ID A0A2Y9MX55_DELLE Unreviewed; 2025 AA.
AC A0A2Y9MX55;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=E3 ubiquitin-protein ligase {ECO:0000256|RuleBase:RU369009};
DE EC=2.3.2.26 {ECO:0000256|RuleBase:RU369009};
GN Name=TRIP12 {ECO:0000313|RefSeq:XP_022423612.1,
GN ECO:0000313|RefSeq:XP_030616262.1};
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749 {ECO:0000313|Proteomes:UP000248483, ECO:0000313|RefSeq:XP_022423612.1};
RN [1] {ECO:0000313|RefSeq:XP_022423612.1, ECO:0000313|RefSeq:XP_030616262.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022423612.1,
RC ECO:0000313|RefSeq:XP_030616262.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: E3 ubiquitin-protein ligase involved in ubiquitin fusion
CC degradation (UFD) pathway and regulation of DNA repair. Part of the
CC ubiquitin fusion degradation (UFD) pathway, a process that mediates
CC ubiquitination of protein at their N-terminus, regardless of the
CC presence of lysine residues in target proteins.
CC {ECO:0000256|RuleBase:RU369009}.
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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885,
CC ECO:0000256|RuleBase:RU369009};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906, ECO:0000256|RuleBase:RU369009}.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm
CC {ECO:0000256|ARBA:ARBA00004642, ECO:0000256|RuleBase:RU369009}.
CC -!- SIMILARITY: Belongs to the UPL family. K-HECT subfamily.
CC {ECO:0000256|ARBA:ARBA00006331, ECO:0000256|RuleBase:RU369009}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR RefSeq; XP_022423612.1; XM_022567904.1.
DR RefSeq; XP_030616262.1; XM_030760402.1.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000248483; Unplaced.
DR GO; GO:0005654; C:nucleoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:UniProtKB-UniRule.
DR CDD; cd00078; HECTc; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR045322; HECTD1/TRIP12-like.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR018123; WWE-dom_subgr.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR45670; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR PANTHER; PTHR45670:SF1; E3 UBIQUITIN-PROTEIN LIGASE TRIP12; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00678; WWE; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50918; WWE; 1.
PE 3: Inferred from homology;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|RuleBase:RU369009};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000248483};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 755..831
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1628..2025
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 971..1077
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1440..1467
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1601..1620
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..33
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..218
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..294
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..336
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 344..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..1020
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1060
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1992
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2025 AA; 223724 MW; 7059B08CF356CB75 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSCGPSSA GIVPQPEDPD RANASERPKT
GQVPKKDSSR GVKRSASPDY NRTSSPSSAK KPRALQHTES PSETSKPHSK SKKRHLDQEQ
QLKSAQSPST SKAHNRKSGA TASSRSQKRK RTESSCIKSG SVSEATGAEE RSAKPTKLAS
KSAASAKAGC STITDSSSAA STSSSSSAVA SASSTVPPGA RVKQGKDQNK ARRSRSASSP
SPRRSSREKE QSKTGGSSKF DWAARFSPKV SLPKTKLSLP GSSKSETSKP GPSGLQAKLA
SLRKSTKKRS ESPPAELPSL RRSTRQKTTG SCASASRRGS GLGKRGAAEA RRQEKMADPE
GNQETVNSSA ARTDETPQGA AASSSVAGAV GMTTSGESES DDSEMGRLQA LLEARGLPPH
LFGPLGPRMS QLFHRTIGSG ASSKAQQLLQ GLQASDESQQ LQAVIEMCQL LVMGNEETLG
GFPVKSVVPA LITLLQMEHN FDIMNHACRA LTYMMEALPR SSAVVVDAIP VFLEKLQVIQ
CIDVAEQALT ALEMLSRRHS KAILQAGGLA DCLLYLEFFS INAQRNALAI AANCCQSITP
DEFHFVADSL PLLTQRLTHQ DKKSVESTCL CFARLVDNFQ HEENLLQQVA SKDLLTNVQQ
LLVVTPPILS SGMFIMVVRM FSLMCSNCPT LAVQLMKQNI AETLHFLLCG ASNGSCQEQI
DLVPRSPQEL YELTSLICEL MPCLPKEGIF AVDTMLKKGN AQNTDGAIWQ WRDDRGLWHP
YNRIDSRIIE AAHQVGEDEI SLSTLGRVYT IDFNSMQQIN EDTGTARAIQ RKPNPLANTN
SSGYSELKKD DARAQLMKED PELAKSFIKT LFGVLYEVYS SSAGPAVRHK CLRAILRIIY
FADAELLKDV LKNHAVSSHI ASMLSSQDLK IVVGALQMAE ILMQKLPDIF SVYFRREGVM
HQVKHLAESE SLLTSPPKAC TNGSGSLGST TSVSSGTATA ATNASADLGS PSLQHSRDDS
LDLSPQGRLS DVLKRKRLPK RGSRRPKYSP PRDDDKVDNQ AKSPTTTQSP KSSFLASLNP
KTWGRLSAQS HSNNIEPARA AGVSGLARAA SKDTISNNRE KIKGWIKEQA HKFVERYFSS
ENMDGSNPAL NVLQRLCAAT EQLNLQVDGG AECLVEIRSI VSESDVSSFE IQHSGFVKQL
LLYLTSKSEK DAVSREIRLK RFLHVFFSSP LPGEEPTGRV EPVGNAPLLA LVHKMNNCLS
QMEQFPVKVH DFPSGNGTGG SFSLNRGSQA LKFFNTHQLK CQLQRHPDCA NVKQWKGGPV
KIDPLALVQA IERYLVVRGY GRVREDDEDS DDDGSDEEID ESLAAQFLNS GNVRHRLQFY
IGEHLLPYNM TVYQAVRQFS VQAEDEREST DDESNPLGRA GIWTKTHTIW YKPVREDEES
NKDCVGGKRG RAQTAPTKTS PRNAKKHDEL WNDGVCPSVS NPLEVYLIPT PPENITFEDP
SLDVILLLRV LHAISRYWYY LYDNAVCKEI IPTSEFINSK LTAKANRQLQ DPLVIMTGNI
PTWLTELGKT CPFFFPFDTR QMLFYVTAFD RDRAMQRLLD TNPEINQSDS QDSRVAPRLD
RKKRTVNREE LLKQAESVMQ DLGSSRAMLE IQYENEVGTG LGPTLEFYAL VSQELQRADL
GLWRGEEVTL SNPKGSQEGT KYIQNLQGLF ALPFGRTAKP AHIAKVKMKF RFLGKLMAKA
IMDFRLVDLP LGLPFYKWML RQETSLTSHD LFDIDPVVAR SVYHLEDIVR QKKRLEQDKS
QTKESLQYAL ETLTMNGCSV EDLGLDFTLP GFPNIELKKG GKDIPVTIHN LEEYLRLVIF
WALNEGVSRQ FDSFRDGFES VFPLSHLQYF YPEELDQLLC GSKADTWDAK TLMECCRPDH
GYTHDSRAVK FLFEILSSFD NEQQRLFLQF VTGSPRLPVG GFRSLNPPLT IVRKTFESTE
NPDDFLPSVM TCVNYLKLPD YSSIEIMREK LLMAAREGQQ SFHLS
//
