Q9Y383 · LC7L2_HUMAN
- ProteinPutative RNA-binding protein Luc7-like 2
- GeneLUC7L2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids392 (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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | nuclear speck | |
Cellular Component | U1 snRNP | |
Cellular Component | U2-type prespliceosome | |
Molecular Function | enzyme binding | |
Molecular Function | mRNA binding | |
Molecular Function | RNA binding | |
Biological Process | mRNA splice site recognition |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePutative RNA-binding protein Luc7-like 2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y383
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Colocalizes with SCNM1 and SNRNP70 in nuclear speckles.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 266 | Induces a decrease in lysyl-hydroxylation. Abolishes lysyl-hydroxylation; when associated with R-269. | ||||
Sequence: K → R | ||||||
Mutagenesis | 269 | Induces a decrease in lysyl-hydroxylation. Abolishes lysyl-hydroxylation; when associated with R-266. | ||||
Sequence: K → R | ||||||
Natural variant | VAR_034067 | 361 | in dbSNP:rs3757435 | |||
Sequence: D → E |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 325 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 (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000187282 | 1-392 | UniProt | Putative RNA-binding protein Luc7-like 2 | |||
Sequence: MSAQAQMRAMLDQLMGTSRDGDTTRQRIKFSDDRVCKSHLLNCCPHDVLSGTRMDLGECLKVHDLALRADYEIASKEQDFFFELDAMDHLQSFIADCDRRTEVAKKRLAETQEEISAEVAAKAERVHELNEEIGKLLAKVEQLGAEGNVEESQKVMDEVEKARAKKREAEEVYRNSMPASSFQQQKLRVCEVCSAYLGLHDNDRRLADHFGGKLHLGFIEIREKLEELKRVVAEKQEKRNQERLKRREEREREEREKLRRSRSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSRERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 18 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 18 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 266 | UniProt | 5-hydroxylysine; by JMJD6 | ||||
Sequence: K | |||||||
Modified residue | 269 | UniProt | 5-hydroxylysine; by JMJD6 | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 347 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 354 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 370 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 383 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 384 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with SCNM1.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y383 | APPBP2 Q92624 | 6 | EBI-352851, EBI-743771 | |
BINARY | Q9Y383 | DZIP1 Q86YF9 | 3 | EBI-352851, EBI-998108 | |
BINARY | Q9Y383 | HTT P42858 | 9 | EBI-352851, EBI-466029 | |
BINARY | Q9Y383 | MAP1LC3B Q9GZQ8 | 3 | EBI-352851, EBI-373144 | |
BINARY | Q9Y383 | MEOX2 Q6FHY5 | 3 | EBI-352851, EBI-16439278 | |
BINARY | Q9Y383 | NFYA P23511 | 4 | EBI-352851, EBI-389739 | |
BINARY | Q9Y383 | NFYA P23511-2 | 3 | EBI-352851, EBI-11061759 | |
BINARY | Q9Y383 | SRPK1 Q96SB4 | 4 | EBI-352851, EBI-539478 | |
BINARY | Q9Y383 | SRPK2 P78362 | 4 | EBI-352851, EBI-593303 | |
BINARY | Q9Y383 | SRRM4 A7MD48 | 6 | EBI-352851, EBI-3867173 | |
BINARY | Q9Y383 | SRSF6 Q13247 | 7 | EBI-352851, EBI-745230 | |
BINARY | Q9Y383 | SRSF7 Q16629 | 7 | EBI-352851, EBI-398885 | |
BINARY | Q9Y383 | ZRSR2 Q15696 | 3 | EBI-352851, EBI-6657923 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for coiled coil, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 102-177 | |||||
Sequence: EVAKKRLAETQEEISAEVAAKAERVHELNEEIGKLLAKVEQLGAEGNVEESQKVMDEVEKARAKKREAEEVYRNSM | ||||||
Compositional bias | 235-261 | Basic and acidic residues | ||||
Sequence: KQEKRNQERLKRREEREREEREKLRRS | ||||||
Region | 235-392 | Disordered | ||||
Sequence: KQEKRNQERLKRREEREREEREKLRRSRSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSRERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI | ||||||
Compositional bias | 262-328 | Basic residues | ||||
Sequence: RSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSR | ||||||
Compositional bias | 329-392 | Basic and acidic residues | ||||
Sequence: ERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI |
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.
Q9Y383-1
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
- Length392
- Mass (Da)46,514
- Last updated2004-05-10 v2
- Checksum1C559CCE0F23F693
Q9Y383-2
- Name2
- Differences from canonical
- 1-21: MSAQAQMRAMLDQLMGTSRDG → MPAYLNLQGSVRKAPHSPSR
Q9Y383-3
- Name3
- Differences from canonical
- 1-20: MSAQAQMRAMLDQLMGTSRD → MVIHSQLKKIQGASERM
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
F8WEU3 | F8WEU3_HUMAN | LUC7L2 | 83 | ||
V9GZ75 | V9GZ75_HUMAN | LUC7L2 | 54 | ||
A0A0A6YYJ8 | A0A0A6YYJ8_HUMAN | LUC7L2 | 458 |
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_044896 | 1-20 | in isoform 3 | |||
Sequence: MSAQAQMRAMLDQLMGTSRD → MVIHSQLKKIQGASERM | ||||||
Alternative sequence | VSP_010217 | 1-21 | in isoform 2 | |||
Sequence: MSAQAQMRAMLDQLMGTSRDG → MPAYLNLQGSVRKAPHSPSR | ||||||
Sequence conflict | 27 | in Ref. 2; BAA91737 | ||||
Sequence: R → Q | ||||||
Compositional bias | 235-261 | Basic and acidic residues | ||||
Sequence: KQEKRNQERLKRREEREREEREKLRRS | ||||||
Compositional bias | 262-328 | Basic residues | ||||
Sequence: RSHSKNPKRSRSREHRRHRSRSMSRERKRRTRSKSREKRHRHRSRSSSRSRSRSHQRSRHSSRDRSR | ||||||
Compositional bias | 329-392 | Basic and acidic residues | ||||
Sequence: ERSKRRSSKERFRDQDLASCDRDRSSRDRSPRDRDRKDKKRSYESANGRSEDRRSSEEREAGEI | ||||||
Sequence conflict | 389-390 | in Ref. 1; AAD34054 | ||||
Sequence: AG → QR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF151817 EMBL· GenBank· DDBJ | AAD34054.1 EMBL· GenBank· DDBJ | mRNA | ||
AF151832 EMBL· GenBank· DDBJ | AAD34069.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK001476 EMBL· GenBank· DDBJ | BAA91713.1 EMBL· GenBank· DDBJ | mRNA | ||
AK001519 EMBL· GenBank· DDBJ | BAA91737.1 EMBL· GenBank· DDBJ | mRNA | ||
AK022895 EMBL· GenBank· DDBJ | BAB14297.1 EMBL· GenBank· DDBJ | mRNA | ||
AK298166 EMBL· GenBank· DDBJ | BAH12736.1 EMBL· GenBank· DDBJ | mRNA | ||
BC017163 EMBL· GenBank· DDBJ | AAH17163.1 EMBL· GenBank· DDBJ | mRNA | ||
BC042625 EMBL· GenBank· DDBJ | AAH42625.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050708 EMBL· GenBank· DDBJ | AAH50708.1 EMBL· GenBank· DDBJ | mRNA | ||
BC056886 EMBL· GenBank· DDBJ | AAH56886.1 EMBL· GenBank· DDBJ | mRNA |