O95155 · UBE4B_HUMAN
- ProteinUbiquitin conjugation factor E4 B
- GeneUBE4B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1302 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May also function as an E4 ligase mediating the assembly of polyubiquitin chains on substrates ubiquitinated by another E3 ubiquitin ligase (By similarity).
May regulate myosin assembly in striated muscles together with STUB1 and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820).
Catalytic activity
Pathway
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 109-110 | Cleavage; by caspase-3 and caspase-7 | ||||
Sequence: DG | ||||||
Site | 123-124 | Cleavage; by caspase-6 and granzyme B | ||||
Sequence: DS |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | enzyme binding | |
Molecular Function | ubiquitin-ubiquitin ligase activity | |
Biological Process | ERAD pathway | |
Biological Process | granzyme-mediated apoptotic signaling pathway | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process | |
Biological Process | protein polyubiquitination | |
Biological Process | response to UV | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
MAPK3 , PRMT1 , PGAM5, OTUB1 and PPP3CA are ubiquitinated by E4B for degradation.
Names & Taxonomy
Protein names
- Recommended nameUbiquitin conjugation factor E4 B
- EC number
- Alternative names
Gene names
- Community suggested namesE4b
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95155
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 109 | Abolishes cleavage by caspase-3 and caspase-7. | ||||
Sequence: D → A | ||||||
Mutagenesis | 121 | Abolishes cleavage by caspase-6. No effect on cleavage by granzyme B. | ||||
Sequence: D → A | ||||||
Mutagenesis | 123 | Abolishes cleavage by caspase-6 and granzyme B. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_052437 | 605 | in dbSNP:rs17034499 | |||
Sequence: V → I |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,051 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000194993 | 1-1302 | UniProt | Ubiquitin conjugation factor E4 B | |||
Sequence: MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSEEQALQLVCKIFRVSWKDRDRDVIFLSSLSAQFKQNPKEVFSDFKDLIGQILMEVLMMSTQTRDENPFASLTATSQPIAAAARSPDRNLLLNTGSNPGTSPMFCSVASFGASSLSSLYESSPAPTPSFWSSVPVMGPSLASPSRAASQLAVPSTPLSPHSAASGTAAGSQPSSPRYRPYTVTHPWASSGVSILSSSPSPPALASSPQAVPASSSRQRPSSTGPPLPPASPSATSRRPSSLRISPSLGASGGASNWDSYSDHFTIETCKETDMLNYLIECFDRVGIEEKKAPKMCSQPAVSQLLSNIRSQCISHTALVLQGSLTQPRSLQQPSFLVPYMLCRNLPYGFIQELVRTTHQDEEVFKQIFIPILQGLALAAKECSLDSDYFKYPLMALGELCETKFGKTHPVCNLVASLRLWLPKSLSPGCGRELQRLSYLGAFFSFSVFAEDDVKVVEKYFSGPAITLENTRVVSQSLQHYLELGRQELFKILHSILLNGETREAALSYMAAVVNANMKKAQMQTDDRLVSTDGFMLNFLWVLQQLSTKIKLETVDPTYIFHPRCRITLPNDETRVNATMEDVNDWLTELYGDQPPFSEPKFPTECFFLTLHAHHLSILPSCRRYIRRLRAIRELNRTVEDLKNNESQWKDSPLATRHREMLKRCKTQLKKLVRCKACADAGLLDESFLRRCLNFYGLLIQLLLRILDPAYPDITLPLNSDVPKVFAALPEFYVEDVAEFLFFIVQYSPQALYEPCTQDIVMFLVVMLCNQNYIRNPYLVAKLVEVMFMTNPAVQPRTQKFFEMIENHPLSTKLLVPSLMKFYTDVEHTGATSEFYDKFTIRYHISTIFKSLWQNIAHHGTFMEEFNSGKQFVRYINMLINDTTFLLDESLESLKRIHEVQEEMKNKEQWDQLPRDQQQARQSQLAQDERVSRSYLALATETVDMFHILTKQVQKPFLRPELGPRLAAMLNFNLQQLCGPKCRDLKVENPEKYGFEPKKLLDQLTDIYLQLDCARFAKAIADDQRSYSKELFEEVISKMRKAGIKSTIAIEKFKLLAEKVEEIVAKNARAEIDYSDAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQNSDH | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 26 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 30 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 31 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 31 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 76 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 78 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 84 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 84 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 87 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 88 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 90 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 101 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 103 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 103 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 105 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 105 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 124 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 143 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 229 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 238 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 238 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 311 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 323 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 383 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 798 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 803 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 803 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 969 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1256 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1265 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1265 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1267 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest expression in ovary, testis, heart and skeletal muscle (PubMed:11802788).
Expression is low in colon, thymus and peripheral blood leukocytes (PubMed:11802788).
Almost undetectable in lung and spleen (PubMed:11802788).
