Q6UWE0 · LRSM1_HUMAN
- ProteinE3 ubiquitin-protein ligase LRSAM1
- GeneLRSAM1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids723 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Bacterial recognition protein that defends the cytoplasm from invasive pathogens (PubMed:23245322).
Localizes to several intracellular bacterial pathogens and generates the bacteria-associated ubiquitin signal leading to autophagy-mediated intracellular bacteria degradation (xenophagy) (PubMed:23245322, PubMed:25484098).
Catalytic activity
Pathway
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 | cytosol | |
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | ubiquitin-protein transferase activity | |
Biological Process | autophagy | |
Biological Process | negative regulation of endocytosis | |
Biological Process | positive regulation of autophagosome assembly | |
Biological Process | positive regulation of xenophagy | |
Biological Process | protein autoubiquitination | |
Biological Process | protein catabolic process | |
Biological Process | protein polyubiquitination | |
Biological Process | ubiquitin-dependent endocytosis | |
Biological Process | viral budding |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase LRSAM1
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6UWE0
- Secondary accessions
Proteomes
Organism-specific databases
Disease & Variants
Involvement in disease
Charcot-Marie-Tooth disease, axonal, 2P (CMT2P)
- Note
- DescriptionAn axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy.
- See alsoMIM:614436
Natural variants in CMT2P
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_077460 | 694 | C>R | in CMT2P; abolishes interaction with FUS; dbSNP:rs759312530 | |
VAR_077461 | 694 | C>Y | in CMT2P; uncertain significance; dbSNP:rs886041051 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_021051 | 318 | in dbSNP:rs1539567 | |||
Sequence: N → D | ||||||
Mutagenesis | 649-664 | Abolishes interaction with TSG101. | ||||
Sequence: Missing | ||||||
Mutagenesis | 675 | Abolishes ubiquitination of TSG101. | ||||
Sequence: C → A | ||||||
Mutagenesis | 692 | Abolishes ubiquitination of TSG101. | ||||
Sequence: H → A | ||||||
Natural variant | VAR_077460 | 694 | in CMT2P; abolishes interaction with FUS; dbSNP:rs759312530 | |||
Sequence: C → R | ||||||
Natural variant | VAR_077461 | 694 | in CMT2P; uncertain significance; dbSNP:rs886041051 | |||
Sequence: C → Y |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 961 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000055923 | 1-723 | UniProt | E3 ubiquitin-protein ligase LRSAM1 | |||
Sequence: MPLFFRKRKPSEEARKRLEYQMCLAKEAGADDILDISKCELSEIPFGAFATCKVLQKKVLIVHTNHLTSLLPKSCSLLSLATIKVLDLHDNQLTALPDDLGQLTALQVLNVERNQLMQLPRSIGNLTQLQTLNVKDNKLKELPDTVGELRSLRTLNISGNEIQRLPQMLAHVRTLEMLSLDASAMVYPPREVCGAGTAAILQFLCKESGLEYYPPSQYLLPILEQDGIENSRDSPDGPTDRFSREELEWQNRFSDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESLRRRDVASAMQQMLTESCKNRLIQMAYESQRQNLVQQACSSMAEMDERFQQILSWQQMDQNKAISQILQESAMQKAAFEALQVKKDLMHRQIRSQIKLIETELLQLTQLELKRKSLDTESLQEMISEQRWALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQYQRLLNQKPLSLKLQEEGMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLDAARIQPELKPPMGEVVTPTAPQEPPESVRPSAPPAELEVQASECVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCRQDIAQRLRIYHSS | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 234 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 234 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 243 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 289 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 290 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 494 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 562 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 604 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 604 | PRIDE | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with PHF23 (PubMed:25484098).
Interacts with FUS (PubMed:27615052).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6UWE0 | ATXN1 P54253 | 4 | EBI-720984, EBI-930964 | |
BINARY | Q6UWE0 | CCDC6 Q16204 | 3 | EBI-720984, EBI-1045350 | |
BINARY | Q6UWE0 | DMAP1 Q9NPF5 | 3 | EBI-720984, EBI-399105 | |
