GenomeNet

Database: UniProt
Entry: A0A2I3S6N7_PANTR
LinkDB: A0A2I3S6N7_PANTR
Original site: A0A2I3S6N7_PANTR 
ID   A0A2I3S6N7_PANTR        Unreviewed;      4374 AA.
AC   A0A2I3S6N7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:ENSPTRP00000072651.1,
GN   ECO:0000313|VGNC:VGNC:55717};
OS   Pan troglodytes (Chimpanzee).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pan.
OX   NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000072651.1, ECO:0000313|Proteomes:UP000002277};
RN   [1] {ECO:0000313|Ensembl:ENSPTRP00000072651.1, ECO:0000313|Proteomes:UP000002277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16136131; DOI=10.1038/nature04072;
RG   Chimpanzee sequencing and analysis consortium;
RT   "Initial sequence of the chimpanzee genome and comparison with the human
RT   genome.";
RL   Nature 437:69-87(2005).
RN   [2] {ECO:0000313|Ensembl:ENSPTRP00000072651.1}
RP   IDENTIFICATION.
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}.
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   EMBL; AACZ04058781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   Ensembl; ENSPTRT00000089340.1; ENSPTRP00000072651.1; ENSPTRG00000021930.6.
DR   VGNC; VGNC:55717; HUWE1.
DR   GeneTree; ENSGT00940000156319; -.
DR   UniPathway; UPA00143; -.
DR   Proteomes; UP000002277; Chromosome X.
DR   Bgee; ENSPTRG00000021930; Expressed in lymph node and 21 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:UP000002277};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          1354..1393
FT                   /note="UBA"
FT                   /evidence="ECO:0000259|PROSITE:PS50030"
FT   DOMAIN          1641..1718
FT                   /note="WWE"
FT                   /evidence="ECO:0000259|PROSITE:PS50918"
FT   DOMAIN          4038..4374
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          744..797
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1016..1039
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1052..1075
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1329..1358
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1434..1453
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1727..1773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2056..2103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2300..2359
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2395..2485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2699..2836
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2853..2985
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3052..3074
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3260..3282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3419..3439
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3486..3527
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3552..3583
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3752..3773
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3794..3848
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          3894..3948
