ID H0ZK83_TAEGU Unreviewed; 1562 AA.
AC H0ZK83;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 2.
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};
GN Name=HECW2 {ECO:0000313|Ensembl:ENSTGUP00000011003.2};
OS Taeniopygia guttata (Zebra finch) (Poephila guttata).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Estrildidae;
OC Estrildinae; Taeniopygia.
OX NCBI_TaxID=59729 {ECO:0000313|Ensembl:ENSTGUP00000011003.2, ECO:0000313|Proteomes:UP000007754};
RN [1] {ECO:0000313|Ensembl:ENSTGUP00000011003.2, ECO:0000313|Proteomes:UP000007754}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20360741; DOI=10.1038/nature08819;
RA Warren W.C., Clayton D.F., Ellegren H., Arnold A.P., Hillier L.W.,
RA Kunstner A., Searle S., White S., Vilella A.J., Fairley S., Heger A.,
RA Kong L., Ponting C.P., Jarvis E.D., Mello C.V., Minx P., Lovell P.,
RA Velho T.A., Ferris M., Balakrishnan C.N., Sinha S., Blatti C., London S.E.,
RA Li Y., Lin Y.C., George J., Sweedler J., Southey B., Gunaratne P.,
RA Watson M., Nam K., Backstrom N., Smeds L., Nabholz B., Itoh Y., Whitney O.,
RA Pfenning A.R., Howard J., Volker M., Skinner B.M., Griffin D.K., Ye L.,
RA McLaren W.M., Flicek P., Quesada V., Velasco G., Lopez-Otin C.,
RA Puente X.S., Olender T., Lancet D., Smit A.F., Hubley R., Konkel M.K.,
RA Walker J.A., Batzer M.A., Gu W., Pollock D.D., Chen L., Cheng Z.,
RA Eichler E.E., Stapley J., Slate J., Ekblom R., Birkhead T., Burke T.,
RA Burt D., Scharff C., Adam I., Richard H., Sultan M., Soldatov A.,
RA Lehrach H., Edwards S.V., Yang S.P., Li X., Graves T., Fulton L.,
RA Nelson J., Chinwalla A., Hou S., Mardis E.R., Wilson R.K.;
RT "The genome of a songbird.";
RL Nature 464:757-762(2010).
RN [2] {ECO:0000313|Ensembl:ENSTGUP00000011003.2}
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 RefSeq; XP_002193359.1; XM_002193323.2.
DR STRING; 59729.ENSTGUP00000011003; -.
DR Ensembl; ENSTGUT00000011118.2; ENSTGUP00000011003.2; ENSTGUG00000010653.2.
DR GeneID; 100225246; -.
DR KEGG; tgu:100225246; -.
DR CTD; 57520; -.
DR GeneTree; ENSGT00940000155466; -.
DR HOGENOM; CLU_002173_14_0_1; -.
DR InParanoid; H0ZK83; -.
DR OMA; TAGQHRE; -.
DR OrthoDB; 5480520at2759; -.
DR TreeFam; TF313938; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000007754; Chromosome 7.
DR GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IEA:Ensembl.
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:SF127; E3 UBIQUITIN-PROTEIN LIGASE HECW2; 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 Reference proteome {ECO:0000313|Proteomes:UP000007754};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 168..299
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 797..830
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 975..1008
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 1227..1562
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT REGION 327..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 764..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1055
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1151..1177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..414
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..513
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..655
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..786
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1006..1023
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1153..1171
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1530
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00104"
SQ SEQUENCE 1562 AA; 175119 MW; E1B5394C600A106B CRC64;
MASSAREHLL FVRRRNPQLR YTLSPENLQS LASQGTMPEN MNLQRANSDT DLVTSDSRSS
LTASMYEYTL GQSQNLIIFW DIKEEVDPTD WIGLYHIDEN SPANFWDSKN RGVTGTQKGQ
IVWRIEPGPY FMESEIKICF KYYHGVSGAL RATTPCITVK NPAVMMGVEG TDEGASGAQH
SRKLVSFTLS DIRAAGLKKG MFFNPDPYLK MSIQPGKKST FPTFAHHGQE RRSTIISNTT
NPVWHREKYS FVALLTDVLE IEVKDKFAKS RPIIKRFLGK LTIPVQRLLE RHAIGDQVLS
YNLGRRLPAD HVSGYLQFKV EITSSVHEDA SPETVGTLLG TNSVNGDLGS PSDDEDMPAG
HHDTSTVCSN GPVFEESSGD TILRQSLRTS RTLETDQDEL TSGASRSSPP RGRQDSLNDY
LDAIEHNNHP RPGTSACGDR PRGASPKLRS SFPTDTRLNA MLHIDSDEEE HELHQDLGFP
SSLEDDGGLV MLNGATRNVE RNEVSSSSDQ VMPGPAESER VSASADDQQD SLPELPPPEE
GAECLQGSQA EAPAEQAGSE SSAPPEAEQP PGSADSGAAE AAGGSRRGVS ETESIDQGSE
PSQLSSETEQ SDPARTESVS EASTRPEGES DAEGADSSCN ESATVRRSSV EMRCSSCESA
RFPETPAFSP QEEEEEGACA PEAAAAEPGA EAQDSAGAAG SLPAVQLPQE EAQEAEAGEL
QDQEEAEEIW QRRRSLQAAA AQSQSQDEEV EGAQAACEGA TAQLEGATGG SPANGHQPLR
SLPSVRQDVS RYQRVDEALP PNWEARIDSH GRIFYVDHVN RTTTWQRPTA PPAPQILQRS
NSIQQMEQLN RRYQSIRRTM TNDRPEEHTN AVDGAAEEAE FHHSNSDFRR ENVLPHSTSR
SRLTLLLQSP PVKFLISPEF FTVLHSNPSA YRMFTNNTCL KHMITKVRRD THHFERYQHN
RDLVGFLNMF ANKQLELPRG WEMKHDHQGK AFFVDHNSRT TTFIDPRLPL QSSRPTSALV
HRQHLTRQRS HSAGEVGEDS RHSGPPVLPR PSSTFNTVSR AQYQDVVPVA YNDKIVAFLR
QPNIFEILQE RQPDLTRNHS LREKIQFIRT EGTPGLVRLS SDADLVMLLS LFEEEIMSYV
PPHALLHPSY CQSPRGSPVS SPQNSPGTQR ANARAPAPYK RDFEAKLRNF YRKLETKGYG
QGPGKLKLII RRDHLLEDAF NQIMGYSRKD LQRNKLYVTF VGEEGLDYSG PSREFFFLVS
RELFNPYYGL FEYSANDTYT VQISPMSAFV DNHHEWFRFS GRILGLALIH QYLLDAFFTR
PFYKALLRIL CDLSDLEYLD EEFHQSLQWM KDNDIHDILD LTFTVNEEVF GQITERELKP
GGANIPVTEK NKKEYIERMV KWRIERGVVQ QTESLVRGFY EVVDARLVSV FDARELELVI
AGTAEIDLSD WRNNTEYRGG YHDNHIVIRW FWAAVERFNN EQRLRLLQFV TGTSSIPYEG
FASLRGSNGP RRFCVEKWGK ITALPRAHTC FNRLDLPPYP SFSMLYEKLL TAVEETSTFG
LE
//
