Q5D006 · UBP11_RAT
- ProteinUbiquitin carboxyl-terminal hydrolase 11
- GeneUsp11
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids921 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-33'-linked ubiquitin chains, and extremely low activity with 'Lys-27', 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like comple. Promotes cell proliferation by deubiquitinating phosphorylated E2F1x.
Catalytic activity
Features
Showing features for active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 266 | Nucleophile | ||||
Sequence: C | ||||||
Active site | 847 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Cellular Component | cytoplasm | |
Cellular Component | nucleus | |
Molecular Function | cysteine-type deubiquitinase activity | |
Molecular Function | cysteine-type endopeptidase activity | |
Molecular Function | transcription corepressor binding | |
Biological Process | protein deubiquitination | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameUbiquitin carboxyl-terminal hydrolase 11
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionQ5D006
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Predominantly nuclear. Associates with chromatin.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000435845 | 1-921 | Ubiquitin carboxyl-terminal hydrolase 11 | |||
Sequence: MAAVAADPAAAAVPASAEDRETQPEAMPDLDQQWRQIGNGRERPLRAGESWFLVEKHWYKQWEAYVKGGDQDASTFPGSINNSGLFEDQISWHLRERLVEGDDYVLLPAPAWNYLVSWYGLKDDQPPIERKVIELPGIRKVEVYPIELLLVQHSDMETALTIQFSYSDSVDLVLQTAREQFLVEPQEDTRLWTKNSEGSLDRLCNTQITLLDACLETGQLVIMETRNKDGTWPSAQLCGMNNMPDEDEDFQGQPGICGLTNLGNTCFMNSALQCLSNVPQLTEYFLNNRYLEELNFRNPLGMKGELAEAYADLVKQTWSGYHRSIVPNVFKNKVGHFASQFLGYQQHDSQELLSFLLDGLHEDLNRVKKKEYVELCNGAGRPDLEVAQEAWQNHKRRNDSVIVDTFHGLFKSTLVCPDCGNVSVTFDPFCYLSVPLPVCSRRVLEVFFVPMDPRRKPEQHRVVVPKKGNISDLCVALSTHTSVAPDKMIVADVFSHRFYKLYQLEDPLSGILDRDDIFVYEVTGRIEPVEGSRDDIVVPVYLRERTPSRDYNNSYYGLILFGHPLLVSVPRDRFSWEGLYNILMYRLSRYVTKPTSDDDDGDEKGDENEDEDVEDDSSSEEEKEEMSGPTDNDGTQESEQEQAGTSSGVTGRCPSLLDNSLHTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEAQTQPYIAMDWEPEMKRRYYDEVEAEGYVKHDCVGYMLKKNPVQLKECIKLFTTVETLEKENPWYCSSCKQHQLATKKLDLWMLPEVLIIHLKRFSFSKFSREKLDTLVQFPIRDLDFSEFVIKPKNESAPDLYKYDLIAVSNHYGGMRDGHYTTFACNKDSGQWHYFDDNSVSPVNENQIESKAAYVLFYQRQDVGRRQSQTASSETPTSPASSSTPNSDIMDVN | ||||||
Modified residue | 194 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 596 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 692 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 906 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer (By similarity).
Associated component of the Polycomb group (PcG) multiprotein PRC1-like complex (By similarity).
Interacts with RANBP9/RANBPM (By similarity).
Interacts with BRCA2 (By similarity).
Interacts with CHUK/IKKA (By similarity).
Interacts with NFKBIA (By similarity).
Interacts with SPRY3, RAE1, MYCBP2/PAM, and KCTD6 (By similarity).
Associated component of the Polycomb group (PcG) multiprotein PRC1-like complex (By similarity).
Interacts with RANBP9/RANBPM (By similarity).
Interacts with BRCA2 (By similarity).
Interacts with CHUK/IKKA (By similarity).
Interacts with NFKBIA (By similarity).