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        775..794
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1348
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1737..1759
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2056..2073
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2074..2098
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2300..2333
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2411..2476
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2699..2723
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2739..2779
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2818..2836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2859..2902
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2920..2949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3056..3074
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3260..3275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3486..3517
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3813..3830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3894..3911
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        3929..3948
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        4341
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   4374 AA;  481654 MW;  D58FD61C7A410D8D CRC64;
     GEKLKETPVR FHPADCRALI DKLKVCNDEQ LLLELQQIKT WNIGKCELYH WVDLLDRFDG
     ILADAGQTVE NMSWMLVCDR PEREQLKMLL LAVLNFTALL IEYSFSRHLY SSIEHLTTLL
     ASSDMQVVLA VLNLLYVFSK RSNYITRLGS DKRTPLLTRL QHLAESWGGK ENGFGLAECC
     RDLHMMKYPP SATTLHFEFY ADPGAEVKIE KRTTSNTLHY IHIEQLDKIS ESPSEIMESL
     TKMYSIPKDK QMLLFTHIRL AHGFSNHRKR LQAVQARLHA ISILVYSNAL QESANSILYN
     GLIEELVDVL QITDKQLMEI KAASLRTLTS IVHLERTPKL SSIIDCTGTA SYHGFLPVLV
     RNCIQAMIDP SMDPYPHQFA TALFSFLYHL ASYDAGGEAL VSCGMMEALL KVIKFLGDEQ
     DQITFVTRAV RVVDLITNLD MAAFQSHSGL SIFIYRLEHE VDLCRKECPF VIKPKIQRPN
     TTQEGEEMET DMDVADVAME SSPGSSISME HRLDVELRAS GSSSSTNISS GPSPGVQCIP
     QRAALLKSML NFLKKAIQDP AFSDGIRHVM DGSLPTSLKH IISNAEYYGP SLFLLATEVV
     TVFVFQEPSL LSSLQDNGLT DVMLHALLIK DVPATREVLG SLPNVFSALC LNARGLQSFV
     QCQPFERLFK VLLSPDYLPA MRRRRSSDPL GDTASNLGSA VDELMRHQPT LKTDATTAII
     KLLEEICNLG RDPKYICQKP SIQKADGTAT APPPRSNHAA EEASSEDEEE EEVQAMQSFN
     STQQNETEPN QQVVGTEERI PIPLMDYILN VMKFVESILS NNTTDDHCQE FVNQKGLLPL
     VTILGLPNLP IDFPTSAACQ AVAGVCKSIL TLSHEPKVLQ EGLLQLDSIL SSLEPLHRPI
     ESPGGSVLLR ELACAGNVAD ATLSAQATPL LHALTAAHAY IMMFVHTCRV GQSEIRSISV
     NQWGSQLGLS VLSKLSQLYC SLVWESTVLL SLCTPNSLPS GCEFGQADMQ KLVPKDEKAG
     TTQGGKRSDG EQDGAAGSMD ASTQGLLEGI GLDGDTLAPM ETDEPTASDS KGKSKITPAM
     AARIKQIKPL LSASSRLGRA LAELFGLLVK LCVGSPVRQR RSHHAASTTT APTPAARSTA
     SALTKLLTKG LSWQPPPYTP TPRFRLTFFI CSVGFTSPML FDERKYPYHL MLQKFLCSGG
     HNALFETFNW ALSMGGKVPV SEGLEHSDLP DGTGEFLDAW LMLVEKMVNP TTVLESPHSL
     PAKLPGGVQN FPQFSALRFL VVTQKAAFTC IKNLWNRKPL KVYGGRMAES MLAILCHILR
     GEPVIRERLS KEKEGSRGEE DTGQEEGGSR REPQVNQQQL QQLMDMGFTR EHAMEALLNT
