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Database: UniProt
Entry: Q5F4A1
LinkDB: Q5F4A1
Original site: Q5F4A1 
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   27-MAR-2024, entry version 98.
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   SMR; Q5F4A1; -.
DR   STRING; 9031.ENSGALP00000016094; -.
DR   PaxDb; 9031-ENSGALP00000016094; -.
DR   GeneID; 423305; -.
DR   KEGG; gga:423305; -.
DR   CTD; 55632; -.
DR   VEuPathDB; HostDB:geneid_423305; -.
DR   eggNOG; KOG1084; Eukaryota.
DR   InParanoid; Q5F4A1; -.
DR   PhylomeDB; Q5F4A1; -.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5F4A1; -.
DR   Proteomes; UP000000539; Unassembled WGS sequence.
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   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   CDD; cd15669; ePHD_PHF7_G2E3_like; 1.
DR   CDD; cd15496; PHD_PHF7_G2E3_like; 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   Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 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   PANTHER; PTHR12420:SF37; G2_M PHASE-SPECIFIC E3 UBIQUITIN-PROTEIN LIGASE; 1.
DR   PANTHER; PTHR12420; PHD FINGER PROTEIN; 1.
DR   Pfam; PF00632; HECT; 1.
DR   Pfam; PF13771; zf-HC5HC2H; 1.
DR   SMART; SM00119; HECTc; 1.
DR   SMART; SM00249; PHD; 3.
DR   SUPFAM; SSF57903; FYVE/PHD zinc finger; 1.
DR   SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 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
//
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