O70263 · LNX1_MOUSE
- ProteinE3 ubiquitin-protein ligase LNX
- GeneLnx1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids728 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of NUMB. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates ubiquitination of isoform p66 and isoform p72 of NUMB, but not that of isoform p71 or isoform p65.
Isoform 2 provides an endocytic scaffold for IGSF5/JAM4.
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 | hippocampal mossy fiber to CA3 synapse | |
Cellular Component | postsynapse | |
Molecular Function | identical protein binding | |
Molecular Function | metal ion binding | |
Molecular Function | PDZ domain binding | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | protein ubiquitination | |
Biological Process | synapse maturation | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase LNX
- 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 > Mus > Mus
Accessions
- Primary accessionO70263
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 48 | Loss of function. | ||||
Sequence: C → A | ||||||
Mutagenesis | 181 | No effect on binding to NUMB protein. | ||||
Sequence: P → A | ||||||
Mutagenesis | 182 | Slightly affects binding to NUMB protein. | ||||
Sequence: G → A | ||||||
Mutagenesis | 183 | Abolishes binding to NUMB protein. | ||||
Sequence: L → A | ||||||
Mutagenesis | 184 | Slightly affects binding to NUMB protein. | ||||
Sequence: D → A | ||||||
Mutagenesis | 185 | Abolishes binding to NUMB protein. | ||||
Sequence: N → A | ||||||
Mutagenesis | 186 | Slightly affects binding to NUMB protein. | ||||
Sequence: P → A | ||||||
Mutagenesis | 188 | Abolishes binding to NUMB protein. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 188 | No effect on binding to NUMB protein. | ||||
Sequence: Y → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 51 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000055914 | 1-728 | E3 ubiquitin-protein ligase LNX | |||
Sequence: MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTSCKGASHYGLTKDRKRRSQDGCPDGCASLMATTLSPEVSAAATISLMTDEPGLDNPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVVANHVDQGRDNSENTTVPEVFPRLFHLIPDGEITSIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDGRLLPGDIILKVNGMDISNVPHNYAVRLLRQPCQVLRLTVLREQKFRSRSNAHVPDSYGPRDDSFHVILNKSSPEEQLGIKLVRRVDEPGVFIFNVLNGGVADRHGQLEENDRVLAINGHDLRFGSPESAAHLIQASERRVHLVVSRQVRQSSPDIFQEAGWISNGQQSPGPGERNTASKPAATCHEKVVSVWKDPSESLGMTVGGGASHREWDLPIYVISVEPGGVISRDGRIKTGDILLNVNGIELTEVSRTEAVAILKSAPSSVVLKALEVKEQEAQEDCSPAALDSNHNVTPPGDWSPSWVMWLELPQYLCNCKDVILRRNTAGSLGFCIVGGYEEYSGNKPFFIKSIVEGTPAYNDGRIRCGDILLAVNGRSTSGMIHACLARMLKELKGRITLTIASWPGTFL | ||||||
Modified residue | 445 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with CXADR. Interacts with MAGEB18 and MAGEF1 (By similarity).
Interacts with the phosphotyrosine interaction domain of all isoforms of NUMB. IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain, other isoforms may also interact with IGSF5/JAM4.
Interacts with the phosphotyrosine interaction domain of all isoforms of NUMB. IGSF5/JAM4 interacts with isoform 2 through the second PDZ domain, other isoforms may also interact with IGSF5/JAM4.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, motif, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 45-83 | RING-type | ||||
Sequence: CHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDR | ||||||
Motif | 185-188 | NPXY motif | ||||
Sequence: NPAY | ||||||
Region | 185-220 | Disordered | ||||
Sequence: NPAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTM | ||||||
Region | 186-244 | Interaction with MAGEB18 | ||||
Sequence: PAYVSSVEDGEPVANSSDSGRSNRTRARPFERSTMRSRSFKKINRALSALRRTKSGSVV | ||||||
Domain | 278-362 | PDZ 1 | ||||
Sequence: SIKINRADPSESLSIRLVGGSETPLVHIIIQHIYRDGVIARDGRLLPGDIILKVNGMDISNVPHNYAVRLLRQPCQVLRLTVLRE | ||||||
Domain | 385-467 | PDZ 2 | ||||
Sequence: HVILNKSSPEEQLGIKLVRRVDEPGVFIFNVLNGGVADRHGQLEENDRVLAINGHDLRFGSPESAAHLIQASERRVHLVVSRQ | ||||||
Region | 481-500 | Disordered | ||||
Sequence: WISNGQQSPGPGERNTASKP | ||||||
Domain | 508-593 | PDZ 3 | ||||
Sequence: VVSVWKDPSESLGMTVGGGASHREWDLPIYVISVEPGGVISRDGRIKTGDILLNVNGIELTEVSRTEAVAILKSAPSSVVLKALEV | ||||||
Domain | 638-723 | PDZ 4 | ||||
Sequence: DVILRRNTAGSLGFCIVGGYEEYSGNKPFFIKSIVEGTPAYNDGRIRCGDILLAVNGRSTSGMIHACLARMLKELKGRITLTIASW |
Domain
The NPXY motif is required for the interaction with the PID domain of NUMB. It is however not sufficient.
The PDZ 1 domain participates in the interaction with the PID domain of NUMB, and participates in the isoform-specific ubiquitination of NUMB. The PDZ 2 domain of isoform 2 participates in the interaction with IGSF5/JAM4, other isoforms containing this domain may also interact with IGSF5/JAM4.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O70263-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- SynonymsLNX, LNXp80
- Length728
- Mass (Da)80,157
- Last updated1998-08-01 v1
- ChecksumE2914BD364C0CEC4
O70263-2
- Name2
- SynonymsLNX-B, LNXp70
- Differences from canonical
- 1-131: MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL
O70263-3
- Name3
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_005734 | 1-131 | in isoform 2 and isoform 3 | |||
Sequence: MNQPDLADDPDPSPEPLCIVCGQNHSPEENHFYTYTEDVDDDLICHICLQALLDPLDTPCGHTYCTLCLTNFLVEKDFCPVDRKPVVLQHCKKSSILVNKLLNKLLVTCPFTEHCTEVLQRCDLQHHFQTS → MKALLLLVLPWLSPANYIDNVGNLHFLYSEL | ||||||
Sequence conflict | 258 | in Ref. 2; BAC31789 | ||||
Sequence: T → N | ||||||
Alternative sequence | VSP_012588 | 332-357 | in isoform 3 | |||
Sequence: NGMDISNVPHNYAVRLLRQPCQVLRL → PMRRELVTIGYKIVSCRLCVAHNLSP | ||||||
Alternative sequence | VSP_012589 | 358-728 | in isoform 3 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF034745 EMBL· GenBank· DDBJ | AAC40075.1 EMBL· GenBank· DDBJ | mRNA | ||
AF034746 EMBL· GenBank· DDBJ | AAC40076.1 EMBL· GenBank· DDBJ | mRNA | ||
AK044127 EMBL· GenBank· DDBJ | BAC31789.1 EMBL· GenBank· DDBJ | mRNA | ||
BC040367 EMBL· GenBank· DDBJ | AAH40367.1 EMBL· GenBank· DDBJ | mRNA |