     STMEQATEYL LTHPPPIMGG VVRDLSMSEE DQMMRAIAMS LGQDIPMDQR AESPEEVACR
     KEEEERKARE KQEEEEAKCL EKFQDADPLE QDELHTFTDT MLPGCFHLLD ELPDTVYRVC
     DLIMTAIKRN GADYRDMILK QVVNQVWEAA DVLIKAALPL TTSDTKTVSE WISQMATLPQ
     ASNLATRILL LTLLFEELKL PCAWVVESSG ILNVLIKLLE VVQPCLQAAK EQKEVQTPKW
     ITPVLLLIDF YEKTAISSKR RAQMTKYLQS NSNNWRWFDD RSGRWCSYSA SNNSTIDSAW
     KSGETSVRFT AGRRRYTVQF TTMVQVNEET GNRRPVMLTL LRVPRLNKNS KNSNGQELEK
     TLEESKEMDI KRKENKGNDT PLALESTNTE KETSLEETKI GEILIQGLTE DMVTVLIRAC
     VSMLGVPVDP DTLHATLRLC LRLTRDHKYA MMFAELKSTR MILNLTQSSG FNGFTPLVTL
     LLRHIIEDPC TLRHTMEKVV RSAATSGAGS TTSGVVSGSL GSREINYILR VLGPAACRNP
     DIFTEVANCC IRIALPAPRG SGTASDDEFE NLRIKGPNAV QLVKTTPLKP SPLPVIPDTI
     KEVIYDMLNA LAAYHAPEEA DKSDPKPGVM TQEVGQLLQD MGDDVYQQYR SLTRQSSDFD
     TQSGFSINSQ VFAADGASTE TSASGTSQGE ASTPEESRDG KKDKEGDRAS EEGKQKGKGS
     KPLMPTSTIL RLLAELVRSY VGIATLIANY SYTVGQSELI KEDCSVLAFV LDHLLPHTQN
     AEDKDTPALA RLFLASLAAA GSGTDAQVAL VNEVKAALGR ALAMAESTEK HARLQAVMCI
     ISTIMESCPS TSSFYSSATA KTQHNGMNNI IRLFLKKGLV NDLARVPHSL DLSSPNMANT
     VNAALKPLET LSRIVNQPSS LFGSKSASSK NKSEQDAQGA SQDSSSNQQD PGEPGEAEVQ
     EEDHDVTQTE VADGDIMDGE AETDSVVIAG QPEVLSSQEM QVENELEDLI DELLERDGGS
     GNSTIIDSMN ILDPEDEEEH TQEEDSSGSN EDEDDSQDEE EEEEEDEEDD QEDDEGEEGD
     EDDDDDGSEM ELDEDYPDMN ASPLVRFERF DREDDLIIEF DNMFSSATDI PPSPGNIPTT
     HPLMVRHADH SSLTLGSGSS TTRLTQGIGR SQRTLRQLTA NTGHTIHVHY PGNRQPNPPL
     ILQRLLGPSA AADILQLSSS LPLQSRGRAR LLVGNDDVHI IARSDDELLD DFFHDQSTAT
     SQAGTLSSIP TALTRWTEEC KVLDAESMHD CVSVVKVSIV NHLEFLRDEE LEERREKRRK
     QLAEEETKIT DKGKEDKENR DQSAQVIPKG WEDSSLTKDG TPMPDSYPTT PSSTDAATSE
     SKETLGTLQS SQQQPTLPTP PALGEVPQEL QSPAGEGGSS TQLLMPVEPE ELGPTRPSGE
     AETTQMELSP APTINRNVIS PCDFFLASLS PERAEDSDAL TAVSSQLEGS PMDTSSLASC
     TLEEAVGDTS AAGSSEQPRA GSSTPGDAPP AVAEVQGRSD GSGESAQPPE DSSPPASSES
     SSTRDSAVAI SGADSRGILE EPLPSTSSEE EDPLAGISLP EGVDPSFLAA LPDDIRREVL
     QNQLGIRPPT RTAPSTNSSA PAVVGNPGVT EVSPEFLAAL PPAIQEEVLA QQRAEQQRRE
     LAQNASSDTP MDPVTFIQTL PSDLRRSVLE DMEDSVLAVM PPDIAAEAQA LRREQEARQR
     QLMHERLFGH SSTSALSAIL RSPAFTSRLS GNRGVQYTRL AVQRGGTFQM GGSSSHNRPS
     GSNVDTLLRL RGRLLLDHEA LSCLLVLLFV DEPKLNTSRL HRVLRNLCYH AQTRHWVIRS
     LLSILQRSSE SELCIETPKL TTSEEKGKKS SKSCGSSSHE NRPLDLLHKM ESKSSNQLSW
     LSVSMDAALG CRTNIFQIQR SGGRKHTEKH ASGGSTVHIH PQAAPVVCRH VLDTLIQLAK
     VFPSHFTQQR TKETNCESDR ERGNKACSPC SSQSSNSGIC TDFWDLLVKL DNMNVSRKGK
     NSVKSVPVSA GGEGETSPYS LEASPLGQLM NMLSHPVIRR SSLLTEKLLR LLSLISIALP
     ENKVSEAQAN SGSGASSTTT ATSTTSTTTT TAASTTPTPP TAPTPVTSAP ALVAATAIST
     IVVAASTTVT TPTTATTTVS ISPTTKGSKS PAKVSDGGSS STDFKMVSSG LTENQLQLSV
     EVLTSHSCSE EGLEDAANVL LQLSRGDSGT RDTVLKLLLN GARHLGYTLC KQIGTLLAEL
     REYNLEQQRR AQCETLSPDG LPEEQPQTTK LKGKMQSRFD MAENVVIVAS QKRPLGGREL
     QLPSMSMLTS KTSTQKFFLR VLQVIIQLRD DTRRANKKAK QTGRLGSSGL GSASSIQAAV
     RQLEAEADAI IQMSESSQSE ASVRREESPM DVDQPSPSAQ DTQSIASDGT PQGEKEKEER
     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
//
DBGET integrated database retrieval system