Interacts with SPRY3, RAE1, MYCBP2/PAM, and KCTD6 (By similarity).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-29 | Disordered | ||||
Sequence: MAAVAADPAAAAVPASAEDRETQPEAMPD | ||||||
Domain | 28-133 | DUSP | ||||
Sequence: PDLDQQWRQIGNGRERPLRAGESWFLVEKHWYKQWEAYVKGGDQDASTFPGSINNSGLFEDQISWHLRERLVEGDDYVLLPAPAWNYLVSWYGLKDDQPPIERKVI | ||||||
Domain | 257-889 | USP | ||||
Sequence: CGLTNLGNTCFMNSALQCLSNVPQLTEYFLNNRYLEELNFRNPLGMKGELAEAYADLVKQTWSGYHRSIVPNVFKNKVGHFASQFLGYQQHDSQELLSFLLDGLHEDLNRVKKKEYVELCNGAGRPDLEVAQEAWQNHKRRNDSVIVDTFHGLFKSTLVCPDCGNVSVTFDPFCYLSVPLPVCSRRVLEVFFVPMDPRRKPEQHRVVVPKKGNISDLCVALSTHTSVAPDKMIVADVFSHRFYKLYQLEDPLSGILDRDDIFVYEVTGRIEPVEGSRDDIVVPVYLRERTPSRDYNNSYYGLILFGHPLLVSVPRDRFSWEGLYNILMYRLSRYVTKPTSDDDDGDEKGDENEDEDVEDDSSSEEEKEEMSGPTDNDGTQESEQEQAGTSSGVTGRCPSLLDNSLHTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEAQTQPYIAMDWEPEMKRRYYDEVEAEGYVKHDCVGYMLKKNPVQLKECIKLFTTVETLEKENPWYCSSCKQHQLATKKLDLWMLPEVLIIHLKRFSFSKFSREKLDTLVQFPIRDLDFSEFVIKPKNESAPDLYKYDLIAVSNHYGGMRDGHYTTFACNKDSGQWHYFDDNSVSPVNENQIESKAAYVLFYQRQ | ||||||
Region | 592-697 | Disordered | ||||
Sequence: TKPTSDDDDGDEKGDENEDEDVEDDSSSEEEKEEMSGPTDNDGTQESEQEQAGTSSGVTGRCPSLLDNSLHTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEAQ | ||||||
Compositional bias | 600-622 | Acidic residues | ||||
Sequence: DGDEKGDENEDEDVEDDSSSEEE | ||||||
Compositional bias | 631-664 | Polar residues | ||||
Sequence: DNDGTQESEQEQAGTSSGVTGRCPSLLDNSLHTS | ||||||
Compositional bias | 675-697 | Polar residues | ||||
Sequence: LFTLQTVNSNGTSDRTTSPEEAQ | ||||||
Region | 893-921 | Disordered | ||||
Sequence: RRQSQTASSETPTSPASSSTPNSDIMDVN |
Sequence similarities
Belongs to the peptidase C19 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length921
- Mass (Da)105,239
- Last updated2005-03-29 v1
- ChecksumF0481AB43C394731
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A8L2QN44 | A0A8L2QN44_RAT | Usp11 | 700 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 600-622 | Acidic residues | ||||
Sequence: DGDEKGDENEDEDVEDDSSSEEE | ||||||
Compositional bias | 631-664 | Polar residues | ||||
Sequence: DNDGTQESEQEQAGTSSGVTGRCPSLLDNSLHTS | ||||||
Compositional bias | 675-697 | Polar residues | ||||
Sequence: LFTLQTVNSNGTSDRTTSPEEAQ |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AC120727 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH474009 EMBL· GenBank· DDBJ | EDL97708.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC090333 EMBL· GenBank· DDBJ | AAH90333.1 EMBL· GenBank· DDBJ | mRNA | ||
BC105613 EMBL· GenBank· DDBJ | AAI05614.1 EMBL· GenBank· DDBJ | mRNA |