A0A6Q8JFT6 · A0A6Q8JFT6_HUMAN
- ProteinPolyadenylate-binding protein
- GenePABPC1L
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids619 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
function
Binds the poly(A) tail of mRNA.
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 | cytoplasm | |
Molecular Function | RNA binding | |
Biological Process | cytosolic mRNA polyadenylation | |
Biological Process | nucleus localization | |
Biological Process | oocyte maturation | |
Biological Process | transcription initiation-coupled chromatin remodeling |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended namePolyadenylate-binding protein
- Short namesPABP
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A6Q8JFT6
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 771 variants from UniProt as well as other sources including ClinVar and dbSNP.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 39 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 96 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 341 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 342 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 364 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-89 | RRM | ||||
Sequence: ASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDVATRRSLGYAYINFQQPADAERALDTMNFEMLKGQPIRIMWSQR | ||||||
Domain | 99-175 | RRM | ||||
Sequence: GNIFIKNLEDSIDNKALYDTFSTFGNILSCKVACDEHGSRGFGFVHFETHEAAQQAINTMNGMLLNDRKVFVGHFKS | ||||||
Domain | 191-268 | RRM | ||||
Sequence: TNIYVKNLPVDVDEQGLQDLFSQFGKMLSVKVMRDNSGHSRCFGFVNFEKHEEAQKAVVHMNGKEVSGRLLYAGRAQK | ||||||
Domain | 294-370 | RRM | ||||
Sequence: VNLYVKNLDDSIDDDKLRKEFSPYGVITSAKVMTEGGHSKGFGFVCFSSPEEATKAVTEMNGRIVGTKPLYVALAQR | ||||||
Region | 430-455 | Disordered | ||||
Sequence: QPAPRWTSQPPRPSSAYPPGASMVRP | ||||||
Compositional bias | 432-446 | Pro residues | ||||
Sequence: APRWTSQPPRPSSAY | ||||||
Domain | 533-610 | PABC | ||||
Sequence: QEPLTASMLAAAPLHEQKQMIGERLYPLIHDVHTQLAGKITGMLLEIDNSELLLMLESPESLHAKIDEAVAVLQAHQA |
Sequence similarities
Belongs to the polyadenylate-binding protein type-1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length619
- Mass (Da)68,862
- Last updated2020-12-02 v1
- ChecksumC18A08C2DC5B6825
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q4VXU2 | PAP1L_HUMAN | PABPC1L | 614 | ||
H0Y386 | H0Y386_HUMAN | PABPC1L | 152 | ||
A0A6I8PL98 | A0A6I8PL98_HUMAN | PABPC1L | 38 | ||
A0A6I8PLA1 | A0A6I8PLA1_HUMAN | PABPC1L | 199 | ||
A0A6I8PIK9 | A0A6I8PIK9_HUMAN | PABPC1L | 73 | ||
A0A6I8PS38 | A0A6I8PS38_HUMAN | PABPC1L | 174 | ||
Q4VXT5 | Q4VXT5_HUMAN | PABPC1L | 163 | ||
Q4VXT8 | Q4VXT8_HUMAN | PABPC1L | 134 | ||
A0A6Q8JFV4 | A0A6Q8JFV4_HUMAN | PABPC1L | 192 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 432-446 | Pro residues | ||||
Sequence: APRWTSQPPRPSSAY |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL008725 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL109839 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |