G3XAH6 · G3XAH6_HUMAN
- ProteinPoly(A) polymerase
- GenePAPOLA
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids724 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Polymerase that creates the 3'-poly(A) tail of mRNA's.
Catalytic activity
- ATP + RNA(n) = diphosphate + RNA(n)-3'-adenine ribonucleotide
Cofactor
Protein has several cofactor binding sites:
Note: Binds 2 magnesium ions. Also active with manganese.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 100-102 | ATP (UniProtKB | ChEBI) | ||||
Sequence: FGS | ||||||
Binding site | 109 | ATP (UniProtKB | ChEBI) | ||||
Sequence: T | ||||||
Binding site | 113 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 113 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 113-115 | ATP (UniProtKB | ChEBI) | ||||
Sequence: DID | ||||||
Binding site | 115 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 115 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 167 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 167 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 228 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 237 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 246-247 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GV |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | nucleoplasm | |
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | poly(A) RNA polymerase activity | |
Molecular Function | RNA binding | |
Biological Process | mRNA processing | |
Biological Process | RNA 3'-end processing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePoly(A) polymerase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionG3XAH6
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 559 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) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 24 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 27 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 109 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 537 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 545 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 617 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 628 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 629 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 654 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 660 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 717 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MPFPVTTQGSQQTQPPQKHYG | ||||||
Region | 1-22 | Disordered | ||||
Sequence: MPFPVTTQGSQQTQPPQKHYGI | ||||||
Domain | 21-214 | Poly(A) polymerase nucleotidyltransferase | ||||
Sequence: GITSPISLAAPKETDCVLTQKLIETLKPFGVFEEEEELQRRILILGKLNNLVKEWIREISESKNLPQSVIENVGGKIFTFGSYRLGVHTKGADIDALCVAPRHVDRSDFFTSFYDKLKLQEEVKDLRAVEEAFVPVIKLCFDGIEIDILFARLALQTIPEDLDLRDDSLLKNLDIRCIRSLNGCRVTDEILHLV | ||||||
Domain | 219-363 | Poly(A) polymerase central | ||||
Sequence: NFRLTLRAIKLWAKRHNIYSNILGFLGGVSWAMLVARTCQLYPNAIASTLVHKFFLVFSKWEWPNPVLLKQPEECNLNLPVWDPRVNPSDRYHLMPIITPAYPQQNSTYNVSVSTRMVMVEEFKQGLAITDEILLSKAEWSKLFE | ||||||
Domain | 366-434 | Poly(A) polymerase RNA-binding | ||||
Sequence: NFFQKYKHYIVLLASAPTEKQRLEWVGLVESKIRILVGSLEKNEFITLAHVNPQSFPAPKENPDKEEFR | ||||||
Domain | 426-506 | Poly(A) polymerase RNA-binding | ||||
Sequence: ENPDKEEFRTMWVIGLVFKKTENSENLSVDLTYDIQSFTDTVYRQAINSKMFEVDMKIAAMHVKRKQLHQLLPNHVLQKKK | ||||||
Region | 523-565 | Disordered | ||||
Sequence: LDLSMDSDNSMSVPSPTSATKTSPLNSSGSSQGRNSPAPAVTA | ||||||
Compositional bias | 577-600 | Polar residues | ||||
Sequence: SVPQVNSSESSGGTSSESIPQTAT | ||||||
Region | 577-690 | Disordered | ||||
Sequence: SVPQVNSSESSGGTSSESIPQTATQPAISPPPKPTVSRVVSSTRLVNPPPRSSGNAATSGNAATKIPTPIVGVKRTSSPHKEESPKKTKTEEEQLDTETSTTQSETIQTAASLL | ||||||
Compositional bias | 611-641 | Polar residues | ||||
Sequence: TVSRVVSSTRLVNPPPRSSGNAATSGNAATK | ||||||
Compositional bias | 652-672 | Basic and acidic residues | ||||
Sequence: TSSPHKEESPKKTKTEEEQLD | ||||||
Compositional bias | 673-690 | Polar residues | ||||
Sequence: TETSTTQSETIQTAASLL |
Sequence similarities
Belongs to the poly(A) polymerase family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length724
- Mass (Da)80,626
- Last updated2011-11-16 v1
- Checksum81465859D6E351F0
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MPFPVTTQGSQQTQPPQKHYG | ||||||
Compositional bias | 577-600 | Polar residues | ||||
Sequence: SVPQVNSSESSGGTSSESIPQTAT | ||||||
Compositional bias | 611-641 | Polar residues | ||||
Sequence: TVSRVVSSTRLVNPPPRSSGNAATSGNAATK | ||||||
Compositional bias | 652-672 | Basic and acidic residues | ||||
Sequence: TSSPHKEESPKKTKTEEEQLD | ||||||
Compositional bias | 673-690 | Polar residues | ||||
Sequence: TETSTTQSETIQTAASLL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL163051 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |