O94888 · UBXN7_HUMAN
- ProteinUBX domain-containing protein 7
- GeneUBXN7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids489 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
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 | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | VCP-NPL4-UFD1 AAA ATPase complex | |
Molecular Function | RNA polymerase II-specific DNA-binding transcription factor binding | |
Molecular Function | ubiquitin binding | |
Molecular Function | ubiquitin protein ligase binding | |
Biological Process | proteasome-mediated ubiquitin-dependent protein catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameUBX domain-containing protein 7
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO94888
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 288 | No effect on interactions with CUL2 and HIF1A. | ||||
Sequence: S → A or D | ||||||
Mutagenesis | 297 | Severely reduces interaction with neddylated CUL2. | ||||
Sequence: S → A or H | ||||||
Mutagenesis | 459 | Abolishes interaction with VCP/p97. | ||||
Sequence: P → G |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 337 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 initiator methionine, modified residue, chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylalanine | ||||
Sequence: A | |||||||
Chain | PRO_0000211035 | 2-489 | UniProt | UBX domain-containing protein 7 | |||
Sequence: AAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN | |||||||
Modified residue (large scale data) | 7 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 29 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Cross-link | 84 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 99 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Cross-link | 134 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 270 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 278 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 278 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 280 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 280 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 285 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 288 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 288 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 305 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 306 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 306 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 350 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with neddylated CUL2, ubiquitinated HIF1A, and VCP/p97.
Binary interactions
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-54 | UBA | ||||
Sequence: AAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGG | ||||||
Region | 56-77 | Disordered | ||||
Sequence: AEEPSTSSASVSTVRPHTEEEV | ||||||
Domain | 285-304 | UIM | ||||
Sequence: SEDSQLEAAIRASLQETHFD | ||||||
Region | 300-384 | Disordered | ||||
Sequence: ETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGL | ||||||
Compositional bias | 306-320 | Basic and acidic residues | ||||
Sequence: TQTKQDSRSDEESES | ||||||
Compositional bias | 339-368 | Basic and acidic residues | ||||
Sequence: EEVENLAKSRKSPHKDLGHRKEENRRPLTE | ||||||
Domain | 408-485 | UBX | ||||
Sequence: VNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFV |
Domain
The UIM (ubiquitin-interacting motif) is required to engage the NEDD8 modification on cullins.
The UBX domain mediates interaction with VCP/p97.
The UBA domain is required for binding ubiquitinated-protein substrates.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length489
- Mass (Da)54,862
- Last updated2005-08-16 v2
- Checksum3C894533B1A2C41A
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 306-320 | Basic and acidic residues | ||||
Sequence: TQTKQDSRSDEESES | ||||||
Compositional bias | 339-368 | Basic and acidic residues | ||||
Sequence: EEVENLAKSRKSPHKDLGHRKEENRRPLTE |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB018337 EMBL· GenBank· DDBJ | BAA34514.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK129880 EMBL· GenBank· DDBJ | BAC85247.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
CH471191 EMBL· GenBank· DDBJ | EAW53652.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471191 EMBL· GenBank· DDBJ | EAW53654.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC028986 EMBL· GenBank· DDBJ | AAH28986.1 EMBL· GenBank· DDBJ | mRNA |