DTX3_HUMAN
ID DTX3_HUMAN Reviewed; 347 AA.
AC Q8N9I9; Q53ZZ2; Q8NAU6; Q8NDS8;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Probable E3 ubiquitin-protein ligase DTX3;
DE EC=2.3.2.27 {ECO:0000250|UniProtKB:Q61010};
DE AltName: Full=Protein deltex-3;
DE Short=Deltex3;
DE AltName: Full=RING finger protein 154;
DE AltName: Full=RING-type E3 ubiquitin transferase DTX3 {ECO:0000305};
GN Name=DTX3; Synonyms=RNF154;
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] (ISOFORM 1), IN VITRO UBIQUITIN LIGASE ACTIVITY,
RP AND SUBUNIT.
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Cerebellum, 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-201 (ISOFORM 1).
RC TISSUE=Brain;
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).
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 (By
CC similarity). Functions as an ubiquitin ligase protein in vitro,
CC suggesting that it may regulate the Notch pathway via some ubiquitin
CC ligase activity. {ECO:0000250}.
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 heterodimers with other members of the
CC Deltex family. Interacts with NOTCH1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N9I9; P84085: ARF5; NbExp=3; IntAct=EBI-2340258, EBI-4289908;
CC Q8N9I9; O95817: BAG3; NbExp=3; IntAct=EBI-2340258, EBI-747185;
CC Q8N9I9; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-2340258, EBI-6255981;
CC Q8N9I9; Q86YD7: FAM90A1; NbExp=5; IntAct=EBI-2340258, EBI-6658203;
CC Q8N9I9; P06241-3: FYN; NbExp=4; IntAct=EBI-2340258, EBI-10691738;
CC Q8N9I9; P62993: GRB2; NbExp=3; IntAct=EBI-2340258, EBI-401755;
CC Q8N9I9; P45984: MAPK9; NbExp=3; IntAct=EBI-2340258, EBI-713568;
CC Q8N9I9; O43639: NCK2; NbExp=5; IntAct=EBI-2340258, EBI-713635;
CC Q8N9I9; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-2340258, EBI-10271199;
CC Q8N9I9; Q9NR21-1: PARP11; NbExp=3; IntAct=EBI-2340258, EBI-17644640;
CC Q8N9I9; Q13882: PTK6; NbExp=3; IntAct=EBI-2340258, EBI-1383632;
CC Q8N9I9; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-2340258, EBI-5235340;
CC Q8N9I9; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-2340258, EBI-11955057;
CC Q8N9I9; Q9BUZ4: TRAF4; NbExp=4; IntAct=EBI-2340258, EBI-3650647;
CC Q8N9I9; Q15642-2: TRIP10; NbExp=3; IntAct=EBI-2340258, EBI-6550597;
CC Q8N9I9; P57075-2: UBASH3A; NbExp=3; IntAct=EBI-2340258, EBI-7353612;
CC Q8N9I9; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-2340258, EBI-1380492;
CC Q8N9I9; P51668: UBE2D1; NbExp=6; IntAct=EBI-2340258, EBI-743540;
CC Q8N9I9; P61077: UBE2D3; NbExp=4; IntAct=EBI-2340258, EBI-348268;
CC Q8N9I9; Q9Y2X8: UBE2D4; NbExp=4; IntAct=EBI-2340258, EBI-745527;
CC Q8N9I9; P61086: UBE2K; NbExp=10; IntAct=EBI-2340258, EBI-473850;
CC Q8N9I9; O14933: UBE2L6; NbExp=6; IntAct=EBI-2340258, EBI-2129974;
CC Q8N9I9; O75604: USP2; NbExp=3; IntAct=EBI-2340258, EBI-743272;
CC Q8N9I9; P07947: YES1; NbExp=3; IntAct=EBI-2340258, EBI-515331;
CC Q8N9I9; Q96E35: ZMYND19; NbExp=3; IntAct=EBI-2340258, EBI-746595;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8N9I9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N9I9-2; Sequence=VSP_008354;
CC -!- SIMILARITY: Belongs to the Deltex family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD38593.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
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DR EMBL; AY225126; AAP57520.1; -; mRNA.
DR EMBL; AK092085; BAC03801.1; -; mRNA.
DR EMBL; AK094385; BAC04344.1; -; mRNA.
DR EMBL; AK128752; BAG54727.1; -; mRNA.
DR EMBL; CH471054; EAW97033.1; -; Genomic_DNA.
DR EMBL; BC114441; AAI14442.1; -; mRNA.
DR EMBL; BC114498; AAI14499.1; -; mRNA.
DR EMBL; AL831941; CAD38593.2; ALT_SEQ; mRNA.
DR CCDS; CCDS41800.1; -. [Q8N9I9-1]
DR CCDS; CCDS66410.1; -. [Q8N9I9-2]
DR RefSeq; NP_001273174.1; NM_001286245.1. [Q8N9I9-2]
DR RefSeq; NP_001273175.1; NM_001286246.1. [Q8N9I9-1]
DR RefSeq; NP_848597.1; NM_178502.3. [Q8N9I9-1]
DR RefSeq; XP_005268754.1; XM_005268697.1. [Q8N9I9-2]
DR RefSeq; XP_005268755.1; XM_005268698.1. [Q8N9I9-2]
DR RefSeq; XP_005268757.1; XM_005268700.1. [Q8N9I9-2]
DR RefSeq; XP_005268760.1; XM_005268703.1. [Q8N9I9-1]
DR RefSeq; XP_011536324.1; XM_011538022.2. [Q8N9I9-1]
DR AlphaFoldDB; Q8N9I9; -.
