ID DTX2_HUMAN Reviewed; 622 AA.
AC Q86UW9; Q4ZH49; Q6XM87; Q6XM88; Q96H69; Q9H890; Q9P200;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 3.
DT 27-MAR-2024, entry version 176.
DE RecName: Full=Probable E3 ubiquitin-protein ligase DTX2;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE AltName: Full=Protein deltex-2;
DE Short=Deltex2;
DE Short=hDTX2;
DE AltName: Full=RING finger protein 58;
DE AltName: Full=RING-type E3 ubiquitin transferase DTX2 {ECO:0000305};
GN Name=DTX2; Synonyms=KIAA1528, RNF58;
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 [MRNA], ALTERNATIVE SPLICING (ISOFORMS 1 AND 2),
RP VARIANT GLU-384, SUBUNIT, AND IN VITRO UBIQUITIN LIGASE ACTIVITY.
RX PubMed=12670957; DOI=10.1074/jbc.m301157200;
RA Takeyama K., Aguiar R.C.T., Gu L., He C., Freeman G.J., Kutok J.L.,
RA Aster J.C., Shipp M.A.;
RT "The BAL-binding protein BBAP and related Deltex family members exhibit
RT ubiquitin-protein isopeptide ligase activity.";
RL J. Biol. Chem. 278:21930-21937(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-421.
RA Yi Z., Yi T., Wu Z.;
RT "cDNA cloning, characterization and expression analysis of DTX2, a human
RT WWE and RING-finger gene, in human embryos.";
RL DNA Seq. 17:175-180(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS GLU-384
RP AND ALA-421.
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT ALA-421.
RC TISSUE=Thyroid;
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 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-384.
RC TISSUE=Brain, Lymph, and Muscle;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=11564735; DOI=10.1074/jbc.m105245200;
RA Yamamoto N., Yamamoto S., Inagaki F., Kawaichi M., Fukamizu A., Kishi N.,
RA Matsuno K., Nakamura K., Weinmaster G., Okano H., Nakafuku M.;
RT "Role of Deltex-1 as a transcriptional regulator downstream of the Notch
RT receptor.";
RL J. Biol. Chem. 276:45031-45040(2001).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-249, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-213; ARG-215; ARG-233 AND
RP ARG-256, AND IDENTIFICATION BY MASS 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: Regulator of Notch signaling, a signaling pathway involved in
CC cell-cell communications that regulates a broad spectrum of cell-fate
CC determinations. Probably acts both as a positive and negative regulator
CC of Notch, depending on the developmental and cell context. Mediates the
CC antineural activity of Notch, possibly by inhibiting the
CC transcriptional activation mediated by MATCH1. Functions as a ubiquitin
CC ligase protein in vitro, suggesting that it may regulate the Notch
CC pathway via some ubiquitin ligase activity.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.27; Evidence={ECO:0000250|UniProtKB:Q61010};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBUNIT: Homodimer. May form a heterodimer with other members of the
CC Deltex family. Interacts with NOTCH1. {ECO:0000250|UniProtKB:Q61010}.