XENO | Q6UWE0 | Fus P56959 | 2 | EBI-720984, EBI-400452 | |
BINARY | Q6UWE0 | LIPF P07098 | 2 | EBI-720984, EBI-3386192 | |
BINARY | Q6UWE0 | TERF1 P54274 | 2 | EBI-720984, EBI-710997 | |
BINARY | Q6UWE0 | TSG101 Q99816 | 8 | EBI-720984, EBI-346882 | |
BINARY | Q6UWE0 | UBE2I Q7KZS0 | 3 | EBI-720984, EBI-10180829 | |
BINARY | Q6UWE0 | UBE2N P61088 | 3 | EBI-720984, EBI-1052908 | |
BINARY | Q6UWE0 | XAF1 Q6GPH4 | 3 | EBI-720984, EBI-2815120 | |
BINARY | Q6UWE0 | ZMAT4 Q9H898-2 | 3 | EBI-720984, EBI-11529334 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, coiled coil, region, compositional bias, domain, motif, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 30-51 | LRR 1 | ||||
Sequence: ADDILDISKCELSEIPFGAFAT | ||||||
Repeat | 56-77 | LRR 2 | ||||
Sequence: QKKVLIVHTNHLTSLLPKSCSL | ||||||
Repeat | 82-103 | LRR 3 | ||||
Sequence: TIKVLDLHDNQLTALPDDLGQL | ||||||
Repeat | 105-127 | LRR 4 | ||||
Sequence: ALQVLNVERNQLMQLPRSIGNLT | ||||||
Repeat | 128-149 | LRR 5 | ||||
Sequence: QLQTLNVKDNKLKELPDTVGEL | ||||||
Repeat | 151-172 | LRR 6 | ||||
Sequence: SLRTLNISGNEIQRLPQMLAHV | ||||||
Coiled coil | 254-380 | |||||
Sequence: SDYEKRKEQKMLEKLEFERRLELGQREHTQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQRHLNAERQRLQEQLKQTEQNISSRIQKLLQDNQRQKKSSEILKSLENERIRMEQLMSITQEETESL | ||||||
Region | 282-314 | Disordered | ||||
Sequence: TQLLQQSSSQKDEILQTVKEEQSRLEQGLSEHQ | ||||||
Compositional bias | 295-314 | Basic and acidic residues | ||||
Sequence: ILQTVKEEQSRLEQGLSEHQ | ||||||
Coiled coil | 510-562 | |||||
Sequence: ALSSLLQQLLKEKQQREEELREILTELEAKSETRQENYWLIQYQRLLNQKPLS | ||||||
Domain | 569-632 | SAM | ||||
Sequence: GMERQLVALLEELSAEHYLPIFAHHRLSLDLLSQMSPGDLAKVGVSEAGLQHEILRRVQELLDA | ||||||
Region | 642-665 | Disordered | ||||
Sequence: PMGEVVTPTAPQEPPESVRPSAPP | ||||||
Motif | 649-652 | PTAP motif 1 | ||||
Sequence: PTAP | ||||||
Motif | 661-664 | PTAP motif 2 | ||||
Sequence: PSAP | ||||||
Zinc finger | 675-710 | RING-type | ||||
Sequence: CVVCLEREAQMIFLNCGHVCCCQQCCQPLRTCPLCR |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q6UWE0-1
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
- Length723
- Mass (Da)83,594
- Last updated2004-07-05 v1
- Checksum4A59461C92467BB1
Q6UWE0-2
- Name2
- Differences from canonical
- 474-500: Missing
Q6UWE0-3
- Name3
- Differences from canonical
- 1-420: Missing
Computationally mapped potential isoform sequences
There are 17 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A6Q8PFL5 | A0A6Q8PFL5_HUMAN | LRSAM1 | 653 | ||
A0A6Q8PFI6 | A0A6Q8PFI6_HUMAN | LRSAM1 | 420 | ||
A0A6Q8PFL1 | A0A6Q8PFL1_HUMAN | LRSAM1 | 254 | ||
A0A6Q8PG90 | A0A6Q8PG90_HUMAN | LRSAM1 | 173 | ||
A0A6Q8PFW1 | A0A6Q8PFW1_HUMAN | LRSAM1 | 432 | ||
A0A6Q8PFT9 | A0A6Q8PFT9_HUMAN | LRSAM1 | 663 | ||
A0A6Q8PG02 | A0A6Q8PG02_HUMAN | LRSAM1 | 704 | ||
A0A6Q8PGH9 | A0A6Q8PGH9_HUMAN | LRSAM1 | 149 | ||
A0A6Q8PGB2 | A0A6Q8PGB2_HUMAN | LRSAM1 | 750 | ||
A0A6Q8PGF7 | A0A6Q8PGF7_HUMAN | LRSAM1 | 708 | ||
A0A6Q8PGZ2 | A0A6Q8PGZ2_HUMAN | LRSAM1 | 165 | ||
A0A6Q8PGT8 | A0A6Q8PGT8_HUMAN | LRSAM1 | 638 | ||
A0A6Q8PH70 | A0A6Q8PH70_HUMAN | LRSAM1 | 428 | ||
A0A6Q8PGW1 | A0A6Q8PGW1_HUMAN | LRSAM1 | 690 | ||
A0A6Q8PEU7 | A0A6Q8PEU7_HUMAN | LRSAM1 | 85 | ||
A0A6Q8PF55 | A0A6Q8PF55_HUMAN | LRSAM1 | 236 | ||
A0A6Q8PHH6 | A0A6Q8PHH6_HUMAN | LRSAM1 | 407 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_012660 | 1-420 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 295-314 | Basic and acidic residues | ||||
Sequence: ILQTVKEEQSRLEQGLSEHQ | ||||||
Sequence conflict | 385 | in Ref. 2; BAB71119 | ||||
Sequence: V → F | ||||||
Sequence conflict | 402 | in Ref. 2; BAC03703 | ||||
Sequence: I → V | ||||||
Alternative sequence | VSP_012661 | 474-500 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY358830 EMBL· GenBank· DDBJ | AAQ89189.1 EMBL· GenBank· DDBJ | mRNA | ||
AK056203 EMBL· GenBank· DDBJ | BAB71119.1 EMBL· GenBank· DDBJ | mRNA | ||
AK056305 EMBL· GenBank· DDBJ | BAB71144.1 EMBL· GenBank· DDBJ | mRNA | ||
AK091589 EMBL· GenBank· DDBJ | BAC03703.1 EMBL· GenBank· DDBJ | mRNA | ||
AL445222 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC009239 EMBL· GenBank· DDBJ | AAH09239.1 EMBL· GenBank· DDBJ | mRNA |