ID A0A3Q2HF72_HORSE Unreviewed; 4384 AA.
AC A0A3Q2HF72;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 2.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HUWE1 {ECO:0000313|Ensembl:ENSECAP00000032253.2,
GN ECO:0000313|VGNC:VGNC:18916};
OS Equus caballus (Horse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX NCBI_TaxID=9796 {ECO:0000313|Ensembl:ENSECAP00000032253.2, ECO:0000313|Proteomes:UP000002281};
RN [1] {ECO:0000313|Ensembl:ENSECAP00000032253.2, ECO:0000313|Proteomes:UP000002281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000032253.2,
RC ECO:0000313|Proteomes:UP000002281};
RX PubMed=19892987; DOI=10.1126/science.1178158;
RG Broad Institute Genome Sequencing Platform;
RG Broad Institute Whole Genome Assembly Team;
RA Wade C.M., Giulotto E., Sigurdsson S., Zoli M., Gnerre S., Imsland F.,
RA Lear T.L., Adelson D.L., Bailey E., Bellone R.R., Bloecker H., Distl O.,
RA Edgar R.C., Garber M., Leeb T., Mauceli E., MacLeod J.N., Penedo M.C.T.,
RA Raison J.M., Sharpe T., Vogel J., Andersson L., Antczak D.F., Biagi T.,
RA Binns M.M., Chowdhary B.P., Coleman S.J., Della Valle G., Fryc S.,
RA Guerin G., Hasegawa T., Hill E.W., Jurka J., Kiialainen A., Lindgren G.,
RA Liu J., Magnani E., Mickelson J.R., Murray J., Nergadze S.G., Onofrio R.,
RA Pedroni S., Piras M.F., Raudsepp T., Rocchi M., Roeed K.H., Ryder O.A.,
RA Searle S., Skow L., Swinburne J.E., Syvaenen A.C., Tozaki T., Valberg S.J.,
RA Vaudin M., White J.R., Zody M.C., Lander E.S., Lindblad-Toh K.;
RT "Genome sequence, comparative analysis, and population genetics of the
RT domestic horse.";
RL Science 326:865-867(2009).
RN [2] {ECO:0000313|Ensembl:ENSECAP00000032253.2}
RP IDENTIFICATION.
RC STRAIN=Thoroughbred {ECO:0000313|Ensembl:ENSECAP00000032253.2};
RG Ensembl;
RL Submitted (NOV-2023) 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=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
CC -!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
CC {ECO:0000256|ARBA:ARBA00034494}.
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DR Ensembl; ENSECAT00000038901.3; ENSECAP00000032253.2; ENSECAG00000021385.4.
DR VGNC; VGNC:18916; HUWE1.
DR GeneTree; ENSGT00940000156319; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000002281; Chromosome X.
DR Bgee; ENSECAG00000021385; Expressed in trophectoderm and 23 other cell types or tissues.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd14288; UBA_HUWE1; 1.
DR Gene3D; 3.30.720.50; -; 1.
DR Gene3D; 6.10.250.1630; -; 1.
DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 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 InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR010309; E3_Ub_ligase_DUF908.
DR InterPro; IPR010314; E3_Ub_ligase_DUF913.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR025527; HUWE1/Rev1_UBM.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041918; UBA_HUWE1.
DR InterPro; IPR004170; WWE-dom.
DR InterPro; IPR037197; WWE_dom_sf.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF06012; DUF908; 1.
DR Pfam; PF06025; DUF913; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF14377; UBM; 3.
DR Pfam; PF02825; WWE; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00165; UBA; 1.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF46934; UBA-like; 1.