CC -!- INTERACTION:
CC Q86UW9; Q8NFV4-4: ABHD11; NbExp=3; IntAct=EBI-740376, EBI-12318443;
CC Q86UW9; O95870: ABHD16A; NbExp=7; IntAct=EBI-740376, EBI-348517;
CC Q86UW9; Q5BKX5-3: ACTMAP; NbExp=3; IntAct=EBI-740376, EBI-11976299;
CC Q86UW9; Q9NXW9: ALKBH4; NbExp=11; IntAct=EBI-740376, EBI-8637516;
CC Q86UW9; Q9NYG5-2: ANAPC11; NbExp=3; IntAct=EBI-740376, EBI-12224467;
CC Q86UW9; Q9BQD7: ANTKMT; NbExp=3; IntAct=EBI-740376, EBI-713602;
CC Q86UW9; Q03989: ARID5A; NbExp=3; IntAct=EBI-740376, EBI-948603;
CC Q86UW9; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-740376, EBI-742909;
CC Q86UW9; Q9HBZ2: ARNT2; NbExp=4; IntAct=EBI-740376, EBI-765971;
CC Q86UW9; O43521: BCL2L11; NbExp=3; IntAct=EBI-740376, EBI-526406;
CC Q86UW9; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-740376, EBI-1012434;
CC Q86UW9; A0A0B4J295: BOLA2-SMG1P6; NbExp=3; IntAct=EBI-740376, EBI-12906362;
CC Q86UW9; Q5SWW7: C10orf55; NbExp=3; IntAct=EBI-740376, EBI-12809220;
CC Q86UW9; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-740376, EBI-946029;
CC Q86UW9; Q6P5X5: C22orf39; NbExp=5; IntAct=EBI-740376, EBI-7317823;
CC Q86UW9; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-740376, EBI-10961624;
CC Q86UW9; Q9H5F2: CFAP68; NbExp=3; IntAct=EBI-740376, EBI-718615;
CC Q86UW9; Q9H1P6: CIMIP1; NbExp=3; IntAct=EBI-740376, EBI-12155483;
CC Q86UW9; Q16740: CLPP; NbExp=5; IntAct=EBI-740376, EBI-1056029;
CC Q86UW9; Q5JTJ3: COA6; NbExp=3; IntAct=EBI-740376, EBI-2874677;
CC Q86UW9; Q8NI60: COQ8A; NbExp=3; IntAct=EBI-740376, EBI-745535;
CC Q86UW9; Q15038: DAZAP2; NbExp=3; IntAct=EBI-740376, EBI-724310;
CC Q86UW9; Q7L591-3: DOK3; NbExp=3; IntAct=EBI-740376, EBI-10694655;
CC Q86UW9; Q16610: ECM1; NbExp=3; IntAct=EBI-740376, EBI-947964;
CC Q86UW9; Q9BQ95: ECSIT; NbExp=3; IntAct=EBI-740376, EBI-712452;
CC Q86UW9; Q9NRA8: EIF4ENIF1; NbExp=7; IntAct=EBI-740376, EBI-301024;
CC Q86UW9; Q04637-9: EIF4G1; NbExp=3; IntAct=EBI-740376, EBI-12012124;
CC Q86UW9; O00167-2: EYA2; NbExp=3; IntAct=EBI-740376, EBI-12807776;
CC Q86UW9; Q92567: FAM168A; NbExp=6; IntAct=EBI-740376, EBI-7957930;
CC Q86UW9; Q92567-2: FAM168A; NbExp=3; IntAct=EBI-740376, EBI-11978259;
CC Q86UW9; Q96PJ5: FCRL4; NbExp=3; IntAct=EBI-740376, EBI-4314687;
CC Q86UW9; Q14192: FHL2; NbExp=6; IntAct=EBI-740376, EBI-701903;
CC Q86UW9; Q5TD97: FHL5; NbExp=3; IntAct=EBI-740376, EBI-750641;
CC Q86UW9; Q12951-2: FOXI1; NbExp=3; IntAct=EBI-740376, EBI-12018822;
CC Q86UW9; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-740376, EBI-18138793;
CC Q86UW9; Q8IVS8: GLYCTK; NbExp=6; IntAct=EBI-740376, EBI-748515;
CC Q86UW9; Q08379: GOLGA2; NbExp=3; IntAct=EBI-740376, EBI-618309;
CC Q86UW9; P19113: HDC; NbExp=6; IntAct=EBI-740376, EBI-10200283;
CC Q86UW9; O14964: HGS; NbExp=3; IntAct=EBI-740376, EBI-740220;
CC Q86UW9; Q14774: HLX; NbExp=3; IntAct=EBI-740376, EBI-6678255;
CC Q86UW9; P49639: HOXA1; NbExp=6; IntAct=EBI-740376, EBI-740785;
