Q9NQ29 · LUC7L_HUMAN
- ProteinPutative RNA-binding protein Luc7-like 1
- GeneLUC7L
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids371 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May bind to RNA via its Arg/Ser-rich domain.
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 | U1 snRNP | |
Cellular Component | U2-type prespliceosome | |
Molecular Function | identical protein binding | |
Molecular Function | mRNA binding | |
Molecular Function | RS domain binding | |
Biological Process | mRNA splice site recognition | |
Biological Process | negative regulation of striated muscle tissue development |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative RNA-binding protein Luc7-like 1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9NQ29
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 358 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 chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000187280 | 1-371 | UniProt | Putative RNA-binding protein Luc7-like 1 | |||
Sequence: MSAQAQMRALLDQLMGTARDGDETRQRVKFTDDRVCKSHLLDCCPHDILAGTRMDLGECTKIHDLALRADYEIASKERDLFFELDAMDHLESFIAECDRRTELAKKRLAETQEEISAEVSAKAEKVHELNEEIGKLLAKAEQLGAEGNVDESQKILMEVEKVRAKKKEAEEEYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIQIREKLDQLRKTVAEKQEKRNQDRLRRREEREREERLSRRSGSRTRDRRRSRSRDRRRRRSRSTSRERRKLSRSRSRDRHRRHRSRSRSHSRGHRRASRDRSAKYKFSRERASREESWESGRSERGPPDWRLESSNGKMASRRSEEKEAGEI | |||||||
Modified residue | 332 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 336 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 363 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitous.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9NQ29 | CHERP Q8IWX8 | 2 | EBI-473747, EBI-2555370 | |
BINARY | Q9NQ29 | LUC7L Q9NQ29 | 2 | EBI-473747, EBI-473747 | |
BINARY | Q9NQ29 | RNASEH1 O60930 | 2 | EBI-473747, EBI-2372399 | |
BINARY | Q9NQ29 | SPRED1 Q7Z699 | 3 | EBI-473747, EBI-5235340 | |
BINARY | Q9NQ29 | SRPK1 Q96SB4 | 4 | EBI-473747, EBI-539478 | |
BINARY | Q9NQ29 | SRPK2 P78362 | 6 | EBI-473747, EBI-593303 | |
BINARY | Q9NQ29-3 | SRSF6 Q13247 | 3 | EBI-6654742, EBI-745230 | |
BINARY | Q9NQ29-3 | SRSF7 Q16629 | 3 | EBI-6654742, EBI-398885 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 87-177 | |||||
Sequence: MDHLESFIAECDRRTELAKKRLAETQEEISAEVSAKAEKVHELNEEIGKLLAKAEQLGAEGNVDESQKILMEVEKVRAKKKEAEEEYRNSM | ||||||
Coiled coil | 218-259 | |||||
Sequence: FIQIREKLDQLRKTVAEKQEKRNQDRLRRREEREREERLSRR | ||||||
Compositional bias | 232-261 | Basic and acidic residues | ||||
Sequence: VAEKQEKRNQDRLRRREEREREERLSRRSG | ||||||
Region | 232-371 | Disordered | ||||
Sequence: VAEKQEKRNQDRLRRREEREREERLSRRSGSRTRDRRRSRSRDRRRRRSRSTSRERRKLSRSRSRDRHRRHRSRSRSHSRGHRRASRDRSAKYKFSRERASREESWESGRSERGPPDWRLESSNGKMASRRSEEKEAGEI | ||||||
Compositional bias | 262-321 | Basic residues | ||||
Sequence: SRTRDRRRSRSRDRRRRRSRSTSRERRKLSRSRSRDRHRRHRSRSRSHSRGHRRASRDRS | ||||||
Compositional bias | 322-371 | Basic and acidic residues | ||||
Sequence: AKYKFSRERASREESWESGRSERGPPDWRLESSNGKMASRRSEEKEAGEI |
Sequence similarities
Belongs to the Luc7 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9NQ29-1
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
- Length371
- Mass (Da)43,728
- Last updated2000-10-01 v1
- ChecksumC277F424F5F5659C
Q9NQ29-2
- Name2
- NoteMay be due to an intron retention.
- Differences from canonical
- 326-371: Missing
Q9NQ29-3
- Name3
- Differences from canonical
- 1-20: MSAQAQMRALLDQLMGTARD → MQM
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_010214 | 1-20 | in isoform 3 | |||
Sequence: MSAQAQMRALLDQLMGTARD → MQM | ||||||
Sequence conflict | 171 | in Ref. 3; AAK61218 | ||||
Sequence: E → V | ||||||
Compositional bias | 232-261 | Basic and acidic residues | ||||
Sequence: VAEKQEKRNQDRLRRREEREREERLSRRSG | ||||||
Compositional bias | 262-321 | Basic residues | ||||
Sequence: SRTRDRRRSRSRDRRRRRSRSTSRERRKLSRSRSRDRHRRHRSRSRSHSRGHRRASRDRS | ||||||
Compositional bias | 322-371 | Basic and acidic residues | ||||
Sequence: AKYKFSRERASREESWESGRSERGPPDWRLESSNGKMASRRSEEKEAGEI | ||||||
Alternative sequence | VSP_010215 | 326-371 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AJ404326 EMBL· GenBank· DDBJ | CAB93981.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ404326 EMBL· GenBank· DDBJ | CAB93982.1 EMBL· GenBank· DDBJ | mRNA | ||
AY005111 EMBL· GenBank· DDBJ | AAG22846.1 EMBL· GenBank· DDBJ | mRNA | ||
AE006462 EMBL· GenBank· DDBJ | AAK61218.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK001093 EMBL· GenBank· DDBJ | BAA91500.1 EMBL· GenBank· DDBJ | mRNA | ||
Z69890 EMBL· GenBank· DDBJ | CAM26671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
Z69706 EMBL· GenBank· DDBJ | CAM26671.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471112 EMBL· GenBank· DDBJ | EAW85853.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003194 EMBL· GenBank· DDBJ | AAH03194.1 EMBL· GenBank· DDBJ | mRNA | ||
BC065198 EMBL· GenBank· DDBJ | AAH65198.1 EMBL· GenBank· DDBJ | mRNA |