ID H2TMN8_TAKRU Unreviewed; 629 AA.
AC H2TMN8;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 2.
DT 18-JUN-2025, entry version 64.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU367105};
DE EC=2.3.2.27 {ECO:0000256|RuleBase:RU367105};
GN Name=LOC101067626 {ECO:0000313|Ensembl:ENSTRUP00000025944.2};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000025944.2, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000025944.2, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000025944.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (MAR-2025) to UniProtKB.
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:0000256|ARBA:ARBA00000900,
CC ECO:0000256|RuleBase:RU367105};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU367105}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU367105}.
CC -!- SIMILARITY: Belongs to the Deltex family.
CC {ECO:0000256|ARBA:ARBA00009413, ECO:0000256|RuleBase:RU367105}.
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DR RefSeq; XP_011609531.1; XM_011611229.2.
DR AlphaFoldDB; H2TMN8; -.
DR STRING; 31033.ENSTRUP00000025944; -.
DR Ensembl; ENSTRUT00000026049.3; ENSTRUP00000025944.2; ENSTRUG00000010312.3.
DR GeneID; 101067626; -.
DR GeneTree; ENSGT00940000157641; -.
DR InParanoid; H2TMN8; -.
DR OMA; ICMEQLS; -.
DR OrthoDB; 2449614at2759; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000005226; Chromosome 15.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniRule.
DR CDD; cd09633; Deltex_C; 1.
DR FunFam; 3.30.40.10:FF:000097; E3 ubiquitin-protein ligase DTX4; 1.
DR FunFam; 3.30.390.130:FF:000001; Probable E3 ubiquitin-protein ligase DTX3; 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; IPR018123; WWE-dom_subgr.
DR InterPro; IPR004170; WWE_dom.
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 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 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU367105};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU367105};
KW Notch signaling pathway {ECO:0000256|ARBA:ARBA00022976};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU367105};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU367105};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 23..111
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 112..188
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 411..475
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 223..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 339..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 231..242
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 343..352
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..370
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..389
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 629 AA; 67417 MW; 39335BD60BB24E83 CRC64;
MAIVSGSCAR INGSRNGPSV SATQSGSVGQ SQPMIAVWEW QDDLGYWRPY SGQVSTYIEQ
CLAPRGHRGG GSGSTSIHLG QSDPTLLPYI IDIRSLKQFR QDTGKTRSVR CSLFAQSSGL
GSGVLWEWIN DEGGWTPYET RTSILLEHSY QARQGTADLS PHGYNYIVDL TSLTQVNKAS
GFRRQVRRQC NFPYPLASPG PPAVPSSAAC SCLRCLNHST TGPMPSRFRH SSSSNSLNRP
SLQGQGRAVA AHLASVYSPY PRRPLSVGGM SWGNPWPPPP SSSQLSAPLL AGSNATKGLS
VPSVPVQLSG STSVSSALAG MASILMSAVG LGVHFTSAPL PPQQQQQSAA FPLPLPPPPL
LPPASRPSDP PSSSSSVRRA KRQHRRGSCH KPEDVIQRYM EEVAAAPDED CIICMDQLSS
PSSYESPSSE DGGQGILPSA VGKFVKCGHT LHMLCMLAMY NNGTKDGSLQ CPSCKTIYGE
KTGTQPKGKM EIYSIGQSLP GHPDCGTIHI IYSIPPGIQG PEHPNPGQPF TCRGFPRFCF
LPDNHKGRKV LELLKVAWMR RLIFTVGTSS TTGEPDTVVW NNIHHKTEMM SNLSGHGYPD
PNYLDNVLSE LASQGVTEDC LKAPSGASS
//