CC Q86UW9; P14652: HOXB2; NbExp=3; IntAct=EBI-740376, EBI-5329558;
CC Q86UW9; P35452-2: HOXD12; NbExp=3; IntAct=EBI-740376, EBI-17244356;
CC Q86UW9; P84074: HPCA; NbExp=3; IntAct=EBI-740376, EBI-12197079;
CC Q86UW9; P37235: HPCAL1; NbExp=4; IntAct=EBI-740376, EBI-749311;
CC Q86UW9; Q9UM19: HPCAL4; NbExp=7; IntAct=EBI-740376, EBI-744820;
CC Q86UW9; Q96LI6: HSFY2; NbExp=3; IntAct=EBI-740376, EBI-3957665;
CC Q86UW9; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-740376, EBI-747204;
CC Q86UW9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-740376, EBI-2556193;
CC Q86UW9; Q6P597: KLC3; NbExp=6; IntAct=EBI-740376, EBI-1643885;
CC Q86UW9; Q96G42: KLHDC7B; NbExp=3; IntAct=EBI-740376, EBI-9478422;
CC Q86UW9; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-740376, EBI-1052037;
CC Q86UW9; Q3SY46: KRTAP13-3; NbExp=3; IntAct=EBI-740376, EBI-10241252;
CC Q86UW9; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-740376, EBI-11992140;
CC Q86UW9; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-740376, EBI-12811111;
CC Q86UW9; Q3LI70: KRTAP19-6; NbExp=3; IntAct=EBI-740376, EBI-12805508;
CC Q86UW9; Q3SYF9: KRTAP19-7; NbExp=3; IntAct=EBI-740376, EBI-10241353;
CC Q86UW9; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-740376, EBI-3957672;
CC Q86UW9; Q3LI64: KRTAP6-1; NbExp=3; IntAct=EBI-740376, EBI-12111050;
CC Q86UW9; Q8IUC3: KRTAP7-1; NbExp=3; IntAct=EBI-740376, EBI-18394498;
CC Q86UW9; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-740376, EBI-10261141;
CC Q86UW9; Q14847-2: LASP1; NbExp=3; IntAct=EBI-740376, EBI-9088686;
CC Q86UW9; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740376, EBI-739832;
CC Q86UW9; Q9P2M1: LRP2BP; NbExp=3; IntAct=EBI-740376, EBI-18273118;
CC Q86UW9; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-740376, EBI-12516603;
CC Q86UW9; A0JLT2-2: MED19; NbExp=3; IntAct=EBI-740376, EBI-13288755;
CC Q86UW9; Q4VC12: MSS51; NbExp=3; IntAct=EBI-740376, EBI-11599933;
CC Q86UW9; Q14764: MVP; NbExp=3; IntAct=EBI-740376, EBI-2816254;
CC Q86UW9; Q9BRK3: MXRA8; NbExp=3; IntAct=EBI-740376, EBI-11721798;
CC Q86UW9; P61601: NCALD; NbExp=12; IntAct=EBI-740376, EBI-749635;
CC Q86UW9; P62166: NCS1; NbExp=13; IntAct=EBI-740376, EBI-746987;
CC Q86UW9; P0CG21: NHLRC4; NbExp=3; IntAct=EBI-740376, EBI-12868744;
CC Q86UW9; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-740376, EBI-740897;
CC Q86UW9; O00746: NME4; NbExp=3; IntAct=EBI-740376, EBI-744871;
CC Q86UW9; O43482: OIP5; NbExp=3; IntAct=EBI-740376, EBI-536879;
CC Q86UW9; Q02548: PAX5; NbExp=3; IntAct=EBI-740376, EBI-296331;
CC Q86UW9; Q9H8W4: PLEKHF2; NbExp=3; IntAct=EBI-740376, EBI-742388;
CC Q86UW9; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-740376, EBI-949255;
CC Q86UW9; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-740376, EBI-1389308;
CC Q86UW9; B1ATL7: PRR32; NbExp=3; IntAct=EBI-740376, EBI-18587059;
CC Q86UW9; Q9NV39: PRR34; NbExp=3; IntAct=EBI-740376, EBI-11959565;