DR SUPFAM; SSF117839; WWE domain; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50030; UBA; 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};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000002281};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1358..1397
FT /note="UBA"
FT /evidence="ECO:0000259|PROSITE:PS50030"
FT DOMAIN 1645..1722
FT /note="WWE"
FT /evidence="ECO:0000259|PROSITE:PS50918"
FT DOMAIN 4048..4384
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 748..800
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1020..1080
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1438..1457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2060..2107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2304..2363
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2399..2489
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2703..2979
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3045..3068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3250..3276
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3363..3390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3414..3434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3480..3519
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3548..3576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3747..3768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3791..3858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3904..3958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 779..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1029..1046
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1333..1352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2060..2077
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2078..2102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2304..2337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2415..2480
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2703..2727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2728..2777
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2778..2792
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2824..2900
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2927..2943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3050..3068
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3253..3269
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3548..3565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3793..3809
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3823..3839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3904..3921
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3939..3958
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 4351
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 4384 AA; 482931 MW; 1DD48A9DB809934D CRC64;
MKVDRTKLKK TPTEAPADCR ALIDKLKVCN DEQLLLELQQ IKTWNIGKCE LYHWVDLLDR
FDGILADAGQ TVENMSWMLV CDRPEREQLK MLLLAVLNFT ALLIEYSFSR HLYSSIEHLT
TLLASSDMQV VLAVLNLLYV FSKRSNYITR LGSDKRTPLL TRLQHLAESW GGKENGFGLA
ECCRDLHMMK YPPSATTLHF EFYADPGAEV KIEKRTTSNT LHYIHIEQLD KISESPSEIM
ESLTKMYSIP KDKQMLLFTH IRLAHGFSNH RKRLQAVQAR LHAISILVYS NALQESANSI
LYNGLIEELV DVLQITDKQL MEIKAASLRT LTSIVHLERT PKLSSIIDCT GTASYHGFLP
VLVRNCIQAM IDPSMDPYPH QFATALFSFL YHLASYDAGG EALVSCGMME ALLKVIKFLG
DEQDQITFVT RAVRVVDLIT NLDMAAFQSH SGLSIFIYRL EHEVDLCRKE CPFVIKPKIQ
RPSTTQEGEE METDMDVADV TMESSSGLSI SMEHRLDVEL RAGPSSSTSI SSGPGPRPGV
QCIPQRAALL KSMLNFLKKA IQDPAFSDGI RHVMDGSLPT SLKHIISNAE YYGPSLFLLA
TEVVTVFVFQ EPSLLSSLQD NGLTDVMLHA LLIKDVPATR EVLGSLPNVF SALCLNARGL
QSFVQCQPFE RLFKVLLSPD YLPAMRRRRS SDPLGDTASN LGSAVDELMR HQPTLKTDAT
TAIIKLLEEI CNLGRDPKYI CQKPSIQKAD GTATAPPPRS NHAAEEASSE DEEEEEVQAM
QSFNSAQQNE TEPNQQVVGT EERIPIPLMD YILNVMKFVE SILSNNTTDD HCQEFVNQKG
LLPLVTILGL PNLPIDFPTS AACQAVAGVC KSILTLSHEP KVLQEGLLQL DSILSSLEPL
