UBE3B

Protein identityUniProt · HPA

UniProt accession

Q7Z3V4

Gene

UBE3B

Ensembl

ENSG00000151148

Chromosome

12

Canonical length

1068 aa

Protein class

Disease related genes, Enzymes, Human disease related genes, Metabolic proteins, Potential drug targets, Predicted intracellular proteins

Subcellular location

Nuclear speckles,Mitochondria

OverviewNCBI Gene

The modification of proteins with ubiquitin is an important cellular mechanism for targeting abnormal or short-lived proteins for degradation. Ubiquitination involves at least three classes of enzymes: E1 ubiquitin-activating enzymes, E2 ubiquitin-conjugating enzymes, and E3 ubiquitin-protein ligases. This gene encodes a member of the E3 ubiquitin-conjugating enzyme family which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme and transfers the ubiquitin to the targeted substrates. A HECT (homology to E6-AP C-terminus) domain in the C-terminus of the longer isoform of this protein is the catalytic site of ubiquitin transfer and forms a complex with E2 conjugases. Shorter isoforms of this protein which lack the C-terminal HECT domain are therefore unlikely to bind E2 enzymes. Alternatively spliced transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Jul 2012]

Canonical amino-acid sequenceUniProt

1068 residues, UniProt reviewed canonical sequence.

>Q7Z3V4|UBE3B
     1  MFTLSQTSRA WFIDRARQAR EERLVQKERE RAAVVIQAHV RSFLCRSRLQ RDIRREIDDF
    61  FKADDPESTK RSALCIFKIA RKLLFLFRIK EDNERFEKLC RSILSSMDAE NEPKVWYVSL
   121  ACSKDLTLLW IQQIKNILWY CCDFLKQLKP EILQDSRLIT LYLTMLVTFT DTSTWKILRG
   181  KGESLRPAMN HICANIMGHL NQHGFYSVLQ ILLTRGLARP RPCLSKGTLT AAFSLALRPV
   241  IAAQFSDNLI RPFLIHIMSV PALVTHLSTV TPERLTVLES HDMLRKFIIF LRDQDRCRDV
   301  CESLEGCHTL CLMGNLLHLG SLSPRVLEEE TDGFVSLLTQ TLCYCRKYVS QKKSNLTHWH
   361  PVLGWFSQSV DYGLNESMHL ITKQLQFLWG VPLIRIFFCD ILSKKLLESQ EPAHAQPASP
   421  QNVLPVKSLL KRAFQKSASV RNILRPVGGK RVDSAEVQKV CNICVLYQTS LTTLTQIRLQ
   481  ILTGLTYLDD LLPKLWAFIC ELGPHGGLKL FLECLNNDTE ESKQLLAMLM LFCDCSRHLI
   541  TILDDIEVYE EQISFKLEEL VTISSFLNSF VFKMIWDGIV ENAKGETLEL FQSVHGWLMV
   601  LYERDCRRRF TPEDHWLRKD LKPSVLFQEL DRDRKRAQLI LQYIPHVIPH KNRVLLFRTM
   661  VTKEKEKLGL VETSSASPHV THITIRRSRM LEDGYEQLRQ LSQHAMKGVI RVKFVNDLGV
   721  DEAGIDQDGV FKEFLEEIIK RVFDPALNLF KTTSGDERLY PSPTSYIHEN YLQLFEFVGK
   781  MLGKAVYEGI VVDVPFASFF LSQLLGHHHS VFYSSVDELP SLDSEFYKNL TSIKRYDGDI
   841  TDLGLTLSYD EDVMGQLVCH ELIPGGKTIP VTNENKISYI HLMAHFRMHT QIKNQTAALI
   901  SGFRSIIKPE WIRMFSTPEL QRLISGDNAE IDLEDLKKHT VYYGGFHGSH RVIIWLWDIL
   961  ASDFTPDERA MFLKFVTSCS RPPLLGFAYL KPPFSIRCVE VSDDQDTGDT LGSVLRGFFT
  1021  IRKREPGGRL PTSSTCFNLL KLPNYSKKSV LREKLRYAIS MNTGFELS

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against UBE3B can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Intracellular

Secreted

No

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.28

Highest tissue expression

32 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about UBE3B.

Disease | AllUniProt

Conditions UBE3B is implicated in, by any mechanism.

• Kaufman oculocerebrofacial syndrome (KOS) MIM:244450

Disease | GeneticClinVar

70 pathogenic / likely-pathogenic of 589 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Oculocerebrofacial syndrome, Kaufman type
• Inborn genetic diseases
• Blepharophimosis - intellectual disability syndrome

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.55

gnomAD pLI

0

gnomAD missense Z

1.36

DepMap mean gene effect

0.02

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• protein polyubiquitination
• regulation of postsynapse assembly
• ubiquitin-dependent protein catabolic process

Molecular functions

• ubiquitin protein ligase activity

Cellular components

• glutamatergic synapse
• mitochondrion
• postsynaptic density

Protein domainsUniProt · Pfam · InterPro

• IQ motif, EF-hand binding site
• HECT domain
• HECT, E3 ligase catalytic domain
• Ubiquitin-protein ligase E3A/B/C-like
• HECT-domain (ubiquitin-transferase)

KeywordsUniProt

• Acetylation
• Intellectual disability
• Phosphoprotein
• Synapse
• Transferase
• Ubl conjugation pathway

InteractionsUniProt · HPA

Protein binding partners of UBE3B in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• CALM1