CC Q86UW9; P28070: PSMB4; NbExp=3; IntAct=EBI-740376, EBI-603350;
CC Q86UW9; P47897-2: QARS1; NbExp=3; IntAct=EBI-740376, EBI-10209725;
CC Q86UW9; P57052: RBM11; NbExp=3; IntAct=EBI-740376, EBI-741332;
CC Q86UW9; Q93062: RBPMS; NbExp=7; IntAct=EBI-740376, EBI-740322;
CC Q86UW9; Q8HWS3: RFX6; NbExp=4; IntAct=EBI-740376, EBI-746118;
CC Q86UW9; Q9UFD9: RIMBP3; NbExp=3; IntAct=EBI-740376, EBI-10182375;
CC Q86UW9; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-740376, EBI-6257312;
CC Q86UW9; Q7Z5V6-2: SAXO4; NbExp=3; IntAct=EBI-740376, EBI-12000762;
CC Q86UW9; Q96IW7: SEC22A; NbExp=10; IntAct=EBI-740376, EBI-8652744;
CC Q86UW9; Q15436: SEC23A; NbExp=3; IntAct=EBI-740376, EBI-81088;
CC Q86UW9; Q15437: SEC23B; NbExp=6; IntAct=EBI-740376, EBI-742673;
CC Q86UW9; Q9HD40-3: SEPSECS; NbExp=3; IntAct=EBI-740376, EBI-12190001;
CC Q86UW9; Q8N1D0-2: SLC22A18AS; NbExp=3; IntAct=EBI-740376, EBI-12829638;
CC Q86UW9; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-740376, EBI-12288855;
CC Q86UW9; Q99932: SPAG8; NbExp=3; IntAct=EBI-740376, EBI-954419;
CC Q86UW9; Q9NZD8: SPG21; NbExp=7; IntAct=EBI-740376, EBI-742688;
CC Q86UW9; Q86Y82: STX12; NbExp=7; IntAct=EBI-740376, EBI-2691717;
CC Q86UW9; P63165: SUMO1; NbExp=3; IntAct=EBI-740376, EBI-80140;
CC Q86UW9; Q96SF7: TBX15; NbExp=3; IntAct=EBI-740376, EBI-10191361;
CC Q86UW9; Q96M29: TEKT5; NbExp=3; IntAct=EBI-740376, EBI-10239812;
CC Q86UW9; Q6PIY7: TENT2; NbExp=3; IntAct=EBI-740376, EBI-2802204;
CC Q86UW9; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-740376, EBI-12038591;
CC Q86UW9; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-740376, EBI-492476;
CC Q86UW9; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-740376, EBI-17716262;
CC Q86UW9; Q9BYV2: TRIM54; NbExp=9; IntAct=EBI-740376, EBI-2130429;
CC Q86UW9; Q15654: TRIP6; NbExp=3; IntAct=EBI-740376, EBI-742327;
CC Q86UW9; P51668: UBE2D1; NbExp=7; IntAct=EBI-740376, EBI-743540;
CC Q86UW9; P62837: UBE2D2; NbExp=3; IntAct=EBI-740376, EBI-347677;
CC Q86UW9; P61077: UBE2D3; NbExp=9; IntAct=EBI-740376, EBI-348268;
CC Q86UW9; Q9Y2X8: UBE2D4; NbExp=13; IntAct=EBI-740376, EBI-745527;
CC Q86UW9; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-740376, EBI-11975223;
CC Q86UW9; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-740376, EBI-11957216;
CC Q86UW9; P62760: VSNL1; NbExp=10; IntAct=EBI-740376, EBI-740943;
CC Q86UW9; Q96F45: ZNF503; NbExp=3; IntAct=EBI-740376, EBI-8832437;
CC Q86UW9; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-740376, EBI-4395669;
CC Q86UW9; Q96H86: ZNF764; NbExp=3; IntAct=EBI-740376, EBI-745775;
CC Q86UW9; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-740376, EBI-10251462;
CC Q86UW9; Q49A12: ZNF85; NbExp=3; IntAct=EBI-740376, EBI-18141506;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11564735}. Nucleus
CC {ECO:0000269|PubMed:11564735}. Note=Predominantly cytoplasmic.
