G2E3_CHICK
ID G2E3_CHICK Reviewed; 742 AA.
AC Q5F4A1;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=G2/M phase-specific E3 ubiquitin-protein ligase;
DE EC=2.3.2.26;
DE AltName: Full=G2/M phase-specific HECT-type E3 ubiquitin transferase;
GN Name=G2E3; ORFNames=RCJMB04_1m6;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=CB; TISSUE=Bursa of Fabricius;
RX PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA Hayashizaki Y., Buerstedde J.-M.;
RT "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT function analysis.";
RL Genome Biol. 6:R6.1-R6.9(2005).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an
CC E2 ubiquitin-conjugating enzyme in the form of a thioester and then
CC directly transfers the ubiquitin to targeted substrates. Essential in
CC early embryonic development to prevent apoptotic death.
CC {ECO:0000250|UniProtKB:Q7L622}.
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;
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus
CC {ECO:0000250|UniProtKB:Q7L622}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q7L622}. Note=Shuttles between the nucleus and
CC the cytoplasm. In the nucleus, delocalizes from the nucleolus to the
CC nucleoplasm in response to DNA damage. {ECO:0000250|UniProtKB:Q7L622}.
CC -!- DOMAIN: Ubiquitin ligase activity is mediated by two distinct domains,
CC PHD-type zinc fingers 2 and 3. The use of these distinct domains may
CC allow ubiquitination of different targets by each domain. The HECT
CC domain is catalytically inactive and does not contribute to this
CC activity (By similarity). {ECO:0000250}.
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DR EMBL; AJ851399; CAH65033.1; -; mRNA.
DR RefSeq; NP_001012918.1; NM_001012900.1.
DR AlphaFoldDB; Q5F4A1; -.
DR STRING; 9031.ENSGALP00000016094; -.
DR PaxDb; Q5F4A1; -.
DR GeneID; 423305; -.
DR KEGG; gga:423305; -.
DR CTD; 55632; -.
DR VEuPathDB; HostDB:geneid_423305; -.
DR eggNOG; KOG1084; Eukaryota.
DR InParanoid; Q5F4A1; -.
DR OrthoDB; 199998at2759; -.
DR PhylomeDB; Q5F4A1; -.
DR UniPathway; UPA00143; -.
DR PRO; PR:Q5F4A1; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IEA:InterPro.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR CDD; cd15669; ePHD_PHF7_G2E3_like; 1.
DR CDD; cd15496; PHD_PHF7_G2E3_like; 1.
DR Gene3D; 3.30.40.10; -; 2.
DR InterPro; IPR034732; EPHD.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR042013; PHF7/G2E3_ePHD.
DR InterPro; IPR042012; PHF7/G2E3_PHD.
DR InterPro; IPR011011; Znf_FYVE_PHD.
DR InterPro; IPR001965; Znf_PHD.
DR InterPro; IPR013083; Znf_RING/FYVE/PHD.
DR Pfam; PF00632; HECT; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00249; PHD; 3.
DR SUPFAM; SSF56204; SSF56204; 1.
DR SUPFAM; SSF57903; SSF57903; 1.
DR PROSITE; PS51805; EPHD; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Cytoplasm; Developmental protein; Metal-binding; Nucleus;
KW Reference proteome; Repeat; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..742
FT /note="G2/M phase-specific E3 ubiquitin-protein ligase"
FT /id="PRO_0000248346"
FT DOMAIN 417..742
FT /note="HECT"
FT ZN_FING 10..50
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 78..127
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 142..192
FT /note="PHD-type 2; degenerate"
FT ZN_FING 236..285
FT /note="PHD-type 3"
SQ SEQUENCE 742 AA; 84905 MW; D91E066CFA5579D3 CRC64;
MSENNFDIQS PPCVLCGWTD NCPEKYGEKR TYVEYNLTLH NYCLLMSSGI WQRGEENEGV
DGFLIEDIRK EVNRAARLMC NICRKKGASI GCVAPKCKRS YHFPCGLQKE CVFQFMEDFR
SYCWEHKPVQ IFSDKESREP SQCTICLDLV EHLPLYSVLR SPCCKNTWFH RECLQYQALS
AGIFFFRCAV CNNKDKFQKE MLRMGIHIPE KDASWELEDN AYQDLLQCYQ HCDIRRCLCK
NGRDYNKPDS KWEIKRCQSC GSRGTHLACS SIKSWEQNWE CVECRSIFAK GKYSKRKKHS
LAPSEKMDGT TCLLEEPSPK LPRQSPGSQR NCLLQSPKII CQNNLSPCSL LELPTSNRVA
MSLSPLMSNR NCSLRKKHLR MQRKEASNIL KELKQQINTK TTRLNINTEN IWNSALKGFR
QRNFRPTNTI EVKFTNCKNR VKTDSFTGSK HLFFHLLMLH IQNSSLFEGS SAKNLSVDPQ
ALKENLYFEA GKMIAVSLVH GGPSPGFFSK ILFDCLVYGP ENVKPNLDDV ADAGVAQTIK
KIKYSESLSS LQSTVRDCYD FLAAAGCLRP ITSLRDKDML VNDLLIHHVI KRIISPLESF
RQGLKTLGLL EKMEMHQDAF SSLFCHKPEN LSAEALCDLF TIHSSPDVNK VGAADFWMGY
LQDVESGESV VTLQDILFFV TGCSSIPPIG FDPEPTIKFL PVHYPIGNRL LNCLELPITR
TYENFKNKME FTIRSTLRGE RE
