A0A7I2V649 · A0A7I2V649_HUMAN
- ProteinPolyadenylate-binding protein 1
- GenePABPC1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids590 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score2/5
Function
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | RNA binding | |
Biological Process | mRNA processing | |
Biological Process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay |
Keywords
- Molecular function
- Biological process
Names & Taxonomy
Protein names
- Recommended namePolyadenylate-binding protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionA0A7I2V649
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 450 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) | 51 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 92 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 96 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 116 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 237 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 269 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 273 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 296 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 314 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 318 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 333 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 336 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 388 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 500 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 553 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 585 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 589 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 11-89 | RRM | ||||
Sequence: ASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQR | ||||||
Domain | 99-175 | RRM | ||||
Sequence: GNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKS | ||||||
Domain | 191-256 | RRM | ||||
Sequence: TNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKGVNLYVKNLD | ||||||
Domain | 248-324 | RRM | ||||
Sequence: VNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQR | ||||||
Domain | 496-573 | PABC | ||||
Sequence: QEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQA |
Sequence similarities
Belongs to the polyadenylate-binding protein type-1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length590
- Mass (Da)65,118
- Last updated2021-04-07 v1
- ChecksumEC7DC68C4DB1751F
Computationally mapped potential isoform sequences
There are 25 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P11940 | PABP1_HUMAN | PABPC1 | 636 | ||
E7ERJ7 | E7ERJ7_HUMAN | PABPC1 | 604 | ||
E7EQV3 | E7EQV3_HUMAN | PABPC1 | 591 | ||
H0YAW6 | H0YAW6_HUMAN | PABPC1 | 187 | ||
H0YB75 | H0YB75_HUMAN | PABPC1 | 183 | ||
H0YB86 | H0YB86_HUMAN | PABPC1 | 165 | ||
H0YAR2 | H0YAR2_HUMAN | PABPC1 | 599 | ||
H0YAS6 | H0YAS6_HUMAN | PABPC1 | 169 | ||
H0YAS7 | H0YAS7_HUMAN | PABPC1 | 136 | ||
H0YC10 | H0YC10_HUMAN | PABPC1 | 42 | ||
H0YBN4 | H0YBN4_HUMAN | PABPC1 | 174 | ||
H0YAP2 | H0YAP2_HUMAN | PABPC1 | 131 | ||
A0A7I2YQ88 | A0A7I2YQ88_HUMAN | PABPC1 | 633 | ||
A0A7I2YQ90 | A0A7I2YQ90_HUMAN | PABPC1 | 604 | ||
A0A7I2YQE4 | A0A7I2YQE4_HUMAN | PABPC1 | 565 | ||
A0A087WTT1 | A0A087WTT1_HUMAN | PABPC1 | 588 | ||
E5RJB9 | E5RJB9_HUMAN | PABPC1 | 129 | ||
E5RJM8 | E5RJM8_HUMAN | PABPC1 | 38 | ||
E5RGC4 | E5RGC4_HUMAN | PABPC1 | 43 | ||
E5RGH3 | E5RGH3_HUMAN | PABPC1 | 108 | ||
E5RH24 | E5RH24_HUMAN | PABPC1 | 118 | ||
E5RHG7 | E5RHG7_HUMAN | PABPC1 | 75 | ||
E5RFD8 | E5RFD8_HUMAN | PABPC1 | 61 | ||
A0A7I2V3J9 | A0A7I2V3J9_HUMAN | PABPC1 | 151 | ||
A0A7I2V4N4 | A0A7I2V4N4_HUMAN | PABPC1 | 577 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AP001205 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |