G2E3_MOUSE
ID G2E3_MOUSE Reviewed; 716 AA.
AC Q5RJY2; E9QK24; Q6ZPT7; Q8BNA4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 128.
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; Synonyms=Kiaa1333;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-356.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=18511420; DOI=10.1074/jbc.m803238200;
RA Brooks W.S., Helton E.S., Banerjee S., Venable M., Johnson L., Schoeb T.R.,
RA Kesterson R.A., Crawford D.F.;
RT "G2E3 is a dual function ubiquitin ligase required for early embryonic
RT development.";
RL J. Biol. Chem. 283:22304-22315(2008).
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 (By
CC similarity). Required for prevention of apoptotic death in early
CC embryogenesis. {ECO:0000250|UniProtKB:Q7L622,
CC ECO:0000269|PubMed:18511420}.
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 -!- TISSUE SPECIFICITY: In the developing embryo, expressed predominantly
CC in the central nervous system and early limb bud. In the adult, highest
CC expression in Purkinje cell bodies and cells lining the ductus
CC deferens. {ECO:0000269|PubMed:18511420}.
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. {ECO:0000250|UniProtKB:Q7L622}.
CC -!- DISRUPTION PHENOTYPE: Embryos die prior to implantation due to massive
CC apoptosis resulting in blastocyst involution.
CC {ECO:0000269|PubMed:18511420}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98142.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129332; BAC98142.1; ALT_INIT; mRNA.
DR EMBL; AC161116; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC086455; AAH86455.1; -; mRNA.
DR EMBL; AK084256; BAC39150.1; -; mRNA.
DR CCDS; CCDS25900.1; -.
DR RefSeq; NP_001015099.2; NM_001015099.2.
DR RefSeq; NP_001161435.1; NM_001167963.1.
DR RefSeq; NP_001161436.1; NM_001167964.1.
DR AlphaFoldDB; Q5RJY2; -.
DR SMR; Q5RJY2; -.
DR BioGRID; 229923; 1.
DR IntAct; Q5RJY2; 1.
DR STRING; 10090.ENSMUSP00000113270; -.
DR iPTMnet; Q5RJY2; -.
DR PhosphoSitePlus; Q5RJY2; -.
DR EPD; Q5RJY2; -.
DR PaxDb; Q5RJY2; -.
DR PRIDE; Q5RJY2; -.
DR ProteomicsDB; 271623; -.
DR Antibodypedia; 11; 126 antibodies from 19 providers.
DR DNASU; 217558; -.
DR Ensembl; ENSMUST00000054308; ENSMUSP00000054474; ENSMUSG00000035293.
DR GeneID; 217558; -.
DR KEGG; mmu:217558; -.
DR UCSC; uc007nml.2; mouse.
DR CTD; 55632; -.
DR MGI; MGI:2444298; G2e3.
DR VEuPathDB; HostDB:ENSMUSG00000035293; -.
DR eggNOG; KOG1084; Eukaryota.
DR GeneTree; ENSGT00950000182865; -.
DR InParanoid; Q5RJY2; -.
DR OMA; SFTMITR; -.
DR OrthoDB; 199998at2759; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 217558; 1 hit in 75 CRISPR screens.
DR ChiTaRS; G2e3; mouse.
DR PRO; PR:Q5RJY2; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q5RJY2; protein.
DR Bgee; ENSMUSG00000035293; Expressed in manus and 230 other tissues.
DR ExpressionAtlas; Q5RJY2; baseline and differential.
DR Genevisible; Q5RJY2; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
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:0061630; F:ubiquitin protein ligase activity; IDA:MGI.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0001824; P:blastocyst development; IMP:MGI.
DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; IMP:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:MGI.
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; IPR019786; Zinc_finger_PHD-type_CS.
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.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01359; ZF_PHD_1; 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..716
FT /note="G2/M phase-specific E3 ubiquitin-protein ligase"
FT /id="PRO_0000248345"
FT DOMAIN 369..696
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ZN_FING 11..51
FT /note="C2HC pre-PHD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 79..128
FT /note="PHD-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01146"
FT ZN_FING 141..195
FT /note="PHD-type 2; degenerate"
FT ZN_FING 237..286
FT /note="PHD-type 3"
FT CONFLICT 675
FT /note="T -> A (in Ref. 3; AAH86455)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 716 AA; 81784 MW; 9A3B7CE4A9F53A52 CRC64;
MNENKPDNSQ SLACVFCRKN DDCPNKYGEK KTYEKWNFSV HYYCLLMSSG IWQRGKEEEG
VYGFLIEDIR KEVQRASKLK CTVCKKNGAS IGCVVPTCKR SYHLPCGLQK ECIFQFTDNF
ASFCWKHRPV QAITSNKYSS SLPCTICLEF VEPIPTYNIL QSPCCKNAWF HRDCLQVQAI
NAGVFFFRCT LCNNTDIFQK EMLRMGIHIP EKDASWELEE NAYQELLQSH DRCDIRRCHC
KKGRDYNEPN SKWEVKRCQS CGSSGTHLAC SSLQSWEQNW ECLDCRRITY TSDFQKAPKH
PLANSTNVTV TDCLLEESSS KLPRQSTVAQ HKELLRQGSK FRRDISTILI ELGFQIKKKT
KTLYINKANV WRSALEQFQS QKFNPSCSID VVYVNGNEVG SQHLGSKQEF LSHLMHHLEN
SSVFEGSLAK NLSLNSQAVK ENLYYEVGKM LAISLVHGGP SPGFFSETLF NCLAYGPENT
LPTLDDVSDI DVAQIIIKID SATDLNILNS VISQHYNYLE VSGCLRLTTS LSDKFMLVKD
ILFYHVINRV KAPFESFKQG LKTLGVLEKI QTYPEAFYKI LCHKPENLSA KNLSDLFTIH
SVADVQTLRF WNSYLKAIED GKSATTMEDI LIFATGCSSV PPTGFKPSLS VECLHVDFPV
ADKYRNHLVL PATNTYEEFQ ENMDFTIRDT LRLEKEERSH ILPRTLNVSS NEEMLI
