A0A8I5KU01 · A0A8I5KU01_HUMAN
- ProteinE3 ubiquitin-protein ligase
- GeneHECTD1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2247 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 2216 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | protein ubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A8I5KU01
Proteomes
Organism-specific databases
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,484 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 248 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 252 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 358 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 481 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 631 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 632 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 640 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 710 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1481 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1493 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1521 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1666 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
Family & Domains
Features
Showing features for region, compositional bias, repeat, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 246-269 | Disordered | ||||
Sequence: TVSGPSSACKPGRSTTGAPSTTAD | ||||||
Compositional bias | 252-269 | Polar residues | ||||
Sequence: SACKPGRSTTGAPSTTAD | ||||||
Repeat | 395-427 | ANK | ||||
Sequence: VGQTLLNWASAFGTQEMVEFLCERGADVNRGQR | ||||||
Repeat | 426-458 | ANK | ||||
Sequence: QRSSSLHYAACFGRPQVAKTLLRHGANPDLRDE | ||||||
Compositional bias | 489-512 | Basic and acidic residues | ||||
Sequence: VNKGDDKKKKDTNKDEEECNEPKG | ||||||
Region | 489-513 | Disordered | ||||
Sequence: VNKGDDKKKKDTNKDEEECNEPKGD | ||||||
Region | 627-657 | Disordered | ||||
Sequence: LAGPSSDDENEEESKPEKEDEPQEDAKELQQ | ||||||
Region | 707-748 | Disordered | ||||
Sequence: SSGSPEGGSDSSESRSEFLEKLQRARGQVKPSTSSQPILSAP | ||||||
Compositional bias | 733-748 | Polar residues | ||||
Sequence: GQVKPSTSSQPILSAP | ||||||
Domain | 1266-1346 | MIB/HERC2 | ||||
Sequence: VRSQVLKYMVPGARVIRGLDWKWRDQDGSPQGEGTVTGELHNASPLMGAQSFPNLTTPGTTSTVTMSTSSVTSSSNVATAT | ||||||
Region | 1288-1341 | Disordered | ||||
Sequence: WRDQDGSPQGEGTVTGELHNASPLMGAQSFPNLTTPGTTSTVTMSTSSVTSSSN | ||||||
Compositional bias | 1312-1341 | Polar residues | ||||
Sequence: MGAQSFPNLTTPGTTSTVTMSTSSVTSSSN | ||||||
Region | 1395-1478 | Disordered | ||||
Sequence: ELDDDEDLPEPDEEDDENEDDNQEDQEYEEVMILRRPSLQRRAGSRSDVTHHAVTSQLPQVPAGAGSRPIGEQEEEEYETKGGR | ||||||
Compositional bias | 1396-1421 | Acidic residues | ||||
Sequence: LDDDEDLPEPDEEDDENEDDNQEDQE | ||||||
Compositional bias | 1422-1442 | Basic and acidic residues | ||||
Sequence: YEEVMILRRPSLQRRAGSRSD | ||||||
Compositional bias | 1464-1478 | Basic and acidic residues | ||||
Sequence: IGEQEEEEYETKGGR | ||||||
Region | 1498-1518 | Disordered | ||||
Sequence: AFDPRPGRTNVQQTTDLEIPP | ||||||
Domain | 1872-2207 | HECT | ||||
Sequence: IHADRKSVLEVEFLGEEGTGLGPTLEFYALVAAEFQRTDLGAWLCDDNFPDDESRHVDLGGGLKPPGYYVQRSCGLFTAPFPQDSDELERITKLFHFLGIFLAKCIQDNRLVDLPISKPFFKLMCMGDIKSNMSKLIYESRGDRDLHCTESQSEASTEEGHDSLSVGSFEEDSKSEFILDPPKPKPPAWFNGILTWEDFELVNPHRARFLKEIKDLAIKRRQILSNKGLSEDEKNTKLQELVLKNPSGSGPPLSIEDLGLNFQFCPSSRIYGFTAVDLKPSGEDEMITMDNAEEYVDLMFDFCMHTGIQKQMEAFRGGLANLHPRLTVVRKVDATD | ||||||
Region | 2018-2039 | Disordered | ||||
Sequence: HCTESQSEASTEEGHDSLSVGS | ||||||
Domain | 2211-2247 | HECT | ||||
Sequence: PSVNTCVHYLKLPEYSSEEIMRERLLAATMEKGFHLN |
Sequence similarities
Belongs to the UPL family. K-HECT subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,247
- Mass (Da)251,381
- Last updated2022-05-25 v1
- Checksum766EC67D9499F7B3
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q9ULT8 | HECD1_HUMAN | HECTD1 | 2610 | ||
A0A8I5QJE9 | A0A8I5QJE9_HUMAN | HECTD1 | 81 | ||
A0A8I5QJU2 | A0A8I5QJU2_HUMAN | HECTD1 | 2563 | ||
H0YJP0 | H0YJP0_HUMAN | HECTD1 | 2520 | ||
H0YJD4 | H0YJD4_HUMAN | HECTD1 | 2329 | ||
H0YJ72 | H0YJ72_HUMAN | HECTD1 | 122 | ||
G3V4V5 | G3V4V5_HUMAN | HECTD1 | 391 | ||
A0A8I5KUD6 | A0A8I5KUD6_HUMAN | HECTD1 | 1176 | ||
A0A087X2H1 | A0A087X2H1_HUMAN | HECTD1 | 2608 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 252-269 | Polar residues | ||||
Sequence: SACKPGRSTTGAPSTTAD | ||||||
Compositional bias | 489-512 | Basic and acidic residues | ||||
Sequence: VNKGDDKKKKDTNKDEEECNEPKG | ||||||
Compositional bias | 733-748 | Polar residues | ||||
Sequence: GQVKPSTSSQPILSAP | ||||||
Compositional bias | 1312-1341 | Polar residues | ||||
Sequence: MGAQSFPNLTTPGTTSTVTMSTSSVTSSSN | ||||||
Compositional bias | 1396-1421 | Acidic residues | ||||
Sequence: LDDDEDLPEPDEEDDENEDDNQEDQE | ||||||
Compositional bias | 1422-1442 | Basic and acidic residues | ||||
Sequence: YEEVMILRRPSLQRRAGSRSD | ||||||
Compositional bias | 1464-1478 | Basic and acidic residues | ||||
Sequence: IGEQEEEEYETKGGR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL121808 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL136418 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
KC877516 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |