ID A0A2K5W146_MACFA Unreviewed; 2010 AA.
AC A0A2K5W146;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 28.
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|Ensembl:ENSMFAP00000030782.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000030782.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000030782.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000030782.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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}.
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DR SMR; A0A2K5W146; -.
DR Ensembl; ENSMFAT00000004989.2; ENSMFAP00000030782.2; ENSMFAG00000042518.2.
DR VEuPathDB; HostDB:ENSMFAG00000042518; -.
DR GeneTree; ENSGT00940000156517; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000233100; Chromosome 12.
DR Bgee; ENSMFAG00000042518; Expressed in pituitary gland and 13 other cell types or tissues.
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:UP000233100};
KW Transferase {ECO:0000256|RuleBase:RU369009};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 740..816
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 1613..2010
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 1..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 817..839
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 993..1097
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1425..1451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1586..1605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..85
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..144
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 219..260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..351
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..372
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 373..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 959..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1031..1045
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1046..1084
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1977
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 2010 AA; 222703 MW; 110C6A1FB823BE67 CRC64;
MSNRPNNNPG GSLRRSQRNT AGAQPQDDSI GGRSHLGQAK HKGYSPPESR KSNSKAPKVQ
SNTTSELSRG HLSKRSCSSS SAVIVPQPED PDRANTSERQ KTGQVPKKDN SRGVKRSASP
DYNRTNSPSS AKKPKALQHT ESPSETNKPH SKSKKRHLDQ EQQLKSAQSP STSKAHTRKS
GATGGSRSQK RKRTESSCVK SGSGSESTGA EERSAKPTKL ASKSATSAKA GCSTITDSSS
AASTSSSSSA VASASSTVPP GARVKQGKDQ NKARRSRSAS SPSPRRSSRE KEQRSSKSET
SKPGPSGLQA KLASLRKSTK KRSESPPAEL PSLRRSTRQK TTGSCASTSR RGSGLGKRGA
AEARRQEKMA DPESNQEAVN SSAARTDEAP QGAAALLEAR GLPPHLFGPL GPRMSQLFHR
TIGSGASSKA QQLLQGLQAS DESQQLQAVI EMCQLLVMGN EETLGGFPVK SVVPALITLL
QMEHNFDIMN HACRALTYMM EALPRSSAVV VDAIPVFLEK LQVIQCIDVA EQALTALEML
SRRHSKAILQ AGGLADCLLY LEFFSINAQR NALAIAANCC QSITPDEFHF VADSLPLLTQ
RLTHQDKKSV ESTCLCFARL VDNFQHEENL LQQVASKDLL TNVQQLLVVT PPILSSGMFI
MVVRMFSLMC SNCPTLAVQL MKQNIAETLH FLLCGASNGS CQEQIDLVPR SPQELYELTS
LICELMPCLP KEGIFAVDTM LKKGNAQNTD GAIWQWRDDR GLWHPYNRID SRIIEAAHQV
GEDEISLSTL GRVYTIDFNS MQQINEDTGT ARAIQRKPNP LANSNTSGYS ESKKDDARAQ
LMKEDPELAK SFIKTLFGVL YEVYSSSAGP AVRHKCLRAI LRIIYFADAE LLKDVLKNHA
VSSHIASMLS SQDLKIVVGA LQMAEILMQK LPDIFSVYFR REGVMHQVKH LAESESLLTS
PPKACTNGSG SLGSTTSVSS GTATAATHAA ADLGSPSLQH SRDDSLDLSP QGRLSDVLKR
KRLPKRGPRR PKYSPPRDDD KVDNQAKSPT TTQSPKSSFL ASLNPKTWGR LSAQSNSNNI
EPARTAGGSG LARAASKDTI SNNREKIKGW IKEQAHKFVE RYFSSENMDG SNPALNVLQR
LCAATEQLNL QVDGGAECLV EIRSIVSESD VSSFEIQHSG FVKQLLLYLT SKSEKDAVSR
EIRLKRFLHV FFSSPLPGEE PIGRVEPVGN APLLALVHKM NNCLSQMEQF PVKVHDFPSG
NGTGGSFSLN RGSQALKFFN THQLKCQLQR HPDCANVKQW KGGPVKIDPL ALVQAIERYL
VVRGYGRVRE DDEDSDDDGS DEEIDESLAA QFLNSGNVRH RLQFYIGEHL LPYNMTVYQA
VRQFSIQAED ERESTDDESN PLGRAGIWTK THTIWYKPVR EDEESNKDCV GGKRGRAQTA
PTKTSPRNAK KHDELWHDGV CPSVSNPLEV YLIPTPPENI TFEDPSLDVI LLLRVLHAIS
RYWYYLYDNA MCKEIIPTSE FINSKLTAKA NRQLQDPLVI MTGNIPTWLT ELGKTCPFFF
PFDTRQMLFY VTAFDRDRAM QRLLDTNPEI NQSDSQDSRV APRLDRKKRT VNREELLKQA
ESVMQDLGSS RAMLEIQYEN EVGTGLGPTL EFYALVSQEL QRADLGLWRG EEVTLSNPKG
SQEGTKYIQN LQGLFALPFG RTAKPAHIAK VKMKFRFLGK LMAKAIMDFR LVDLPLGLPF
YKWMLRQETS LTSHDLFDID PVVARSVYHL EDIVRQKKRL EQDKSQTKES LQYALETLTM
NGCSVEDLGL DFTLPGFPNI ELKKGGKDIP VTIHNLEEYL RLVIFWALNE GVSRQFDSFR
DGFESVFPLS HLQYFYPEEL DQLLCGSKAD TWDAKTLMEC CRPDHGYTHD SRAVKFLFEI
LSSFDNEQQR LFLQFVTGSP RLPVGGFRSL NPPLTIVRKT FESTENPDDF LPSVMTCVNY
LKLPDYSSIE IMREKLLIAA REGQQSFHLS
//