CC Partially nuclear. {ECO:0000269|PubMed:11564735}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=A;
CC IsoId=Q86UW9-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=Q86UW9-2; Sequence=VSP_008350;
CC -!- DOMAIN: The WWE domains are thought to mediate some protein-protein
CC interaction, and are frequently found in ubiquitin ligases.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA96052.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY225124; AAP57518.1; -; mRNA.
DR EMBL; AY225125; AAP57519.1; -; mRNA.
DR EMBL; DQ010329; AAY27263.1; -; mRNA.
DR EMBL; AB040961; BAA96052.1; ALT_INIT; mRNA.
DR EMBL; AK023924; BAB14727.1; -; mRNA.
DR EMBL; AC005522; AAP21881.1; -; Genomic_DNA.
DR EMBL; AC007078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008856; AAH08856.1; -; mRNA.
DR EMBL; BC018555; AAH18555.1; -; mRNA.
DR EMBL; BC026059; AAH26059.1; -; mRNA.
DR EMBL; BC093079; AAH93079.1; -; mRNA.
DR CCDS; CCDS43605.1; -. [Q86UW9-2]
DR CCDS; CCDS5587.1; -. [Q86UW9-1]
DR RefSeq; NP_001096064.1; NM_001102594.1. [Q86UW9-1]
DR RefSeq; NP_001096065.1; NM_001102595.1. [Q86UW9-1]
DR RefSeq; NP_001096066.1; NM_001102596.1. [Q86UW9-2]
DR RefSeq; NP_065943.2; NM_020892.2. [Q86UW9-1]
DR RefSeq; XP_005250188.1; XM_005250131.1.
DR RefSeq; XP_005250189.1; XM_005250132.1.
DR RefSeq; XP_011514074.1; XM_011515772.1.
DR RefSeq; XP_011514075.1; XM_011515773.2.
DR RefSeq; XP_011514076.1; XM_011515774.1. [Q86UW9-1]
DR RefSeq; XP_011514077.1; XM_011515775.1.
DR RefSeq; XP_016867212.1; XM_017011723.1.
DR RefSeq; XP_016867213.1; XM_017011724.1. [Q86UW9-1]
DR RefSeq; XP_016867214.1; XM_017011725.1.
DR RefSeq; XP_016867215.1; XM_017011726.1. [Q86UW9-2]
DR RefSeq; XP_016867216.1; XM_017011727.1.
DR PDB; 6IR0; NMR; -; A=399-474.
DR PDB; 6Y22; X-ray; 2.07 A; A=390-622.
DR PDB; 6Y2X; X-ray; 1.77 A; A/B=390-622.
DR PDB; 6Y3J; X-ray; 2.60 A; A=390-622.
DR PDBsum; 6IR0; -.
DR PDBsum; 6Y22; -.
DR PDBsum; 6Y2X; -.
DR PDBsum; 6Y3J; -.
DR AlphaFoldDB; Q86UW9; -.
DR SMR; Q86UW9; -.
DR BioGRID; 125266; 331.
DR IntAct; Q86UW9; 124.
DR MINT; Q86UW9; -.
DR STRING; 9606.ENSP00000322885; -.
DR GlyGen; Q86UW9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86UW9; -.
