UBE3B_HUMAN
ID UBE3B_HUMAN Reviewed; 1068 AA.
AC Q7Z3V4; A5D8Z3; Q05BX9; Q659F7; Q7Z7Q1; Q9BXZ4;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
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 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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
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] (ISOFORMS 1 AND 2), AND VARIANT
RP GLN-346.
RC TISSUE=Endometrial adenocarcinoma;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLN-346.
RC TISSUE=Brain, Lung, Prostate, and Skin;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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).
RN [7]
RP VARIANT KOS PRO-727.
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=UBE3B_v1;
CC IsoId=Q7Z3V4-1; Sequence=Displayed;
CC Name=2; Synonyms=UBE3B_v2;
CC IsoId=Q7Z3V4-2; Sequence=VSP_024087, VSP_024088;
CC Name=3;
CC IsoId=Q7Z3V4-3; Sequence=VSP_024085, VSP_024086;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:12837265}.
CC -!- DISEASE: Kaufman oculocerebrofacial syndrome (KOS) [MIM:244450]: A
CC syndrome characterized by blepharophimosis, ptosis, mild upslanting of
CC the palpebral fissures, epicanthus, ectodermal anomalies, developmental
CC delay, and severe intellectual disability with absent speech.
CC Proportionate growth retardation with a small head
CC circumference/microcephaly, congenital malformations, muscular
CC hypotonia, anomalies on brain imaging with hypoplasia of the corpus
CC callosum, and low cholesterol levels are variably present.
CC {ECO:0000269|PubMed:23200864}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: [Isoform 1]: Major isoform.
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DR EMBL; AF251046; AAK28419.2; -; mRNA.
DR EMBL; AL096740; CAH56410.1; -; mRNA.
DR EMBL; BX537403; CAD97645.1; -; mRNA.
DR EMBL; AC007570; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC032301; AAH32301.1; -; mRNA.
DR EMBL; BC051266; AAH51266.1; -; mRNA.
DR EMBL; BC068221; AAH68221.1; -; mRNA.
DR EMBL; BC108705; AAI08706.1; -; mRNA.
DR EMBL; BC141880; AAI41881.1; -; mRNA.
DR CCDS; CCDS58277.1; -. [Q7Z3V4-3]
DR CCDS; CCDS9129.1; -. [Q7Z3V4-1]
DR RefSeq; NP_001257378.1; NM_001270449.1. [Q7Z3V4-3]
DR RefSeq; NP_001257379.1; NM_001270450.1. [Q7Z3V4-3]
DR RefSeq; NP_001257380.1; NM_001270451.1. [Q7Z3V4-3]
DR RefSeq; NP_569733.2; NM_130466.3. [Q7Z3V4-1]
DR RefSeq; NP_904324.1; NM_183415.2. [Q7Z3V4-1]
DR RefSeq; XP_005254044.1; XM_005253987.2. [Q7Z3V4-1]
DR RefSeq; XP_011537261.1; XM_011538959.2. [Q7Z3V4-1]
DR RefSeq; XP_016875685.1; XM_017020196.1. [Q7Z3V4-3]
DR AlphaFoldDB; Q7Z3V4; -.
DR SMR; Q7Z3V4; -.
DR BioGRID; 124642; 25.
DR IntAct; Q7Z3V4; 5.
DR MINT; Q7Z3V4; -.
DR STRING; 9606.ENSP00000340596; -.
DR iPTMnet; Q7Z3V4; -.
DR PhosphoSitePlus; Q7Z3V4; -.
DR BioMuta; UBE3B; -.
DR DMDM; 296453010; -.
DR EPD; Q7Z3V4; -.
DR jPOST; Q7Z3V4; -.
DR MassIVE; Q7Z3V4; -.
DR MaxQB; Q7Z3V4; -.
DR PaxDb; Q7Z3V4; -.
DR PeptideAtlas; Q7Z3V4; -.
