Q9VX91 · UBR1_DROME
- ProteinE3 ubiquitin-protein ligase UBR1
- GeneUbr1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1824 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
Function
function
E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
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 | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein ubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process via the N-end rule pathway |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase UBR1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila > Sophophora
Accessions
- Primary accessionQ9VX91
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056139 | 1-1824 | E3 ubiquitin-protein ligase UBR1 | |||
Sequence: MDRYDMEDVVVAPPAECSSPLKEWRLKRQAGTLDRSDIIEFLKRESPKYFDYQTSATVKDTNVITLKCMFKESLAKEEIIDVVVEFMLGDNPSSALEKLRLEGNTATVCGKVFKNGEPTYSCRECGVDPTCVLCVNCFKRSAHRFHKYKMSTSGGGGCCDCGDDEAWKKDQYCELHLANRKNPLESKILTDAVLERVEICFGAILAFCVSYLEIEPNASLQCLDGNVEGGQVDGAQYCTVLYNDESHTFDQVIQTLTKIAKCRAKDAMEIVAAIDREGRAVVKCDTFEECNKLKVSIENQMILPTSLVSTARNNQSLRTSVLHIGAVACQQFALQLLGWFQEFLVRHYLFRKTFSELVQRKQETFCIRHILEYDVKLWKTARTCWHRLLISGMLMEYDNKMILAQEFSRRYATIVEDFISDDHDHAFSIVSLSVQLFTVPSIAHHLIAHEGIFDKLLHTFYHVAIEKFIRNKTLHFSKNIASLTFFKRANYILYDLRYLLSLKPDVLSNDLRNGFLEGCRALMRVLNVMQGMESMTRQTGQHMDYEPEWECAFNLHIKLATTISQVIDWASGDVKLLRKLYKMTMRALVSNSFIVGGEKVMQPKKVADHVANCLVYDISVQPVSIHLPLSRFFAGIYLHLGAHDLTYDGLQTETEALSIKLTPREIIEPVLCTQAMIAQVGAGLWRRNGYTLLHQLYFYRNVRCRVEMLDRDIACLQIGASLMESNEFLIHVLNRFNTIPWLQENYWSLLSGNEMNDDIIREASIFDEFLELLIVIIGERWMPGVSMVTEEDRLRKEIIQLLCIKPYSHSELSRALPDGNSGNSDNVFEEVINTVAVFKKPVGADSKGVYELKEHLLKEFNMYFYHYTKEDKSKAEELQRERRKAKKQLVCCPPPMLPKLTPAFTPMANILQCPVFLNICSLIMERALNAYSRSFTESHLQKVLHLLGYAIQEELSEHYPFLSFYERSQEYGILEKLEELARCPRLEAHYDFVLWTIERFKQLQAKQAPSDGRAGPSCSQQGTGGKLSLSAEEQAREERENRARLAAERRAHIMAQMQKAQKSFISSNAEMFADTENETRKESASTGPMDWEDIPPEEEQGAVALESKVACLGPDRKFYHGTDDTFKCILCFENCAISRGGRQLVSSAFVQTSRVIFTTPNLRNSQSALHISCCGHVMHYSCWLEYFTNEEFKELRRPHRNRAALAQAANVEFQCPYCRTLSNAIIPVTETLPAFSAPPSPNESYLPLDSFVEIMSTLAIELGNVKDHELTTLPSVSNILRLSGVVGGLAQFERSVQLIKNPPRLHADYIEGIEFLKKALLNTMKIQQSHLKDHPAIESIEMVPILWDSCSYTLQALEIYLYAVEKPLKAELSMRHQSCARNLVRACSRSSALEWETDLPLLPPMRSQAEFSSRLLDTIFNQNDTSVLEWDCFRVLVPFQFGVLNLMVPEKGYKTIIPSGSMFDFYIMQTMFLAQLTKAVLCFDVEKEKAKRAEKAPNSELTQLDYIEQLPSRIRDNMIDFYRRYNIPARVLQKTKQKQLVEEESEENQGHGQTVVIPCESHHLALLLEYVQRQMSSFLRCSCLFYRFLTDVDFPDTFPTDQPDRFDLMCQYLGLDPMLGVYFDMETVYATMMHSFASHPHIDREVEQRCQPDARRSLQVEPCLRPLPRLKVLCDDFSDLINSVSDIFCPNNEREEMKTPTMCLICGLILCGQSYCCQPELGKVSVGACTHHAHACGAEVGIFLRIRDCQVVYLGRGKGCFVPPPYLDEYGETDMGLRRGNPLRLSQAAYRKIYLQWLGHGLHGEIARLNDNANVAAAAQWHHM |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for zinc finger, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 107-178 | UBR-type | ||||
Sequence: TVCGKVFKNGEPTYSCRECGVDPTCVLCVNCFKRSAHRFHKYKMSTSGGGGCCDCGDDEAWKKDQYCELHLA | ||||||
Region | 1006-1043 | Disordered | ||||
Sequence: KQAPSDGRAGPSCSQQGTGGKLSLSAEEQAREERENRA | ||||||
Compositional bias | 1013-1028 | Polar residues | ||||
Sequence: RAGPSCSQQGTGGKLS | ||||||
Region | 1073-1093 | Disordered | ||||
Sequence: ADTENETRKESASTGPMDWED | ||||||
Zinc finger | 1126-1220 | RING-type; atypical | ||||
Sequence: FKCILCFENCAISRGGRQLVSSAFVQTSRVIFTTPNLRNSQSALHISCCGHVMHYSCWLEYFTNEEFKELRRPHRNRAALAQAANVEFQCPYCRT |
Domain
The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.
Sequence similarities
Belongs to the E3 ubiquitin-protein ligase UBR1-like family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,824
- Mass (Da)208,361
- Last updated2002-10-01 v2
- Checksum79992C11175E82A0
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
M9NFA7 | M9NFA7_DROME | Ubr1 | 1824 |
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1013-1028 | Polar residues | ||||
Sequence: RAGPSCSQQGTGGKLS | ||||||
Sequence conflict | 1661 | in Ref. 3; AAM11168 | ||||
Sequence: E → V |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE014298 EMBL· GenBank· DDBJ | AAF48687.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AY094815 EMBL· GenBank· DDBJ | AAM11168.1 EMBL· GenBank· DDBJ | mRNA | ||
BT044223 EMBL· GenBank· DDBJ | ACH92288.1 EMBL· GenBank· DDBJ | mRNA |