UBE3D_HUMAN
ID UBE3D_HUMAN Reviewed; 389 AA.
AC Q7Z6J8; B4DP63; Q5T4W2; Q6IPR4; Q75UG0; Q9NT42;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=C6orf157, H10BH, UBE2CBP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH UBE2C AND CYCLIN-B, AND
RP FUNCTION.
RC TISSUE=Cervix carcinoma;
RX PubMed=15749827; DOI=10.1093/jb/mvi026;
RA Kobirumaki F., Miyauchi Y., Fukami K., Tanaka H.;
RT "A novel UbcH10-binding protein facilitates the ubiquitinylation of cyclin
RT B in vitro.";
RL J. Biochem. 137:133-139(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood, and Bone marrow;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 45-226.
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
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:0000269|PubMed:15749827}.
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 In vitro, interacts with cyclin-B. {ECO:0000269|PubMed:15749827}.
CC -!- INTERACTION:
CC Q7Z6J8; P43364: MAGEA11; NbExp=3; IntAct=EBI-9379147, EBI-739552;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: The C-terminal half (AA 188-389) 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 -!- PTM: Ubiquitinated by UBCH10 (E2 ubiquitin-conjugating enzyme).
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH53645.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB126062; BAD01604.1; -; mRNA.
DR EMBL; AK298205; BAG60475.1; -; mRNA.
DR EMBL; AL034377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139333; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL355613; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL357121; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48681.1; -; Genomic_DNA.
DR EMBL; BC053645; AAH53645.1; ALT_INIT; mRNA.
DR EMBL; BC071763; AAH71763.1; -; mRNA.
DR EMBL; BC101512; AAI01513.1; -; mRNA.
DR EMBL; BC101538; AAI01539.1; -; mRNA.
DR EMBL; AL137544; CAB70802.1; -; mRNA.
DR CCDS; CCDS34491.1; -.
DR PIR; T46387; T46387.
DR RefSeq; NP_001291366.1; NM_001304437.1.
DR RefSeq; NP_944602.1; NM_198920.2.
DR AlphaFoldDB; Q7Z6J8; -.
DR BioGRID; 124656; 35.
DR IntAct; Q7Z6J8; 17.
DR MINT; Q7Z6J8; -.
DR STRING; 9606.ENSP00000358762; -.
DR iPTMnet; Q7Z6J8; -.
DR PhosphoSitePlus; Q7Z6J8; -.
DR BioMuta; UBE3D; -.
DR DMDM; 160395569; -.
DR EPD; Q7Z6J8; -.
DR jPOST; Q7Z6J8; -.
DR MassIVE; Q7Z6J8; -.
DR MaxQB; Q7Z6J8; -.
DR PaxDb; Q7Z6J8; -.
DR PeptideAtlas; Q7Z6J8; -.
DR PRIDE; Q7Z6J8; -.
DR ProteomicsDB; 69428; -.
DR Antibodypedia; 18484; 9 antibodies from 7 providers.
DR DNASU; 90025; -.
DR Ensembl; ENST00000369747.8; ENSP00000358762.3; ENSG00000118420.17.
DR GeneID; 90025; -.
DR KEGG; hsa:90025; -.
DR MANE-Select; ENST00000369747.8; ENSP00000358762.3; NM_198920.3; NP_944602.1.
DR UCSC; uc003pjp.4; human.
DR CTD; 90025; -.
DR DisGeNET; 90025; -.
DR GeneCards; UBE3D; -.
DR HGNC; HGNC:21381; UBE3D.
DR HPA; ENSG00000118420; Low tissue specificity.
DR MIM; 612495; gene.
DR neXtProt; NX_Q7Z6J8; -.
DR OpenTargets; ENSG00000118420; -.
DR PharmGKB; PA162407873; -.
DR VEuPathDB; HostDB:ENSG00000118420; -.
DR eggNOG; KOG4784; Eukaryota.
DR GeneTree; ENSGT00390000003986; -.
DR HOGENOM; CLU_060972_0_0_1; -.
DR InParanoid; Q7Z6J8; -.
DR OMA; DPFANRK; -.
DR OrthoDB; 1587082at2759; -.
DR PhylomeDB; Q7Z6J8; -.
DR TreeFam; TF324684; -.
DR PathwayCommons; Q7Z6J8; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q7Z6J8; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 90025; 132 hits in 1133 CRISPR screens.
DR ChiTaRS; UBE3D; human.
DR GenomeRNAi; 90025; -.
DR Pharos; Q7Z6J8; Tbio.
DR PRO; PR:Q7Z6J8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q7Z6J8; protein.
DR Bgee; ENSG00000118420; Expressed in buccal mucosa cell and 156 other tissues.
DR ExpressionAtlas; Q7Z6J8; baseline and differential.
DR Genevisible; Q7Z6J8; HS.
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; IDA:UniProtKB.
DR GO; GO:0030332; F:cyclin binding; IPI:UniProtKB.
DR GO; GO:0031624; F:ubiquitin conjugating enzyme binding; IBA:GO_Central.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB.
DR GO; GO:0044390; F:ubiquitin-like protein conjugating enzyme binding; IPI:UniProtKB.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0051865; P:protein autoubiquitination; IDA:UniProtKB.
DR GO; GO:0006513; P:protein monoubiquitination; IDA:UniProtKB.
DR GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
DR InterPro; IPR019193; UBQ-conj_enz_E2-bd_prot.
DR PANTHER; PTHR31531; PTHR31531; 1.
DR Pfam; PF09814; HECT_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; Reference proteome; Transferase; Ubl conjugation;
KW Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..389
FT /note="E3 ubiquitin-protein ligase E3D"
FT /id="PRO_0000311190"
FT REGION 235..257
FT /note="Interaction with UBE2C"
FT /evidence="ECO:0000269|PubMed:15749827"
FT REGION 353..389
FT /note="HECT-like"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VARIANT 174
FT /note="T -> P (in dbSNP:rs12528542)"
FT /id="VAR_037152"
FT VARIANT 379
FT /note="V -> M (in dbSNP:rs7739323)"
FT /id="VAR_037153"
FT CONFLICT 223..226
FT /note="ETTK -> ARSC (in Ref. 6; CAB70802)"
FT /evidence="ECO:0000305"
FT CONFLICT 340
FT /note="S -> G (in Ref. 5; AAH71763)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 389 AA; 43657 MW; 5F72BE6670863E2B CRC64;
MAASAAETRV FLEVRGQLQS ALLILGEPKE GGMPMNISIM PSSLQMKTPE GCTEIQLPAE
VRLVPSSCRG LQFVVGDGLH LRLQTQAKLG TKLISMFNQS SQTQECCTFY CQSCGEVIIK
DRKLLRVLPL PSENWGALVG EWCCHPDPFA NKSLHPQEND CFIGDSFFLV NLRTSLWQQR
PELSPVEMCC VSSDNHCKLE PKANTKVICK RCKVMLGETV SSETTKFYMT EIIIQSSERS
FPIIPRSWFV QSVIAQCLVQ LSSARSTFRF TIQGQDDKVY ILLWLLNSDS LVIESLRNSK
YIKKFPLLEN TFKADSSSAW SAVKVLYQPC IKSRNEKLVS LWESDISVHP LTLPSATCLE
LLLILSKSNA NLPSSLRRVN SFQVAFLKM