Gene expression databases
Organism-specific databases
Interaction
Subunit
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95155 | UBL7 Q96S82 | 2 | EBI-1641720, EBI-348604 | |
BINARY | O95155-1 | UBE2D2 P62837 | 2 | EBI-15869194, EBI-347677 | |
BINARY | O95155-1 | UBE2D3 P61077-1 | 3 | EBI-15869194, EBI-15567256 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEELSADEIRRRRLA | ||||||
Region | 1-155 | Disordered | ||||
Sequence: MEELSADEIRRRRLARLAGGQTSQPTTPLTSPQRENPPGPPIAASAPGPSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVDSGIENMEVDENDRREKRSLSDKEPSSGPEVSE | ||||||
Compositional bias | 31-45 | Pro residues | ||||
Sequence: SPQRENPPGPPIAAS | ||||||
Compositional bias | 49-123 | Polar residues | ||||
Sequence: PSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVD | ||||||
Compositional bias | 129-151 | Basic and acidic residues | ||||
Sequence: MEVDENDRREKRSLSDKEPSSGP | ||||||
Compositional bias | 299-331 | Polar residues | ||||
Sequence: AASQLAVPSTPLSPHSAASGTAAGSQPSSPRYR | ||||||
Region | 299-406 | Disordered | ||||
Sequence: AASQLAVPSTPLSPHSAASGTAAGSQPSSPRYRPYTVTHPWASSGVSILSSSPSPPALASSPQAVPASSSRQRPSSTGPPLPPASPSATSRRPSSLRISPSLGASGGA | ||||||
Compositional bias | 338-373 | Polar residues | ||||
Sequence: PWASSGVSILSSSPSPPALASSPQAVPASSSRQRPS | ||||||
Compositional bias | 386-406 | Polar residues | ||||
Sequence: ATSRRPSSLRISPSLGASGGA | ||||||
Region | 1057-1077 | Disordered | ||||
Sequence: NKEQWDQLPRDQQQARQSQLA | ||||||
Domain | 1227-1300 | U-box | ||||
Sequence: DAPDEFRDPLMDTLMTDPVRLPSGTIMDRSIILRHLLNSPTDPFNRQTLTESMLEPVPELKEQIQAWMREKQNS |
Domain
Sequence similarities
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O95155-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length1,302
- Mass (Da)146,185
- Last updated1999-05-01 v1
- Checksum6BAA80984B03E43B
O95155-2
- Name2
- Differences from canonical
- 270-398: Missing
O95155-3
- Name3
- Differences from canonical
- 1-116: Missing
- 270-398: Missing
- 1234-1234: D → GKWTH
O95155-4
- Name4
- SynonymsUFD2a-7/7a, UFD2A-III
- NoteExpressed exclusively in mature striated muscle cells.
- Differences from canonical
- 398-398: P → PSMYDNPFSFLFLALSGDSSDEEDEEEDDDDGDGDDEGGGGGDDFSCVQFGS
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-15 | Basic and acidic residues | ||||
Sequence: MEELSADEIRRRRLA | ||||||
Alternative sequence | VSP_007101 | 1-116 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 31-45 | Pro residues | ||||
Sequence: SPQRENPPGPPIAAS | ||||||
Compositional bias | 49-123 | Polar residues | ||||
Sequence: PSQSLGLNVHNMTPATSPIGASGVAHRSQSSEGVSSLSSSPSNSLETQSQSLSRSQSMDIDGVSCEKSMSQVDVD | ||||||
Compositional bias | 129-151 | Basic and acidic residues | ||||
Sequence: MEVDENDRREKRSLSDKEPSSGP | ||||||
Alternative sequence | VSP_007102 | 270-398 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 299-331 | Polar residues | ||||
Sequence: AASQLAVPSTPLSPHSAASGTAAGSQPSSPRYR | ||||||
Compositional bias | 338-373 | Polar residues | ||||
Sequence: PWASSGVSILSSSPSPPALASSPQAVPASSSRQRPS | ||||||
Compositional bias | 386-406 | Polar residues | ||||
Sequence: ATSRRPSSLRISPSLGASGGA | ||||||
Alternative sequence | VSP_053372 | 398 | in isoform 4 | |||
Sequence: P → PSMYDNPFSFLFLALSGDSSDEEDEEEDDDDGDGDDEGGGGGDDFSCVQFGS | ||||||
Alternative sequence | VSP_007103 | 1234 | in isoform 3 | |||
Sequence: D → GKWTH |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF043117 EMBL· GenBank· DDBJ | AAD02233.1 EMBL· GenBank· DDBJ | mRNA | ||
AB028839 EMBL· GenBank· DDBJ | BAB40446.1 EMBL· GenBank· DDBJ | mRNA | ||
AF331520 EMBL· GenBank· DDBJ | AAK69622.1 EMBL· GenBank· DDBJ | mRNA | ||
JF289274 EMBL· GenBank· DDBJ | AEK06331.1 EMBL· GenBank· DDBJ | mRNA | ||
AB014584 EMBL· GenBank· DDBJ | BAA31659.3 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK292444 EMBL· GenBank· DDBJ | BAF85133.1 EMBL· GenBank· DDBJ | mRNA | ||
AL096841 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL590639 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC093696 EMBL· GenBank· DDBJ | AAH93696.1 EMBL· GenBank· DDBJ | mRNA | ||
AF091093 EMBL· GenBank· DDBJ | AAC72962.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. |