Q9HCG8 · CWC22_HUMAN
- ProteinPre-mRNA-splicing factor CWC22 homolog
- GeneCWC22
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids908 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:12226669, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106).
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Promotes exon-junction complex (EJC) assembly (PubMed:22959432, PubMed:22961380).
Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay
As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Promotes exon-junction complex (EJC) assembly (PubMed:22959432, PubMed:22961380).
Hinders EIF4A3 from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs. Through its role in EJC assembly, required for nonsense-mediated mRNA decay
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 | catalytic step 2 spliceosome | |
Cellular Component | cytosol | |
Cellular Component | nuclear speck | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | spliceosomal complex | |
Cellular Component | U2-type catalytic step 1 spliceosome | |
Cellular Component | U2-type catalytic step 2 spliceosome | |
Cellular Component | U2-type precatalytic spliceosome | |
Molecular Function | RNA binding | |
Biological Process | mRNA splicing, via spliceosome | |
Biological Process | regulation of mRNA splicing, via spliceosome |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePre-mRNA-splicing factor CWC22 homolog
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9HCG8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Concentrates around speckles, which are sites of pre-mRNA synthesis and processing, where it colocalizes with EJC core proteins.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 168 | No effect on EIF4A3 incorporation into EJCs. | ||||
Sequence: G → Y | ||||||
Mutagenesis | 171-172 | Loss of EIF4A3-binding. | ||||
Sequence: NK → DE | ||||||
Mutagenesis | 171-174 | Loss of EIF4A3-binding. | ||||
Sequence: NKVN → AAVA | ||||||
Mutagenesis | 331 | Decreased EIF4A3-binding; when associated with A-334. | ||||
Sequence: R → A | ||||||
Mutagenesis | 334 | Decreased EIF4A3-binding; when associated with A-331. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_057513 | 656 | in dbSNP:rs17778270 | |||
Sequence: A → V | ||||||
Natural variant | VAR_057514 | 741 | in dbSNP:rs11903115 | |||
Sequence: D → V | ||||||
Natural variant | VAR_057515 | 794 | in dbSNP:rs1046356 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 886 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_0000302005 | 1-908 | UniProt | Pre-mRNA-splicing factor CWC22 homolog | |||
Sequence: MKSSVAQIKPSSGHDRRENLNSYQRNSSPEDRYEEQERSPRDRDYFDYSRSDYEHSRRGRSYDSSMESRNRDREKRRERERDTDRKRSRKSPSPGRRNPETSVTQSSSAQDEPATKKKKDELDPLLTRTGGAYIPPAKLRMMQEQITDKNSLAYQRMSWEALKKSINGLINKVNISNISIIIQELLQENIVRGRGLLSRSVLQAQSASPIFTHVYAALVAIINSKFPQIGELILKRLILNFRKGYRRNDKQLCLTASKFVAHLINQNVAHEVLCLEMLTLLLERPTDDSVEVAIGFLKECGLKLTQVSPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDGFKDHPIILEGLDLVEEDDQFTHMLPLEDDYNPEDVLNVFKMDPNFMENEEKYKAIKKEILDEGDTDSNTDQDAGSSEEDEEEEEEEGEEDEEGQKVTIHDKTEINLVSFRRTIYLAIQSSLDFEECAHKLLKMEFPESQTKELCNMILDCCAQQRTYEKFFGLLAGRFCMLKKEYMESFEGIFKEQYDTIHRLETNKLRNVAKMFAHLLYTDSLPWSVLECIKLSEETTTSSSRIFVKIFFQELCEYMGLPKLNARLKDETLQPFFEGLLPRDNPRNTRFAINFFTSIGLGGLTDELREHLKNTPKVIVAQKPDVEQNKSSPSSSSSASSSSESDSSDSDSDSSDSSSESSSEESDSSSISSHSSASANDVRKKGHGKTRSKEVDKLIRNQQTNDRKQKERRQEHGHQETRTERERRSEKHRDQNSSGSNWRDPITKYTSDKDVPSERNNYSRVANDRDQEMHIDLENKHGDPKKKRGERRNSFSENEKHTHRIKDSENFRRKDRSKSKEMNRKHSGSRSDEDRYQNGAERRWEKSSRYSEQSRESKKNQDRRREKSPAKQK | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 28 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 39 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 61 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 61 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 93 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 107 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 785 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 786 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 786 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 792 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 829 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 829 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 831 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 862 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 864 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 866 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the pre-catalytic spliceosome B and the catalytic spliceosome C complexes (PubMed:11991638, PubMed:22961380, PubMed:28076346, PubMed:28502770, PubMed:29301961, PubMed:29360106).
Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932).
Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is mediated by the MIF4G domain (PubMed:24218557).
Full interaction with EIF4A3 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA
Component of the minor spliceosome, which splices U12-type introns (PubMed:33509932).
Interacts with EIF4A3 and PRPF19 in an RNA-independent manner. Direct interaction with EIF4A3 is mediated by the MIF4G domain (PubMed:24218557).
Full interaction with EIF4A3 occurs only when EIF4A3 is not part of the EJC and prevents EIF4A3 binding to RNA
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9HCG8 | EIF4A3 P38919 | 6 | EBI-373289, EBI-299104 | |
BINARY | Q9HCG8 | FAM32A Q9Y421 | 2 | EBI-373289, EBI-726146 | |
BINARY | Q9HCG8 | FRG1 Q14331 | 2 | EBI-373289, EBI-2515248 | |
BINARY | Q9HCG8 | KLHL2 O95198 | 3 | EBI-373289, EBI-746999 | |
BINARY | Q9HCG8 | PTPN21 Q16825 | 3 | EBI-373289, EBI-2860264 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-129 | Disordered | ||||
Sequence: MKSSVAQIKPSSGHDRRENLNSYQRNSSPEDRYEEQERSPRDRDYFDYSRSDYEHSRRGRSYDSSMESRNRDREKRRERERDTDRKRSRKSPSPGRRNPETSVTQSSSAQDEPATKKKKDELDPLLTRT | ||||||
Compositional bias | 28-89 | Basic and acidic residues | ||||
Sequence: SPEDRYEEQERSPRDRDYFDYSRSDYEHSRRGRSYDSSMESRNRDREKRRERERDTDRKRSR | ||||||
Compositional bias | 95-111 | Polar residues | ||||
Sequence: GRRNPETSVTQSSSAQD | ||||||
Domain | 163-346 | MIF4G | ||||
Sequence: KKSINGLINKVNISNISIIIQELLQENIVRGRGLLSRSVLQAQSASPIFTHVYAALVAIINSKFPQIGELILKRLILNFRKGYRRNDKQLCLTASKFVAHLINQNVAHEVLCLEMLTLLLERPTDDSVEVAIGFLKECGLKLTQVSPRGINAIFERLRNILHESEIDKRVQYMIEVMFAVRKDG | ||||||
Region | 404-443 | Disordered | ||||
Sequence: EILDEGDTDSNTDQDAGSSEEDEEEEEEEGEEDEEGQKVT | ||||||
Compositional bias | 411-437 | Acidic residues | ||||
Sequence: TDSNTDQDAGSSEEDEEEEEEEGEEDE | ||||||
Domain | 454-570 | MI | ||||
Sequence: SFRRTIYLAIQSSLDFEECAHKLLKMEFPESQTKELCNMILDCCAQQRTYEKFFGLLAGRFCMLKKEYMESFEGIFKEQYDTIHRLETNKLRNVAKMFAHLLYTDSLPWSVLECIKL | ||||||
Region | 654-908 | Disordered | ||||
Sequence: IVAQKPDVEQNKSSPSSSSSASSSSESDSSDSDSDSSDSSSESSSEESDSSSISSHSSASANDVRKKGHGKTRSKEVDKLIRNQQTNDRKQKERRQEHGHQETRTERERRSEKHRDQNSSGSNWRDPITKYTSDKDVPSERNNYSRVANDRDQEMHIDLENKHGDPKKKRGERRNSFSENEKHTHRIKDSENFRRKDRSKSKEMNRKHSGSRSDEDRYQNGAERRWEKSSRYSEQSRESKKNQDRRREKSPAKQK | ||||||
Compositional bias | 660-714 | Polar residues | ||||
Sequence: DVEQNKSSPSSSSSASSSSESDSSDSDSDSSDSSSESSSEESDSSSISSHSSASA | ||||||
Compositional bias | 715-773 | Basic and acidic residues | ||||
Sequence: NDVRKKGHGKTRSKEVDKLIRNQQTNDRKQKERRQEHGHQETRTERERRSEKHRDQNSS | ||||||
Compositional bias | 782-908 | Basic and acidic residues | ||||
Sequence: TKYTSDKDVPSERNNYSRVANDRDQEMHIDLENKHGDPKKKRGERRNSFSENEKHTHRIKDSENFRRKDRSKSKEMNRKHSGSRSDEDRYQNGAERRWEKSSRYSEQSRESKKNQDRRREKSPAKQK |
