EKKTYQCIKC
QMVFYNEWDI QVHVANHMID EGLNHECKLC SQTFDSPAKL QCHLIEHSFE GMGGTFKCPV
CFTVFVQANK LQQHIFSAHG QEDKIYDCTQ CPQKFFFQTE LQNHTMTQHS S
