Q86US8 · EST1A_HUMAN
- ProteinTelomerase-binding protein EST1A
- GeneSMG6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1419 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
May have a general role in telomere regulation (PubMed:12676087, PubMed:12699629).
Promotes in vitro the ability of TERT to elongate telomeres (PubMed:12676087, PubMed:12699629).
Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization (PubMed:12676087, PubMed:12699629).
Binds to the single-stranded 5'-(GTGTGG)4GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER) (PubMed:12676087, PubMed:12699629).
Is thought to provide a link to the mRNA degradation machinery as it has endonuclease activity required to initiate NMD, and to serve as an adapter for UPF1 to protein phosphatase 2A (PP2A), thereby triggering UPF1 dephosphorylation (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030).
Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA (PubMed:17053788, PubMed:18974281, PubMed:19060897, PubMed:20930030).
Cofactor
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome, telomeric region | |
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | nucleolus | |
Cellular Component | nucleus | |
Cellular Component | telomerase holoenzyme complex | |
Molecular Function | DNA polymerase binding | |
Molecular Function | metal ion binding | |
Molecular Function | ribonucleoprotein complex binding | |
Molecular Function | RNA binding | |
Molecular Function | RNA endonuclease activity | |
Molecular Function | telomerase RNA binding | |
Molecular Function | telomeric DNA binding | |
Biological Process | mRNA export from nucleus | |
Biological Process | negative regulation of telomere capping | |
Biological Process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay | |
Biological Process | regulation of dephosphorylation | |
Biological Process | regulation of telomerase activity | |
Biological Process | regulation of telomere maintenance | |
Biological Process | regulation of telomere maintenance via telomerase |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameTelomerase-binding protein EST1A
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ86US8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 46-52 | Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 140-E--E-146. | ||||
Sequence: RPDLEIY → EPDLEIE | ||||||
Mutagenesis | 140-146 | Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 46-E--E-52. | ||||
Sequence: KPDLQIY → EPDLQIE | ||||||
Natural variant | VAR_018499 | 291 | in dbSNP:rs1885986 | |||
Sequence: R → P | ||||||
Natural variant | VAR_018500 | 294 | in dbSNP:rs216195 | |||
Sequence: K → Q | ||||||
Natural variant | VAR_018501 | 341 | in dbSNP:rs1885987 | |||
Sequence: N → T | ||||||
Natural variant | VAR_050978 | 575 | in dbSNP:rs34047637 | |||
Sequence: N → S | ||||||
Natural variant | VAR_018502 | 972 | in dbSNP:rs903160 | |||
Sequence: A → T | ||||||
Natural variant | VAR_050979 | 984 | in dbSNP:rs35173108 | |||
Sequence: R → C | ||||||
Natural variant | VAR_061648 | 1189 | in dbSNP:rs58801957 | |||
Sequence: E → K | ||||||
Natural variant | VAR_018503 | 1233 | in dbSNP:rs2273980 | |||
Sequence: H → R | ||||||
Mutagenesis | 1251 | Impaired nonsense-mediated RNA decay. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1251 | Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1392. | ||||
Sequence: D → N | ||||||
Mutagenesis | 1353 | Abolishes RNase activity. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1392 | Impaired nonsense-mediated RNA decay; when associated with A-1251. | ||||
Sequence: D → A | ||||||
Mutagenesis | 1392 | Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1251. | ||||
Sequence: D → N |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,616 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000087069 | 1-1419 | UniProt | Telomerase-binding protein EST1A | |||
