ID G3RT74_GORGO Unreviewed; 1401 AA.
AC G3RT74;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 2.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
GN Name=HECW1 {ECO:0000313|Ensembl:ENSGGOP00000018999.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000018999.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000018999.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000018999.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000018999.2}
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}.
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DR EMBL; CABD030050980; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050981; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050983; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050984; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050985; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050986; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030050988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Ensembl; ENSGGOT00000026678.2; ENSGGOP00000018999.2; ENSGGOG00000024448.2.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000158294; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR TreeFam; TF313938; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000001519; Chromosome 7.
DR Bgee; ENSGGOG00000024448; Expressed in prefrontal cortex and 3 other cell types or tissues.
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; 1.
DR Gene3D; 2.20.70.10; -; 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; 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 SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 1.
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; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 8..144
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 818..851
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1071..1401
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 175..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 277..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 556..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 692..738
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..329
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..587
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 720..738
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1369
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1401 AA; 156240 MW; FFB2EA8F095B8CF9 CRC64;
QIHLPEHSGD RIFKSIGADE TVQGQGSRRL ISFSLSDFQA MGLKKGMFFN PDPYLKISIQ
PGKHSIFPAL PHHGQERRSK IIGNTVNPIW QAEQFSFVSL PTDVLEIEVK DKFAKSRPII
KRFLGKLSMP VQRLLERHAI GDRVVSYTLG RRLPTDHVSG QLQFRFEITS SIHPDDEEIS
LSTEPESAQI QDSPMNNLME SSSGEPRSEA PESSESWKPE QLGEGSVPDG PGNQSMELSR
PAEEAAVITE AGDQGMVSVG PEEAGELLAQ VQKDIQPAPS AEELAEQLDL GEEASALLLE
DGEAPASTKE EPLEEEAMTQ SRAGREEEEK EQEEEGDVST LEQGEGRLQL RASVKRKSRP
CSLPVSELET VIASACGDPE TPRTHYIRIH TLLHSMPSAQ GGSAAEEEDG AEEESTLKDS
SEKDGLSEVD TVAADPSALE EDREEPEGAT PGTAHPGHSG GHFPSLANGA AQDGDTHPST
GSESDSSPRQ GGDHSCEGCD ASCCSPSCYS SSCYSTSCYS SSCYSASCYS PSCYNGNRFA
SHTRFSSVDS AKISESTVFS SQDDEEEENS AFESVPDSMQ SPELDPESTN GAGPWQDELA
APSGHVERSP EGLESPVAGP SNRREGECPI LHNSQPVSQL PSLRPEHHHY PTIDEPLPPK
ILVLLIVLAI LQFFTDFSNY LIQSFGPQGR TIATERSEED SGSQSCEQAP AGGGGGGGSD
SEAESSQSSL DLRREGSLSP VNSQKITLLL QSPAVKFITN PEFFTVLHAN YSAYRVFTSS
TCLKHMILKV RRDARNFERY QHNRDLVNFI NMFADTRLEL PRGWEIKTDQ QGKSFFVDHN
SRATTFIDPR IPLQNGRLPN HLTHRQHLQR LRSYSAGEAS EVSRNRGASL LARPGHSLVA
AIRSQHQHES LPLAYNDKIV AFLRQPNIFE MLQERQPSLA RNHTLREKIH YIRTEGNHGL
EKLSCDADLV ILLSLFEEEI MSYVPLQAAF HPGYSFSPRC SPCSSPQNSP GLQRASARAP
SPYRRDFEAK LRNFYRKLEA KGFGQGPGKI KLIIRRDHLL EGTFNQVMAY SRKELQRNKL
YVTFVGEEGL DYSGPSREFF FLLSQELFNP YYGLFEYSAN DTYTVQISPM SAFVENHLEW
FRFSGRILGL ALIHQYLLDA FFTRPFYKAL LRLPCFQPSP EFHQSLQWMK DNNITDILDL
TFTVNEEVFG QVTERELKSG GANTQVTEKN KKEYIERMVK WRVERGVVQQ TEALVRGFYE
VVDSRLVSVF DARELELVIA GTAEIDLNDW RNNTEYRGGY HDGHLVIRWF WAAVERFNNE
QRLRLLQFVT GTSSVPYEGF AALRGSNGLR RFCIEKWGKI TSLPRAHTCF NRLDLPPYPS
YSMLYEKLLT AVEETSTFGL E
//