DR SMR; Q8N9I9; -.
DR BioGRID; 128203; 100.
DR IntAct; Q8N9I9; 49.
DR STRING; 9606.ENSP00000448696; -.
DR iPTMnet; Q8N9I9; -.
DR PhosphoSitePlus; Q8N9I9; -.
DR BioMuta; DTX3; -.
DR DMDM; 37077338; -.
DR EPD; Q8N9I9; -.
DR MassIVE; Q8N9I9; -.
DR MaxQB; Q8N9I9; -.
DR PaxDb; Q8N9I9; -.
DR PeptideAtlas; Q8N9I9; -.
DR PRIDE; Q8N9I9; -.
DR ProteomicsDB; 72545; -. [Q8N9I9-1]
DR ProteomicsDB; 72546; -. [Q8N9I9-2]
DR TopDownProteomics; Q8N9I9-1; -. [Q8N9I9-1]
DR Antibodypedia; 28813; 164 antibodies from 29 providers.
DR DNASU; 196403; -.
DR Ensembl; ENST00000337737.8; ENSP00000338050.3; ENSG00000178498.16. [Q8N9I9-1]
DR Ensembl; ENST00000548198.5; ENSP00000447873.1; ENSG00000178498.16. [Q8N9I9-1]
DR Ensembl; ENST00000548804.5; ENSP00000449294.1; ENSG00000178498.16. [Q8N9I9-1]
DR Ensembl; ENST00000551632.1; ENSP00000448696.1; ENSG00000178498.16. [Q8N9I9-2]
DR GeneID; 196403; -.
DR KEGG; hsa:196403; -.
DR MANE-Select; ENST00000337737.8; ENSP00000338050.3; NM_178502.4; NP_848597.1.
DR UCSC; uc001sow.3; human. [Q8N9I9-1]
DR CTD; 196403; -.
DR DisGeNET; 196403; -.
DR GeneCards; DTX3; -.
DR HGNC; HGNC:24457; DTX3.
DR HPA; ENSG00000178498; Low tissue specificity.
DR MIM; 613142; gene.
DR neXtProt; NX_Q8N9I9; -.
DR OpenTargets; ENSG00000178498; -.
DR PharmGKB; PA134887936; -.
DR VEuPathDB; HostDB:ENSG00000178498; -.
DR eggNOG; ENOG502QUYA; Eukaryota.
DR GeneTree; ENSGT00940000161404; -.
DR HOGENOM; CLU_030422_1_0_1; -.
DR InParanoid; Q8N9I9; -.
DR OMA; PRTLERC; -.
DR OrthoDB; 143182at2759; -.
DR PhylomeDB; Q8N9I9; -.
DR TreeFam; TF325526; -.
DR PathwayCommons; Q8N9I9; -.
DR SignaLink; Q8N9I9; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 196403; 5 hits in 1106 CRISPR screens.
DR GenomeRNAi; 196403; -.
DR Pharos; Q8N9I9; Tbio.
DR PRO; PR:Q8N9I9; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N9I9; protein.
DR Bgee; ENSG00000178498; Expressed in right hemisphere of cerebellum and 165 other tissues.
DR ExpressionAtlas; Q8N9I9; baseline and differential.
DR Genevisible; Q8N9I9; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
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 Gene3D; 3.30.390.130; -; 1.
DR Gene3D; 3.30.40.10; -; 1.
DR InterPro; IPR039396; Deltex_C.
DR InterPro; IPR039399; Deltex_C_sf.
DR InterPro; IPR039398; Deltex_fam.
DR InterPro; IPR001841; Znf_RING.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR InterPro; IPR017907; Znf_RING_CS.
DR PANTHER; PTHR12622; PTHR12622; 1.
DR Pfam; PF18102; DTC; 1.
DR SMART; SM00184; RING; 1.
DR PROSITE; PS00518; ZF_RING_1; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Metal-binding; Notch signaling pathway;
KW Reference proteome; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..347
FT /note="Probable E3 ubiquitin-protein ligase DTX3"
FT /id="PRO_0000219085"
FT ZN_FING 164..205
FT /note="RING-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT REGION 113..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..151
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..7
FT /note="MSFVLSR -> MPILSSSGSK (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_008354"
SQ SEQUENCE 347 AA; 37988 MW; FDB4CDC982F1B707 CRC64;
MSFVLSRMAA CGGTCKNKVT VSKPVWDFLS KETPARLARL REEHRVSILI DGETSDIYVL
QLSPQGPPPA PPNGLYLARK ALKGLLKEAE KELKKAQRQG ELMGCLALGG GGEHPEMHRA
GPPPLRAAPL LPPGARGLPP PPPPLPPPLP PRLREEAEEQ ESTCPICLGE IQNAKTLEKC
RHSFCEGCIT RALQVKKACP MCGRFYGQLV GNQPQNGRML VSKDATLLLP SYEKYGTIVI
QYVFPPGVQG AEHPNPGVRY PGTTRVAYLP DCPEGNKVLT LFRKAFDQRL TFTIGTSMTT
GRPNVITWND IHHKTSCTGG PQLFGYPDPT YLTRVQEELR AKGITDD