HRPIESPGGS VLLRELACAG NVADATLSAQ ATPLLHALTA AHAYIMMFVH TCRVGQSEIR
SISVNQWGSQ LGLSVLSKLS QLYCSLVWES TVLLSLCTPN SLPSGCEFGQ ADMQKLVPKD
EKAGTTQGGK RSDGEQDGTA GSMDASTQGL LEGIGLDGDT LAPMETDEPT TSDSKGKSKI
TPAMAARIKQ IKPLLSASSR LGRALAELFG LLVKLCVGSP VRQRRSHHAA STTTAPTPAA
RSTASALTKL LTKGLSWQPP PYTPTPRFRL TFFICSVGFT SPMLFDERKY PYHLMLQKFL
CSGGHNALFE TFNWALSMGG KVPVAEGLEH SELPDGTGEF LDAWLMLVEK MVNPTTVLES
PHSLPAKLPG GVQNFPQFSA LRFLVVTQKA AFTCIKNLWN RKPLKVYGGR MAESMLAILC
HILRGEPVIR ERLSKEKEGS RGEEDTGQEE GGSRREPQVN QQQLQQLMDM GFTREHAMEA
LLNTSTMEQA TEYLLTHPPP IMGGVVRDLS MSEEDQMMRA IAMSLGQDIP MDQRAESPEE
VACRKEEEER KAREKQEEEE AKCLEKFQDA DPLEQDELHT FTDTMLPGCF HLLDELPDTV
YRVCDLIMTA IKRNGADYRD MILKQVVNQV WEAADVLIKA ALPLTTSDTK TVSEWISQMA
TLPQASNLAT RILLLTLLFE ELKLPCAWVV ESSGILNVLI KLLEVVQPCL QAAKEQKEVQ
TPKWITPVLL LIDFYEKTAI SSKRRAQMTK YLQSNNNNWR WFDDRSGRWC SYSASNNSTI
DSAWKSGETS VRFTAGRRRY TVQFTTMVQV NEETGNRRPV MLTLLRVPRL NKNSKNSNGQ
ELEKTLEESK EMDIKRKENK ANDTPLALES TNIEKETSLE ETKIGEILIQ GLTEDMVTVL
IRACVSMLGV PVDPDTLHAT LRLCLRLTRD HKYAMMFAEL KSTRMILNLT QSSGFNGFTP
LVTLLLRHII EDPCTLRHTM EKVVRSAATS GAGSTTSGVV SGSLGSREIN YILRVLGPAA
CRNPDIFTEV ANCCIRIALP APRGSGTASD DEFENLRIKG PNAVQLVKTT PLKPSPLPVI
PDTIKEVIYD MLNALAAYHA PEEADKSDPK PGGMTQEVGQ LLQDMGDDVY QQYRSLTRQS
SDFDTQSGFS LNSQVFAADG TSTETSTSGA TQGEASTPEE SRDGKKDKEG DRASEEGKQK
GKGSKPLMPT STILRLLAEL VRSYVGIATL IANYSYTVGQ SELIKEDCSV LAFVLDHLLP
HTQNAEDKDT PALARLFLAS LAAAGSGTDA QVALVNEVKA ALGRALAMAE STEKHARLQA
VMCIISTIME SCPSTSSFYS SATAKTQHNG MNNIIRLFLK KGLVNDLARV PHSLDLSSPN
MANTVNAALK PLETLSRIVN QPSSLFGSKS ASSKSKSEQD AQGASQDSNS NQQDPGEPGE
AEVQEEDHDV TQTEVADGDI MDGEAETDSV VIAGQPEVLS SQEMQVENEL EDLIDELLER
DGGSGNSTII DSMNILDPED EEEHTQEEDS SGSNEDEDDS QDEEEEEEED EEDDQEDDEG
EEGDEDDDDD GSEMELDEDY PDMNASPLVR FERFDREDDL IIEFDNMFSS ATDIPPSPGN
IPTTHPLMVR HADHSSLTLG SGSSTTRLTQ GIGRSQRTLR QLTANTGHTI HVHYPGNRQP
NPPLILQRLL GPSAAADILQ LSSSLPLQSR GRARLLVGND DVHIIARSDD ELLDDFFHDQ
STATSQAGTL SSIPTALTRW TEECKVLDAE SMHDCVSVVK VPIVNHLEFL RDEELEERRE
KRRKQLAEEE TKITDKGKED KENRDQSAQC TASKTNDSTE QNLSDGTPMP DSYPTTPSST
DAATSEPKET LVTLQPSQQP PTLPPPPALG EIPQELQSPA GERGSSTQLL MPVEPEELGP
TRPSGEAETT QMELSPAPTI TSLSPERAED SDALTAVSSQ LEGSPMDTSS LASCTLEEAV
GDTSAAGSSE QPTAGSSTPG DAPPVVTELQ GGGDESGEPA QPPEDSSPPA SSESSSTRDS
AVAISGADSR GILEEPLPST SSEEEDPLAG ISLPEGVDPS FLAALPDDIR REVLQNQLGI
RPPTRTAPST NSSAPAVVGN PGVTEVSPEF LAALPPAIQE EVLAQQRAEQ QRRELAQNAS
SDTPMDPVTF IQTLPSDLRR SVLEDMEDSV LAVMPPDIAA EAQALRREQE ARQRQLMHER
LFGHSSTSAL SAILRSPAFT SRLSGNRGVQ YTRLAVQRGG TFQMGGSSSH NRPSGSNVDT
LLRLRGRLLL DHEALSCLLV LLFVDEPKLN TSRLHRVLRN LCYHAQTRHW VIRSLLSILQ
RSSESELCIE TPKLSSSEEK GKKSSKSCGS SSHENRPLDL LHKMESKSSN QLSWLSVSMD
AALGCRTNIF QIQRSGGRKH TEKHASSGST VHIHPQAAPV VCRHVLDTLI QLAKVFPSHF
TQQRTKETNC ESDRERGSKQ TCSPCSSQPN SSGICTDFWD LLVKLDNMNV SRKGKNSVKS
VPVSASGEGE TSPYSLEASP LGQLMNMLSH PVIRRSSLLT EKLLRLLSLI SIALPENKVS
EAQTNSGSSA SSTTVTTSTT STTTTTAASS TPTPATATTP VTSAPALVAA TAISTIAVAA
STTVTTPTTA TTTVSTCTTT KASKSPAKVG DGGSSSADFK MVSSGLTENQ LQLSVEVLTS
HSCSEEGLED AANVLLQLSR GDSGTRDTVL KLLLNGARHL GYTLCKQIGT LLAELREYNL
EQQRRAQCET LSPDGLPEEQ PQTTKLKGKM QSRFDMAENV VIVASQKRPL GGRELQLPSM
SMLTSKTSTQ KFFLRVLQVI IQLRDDTRRA NKKAKQTGRL GSSGLGSASS IQAAVRQLEA
EADAIIQMVR EGQRARRQQQ AATSESSQSE ASVRREESPM DVDQPSPSAQ DTQSIGSDGA
LQGEKEKEER PPELPLLSEQ LSLDELWDML GECLKELEES HDQHAVLVLQ PAVEAFFLVH
ATERESKPPV RDTRESQLAH IKDEPPPLSP APLTPATPSS LDPFFSREPS SMHISSSLPP
DTQKFLRFAE THRTVLNQIL RQSTTHLADG PFAVLVDYIR VLDFDVKRKY FRQELERLDE
GLRKEDMAVH VRRDHVFEDS YRELHRKSPE EMKNRLYIVF EGEEGQDAGG LLREWYMIIS
REMFNPMYAL FRTSPGDRVT YTINPSSHCN PNHLSYFKFV GRIVAKAVYD NRLLECYFTR
SFYKHILGKS VRYTDMESED YHFYQGLVYL LENDVSTLGY DLTFSTEVQE FGVCEVRDLK
PNGANILVTE ENKKEYVHLV CQMRMTGAIR KQLAAFLEGF YEIIPKRLIS IFTEQELELL
ISGLPTIDID DLKSNTEYHK YQSNSIQIQW FWRALRSFDQ ADRAKFLQFV TGTSKVPLQG
FAALEGMNGI QKFQIHRDDR STDRLPSAHT CFNQLDLPAY ESFEKLRHML LLAIQECSEG
FGLA
//
