UBE3D_MOUSE
ID UBE3D_MOUSE Reviewed; 368 AA.
AC Q8BX13;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=E3 ubiquitin-protein ligase E3D;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type E3 ubiquitin transferase E3D {ECO:0000305};
DE AltName: Full=UbcH10-binding protein with a HECT-like domain;
DE AltName: Full=Ubiquitin-conjugating enzyme E2C-binding protein;
GN Name=Ube3d; Synonyms=H10bh, Ube2cbp;
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 STRAIN=C57BL/6J;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
CC -!- FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from
CC specific E2 ubiquitin-conjugating enzymes, and transfers it to
CC substrates, generally promoting their degradation by the proteasome.
CC {ECO:0000250|UniProtKB:Q7Z6J8}.
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 -!- SUBUNIT: Interacts with UBE2C/UbcH10 (E2 ubiquitin-conjugating enzyme).
CC {ECO:0000250|UniProtKB:Q7Z6J8}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The C-terminal half (AA 167-368) is able to bind cyclin-B and
CC shows a self-ubiquitination activity (mono-, poly, or multi-
CC ubiquitination) in a HECT-like sequence dependent manner.
CC {ECO:0000250|UniProtKB:Q7Z6J8}.
CC -!- PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).
CC {ECO:0000250|UniProtKB:Q7Z6J8}.
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DR EMBL; AK049229; BAC33623.1; -; mRNA.
DR EMBL; BC115686; AAI15687.1; -; mRNA.
DR EMBL; BC115687; AAI15688.1; -; mRNA.
DR CCDS; CCDS40713.1; -.
DR RefSeq; NP_081670.1; NM_027394.2.
DR AlphaFoldDB; Q8BX13; -.
DR STRING; 10090.ENSMUSP00000034986; -.
DR PhosphoSitePlus; Q8BX13; -.
DR EPD; Q8BX13; -.
DR MaxQB; Q8BX13; -.
DR PaxDb; Q8BX13; -.
DR PRIDE; Q8BX13; -.
DR ProteomicsDB; 297788; -.
DR Antibodypedia; 18484; 9 antibodies from 7 providers.
DR Ensembl; ENSMUST00000034986; ENSMUSP00000034986; ENSMUSG00000032415.
DR GeneID; 70348; -.
DR KEGG; mmu:70348; -.
DR UCSC; uc009qxc.1; mouse.
DR CTD; 70348; -.
DR MGI; MGI:1917598; Ube2cbp.
DR VEuPathDB; HostDB:ENSMUSG00000032415; -.
DR eggNOG; KOG4784; Eukaryota.
DR GeneTree; ENSGT00390000003986; -.
DR HOGENOM; CLU_060972_0_0_1; -.
DR InParanoid; Q8BX13; -.
DR OMA; DPFANRK; -.
DR OrthoDB; 1587082at2759; -.
DR PhylomeDB; Q8BX13; -.
DR TreeFam; TF324684; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 70348; 14 hits in 73 CRISPR screens.
DR ChiTaRS; Ube2cbp; mouse.
DR PRO; PR:Q8BX13; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BX13; protein.
DR Bgee; ENSMUSG00000032415; Expressed in floor plate of midbrain and 115 other tissues.
DR ExpressionAtlas; Q8BX13; baseline and differential.
DR Genevisible; Q8BX13; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000151; C:ubiquitin ligase complex; ISO:MGI.
DR GO; GO:0030332; F:cyclin binding; ISO:MGI.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0006513; P:protein monoubiquitination; ISO:MGI.
DR GO; GO:0000209; P:protein polyubiquitination; ISO:MGI.
DR InterPro; IPR019193; UBQ-conj_enz_E2-bd_prot.
DR PANTHER; PTHR31531; PTHR31531; 1.
DR Pfam; PF09814; HECT_2; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J8"
FT CHAIN 2..368
FT /note="E3 ubiquitin-protein ligase E3D"
FT /id="PRO_0000311191"
FT REGION 214..236
FT /note="Interaction with UBE2C"
FT /evidence="ECO:0000250"
FT REGION 332..368
FT /note="HECT-like"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6J8"
SQ SEQUENCE 368 AA; 40753 MW; 5AE96DD625A7277D CRC64;
MAVAAAETRV FLEVRRRLQS ALLILGGPDE GGMHLDISIT PTSLLVRTPD GCTEIRLPAG
VRLVPSSCGG LQYISGDGLH LRLRVQAESS PQPISVFNQS LQAQECCTFY CQSCGEVTIK
DRKLLRVLPL PSENWSALVG EWCCHPDPFA NRPLHPREND CFIGDSFFLV NLKSDLEQEP
KANTKVICKR CKVTLGETMS SETTKFYMTE VIIRPSEGSF PNIPRSQFLQ SIIAQCLVEL
SSARSTFRFT IQGQDGKVYI LLWVLNSDSL VIEPLRSSSC SRKFPLLESS LEAGSGSAWN
AIKVLYQPCI KSRNKELASS WEGDISVHPL TLPSATCLEL LLILSRNNAS LPLSLRQMNS
FQVAFLKM
