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Database: UniProt
Entry: A4D1V5_HUMAN
LinkDB: A4D1V5_HUMAN
Original site: A4D1V5_HUMAN 
ID   A4D1V5_HUMAN            Unreviewed;      1585 AA.
AC   A4D1V5;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   24-JAN-2024, entry version 106.
DE   RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE            EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN   Name=NEDL1 {ECO:0000313|EMBL:EAL24007.1};
GN   ORFNames=tcag7.989 {ECO:0000313|EMBL:EAL24007.1};
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:EAL24007.1};
RN   [1] {ECO:0000313|EMBL:EAL24007.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12690205; DOI=10.1126/science.1083423;
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Lai Z., Nusskern D., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA   Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA   Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA   Friedman J.M., Heng H.H., Pelicci P.G., Lo-Coco F., Belloni E.,
RA   Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A., Korf B.R.,
RA   Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA   Herrick S.R., Lemyre E., Farra C.G., Kim H.G., Summers A.M., Gripp K.W.,
RA   Roberts W., Szatmari P., Winsor E.J., Grzeschik K.H., Teebi A.,
RA   Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA   Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA   Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Dohner H.,
RA   Dohner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA   Adams M.D., Tsui L.C.;
RT   "Human chromosome 7: DNA sequence and biology.";
RL   Science 300:767-772(2003).
RN   [2] {ECO:0000313|EMBL:EAL24007.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA   Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA   Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA   Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA   Zheng X.H., Nusskern D., Zhang Q., Gu Z., Lu F., Zeesman S., Teshima I.,
RA   Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R.,
RA   Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.,
RA   Lococo F., Belloni E., Shaffer L.G., Morton C.C., Pober B., Gusella J.,
RA   Bruns G., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W.,
RA   Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M.,
RA   Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H.,
RA   Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.Angel.,
RA   Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P.,
RA   Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J.,
RA   Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
RA   Mural R.J., Adams M.D., Tsui L.-C.;
RL   Submitted (JUN-2004) 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};
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC       {ECO:0000256|ARBA:ARBA00004906}.
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DR   EMBL; CH236951; EAL24007.1; -; Genomic_DNA.
DR   PeptideAtlas; A4D1V5; -.
DR   UniPathway; UPA00143; -.
DR   ChiTaRS; HECW1; human.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd08691; C2_NEDL1-like; 1.
DR   CDD; cd00078; HECTc; 1.
DR   CDD; cd00201; WW; 2.
DR   Gene3D; 2.20.70.10; -; 2.
DR   Gene3D; 2.60.40.2840; -; 1.
DR   Gene3D; 2.60.40.150; C2 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; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR037795; C2_HECW.
DR   InterPro; IPR000569; HECT_dom.
DR   InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR   InterPro; IPR040524; HECW1_helix.
DR   InterPro; IPR032348; HECW_N.
DR   InterPro; IPR001202; WW_dom.
DR   InterPro; IPR036020; WW_dom_sf.
DR   PANTHER; PTHR11254:SF79; E3 UBIQUITIN-PROTEIN LIGASE HECW1; 1.
DR   PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR   Pfam; PF00168; C2; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF18436; HECW1_helix; 1.
DR   Pfam; PF16562; HECW_N; 1.
DR   Pfam; PF00397; WW; 1.
DR   SMART; SM00239; C2; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00456; WW; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR   SUPFAM; SSF51045; WW domain; 2.
DR   PROSITE; PS50004; C2; 1.
DR   PROSITE; PS50237; HECT; 1.
DR   PROSITE; PS01159; WW_DOMAIN_1; 2.
DR   PROSITE; PS50020; WW_DOMAIN_2; 2.
PE   4: Predicted;
KW   Ligase {ECO:0000313|EMBL:EAL24007.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW   ECO:0000256|PROSITE-ProRule:PRU00104}.