DR PRIDE; Q7Z3V4; -.
DR ProteomicsDB; 69089; -. [Q7Z3V4-1]
DR ProteomicsDB; 69090; -. [Q7Z3V4-2]
DR ProteomicsDB; 69091; -. [Q7Z3V4-3]
DR Antibodypedia; 30872; 81 antibodies from 19 providers.
DR DNASU; 89910; -.
DR Ensembl; ENST00000340074.9; ENSP00000342614.5; ENSG00000151148.14. [Q7Z3V4-3]
DR Ensembl; ENST00000342494.8; ENSP00000340596.3; ENSG00000151148.14. [Q7Z3V4-1]
DR Ensembl; ENST00000434735.6; ENSP00000391529.2; ENSG00000151148.14. [Q7Z3V4-1]
DR Ensembl; ENST00000449510.6; ENSP00000395802.2; ENSG00000151148.14. [Q7Z3V4-2]
DR Ensembl; ENST00000536398.5; ENSP00000440585.1; ENSG00000151148.14. [Q7Z3V4-3]
DR Ensembl; ENST00000540230.5; ENSP00000443565.1; ENSG00000151148.14. [Q7Z3V4-3]
DR GeneID; 89910; -.
DR KEGG; hsa:89910; -.
DR MANE-Select; ENST00000342494.8; ENSP00000340596.3; NM_130466.4; NP_569733.2.
DR UCSC; uc001tom.5; human. [Q7Z3V4-1]
DR CTD; 89910; -.
DR DisGeNET; 89910; -.
DR GeneCards; UBE3B; -.
DR GeneReviews; UBE3B; -.
DR HGNC; HGNC:13478; UBE3B.
DR HPA; ENSG00000151148; Low tissue specificity.
DR MalaCards; UBE3B; -.
DR MIM; 244450; phenotype.
DR MIM; 608047; gene.
DR neXtProt; NX_Q7Z3V4; -.
DR OpenTargets; ENSG00000151148; -.
DR Orphanet; 2707; Oculocerebrofacial syndrome, Kaufman type.
DR PharmGKB; PA134872189; -.
DR VEuPathDB; HostDB:ENSG00000151148; -.
DR eggNOG; KOG4427; Eukaryota.
DR GeneTree; ENSGT00940000156548; -.
DR HOGENOM; CLU_002173_2_0_1; -.
DR InParanoid; Q7Z3V4; -.
DR OMA; VVGWLWD; -.
DR PhylomeDB; Q7Z3V4; -.
DR TreeFam; TF313215; -.
DR BRENDA; 2.3.2.26; 2681.
DR BRENDA; 2.3.2.B11; 2681.
DR PathwayCommons; Q7Z3V4; -.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; Q7Z3V4; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 89910; 10 hits in 1124 CRISPR screens.
DR ChiTaRS; UBE3B; human.
DR GenomeRNAi; 89910; -.
DR Pharos; Q7Z3V4; Tbio.
DR PRO; PR:Q7Z3V4; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q7Z3V4; protein.
DR Bgee; ENSG00000151148; Expressed in oocyte and 200 other tissues.
DR ExpressionAtlas; Q7Z3V4; baseline and differential.
DR Genevisible; Q7Z3V4; HS.
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 SMART; SM00119; HECTc; 1.
DR SMART; SM00015; IQ; 1.
DR SUPFAM; SSF56204; SSF56204; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS50096; IQ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant;
KW Intellectual disability; Phosphoprotein; Reference proteome; Transferase;
KW Ubl conjugation pathway.
