Q2GSX8 · PABP_CHAGB
- ProteinPolyadenylate-binding protein, cytoplasmic and nuclear
- GenePAB1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids783 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, involved in both mRNA cleavage and polyadenylation. Is also required for efficient mRNA export to the cytoplasm. Acts in concert with a poly(A)-specific nuclease (PAN) to affect poly(A) tail shortening, which may occur concomitantly with either nucleocytoplasmic mRNA transport or translational initiation. In the cytoplasm, stimulates translation initiation and regulates mRNA decay through translation termination-coupled poly(A) shortening, probably mediated by PAN (By similarity).
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 | cytosol | |
Cellular Component | nucleus | |
Cellular Component | ribonucleoprotein complex | |
Molecular Function | mRNA 3'-UTR binding | |
Molecular Function | poly(A) binding | |
Molecular Function | poly(U) RNA binding | |
Biological Process | mRNA processing | |
Biological Process | mRNA transport | |
Biological Process | regulation of translation |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePolyadenylate-binding protein, cytoplasmic and nuclear
- Short namesPABP; Poly(A)-binding protein
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Chaetomiaceae > Chaetomium
Accessions
- Primary accessionQ2GSX8
Proteomes
Organism-specific databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000295386 | 1-783 | Polyadenylate-binding protein, cytoplasmic and nuclear | |||
Sequence: MAAPVAPGAVDQLAADLGNTSLGGGDNRAAPAINTNVAPGEYQTADPDTAGPTPSSAAPHPQSSASLYVGELDPSVTEAMLFELFSQIGSVASIRVCRDTITRRSLGYAYVNYNSTSDGEKALEELNYTLIKGRPCRIMWSQRDPALRKTGQGNVFIKNLDVAIDNKALHDTFAAFGNILSCKVAQDENGNSKGYGFVHYETDEAAAQAIKHVNNMLLNEKKVYVGYHIPKKDRQSKFEEMKANFTNIYVKNISLEATDEEFRDLFAKYGDVTSSSLARDSEGKSRGFGFVNFTTHECAAKAVEELNGKEFRGQDLYVGRAQKKHEREEELRKSYEAARLEKANKYQGVNLYIKNLADDIDDDKLRQMFSEYGPITSAKVMRDAVTEGSAEEETEGKDKENKKEGEQAAEAEGEAEGAEKKTEKKGDRRLGKSKGFGFVCFSNPDDATKAVAEMNQRMIEGKPLYVALAQRKDVRKNQLEASIQARNQLRMQQAAAQAGLPQQYMQTPVYYAPGQQPNFMPPGGRGMPFPQGGLGMPAVQGGRPGQFPPYAQQGGRGGMPPQQLPIYPLGQFPPGAYPQPNNPQFLAAIQQVQQQAAALGNGRGGPGGPGGRGMQGMPVPQGMPGGPGMAGFPPNGRPQNGNMGGRGGPGRGGNFAAGRGAPPAGPLAAGGELNASSLLQSQLTATNNPQQQKQILGENLFPKIQALQPDLAGKITGMLLEMDNAELVNLLEDEAALVAKVNEAMAVYDEYVKSQQGPGQGPAPTQGEAEAEKPKEEKAEEKA |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 16-65 | Disordered | ||||
Sequence: DLGNTSLGGGDNRAAPAINTNVAPGEYQTADPDTAGPTPSSAAPHPQSSA | ||||||
Compositional bias | 37-63 | Polar residues | ||||
Sequence: VAPGEYQTADPDTAGPTPSSAAPHPQS | ||||||
Domain | 65-143 | RRM 1 | ||||
Sequence: ASLYVGELDPSVTEAMLFELFSQIGSVASIRVCRDTITRRSLGYAYVNYNSTSDGEKALEELNYTLIKGRPCRIMWSQR | ||||||
Domain | 153-230 | RRM 2 | ||||
Sequence: GNVFIKNLDVAIDNKALHDTFAAFGNILSCKVAQDENGNSKGYGFVHYETDEAAAQAIKHVNNMLLNEKKVYVGYHIP | ||||||
Domain | 246-323 | RRM 3 | ||||
Sequence: TNIYVKNISLEATDEEFRDLFAKYGDVTSSSLARDSEGKSRGFGFVNFTTHECAAKAVEELNGKEFRGQDLYVGRAQK | ||||||
Domain | 349-471 | RRM 4 | ||||
Sequence: VNLYIKNLADDIDDDKLRQMFSEYGPITSAKVMRDAVTEGSAEEETEGKDKENKKEGEQAAEAEGEAEGAEKKTEKKGDRRLGKSKGFGFVCFSNPDDATKAVAEMNQRMIEGKPLYVALAQR | ||||||
Region | 381-428 | Disordered | ||||
Sequence: MRDAVTEGSAEEETEGKDKENKKEGEQAAEAEGEAEGAEKKTEKKGDR | ||||||
Compositional bias | 385-428 | Basic and acidic residues | ||||
Sequence: VTEGSAEEETEGKDKENKKEGEQAAEAEGEAEGAEKKTEKKGDR | ||||||
Region | 596-671 | Disordered | ||||
Sequence: AAALGNGRGGPGGPGGRGMQGMPVPQGMPGGPGMAGFPPNGRPQNGNMGGRGGPGRGGNFAAGRGAPPAGPLAAGG | ||||||
Domain | 676-753 | PABC | ||||
Sequence: SSLLQSQLTATNNPQQQKQILGENLFPKIQALQPDLAGKITGMLLEMDNAELVNLLEDEAALVAKVNEAMAVYDEYVK | ||||||
Region | 752-783 | Disordered | ||||
Sequence: VKSQQGPGQGPAPTQGEAEAEKPKEEKAEEKA | ||||||
Compositional bias | 769-783 | Basic and acidic residues | ||||
Sequence: AEAEKPKEEKAEEKA |
Sequence similarities
Belongs to the polyadenylate-binding protein type-1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length783
- Mass (Da)84,053
- Last updated2006-03-21 v1
- ChecksumFDBC6E39B105A058
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 37-63 | Polar residues | ||||
Sequence: VAPGEYQTADPDTAGPTPSSAAPHPQS | ||||||
Compositional bias | 385-428 | Basic and acidic residues | ||||
Sequence: VTEGSAEEETEGKDKENKKEGEQAAEAEGEAEGAEKKTEKKGDR | ||||||
Compositional bias | 769-783 | Basic and acidic residues | ||||
Sequence: AEAEKPKEEKAEEKA |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CH408034 EMBL· GenBank· DDBJ | EAQ84912.1 EMBL· GenBank· DDBJ | Genomic DNA |