O95639 · CPSF4_HUMAN
- ProteinCleavage and polyadenylation specificity factor subunit 4
- GeneCPSF4
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids269 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. CPSF4 binds RNA polymers with a preference for poly(U).
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 | intracellular membrane-bounded organelle | |
Cellular Component | mRNA cleavage and polyadenylation specificity factor complex | |
Cellular Component | nucleoplasm | |
Molecular Function | RNA binding | |
Molecular Function | sequence-specific double-stranded DNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | mRNA processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCleavage and polyadenylation specificity factor subunit 4
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95639
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 156 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_0000074402 | 1-269 | UniProt | Cleavage and polyadenylation specificity factor subunit 4 | |||
Sequence: MQEIIASVDHIKFDLEIAVEQQLGAQPLPFPGMDKSGAAVCEFFLKAACGKGGMCPFRHISGEKTVVCKHWLRGLCKKGDQCEFLHEYDMTKMPECYFYSKFGECSNKECPFLHIDPESKIKDCPWYDRGFCKHGPLCRHRHTRRVICVNYLVGFCPEGPSCKFMHPRFELPMGTTEQPPLPQQTQPPAKQSNNPPLQRSSSLIQLTSQNSSPNQQRTPQVIGVMQSQNSSAGNRGPRPLEQVTCYKCGEKGHYANRCTKGHLAFLSGQ | |||||||
Modified residue | 200 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 200 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 202 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 202 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 208 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 211 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 212 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 212 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 218 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 231 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 267 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of the cleavage and polyadenylation specificity factor (CPSF) complex, composed of CPSF1, CPSF2, CPSF3, CPSF4 and FIP1L1. Interacts with FIP1L1.
(Microbial infection) Interacts with influenza A virus NS1 blocks processing of pre-mRNAs, thereby preventing nuclear export of host cell mRNAs.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95639 | CDC73 Q6P1J9 | 3 | EBI-725860, EBI-930143 | |
BINARY | O95639 | FIP1L1 Q6UN15 | 5 | EBI-725860, EBI-1021914 | |
BINARY | O95639 | MEOX2 P50222 | 3 | EBI-725860, EBI-748397 | |
XENO | O95639 | NS1 I6T1Z2 | 5 | EBI-725860, EBI-12561553 | |
XENO | O95639 | NS1 Q194T2 | 5 | EBI-725860, EBI-11515076 | |
XENO | O95639-1 | NS P03495 | 4 | EBI-15725265, EBI-2548993 | |
BINARY | O95639-2 | MID2 Q9UJV3-2 | 3 | EBI-13063650, EBI-10172526 | |
BINARY | O95639-2 | MYOG P15173 | 3 | EBI-13063650, EBI-3906629 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for zinc finger, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 35-61 | C3H1-type 1 | ||||
Sequence: KSGAAVCEFFLKAACGKGGMCPFRHIS | ||||||
Zinc finger | 62-89 | C3H1-type 2 | ||||
Sequence: GEKTVVCKHWLRGLCKKGDQCEFLHEYD | ||||||
Zinc finger | 90-117 | C3H1-type 3 | ||||
Sequence: MTKMPECYFYSKFGECSNKECPFLHIDP | ||||||
Zinc finger | 118-142 | C3H1-type 4 | ||||
Sequence: ESKIKDCPWYDRGFCKHGPLCRHRH | ||||||
Zinc finger | 143-169 | C3H1-type 5 | ||||
Sequence: TRRVICVNYLVGFCPEGPSCKFMHPRF | ||||||
Region | 173-199 | Disordered | ||||
Sequence: MGTTEQPPLPQQTQPPAKQSNNPPLQR | ||||||
Zinc finger | 243-260 | CCHC-type | ||||
Sequence: VTCYKCGEKGHYANRCTK |
Sequence similarities
Belongs to the CPSF4/YTH1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
O95639-1
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
- Length269
- Mass (Da)30,255
- Last updated1999-05-01 v1
- Checksum49444E3EB840464A
O95639-2
- Name2
- Differences from canonical
- 191-215: Missing
O95639-3
- Name3
- NoteMay be due to a competing acceptor splice site.
- Differences from canonical
- 191-216: Missing
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U79569 EMBL· GenBank· DDBJ | AAD00321.1 EMBL· GenBank· DDBJ | mRNA | ||
CR542161 EMBL· GenBank· DDBJ | CAG46958.1 EMBL· GenBank· DDBJ | mRNA | ||
EF191081 EMBL· GenBank· DDBJ | ABN05292.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH236956 EMBL· GenBank· DDBJ | EAL23878.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76667.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471091 EMBL· GenBank· DDBJ | EAW76668.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003101 EMBL· GenBank· DDBJ | AAH03101.1 EMBL· GenBank· DDBJ | mRNA | ||
BC050738 EMBL· GenBank· DDBJ | AAH50738.1 EMBL· GenBank· DDBJ | mRNA |