FT CHAIN 1..1068
FT /note="Ubiquitin-protein ligase E3B"
FT /id="PRO_0000281882"
FT DOMAIN 29..58
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 702..1068
FT /note="HECT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT ACT_SITE 1036
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00104"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 419
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VAR_SEQ 211..244
FT /note="ILLTRGLARPRPCLSKGTLTAAFSLALRPVIAAQ -> CCDGLFPDLVSYAP
FT HNNPVRWSVGRSWYDWQLSR (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024085"
FT VAR_SEQ 245..1068
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_024086"
FT VAR_SEQ 693..708
FT /note="DGYEQLRQLSQHAMKG -> SLFECPWPLVINAESC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12837265,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_024087"
FT VAR_SEQ 709..1068
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12837265,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_024088"
FT VARIANT 346
FT /note="R -> Q (in dbSNP:rs7298565)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_031302"
FT VARIANT 727
FT /note="Q -> P (in KOS; dbSNP:rs398123023)"
FT /evidence="ECO:0000269|PubMed:23200864"
FT /id="VAR_069712"
FT CONFLICT 151
FT /note="E -> V (in Ref. 2; CAD97645)"
FT /evidence="ECO:0000305"
FT CONFLICT 907
FT /note="I -> V (in Ref. 2; CAD97645)"
FT /evidence="ECO:0000305"
FT CONFLICT 942
FT /note="Y -> H (in Ref. 2; CAD97645)"
FT /evidence="ECO:0000305"
FT CONFLICT 1018
FT /note="F -> S (in Ref. 2; CAD97645)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1068 AA; 123098 MW; A1740A3DDC5E1A4D CRC64;
MFTLSQTSRA WFIDRARQAR EERLVQKERE RAAVVIQAHV RSFLCRSRLQ RDIRREIDDF
FKADDPESTK RSALCIFKIA RKLLFLFRIK EDNERFEKLC RSILSSMDAE NEPKVWYVSL
ACSKDLTLLW IQQIKNILWY CCDFLKQLKP EILQDSRLIT LYLTMLVTFT DTSTWKILRG
KGESLRPAMN HICANIMGHL NQHGFYSVLQ ILLTRGLARP RPCLSKGTLT AAFSLALRPV
IAAQFSDNLI RPFLIHIMSV PALVTHLSTV TPERLTVLES HDMLRKFIIF LRDQDRCRDV
CESLEGCHTL CLMGNLLHLG SLSPRVLEEE TDGFVSLLTQ TLCYCRKYVS QKKSNLTHWH
PVLGWFSQSV DYGLNESMHL ITKQLQFLWG VPLIRIFFCD ILSKKLLESQ EPAHAQPASP
QNVLPVKSLL KRAFQKSASV RNILRPVGGK RVDSAEVQKV CNICVLYQTS LTTLTQIRLQ
ILTGLTYLDD LLPKLWAFIC ELGPHGGLKL FLECLNNDTE ESKQLLAMLM LFCDCSRHLI
TILDDIEVYE EQISFKLEEL VTISSFLNSF VFKMIWDGIV ENAKGETLEL FQSVHGWLMV
LYERDCRRRF TPEDHWLRKD LKPSVLFQEL DRDRKRAQLI LQYIPHVIPH KNRVLLFRTM
VTKEKEKLGL VETSSASPHV THITIRRSRM LEDGYEQLRQ LSQHAMKGVI RVKFVNDLGV
DEAGIDQDGV FKEFLEEIIK RVFDPALNLF KTTSGDERLY PSPTSYIHEN YLQLFEFVGK
MLGKAVYEGI VVDVPFASFF LSQLLGHHHS VFYSSVDELP SLDSEFYKNL TSIKRYDGDI
TDLGLTLSYD EDVMGQLVCH ELIPGGKTIP VTNENKISYI HLMAHFRMHT QIKNQTAALI
SGFRSIIKPE WIRMFSTPEL QRLISGDNAE IDLEDLKKHT VYYGGFHGSH RVIIWLWDIL
ASDFTPDERA MFLKFVTSCS RPPLLGFAYL KPPFSIRCVE VSDDQDTGDT LGSVLRGFFT
IRKREPGGRL PTSSTCFNLL KLPNYSKKSV LREKLRYAIS MNTGFELS
