V6CL75 · V6CL75_CAEEL
- ProteinE3 ubiquitin-protein ligase
- Genehecd-1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids2613 (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 | 2582 | Glycyl thioester intermediate | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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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
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionV6CL75
Proteomes
Organism-specific databases
PTM/Processing
Proteomic databases
Expression
Gene expression databases
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 409-457 | Disordered | ||||
Sequence: ARERSDDDHNQVANILESPSAFMRNKEDPKVKASTSKQPGTSTKPELPN | ||||||
Compositional bias | 442-456 | Polar residues | ||||
Sequence: STSKQPGTSTKPELP | ||||||
Region | 608-677 | Disordered | ||||
Sequence: PMEIDFENQPSSSTAVPTANDIMDTTVPSSSGGADAESNSNPSTIEMADPESSTPSSSTQQSISKPKATA | ||||||
Compositional bias | 611-677 | Polar residues | ||||
Sequence: IDFENQPSSSTAVPTANDIMDTTVPSSSGGADAESNSNPSTIEMADPESSTPSSSTQQSISKPKATA | ||||||
Region | 1341-1365 | Disordered | ||||
Sequence: DPPKKDSPAGTSSTPGSSSSAALPP | ||||||
Compositional bias | 1347-1365 | Polar residues | ||||
Sequence: SPAGTSSTPGSSSSAALPP | ||||||
Domain | 1403-1475 | MIB/HERC2 | ||||
Sequence: RSRGSYKISESKSKVVRGKDWRWEDQDGGEGKFGRITSPPESGWVDVTWDNGNANSYRFGANGNFDIERVTST | ||||||
Region | 1503-1527 | Disordered | ||||
Sequence: YTPKTTGGPPSSSVFGTSSSAGSSR | ||||||
Compositional bias | 1506-1527 | Polar residues | ||||
Sequence: KTTGGPPSSSVFGTSSSAGSSR | ||||||
Region | 1540-1594 | Disordered | ||||
Sequence: KNTTPAGTPSSGGSSGGAIGKKSMSTTNLVDERQKTSGPSVASTGQAASAESLQH | ||||||
Region | 1617-1761 | Disordered | ||||
Sequence: NQEPEDEPMGGEESDSAASMRSAASSNSQMSMGSSSQQQQQQDSDMTPRDSAGTPSTPRDDKNQTLSVSAPDLAAARQRQASAETDGDADADETNSEDKTVGADDAMEEDDEEEETMEDEEDDDDDDDDESSNENQEKLVELLGG | ||||||
Compositional bias | 1634-1687 | Polar residues | ||||
Sequence: ASMRSAASSNSQMSMGSSSQQQQQQDSDMTPRDSAGTPSTPRDDKNQTLSVSAP | ||||||
Compositional bias | 1719-1750 | Acidic residues | ||||
Sequence: ADDAMEEDDEEEETMEDEEDDDDDDDDESSNE | ||||||
Compositional bias | 1776-1791 | Polar residues | ||||
Sequence: ESLSDASSSAKDATTN | ||||||
Region | 1776-1801 | Disordered | ||||
Sequence: ESLSDASSSAKDATTNEAQKKGGKKP | ||||||
Domain | 2205-2613 | HECT | ||||
Sequence: FHADRKAVLEIEYTNEEGTGLGPTLEFYALVAAELQRKSLALWVCDDDDTHASKSGEEREVDLGEGKKPIGYYVRRVGGLFPAPLPPGTDETKRAADMFRVLGVFLAKVLLDGRLVDLPLSRPFLKLLVHPQIGDDARGPNLHKILSLDDFEEVNPVKGSFLKELRALAQRKRLIENDTSIDSNSKRRKIAELKLHIKGSTCRVEDLALNFTVNPPSKVFQYAEMELVDGGSDIDVTIDNVEQYVEKCEEFYLNTGIAYQMRAFRDGFDRVFPLRTLRAYSPEEVQRLLSGEQCPEWSRDDILNYTEPKLGYTRESPGFLRFVDVMEALTAQERKNFLQFATGCSSLPPGGLANLHPRLTIVRKVESGDGSYPSVNTCVHYLKLPEYSSSAILRERLLTAINEKGFHLN |
Sequence similarities
Belongs to the UPL family. K-HECT subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length2,613
- Mass (Da)288,392
- Last updated2014-02-19 v1
- ChecksumC870F0B647444453
Computationally mapped potential isoform sequences
There are 7 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 442-456 | Polar residues | ||||
Sequence: STSKQPGTSTKPELP | ||||||
Compositional bias | 611-677 | Polar residues | ||||
Sequence: IDFENQPSSSTAVPTANDIMDTTVPSSSGGADAESNSNPSTIEMADPESSTPSSSTQQSISKPKATA | ||||||
Compositional bias | 1347-1365 | Polar residues | ||||
Sequence: SPAGTSSTPGSSSSAALPP | ||||||
Compositional bias | 1506-1527 | Polar residues | ||||
Sequence: KTTGGPPSSSVFGTSSSAGSSR | ||||||
Compositional bias | 1634-1687 | Polar residues | ||||
Sequence: ASMRSAASSNSQMSMGSSSQQQQQQDSDMTPRDSAGTPSTPRDDKNQTLSVSAP | ||||||
Compositional bias | 1719-1750 | Acidic residues | ||||
Sequence: ADDAMEEDDEEEETMEDEEDDDDDDDDESSNE | ||||||
Compositional bias | 1776-1791 | Polar residues | ||||
Sequence: ESLSDASSSAKDATTN |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284604 EMBL· GenBank· DDBJ | CDK13345.1 EMBL· GenBank· DDBJ | Genomic DNA |