FT   DOMAIN          161..297
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          808..841
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          997..1030
FT                   /note="WW"
FT                   /evidence="ECO:0000259|PROSITE:PS50020"
FT   DOMAIN          1250..1585
FT                   /note="HECT"
FT                   /evidence="ECO:0000259|PROSITE:PS50237"
FT   REGION          328..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          428..517
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          709..794
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          873..917
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        336..363
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        625..644
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        726..740
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..917
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        1553
FT                   /note="Glycyl thioester intermediate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ   SEQUENCE   1585 AA;  177167 MW;  49E0928CA583F897 CRC64;
     MASPSRNSQS RRRCKEPLRY SYNPDQFHNM DLRGGPHDGV TIPRSTSDTD LVTSDSRSTL
     MVSSSYYSIG HSQDLVIHWD IKEEVDAGDW IGMYLIDEVL SENFLDYKNR GVNGSHRGQI
     IWKIDASSYF VEPETKICFK YYHGVSGALR ATTPSVTVKN SAAPIFKSIG ADETVQGQGS
     RRLISFSLSD FQAMGLKKGM FFNPDPYLKI SIQPGKHSIF PALPHHGQER RSKIIGNTVN
     PIWQAEQFSF VSLPTDVLEI EVKDKFAKSR PIIKRFLGKL SMPVQRLLER HAIGDRVVSY
     TLGRRLPTDH VSGQLQFRFE ITSSIHPDDE EISLSTEPES AQIQDSPMNN LMESGSGEPR
     SEAPESSESW KPEQLGEGSV PDGPGNQSIE LSRPAEEAAV ITEAGDQGMV SVGPEGAGEL
     LAQVQKDIQP APSAEELAEQ LDLGEEASAL LLEDGEAPAS TKEEPLEEEA TTQSRAGREE
     EEKEQEEEGD VSTLEQGEGR LQLRASVKRK SRPCSLPVSE LETVIASACG DPETPRTHYI
     RIHTLLHSMP SAQGGSAAEE EDGAEEESTL KDSSEKDGLS EVDTVAADPS ALEEDREEPE
     GATPGTAHPG HSGGHFPSLA NGAAQDGDTH PSTGSESDSS PRQGGDHSCE GCDASCCSPS
     CYSSSCYSTS CYSSSCYSAS CYSPSCYNGN RFASHTRFSS VDSAKISEST VFSSQDDEEE
     ENSAFESVPD SMQSPELDPE STNGAGPWQD ELAAPSGHVE RSPEGLESPV AGPSNRREGE
     CPILHNSQPV SQLPSLRPEH HHYPTIDEPL PPNWEARIDS HGRVFYVDHV NRTTTWQRPT
     AAATPDGMRR SGSIQQMEQL NRRYQNIQRT IATERSEEDS GSQSCEQAPA GGGGGGGSDS
     EAESSQSSLD LRREGSLSPV NSQKITLLLQ SPAVKFITNP EFFTVLHANY SAYRVFTSST
     CLKHMILKVR RDARNFERYQ HNRDLVNFIN MFADTRLELP RGWEIKTDQQ GKSFFVDHNS
     RATTFIDPRI PLQNGRLPNH LTHRQHLQRL RSYSAGEASE VSRNRGASLL ARPGHSLVAA
     IRSQHQHESL PLAYNDKIVA FLRQPNIFEM LQERQPSLAR NHTLREKIHY IRTEGNHGLE
     KLSCDADLVI LLSLFEEEIM SYVPLQAAFH PGYSFSPRCS PCSSPQNSPG LQRASARAPS
     PYRRDFEAKL RNFYRKLEAK GFGQGPGKIK LIIRRDHLLE GTFNQVMAYS RKELQRNKLY
     VTFVGEEGLD YSGPSREFFF LLSQELFNPY YGLFEYSAND TYTVQISPMS AFVENHLEWF
     RFSGRILGLA LIHQYLLDAF FTRPFYKALL RLPCDLSDLE YLDEEFHQSL QWMKDNNITD
     ILDLTFTVNE EVFGQVTERE LKSGGANTQV TEKNKKEYIE RMVKWRVERG VVQQTEALVR
     GFYEVVDSRL VSVFDARELE LVIAGTAEID LNDWRNNTEY RGGYHDGHLV IRWFWAAVER
     FNNEQRLRLL QFVTGTSSVP YEGFAALRGS NGLRRFCIEK WGKITSLPRA HTCFNRLDLP
     PYPSYSMLYE KLLTAVEETS TFGLE
//
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