UBE3B_MOUSE
ID UBE3B_MOUSE Reviewed; 1070 AA.
AC Q9ES34; Q8K068;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Ubiquitin-protein ligase E3B;
DE EC=2.3.2.26;
DE AltName: Full=HECT-type ubiquitin transferase E3B;
GN Name=Ube3b;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=C57BL/6J;
RX PubMed=12837265; DOI=10.1016/s0888-7543(03)00111-3;
RA Gong T.-W.L., Huang L., Warner S.J., Lomax M.I.;
RT "Characterization of the human UBE3B gene: structure, expression,
RT evolution, and alternative splicing.";
RL Genomics 82:143-152(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Eye, Liver, and Mammary tumor;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Liver, Lung, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=23200864; DOI=10.1016/j.ajhg.2012.10.011;
RA Basel-Vanagaite L., Dallapiccola B., Ramirez-Solis R., Segref A.,
RA Thiele H., Edwards A., Arends M.J., Miro X., White J.K., Desir J.,
RA Abramowicz M., Dentici M.L., Lepri F., Hofmann K., Har-Zahav A., Ryder E.,
RA Karp N.A., Estabel J., Gerdin A.K., Podrini C., Ingham N.J., Altmueller J.,
RA Nuernberg G., Frommolt P., Abdelhak S., Pasmanik-Chor M., Konen O.,
RA Kelley R.I., Shohat M., Nuernberg P., Flint J., Steel K.P., Hoppe T.,
RA Kubisch C., Adams D.J., Borck G.;
RT "Deficiency for the ubiquitin ligase UBE3B in a blepharophimosis-ptosis-
RT intellectual-disability syndrome.";
RL Am. J. Hum. Genet. 91:998-1010(2012).
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. {ECO:0000250}.
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 -!- TISSUE SPECIFICITY: Widely expressed. High expression is observed in
CC developing central nervous system. {ECO:0000269|PubMed:12837265,
CC ECO:0000269|PubMed:23200864}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH34059.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF244362; AAG16783.3; -; mRNA.
DR EMBL; BC023956; AAH23956.1; -; mRNA.
DR EMBL; BC034059; AAH34059.1; ALT_INIT; mRNA.
DR EMBL; BC096743; AAH96743.1; -; mRNA.
DR CCDS; CCDS19564.1; -.
DR RefSeq; NP_473434.2; NM_054093.3.
DR AlphaFoldDB; Q9ES34; -.
DR SMR; Q9ES34; -.
DR BioGRID; 228169; 3.
DR STRING; 10090.ENSMUSP00000073652; -.
DR iPTMnet; Q9ES34; -.
DR PhosphoSitePlus; Q9ES34; -.
DR SwissPalm; Q9ES34; -.
DR EPD; Q9ES34; -.
DR MaxQB; Q9ES34; -.
DR PaxDb; Q9ES34; -.
DR PeptideAtlas; Q9ES34; -.
DR PRIDE; Q9ES34; -.
DR ProteomicsDB; 297787; -.
DR Antibodypedia; 30872; 81 antibodies from 19 providers.
DR DNASU; 117146; -.
DR Ensembl; ENSMUST00000074002; ENSMUSP00000073652; ENSMUSG00000029577.
DR GeneID; 117146; -.
DR KEGG; mmu:117146; -.
DR UCSC; uc008yzn.1; mouse.
DR CTD; 89910; -.
DR MGI; MGI:1891295; Ube3b.
DR VEuPathDB; HostDB:ENSMUSG00000029577; -.
DR eggNOG; KOG4427; Eukaryota.
DR GeneTree; ENSGT00940000156548; -.
DR HOGENOM; CLU_002173_2_0_1; -.
DR InParanoid; Q9ES34; -.
DR OMA; VVGWLWD; -.
DR OrthoDB; 1163565at2759; -.
DR PhylomeDB; Q9ES34; -.
DR TreeFam; TF313215; -.
DR Reactome; R-MMU-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 117146; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Ube3b; mouse.
DR PRO; PR:Q9ES34; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q9ES34; protein.
DR Bgee; ENSMUSG00000029577; Expressed in hindlimb stylopod muscle and 266 other tissues.
DR ExpressionAtlas; Q9ES34; baseline and differential.
DR Genevisible; Q9ES34; MM.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
DR GO; GO:0000209; P:protein polyubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR CDD; cd00078; HECTc; 1.
DR InterPro; IPR044611; E3B/C.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR PANTHER; PTHR45700; PTHR45700; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00612; IQ; 1.
DR SMART; SM00119; HECTc; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1070
FT /note="Ubiquitin-protein ligase E3B"
FT /id="PRO_0000281883"
FT DOMAIN 29..58
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 704..1070
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 1038
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3V4"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3V4"
SQ SEQUENCE 1070 AA; 122762 MW; AEC9A7F4232A434E CRC64;
MFTVSQTSRA WFIDRARQAR EERLVQKERE RSAVTIQALV RSFLCRRRLH RDIRKEIDEF
FSADESGSSK RSALCIFKIA RRLLFICKTT EDSERLEKLC RSILNSMDAE NEPKVWYVSL
ALSKDLTLLW IKQIKSILWH CCELLGQLKP EILQDSRLIT LYLTMLVTFT DTSTWKILRG
KGESLRPALN HICANIMGHL NQRGLYSVLQ VLLTRGLARP RPCLSKGMLT AAFSLALRPV
VAAQFSDNLM RPFIIHVMSV PALVAHLSTV APERLGVLES HDMLRKFIVF LRDRDRCRDA
CESLEGCHTL CLMGNLLHLG SLSLRLLEEE MDGFVSALTQ MLCYCQKYVA QKKSNLTHWH
PVLGWFSQPV DYGLNDSMYL ITKQLQFLWA VPLIRILFSD ILSRKLLEHA EPAPVQPQPS
SPQTVLPVKS LLKRAFQKSA SVRNILRPVG GRRVDSAEVR KVCNICVLYQ TSLTTLTQIR
LQILTGLTYL DDLLPKLWAF ICELGPHGGL KLFLECLNND TGESKQLLAM LMLFCDCSRH
LITILDDIEV YEEQISFKLE ELVTISSFLN SFVFKMIWDG IVENAKGETL ELFQSVHGWL
MVLYERDCRR RFAPEDHWLR RDLKPGVLFQ ELDKDRRRAQ LVLQHIPHVV PHKNRVLLFR
NMVIKEKEKL GLVETSSASP HVTHITIRRS RMLEDGYEQL RQLSQHAMKG VIRVKFVNDL
GVDEAGIDQD GVFKEFLEEI IKRVFDPALN LFKTTSGDER LYPSPTSYIH ENYLQLFEFV
GKMLGKAVYE GIVVDVPFAS FFLSQMLGHH HSVFYSSVDE LPSLDSEFYK NLTSIKRYDG
DIADLGLTLS YDEDVMGQLV CHELVPGGKT IPVTDENKIS YIHLMAHFRM HTQIKNQTAA
LISGFRSIIK PEWIRMFSTP ELQRLISGDN AEIDLEDLKK HTVYYGGFHG SHRVIIWLWD
ILASDFTPEE RAMFLKFVTS CSRPPLLGFA YLKPPFSIRC VEVSDDQDTG DTLGSVLRGF
FTIRKREPGG RLPTSSTCFN LLKLPNYSKK SVLREKLRYA ISMNTGFELS
