ID Q53FW4_HUMAN Unreviewed; 439 AA.
AC Q53FW4;
DT 24-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 24-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAD96887.1};
RN [1] {ECO:0000313|EMBL:BAD96887.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96887.1};
RX PubMed=8125298; DOI=10.1016/0378-1119(94)90802-8;
RA Maruyama K., Sugano S.;
RT "Oligo-capping: a simple method to replace the cap structure of eukaryotic
RT mRNAs with oligoribonucleotides.";
RL Gene 138:171-174(1994).
RN [2] {ECO:0000313|EMBL:BAD96887.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96887.1};
RX PubMed=9373149; DOI=10.1016/S0378-1119(97)00411-3;
RA Suzuki Y., Yoshitomo K., Maruyama K., Suyama A., Sugano S.;
RT "Construction and characterization of a full length-enriched and a 5'-end-
RT enriched cDNA library.";
RL Gene 200:149-156(1997).
RN [3] {ECO:0000313|EMBL:BAD96887.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Human lung {ECO:0000313|EMBL:BAD96887.1};
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
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};
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DR EMBL; AK223167; BAD96887.1; -; mRNA.
DR AlphaFoldDB; Q53FW4; -.
DR PeptideAtlas; Q53FW4; -.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR CDD; cd00078; HECTc; 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; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR PANTHER; PTHR11254:SF67; E3 UBIQUITIN-PROTEIN LIGASE HUWE1; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR PROSITE; PS50237; HECT; 1.
PE 2: Evidence at transcript level;
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 103..439
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 406
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:BAD96887.1"
SQ SEQUENCE 439 AA; 51326 MW; BB735F2E2D338374 CRC64;
SREPSSMHIS SSLPPDTQKF LRFAETHRTV LNQILRQSTT HLADGPFAVL VDYIRVLDFD
VKRKYFRQEL ERLDEGLRKE DMAVHVRRDH VFEDSYRELH RKSPEEMKNR LYIVFEGEEG
QDAGGLLREW YMIISREMFN PMYALFRTSP GDRVTYTINP SSHCNPNHLS YFKFVGRIVA
KAVYDNRLLE CYFTRSFYKH ILGKSVRYTD MESEDYHFYQ GLVYLLENDV STLGYDLTFS
TEVQEFGVCE VRDLKPNGAN ILVTEENKKE YVHLVCQMRM TGAIRKQLAA FLEGFYEIIP
KRLISIFTEQ ELELLISGLP TIDIDDLKSN TEYHKYQSNS IQIQWFWRAL RSFDQADRAK
FLQFVTGTSK VPLQGFAALE GMNGIQKFQI HRDDRSTDRL PSAHTCFNQL DLPAYESFEK
LHHMLLLAIQ ECSEGFGLA
//