Sequence similarities
Belongs to the CWC22 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length908
- Mass (Da)105,466
- Last updated2010-05-18 v3
- Checksum00EF9B361B5F55AB
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
B7WP74 | B7WP74_HUMAN | CWC22 | 745 |
Sequence caution
Features
Showing features for compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 28-89 | Basic and acidic residues | ||||
Sequence: SPEDRYEEQERSPRDRDYFDYSRSDYEHSRRGRSYDSSMESRNRDREKRRERERDTDRKRSR | ||||||
Compositional bias | 95-111 | Polar residues | ||||
Sequence: GRRNPETSVTQSSSAQD | ||||||
Sequence conflict | 270 | in Ref. 2; BAB15197 | ||||
Sequence: H → Y | ||||||
Compositional bias | 411-437 | Acidic residues | ||||
Sequence: TDSNTDQDAGSSEEDEEEEEEEGEEDE | ||||||
Sequence conflict | 550 | in Ref. 2; BAB15197 | ||||
Sequence: M → V | ||||||
Sequence conflict | 613 | in Ref. 4; AAH31216 | ||||
Sequence: E → G | ||||||
Compositional bias | 660-714 | Polar residues | ||||
Sequence: DVEQNKSSPSSSSSASSSSESDSSDSDSDSSDSSSESSSEESDSSSISSHSSASA | ||||||
Sequence conflict | 685 | in Ref. 4; AAH16651 | ||||
Sequence: S → F | ||||||
Sequence conflict | 701 | in Ref. 4; AAH31216 | ||||
Sequence: S → G | ||||||
Compositional bias | 715-773 | Basic and acidic residues | ||||
Sequence: NDVRKKGHGKTRSKEVDKLIRNQQTNDRKQKERRQEHGHQETRTERERRSEKHRDQNSS | ||||||
Sequence conflict | 742 | in Ref. 4; AAH31216 | ||||
Sequence: R → K | ||||||
Sequence conflict | 773 | in Ref. 2; BAB15612 and 4; AAH53573/AAH93952/AAH93954 | ||||
Sequence: S → R | ||||||
Compositional bias | 782-908 | Basic and acidic residues | ||||
Sequence: TKYTSDKDVPSERNNYSRVANDRDQEMHIDLENKHGDPKKKRGERRNSFSENEKHTHRIKDSENFRRKDRSKSKEMNRKHSGSRSDEDRYQNGAERRWEKSSRYSEQSRESKKNQDRRREKSPAKQK |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB046824 EMBL· GenBank· DDBJ | BAB13430.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK025635 EMBL· GenBank· DDBJ | BAB15197.1 EMBL· GenBank· DDBJ | mRNA | Frameshift | |
AK026978 EMBL· GenBank· DDBJ | BAB15612.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AC068194 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC096587 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC016651 EMBL· GenBank· DDBJ | AAH16651.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC031216 EMBL· GenBank· DDBJ | AAH31216.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC053573 EMBL· GenBank· DDBJ | AAH53573.1 EMBL· GenBank· DDBJ | mRNA | ||
BC057826 EMBL· GenBank· DDBJ | AAH57826.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
BC093952 EMBL· GenBank· DDBJ | AAH93952.1 EMBL· GenBank· DDBJ | mRNA | ||
BC093954 EMBL· GenBank· DDBJ | AAH93954.1 EMBL· GenBank· DDBJ | mRNA |