DR PhosphoSitePlus; Q86UW9; -.
DR BioMuta; DTX2; -.
DR DMDM; 68067880; -.
DR EPD; Q86UW9; -.
DR jPOST; Q86UW9; -.
DR MassIVE; Q86UW9; -.
DR MaxQB; Q86UW9; -.
DR PaxDb; 9606-ENSP00000322885; -.
DR PeptideAtlas; Q86UW9; -.
DR ProteomicsDB; 69923; -. [Q86UW9-1]
DR ProteomicsDB; 69924; -. [Q86UW9-2]
DR Pumba; Q86UW9; -.
DR Antibodypedia; 35109; 221 antibodies from 31 providers.
DR DNASU; 113878; -.
DR Ensembl; ENST00000324432.9; ENSP00000322885.5; ENSG00000091073.20. [Q86UW9-1]
DR Ensembl; ENST00000413936.6; ENSP00000390218.2; ENSG00000091073.20. [Q86UW9-1]
DR Ensembl; ENST00000430490.7; ENSP00000411986.2; ENSG00000091073.20. [Q86UW9-1]
DR Ensembl; ENST00000446820.6; ENSP00000392545.2; ENSG00000091073.20. [Q86UW9-2]
DR GeneID; 113878; -.
DR KEGG; hsa:113878; -.
DR MANE-Select; ENST00000430490.7; ENSP00000411986.2; NM_001102594.3; NP_001096064.1.
DR UCSC; uc003uff.5; human. [Q86UW9-1]
DR AGR; HGNC:15973; -.
DR CTD; 113878; -.
DR DisGeNET; 113878; -.
DR GeneCards; DTX2; -.
DR HGNC; HGNC:15973; DTX2.
DR HPA; ENSG00000091073; Tissue enhanced (esophagus).
DR MIM; 613141; gene.
DR neXtProt; NX_Q86UW9; -.
DR OpenTargets; ENSG00000091073; -.
DR PharmGKB; PA27515; -.
DR VEuPathDB; HostDB:ENSG00000091073; -.
DR eggNOG; ENOG502QQ9M; Eukaryota.
DR GeneTree; ENSGT00940000157641; -.
DR HOGENOM; CLU_030422_4_0_1; -.
DR InParanoid; Q86UW9; -.
DR OMA; DAPEEDC; -.
DR OrthoDB; 5487971at2759; -.
DR PhylomeDB; Q86UW9; -.
DR PathwayCommons; Q86UW9; -.
DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR SignaLink; Q86UW9; -.
DR SIGNOR; Q86UW9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 113878; 35 hits in 1197 CRISPR screens.
DR ChiTaRS; DTX2; human.
DR GeneWiki; DTX2; -.
DR GenomeRNAi; 113878; -.
DR Pharos; Q86UW9; Tbio.
DR PRO; PR:Q86UW9; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q86UW9; Protein.
DR Bgee; ENSG00000091073; Expressed in lower esophagus mucosa and 96 other cell types or tissues.
DR ExpressionAtlas; Q86UW9; baseline and differential.
DR Genevisible; Q86UW9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0007219; P:Notch signaling pathway; IBA:GO_Central.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR CDD; cd09633; Deltex_C; 1.
DR CDD; cd16672; RING-H2_DTX2; 1.
DR Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.720.50; -; 2.
DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR InterPro; IPR018957; Znf_C3HC4_RING-type.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR PANTHER; PTHR12622; DELTEX-RELATED; 1.
DR PANTHER; PTHR12622:SF21; E3 UBIQUITIN-PROTEIN LIGASE DTX2-RELATED; 1.
DR Pfam; PF18102; DTC; 1.
DR Pfam; PF02825; WWE; 2.
DR Pfam; PF00097; zf-C3HC4; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00678; WWE; 2.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF117839; WWE domain; 2.
