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
//