P54105 · ICLN_HUMAN
- ProteinMethylosome subunit pICln
- GeneCLNS1A
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids237 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Involved in both the assembly of spliceosomal snRNPs and the methylation of Sm proteins (PubMed:10330151, PubMed:11713266, PubMed:18984161, PubMed:21081503).
Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:10330151, PubMed:18984161).
Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:10330151).
In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:10330151, PubMed:18984161).
Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (PubMed:10330151, PubMed:18984161).
Chaperone that regulates the assembly of spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs (PubMed:10330151, PubMed:18984161).
Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core) (PubMed:10330151).
In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP (PubMed:10330151, PubMed:18984161).
Dissociation by the SMN complex of CLNS1A from the trapped Sm proteins and their transfer to an SMN-Sm complex triggers the assembly of core snRNPs and their transport to the nucleus (PubMed:10330151, PubMed:18984161).
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 | cytoskeleton | |
Cellular Component | cytosol | |
Cellular Component | methylosome | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | pICln-Sm protein complex | |
Cellular Component | plasma membrane | |
Cellular Component | spliceosomal complex | |
Molecular Function | RNA binding | |
Biological Process | cell volume homeostasis | |
Biological Process | chloride transport | |
Biological Process | mRNA cis splicing, via spliceosome | |
Biological Process | positive regulation of mRNA splicing, via spliceosome | |
Biological Process | spliceosomal snRNP assembly |
Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameMethylosome subunit pICln
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP54105
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: A small fraction is also associated with the cytoskeleton (PubMed:18984161).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_015736 | 20 | ||||
Sequence: Q → H | ||||||
Natural variant | VAR_015737 | 218 | ||||
Sequence: M → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 272 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).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Initiator methionine | 1 | UniProt | Removed | ||||
Sequence: M | |||||||
Modified residue | 2 | UniProt | N-acetylserine | ||||
Sequence: S | |||||||
Chain | PRO_0000185155 | 2-237 | UniProt | Methylosome subunit pICln | |||
Sequence: SFLKSFPPPGPAEGLLRQQPDTEAVLNGKGLGTGTLYIAESRLSWLDGSGLGFSLEYPTISLHALSRDRSDCLGEHLYVMVNAKFEEESKEPVADEEEEDSDDDVEPITEFRFVPSDKSALEAMFTAMCECQALHPDPEDEDSDDYDGEEYDVEAHEQGQGDIPTFYTYEEGLSHLTAEGQATLERLEGMLSQSVSSQYNMAGVRTEDSIRDYEDGMEVDTTPTVAGQFEDADVDH | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 90 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 144 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 193 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 193 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 195 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 195 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 197 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 198 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 198 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 210 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 214 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 223 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 223 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the methylosome, a 20S complex containing at least PRMT5/SKB1, WDR77/MEP50 and CLNS1A/pICln (PubMed:11747828, PubMed:18984161, PubMed:21081503).
May mediate SNRPD1 and SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP (PubMed:18984161).
Interacts with LSM10 and LSM11 (PubMed:16087681).
May mediate SNRPD1 and SNRPD3 methylation. Forms a 6S pICln-Sm complex composed of CLNS1A/pICln, SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG; ring-like structure where CLNS1A/pICln mimics additional Sm proteins and which is unable to assemble into the core snRNP (PubMed:18984161).
Interacts with LSM10 and LSM11 (PubMed:16087681).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P54105 | EPB41 P11171-2 | 3 | EBI-724693, EBI-10197451 | |
BINARY | P54105 | FRMD7 Q6ZUT3 | 3 | EBI-724693, EBI-12325851 | |
BINARY | P54105 | LSM2 Q9Y333 | 8 | EBI-724693, EBI-347416 | |
BINARY | P54105 | LSM3 P62310 | 9 | EBI-724693, EBI-348239 | |
BINARY | P54105 | LSM6 P62312 | 11 | EBI-724693, EBI-373310 | |
BINARY | P54105 | PRMT5 O14744 | 9 | EBI-724693, EBI-351098 | |
BINARY | P54105 | SNRPB P14678 | 7 | EBI-724693, EBI-372458 | |
BINARY | P54105 | SNRPB P14678-2 | 3 | EBI-724693, EBI-372475 | |
BINARY | P54105 | SNRPD1 P62314 | 13 | EBI-724693, EBI-372177 | |
BINARY | P54105 | SNRPD2 P62316 | 13 | EBI-724693, EBI-297993 | |
BINARY | P54105 | SNRPD3 P62318 | 11 | EBI-724693, EBI-372789 | |
BINARY | P54105 | SNRPF P62306 | 9 | EBI-724693, EBI-356900 | |
BINARY | P54105 | SNRPG P62308 | 11 | EBI-724693, EBI-624585 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 135-159 | Disordered | ||||
Sequence: LHPDPEDEDSDDYDGEEYDVEAHEQ | ||||||
Compositional bias | 138-153 | Acidic residues | ||||
Sequence: DPEDEDSDDYDGEEYD |
Sequence similarities
Belongs to the pICln (TC 1.A.47) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length237
- Mass (Da)26,215
- Last updated1996-10-01 v1
- ChecksumAE9C09884A6FF158
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 138-153 | Acidic residues | ||||
Sequence: DPEDEDSDDYDGEEYD |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X91788 EMBL· GenBank· DDBJ | CAA62902.1 EMBL· GenBank· DDBJ | mRNA | ||
U17899 EMBL· GenBank· DDBJ | AAC50111.1 EMBL· GenBank· DDBJ | mRNA | ||
U53454 EMBL· GenBank· DDBJ | AAB03316.1 EMBL· GenBank· DDBJ | mRNA | ||
AF005422 EMBL· GenBank· DDBJ | AAB61444.1 EMBL· GenBank· DDBJ | mRNA | ||
AF026003 EMBL· GenBank· DDBJ | AAB88806.1 EMBL· GenBank· DDBJ | mRNA | ||
AF232708 EMBL· GenBank· DDBJ | AAF76861.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF232224 EMBL· GenBank· DDBJ | AAF76858.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF232225 EMBL· GenBank· DDBJ | AAF76859.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK315259 EMBL· GenBank· DDBJ | BAG37676.1 EMBL· GenBank· DDBJ | mRNA | ||
BT019907 EMBL· GenBank· DDBJ | AAV38710.1 EMBL· GenBank· DDBJ | mRNA | ||
BC119634 EMBL· GenBank· DDBJ | AAI19635.1 EMBL· GenBank· DDBJ | mRNA | ||
BC119635 EMBL· GenBank· DDBJ | AAI19636.1 EMBL· GenBank· DDBJ | mRNA |