UBXN4_HUMAN
ID UBXN4_HUMAN Reviewed; 508 AA.
AC Q92575; A8K9W4; Q4ZG56; Q8IYM5;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=UBX domain-containing protein 4;
DE AltName: Full=Erasin;
DE AltName: Full=UBX domain-containing protein 2;
GN Name=UBXN4; Synonyms=KIAA0242, UBXD2, UBXDC1;
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].
RC TISSUE=Trachea;
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 [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION
RP WITH VCP, TISSUE SPECIFICITY, INDUCTION, AND DOMAIN UBX AND INTRAMEMBRANE
RP DOMAIN.
RX PubMed=16968747; DOI=10.1242/jcs.03163;
RA Liang J., Yin C., Doong H., Fang S., Peterhoff C., Nixon R.A.,
RA Monteiro M.J.;
RT "Characterization of erasin (UBXD2): a new ER protein that promotes ER-
RT associated protein degradation.";
RL J. Cell Sci. 119:4011-4024(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=9039502; DOI=10.1093/dnares/3.5.321;
RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O.,
RA Tanaka A., Kotani H., Miyajima N., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. VI. The
RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of
RT cDNA clones from cell line KG-1 and brain.";
RL DNA Res. 3:321-329(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Fetal skin;
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-489, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [9]
RP FUNCTION, AND INTERACTION WITH UBQLN1 AND VCP.
RX PubMed=19822669; DOI=10.1083/jcb.200903024;
RA Lim P.J., Danner R., Liang J., Doong H., Harman C., Srinivasan D.,
RA Rothenberg C., Wang H., Ye Y., Fang S., Monteiro M.J.;
RT "Ubiquilin and p97/VCP bind erasin, forming a complex involved in ERAD.";
RL J. Cell Biol. 187:201-217(2009).
RN [10]
RP IDENTIFICATION BY MASS 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).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-489, AND IDENTIFICATION BY
RP 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 [12]
RP IDENTIFICATION BY 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [14]
RP STRUCTURE BY NMR OF 317-397.
RA Wu Q., Huang H., Zhang J., Hu Q., Wu J., Shi Y.;
RT "Solution strcture of UBX domain of human UBXD2 protein.";
RL Submitted (MAY-2011) to the PDB data bank.
CC -!- FUNCTION: Involved in endoplasmic reticulum-associated protein
CC degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP
CC to the ER during ERAD (PubMed:19822669). {ECO:0000269|PubMed:16968747,
CC ECO:0000269|PubMed:19822669}.
CC -!- SUBUNIT: Directly interacts with VCP. Interacts with UBQLN1. Forms a
CC complex with VCP and UBQLN1. {ECO:0000269|PubMed:16968747,
CC ECO:0000269|PubMed:19822669}.
CC -!- INTERACTION:
CC Q92575; P63211: GNGT1; NbExp=3; IntAct=EBI-723441, EBI-10220715;
CC Q92575; Q14139: UBE4A; NbExp=2; IntAct=EBI-723441, EBI-1048119;
CC Q92575; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-723441, EBI-741480;
CC Q92575; Q9UMX0-2: UBQLN1; NbExp=3; IntAct=EBI-723441, EBI-10173939;
CC Q92575; P55072: VCP; NbExp=11; IntAct=EBI-723441, EBI-355164;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:16968747}; Peripheral membrane protein
CC {ECO:0000269|PubMed:16968747}. Nucleus envelope
CC {ECO:0000269|PubMed:16968747}. Note=Both the N- and the C-terminus face
CC the cytosol. Also found in the nucleus envelope contiguous to the ER.
CC {ECO:0000269|PubMed:16968747}.
CC -!- TISSUE SPECIFICITY: Expressed in many tissues, including heart, brain,
CC placenta, lung, liver, skeletal muscle, kidney and pancreas.
CC Accumulates in Alzheimer disease-afflicted brains (at protein level).
CC {ECO:0000269|PubMed:16968747}.
CC -!- INDUCTION: By ER stress-inducing agents such as tunicamycin,
CC thapsigargin, DTT and the calcium ionophore A23187 (at protein level).
CC {ECO:0000269|PubMed:16968747}.
CC -!- DOMAIN: The UBX domain is required for interaction with VCP.
CC {ECO:0000269|PubMed:16968747}.
CC -!- DOMAIN: The intramembrane domain also contains the signal for ER
CC targeting. {ECO:0000269|PubMed:16968747}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA13437.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK292829; BAF85518.1; -; mRNA.
DR EMBL; EF199840; ABM90426.1; -; mRNA.
DR EMBL; D87684; BAA13437.1; ALT_INIT; mRNA.
DR EMBL; BX647662; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC011893; AAX88923.1; -; Genomic_DNA.
DR EMBL; CH471058; EAX11623.1; -; Genomic_DNA.
DR EMBL; BC035594; AAH35594.1; -; mRNA.
DR CCDS; CCDS42761.1; -.
DR RefSeq; NP_055422.1; NM_014607.3.
DR PDB; 2KXJ; NMR; -; A=317-397.
DR PDBsum; 2KXJ; -.
DR AlphaFoldDB; Q92575; -.
DR SMR; Q92575; -.
DR BioGRID; 116799; 160.
DR CORUM; Q92575; -.
DR IntAct; Q92575; 35.
DR MINT; Q92575; -.
DR STRING; 9606.ENSP00000272638; -.