DR PROSITE; PS50918; WWE; 2.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm; Metal-binding;
KW Methylation; Notch signaling pathway; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..622
FT /note="Probable E3 ubiquitin-protein ligase DTX2"
FT /id="PRO_0000219083"
FT DOMAIN 8..97
FT /note="WWE 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT DOMAIN 98..174
FT /note="WWE 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00248"
FT ZN_FING 412..473
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 249..324
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 215
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 233
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 249
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 256
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 337..383
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_008350"
FT VARIANT 94
FT /note="A -> T (in dbSNP:rs2462312)"
FT /id="VAR_016920"
FT VARIANT 384
FT /note="G -> E (in dbSNP:rs1638152)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:12670957, ECO:0000269|PubMed:15489334"
FT /id="VAR_016921"
FT VARIANT 421
FT /note="T -> A (in dbSNP:rs6979487)"
FT /evidence="ECO:0000269|PubMed:10819331,
FT ECO:0000269|PubMed:14702039, ECO:0000269|Ref.2"
FT /id="VAR_016922"
FT HELIX 393..399
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 401..403
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:6Y22"
FT TURN 413..415
FT /evidence="ECO:0007829|PDB:6Y2X"
FT TURN 419..421
FT /evidence="ECO:0007829|PDB:6IR0"
FT TURN 424..428
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 439..442
FT /evidence="ECO:0007829|PDB:6Y2X"
FT TURN 443..445
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 448..450
FT /evidence="ECO:0007829|PDB:6Y2X"
FT HELIX 451..457
FT /evidence="ECO:0007829|PDB:6Y2X"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:6IR0"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:6IR0"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 487..494
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 505..511
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 521..523
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 526..529
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 534..542
FT /evidence="ECO:0007829|PDB:6Y2X"
FT HELIX 543..557
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:6Y2X"
FT TURN 568..570
FT /evidence="ECO:0007829|PDB:6Y2X"
FT STRAND 573..578
FT /evidence="ECO:0007829|PDB:6Y2X"
FT TURN 589..592
FT /evidence="ECO:0007829|PDB:6Y2X"
FT HELIX 601..611
FT /evidence="ECO:0007829|PDB:6Y2X"
FT HELIX 616..619
FT /evidence="ECO:0007829|PDB:6Y2X"
SQ SEQUENCE 622 AA; 67246 MW; ABE1398204F2273A CRC64;
MAMAPSPSLV QVYTSPAAVA VWEWQDGLGT WHPYSATVCS FIEQQFVQQK GQRFGLGSLA
HSIPLGQADP SLAPYIIDLP SWTQFRQDTG TMRAVRRHLF PQHSAPGRGV VWEWLSDDGS
WTAYEASVCD YLEQQVARGN QLVDLAPLGY NYTVNYTTHT QTNKTSSFCR SVRRQAGPPY
PVTTIIAPPG HTGVACSCHQ CLSGSRTGPV SGRYRHSMTN LPAYPVPQHP PHRTASVFGT
HQAFAPYNKP SLSGARSAPR LNTTNAWGAA PPSLGSQPLY RSSLSHLGPQ HLPPGSSTSG
AVSASLPSGP SSSPGSVPAT VPMQMPKPSR VQQALAGMTS VLMSAIGLPV CLSRAPQPTS
PPASRLASKS HGSVKRLRKM SVKGATPKPE PEPEQVIKNY TEELKVPPDE DCIICMEKLS
TASGYSDVTD SKAIGSLAVG HLTKCSHAFH LLCLLAMYCN GNKDGSLQCP SCKTIYGEKT
GTQPQGKMEV LRFQMSLPGH EDCGTILIVY SIPHGIQGPE HPNPGKPFTA RGFPRQCYLP
DNAQGRKVLE LLKVAWKRRL IFTVGTSSTT GETDTVVWNE IHHKTEMDRN ITGHGYPDPN
YLQNVLAELA AQGVTEDCLE QQ
//