DR GlyGen; Q92575; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92575; -.
DR PhosphoSitePlus; Q92575; -.
DR BioMuta; UBXN4; -.
DR DMDM; 30913402; -.
DR EPD; Q92575; -.
DR jPOST; Q92575; -.
DR MassIVE; Q92575; -.
DR MaxQB; Q92575; -.
DR PaxDb; Q92575; -.
DR PeptideAtlas; Q92575; -.
DR PRIDE; Q92575; -.
DR ProteomicsDB; 75336; -.
DR Antibodypedia; 33579; 100 antibodies from 25 providers.
DR DNASU; 23190; -.
DR Ensembl; ENST00000272638.14; ENSP00000272638.9; ENSG00000144224.17.
DR GeneID; 23190; -.
DR KEGG; hsa:23190; -.
DR MANE-Select; ENST00000272638.14; ENSP00000272638.9; NM_014607.4; NP_055422.1.
DR UCSC; uc002tur.4; human.
DR CTD; 23190; -.
DR DisGeNET; 23190; -.
DR GeneCards; UBXN4; -.
DR HGNC; HGNC:14860; UBXN4.
DR HPA; ENSG00000144224; Low tissue specificity.
DR MIM; 611216; gene.
DR neXtProt; NX_Q92575; -.
DR OpenTargets; ENSG00000144224; -.
DR PharmGKB; PA37912; -.
DR VEuPathDB; HostDB:ENSG00000144224; -.
DR eggNOG; KOG2507; Eukaryota.
DR GeneTree; ENSGT00940000160205; -.
DR HOGENOM; CLU_039222_1_1_1; -.
DR InParanoid; Q92575; -.
DR OMA; HNNTSEN; -.
DR OrthoDB; 1334491at2759; -.
DR PhylomeDB; Q92575; -.
DR TreeFam; TF317466; -.
DR PathwayCommons; Q92575; -.
DR SignaLink; Q92575; -.
DR BioGRID-ORCS; 23190; 202 hits in 1083 CRISPR screens.
DR ChiTaRS; UBXN4; human.
DR GeneWiki; UBXD2; -.
DR GenomeRNAi; 23190; -.
DR Pharos; Q92575; Tbio.
DR PRO; PR:Q92575; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q92575; protein.
DR Bgee; ENSG00000144224; Expressed in sperm and 208 other tissues.
DR ExpressionAtlas; Q92575; baseline and differential.
DR Genevisible; Q92575; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005635; C:nuclear envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0006986; P:response to unfolded protein; IEA:UniProtKB-KW.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; IMP:UniProtKB.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF52833; SSF52833; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein;
KW Reference proteome; Unfolded protein response.
FT CHAIN 1..508
FT /note="UBX domain-containing protein 4"
FT /id="PRO_0000211027"
FT TOPO_DOM 1..413
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 414..434
FT /evidence="ECO:0000255"
FT TOPO_DOM 435..508
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 315..393
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 1..200
FT /note="Interaction with UBQLN1"
FT /evidence="ECO:0000269|PubMed:19822669"
FT REGION 117..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..459
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..495
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 489
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 458
FT /note="S -> R (in dbSNP:rs2304602)"
FT /id="VAR_052686"
FT STRAND 318..325
FT /evidence="ECO:0007829|PDB:2KXJ"
FT STRAND 331..341
FT /evidence="ECO:0007829|PDB:2KXJ"
FT HELIX 343..353
FT /evidence="ECO:0007829|PDB:2KXJ"
FT STRAND 354..357
FT /evidence="ECO:0007829|PDB:2KXJ"
FT STRAND 362..367
FT /evidence="ECO:0007829|PDB:2KXJ"
FT HELIX 373..377
FT /evidence="ECO:0007829|PDB:2KXJ"
FT STRAND 378..380
FT /evidence="ECO:0007829|PDB:2KXJ"
FT HELIX 381..383
FT /evidence="ECO:0007829|PDB:2KXJ"
FT STRAND 389..393
FT /evidence="ECO:0007829|PDB:2KXJ"
SQ SEQUENCE 508 AA; 56778 MW; 2C3ABCF4D36124CC CRC64;
MLWFQGAIPA AIATAKRSGA VFVVFVAGDD EQSTQMAASW EDDKVTEASS NSFVAIKIDT
KSEACLQFSQ IYPVVCVPSS FFIGDSGIPL EVIAGSVSAD ELVTRIHKVR QMHLLKSETS
VANGSQSESS VSTPSASFEP NNTCENSQSR NAELCEIPPT SDTKSDTATG GESAGHATSS
QEPSGCSDQR PAEDLNIRVE RLTKKLEERR EEKRKEEEQR EIKKEIERRK TGKEMLDYKR
KQEEELTKRM LEERNREKAE DRAARERIKQ QIALDRAERA ARFAKTKEEV EAAKAAALLA
KQAEMEVKRE SYARERSTVA RIQFRLPDGS SFTNQFPSDA PLEEARQFAA QTVGNTYGNF
SLATMFPRRE FTKEDYKKKL LDLELAPSAS VVLLPAGRPT ASIVHSSSGD IWTLLGTVLY
PFLAIWRLIS NFLFSNPPPT QTSVRVTSSE PPNPASSSKS EKREPVRKRV LEKRGDDFKK
EGKIYRLRTQ DDGEDENNTW NGNSTQQM