Sequence: MAEGLERVRISASELRGILATLAPQAGSRENMKELKEARPRKDNRRPDLEIYKPGLSRLRNKPKIKEPPGSEEFKDEIVNDRDCSAVENGTQPVKDVCKELNNQEQNGPIDPENNRGQESFPRTAGQEDRSLKIIKRTKKPDLQIYQPGRRLQTVSKESASRVEEEEVLNQVEQLRVEEDECRGNVAKEEVANKPDRAEIEKSPGGGRVGAAKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYSRSDKRRNRYRTRSTSSAGSNNSAEGAGLTDNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKEYRGTLRVTFDAEAMNKESPMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELRGRGRGILILPAHTTLSVNSAGSPESAPLGPRLLFGSGSKGSRSWGRGGTTRRLWDPNNPDQKPALKTQTPQLHFLDTDDEVSPTSWGDSRQAQASYYKFQNSDNPYYYPRTPGPASQYPYTGYNPLQYPVGPTNGVYPGPYYPGYPTPSGQYVCSPLPTSTMSPEEVEQHMRNLQQQELHRLLRVADNQELQLSNLLSRDRISPEGLEKMAQLRAELLQLYERCILLDIEFSDNQNVDQILWKNAFYQVIEKFRQLVKDPNVENPEQIRNRLLELLDEGSDFFDSLLQKLQVTYKFKLEDYMDGLAIRSKPLRKTVKYALISAQRCMICQGDIARYREQASDTANYGKARSWYLKAQHIAPKNGRPYNQLALLAVYTRRKLDAVYYYMRSLAASNPILTAKESLMSLFEETKRKAEQMEKKQHEEFDLSPDQWRKGKKSTFRHVGDDTTRLEIWIHPSHPRSSQGTESGKDSEQENGLGSLSPSDLNKRFILSFLHAHGKLFTRIGMETFPAVAEKVLKEFQVLLQHSPSPIGSTRMLQLMTINMFAVHNSQLKDCFSEECRSVIQEQAAALGLAMFSLLVRRCTCLLKESAKAQLSSPEDQDDQDDIKVSSFVPDLKELLPSVKVWSDWMLGYPDTWNPPPTSLDLPSHVAVDVWSTLADFCNILTAVNQSEVPLYKDPDDDLTLLILEEDRLLSGFVPLLAAPQDPCYVEKTSDKVIAADCKRVTVLKYFLEALCGQEEPLLAFKGGKYVSVAPVPDTMGKEMGSQEGTRLEDEEEDVVIEDFEEDSEAEGSGGEDDIRELRAKKLALARKIAEQQRRQEKIQAVLEDHSQMRQMELEIRPLFLVPDTNGFIDHLASLARLLESRKYILVVPLIVINELDGLAKGQETDHRAGGYARVVQEKARKSIEFLEQRFESRDSCLRALTSRGNELESIAFRSEDITGQLGNNDDLILSCCLHYCKDKAKDFMPASKEEPIRLLREVVLLTDDRNLRVKALTRNVPVRDIPAFLTWAQVG | |||||||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 146 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 203 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 203 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 267 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 332 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 332 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 406 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 424 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 433 | UniProt | Omega-N-methylarginine | ||||
Sequence: R | |||||||
Modified residue | 471 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 479 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 479 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 484 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 484 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 486 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 508 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 831 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 831 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 868 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 870 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 870 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 874 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 874 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 884 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1000 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
Associated component of the telomerase holoenzyme complex (PubMed:19179534).
Interacts with TERT, independently of the telomerase RNA (PubMed:12676087, PubMed:12699629).
Interacts with SMG1, SMG5, SMG7, UPF1, UPF2, UPF3B and the PP2A catalytic subunits (PubMed:12554878, PubMed:19060897, PubMed:20930030).
Also interacts with the exon junction complex (EJC) composed at least of CASC3, EIF4A3, MAGOH and RBM8A; required for the process of nonsense-mediated mRNA decay (PubMed:20930030).
Interacts with DHX34; the interaction is RNA-independent (PubMed:25220460).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q86US8 | CASP6 P55212 | 3 | EBI-3232100, EBI-718729 | |
BINARY | Q86US8 | HIP1 O00291 | 3 | EBI-3232100, EBI-473886 | |
BINARY | Q86US8 | LAMP2 P13473-2 | 3 | EBI-3232100, EBI-21591415 | |
BINARY | Q86US8 | MEOX2 Q6FHY5 | 3 | EBI-3232100, EBI-16439278 | |
BINARY | Q86US8 | PRPF40A O75400-2 | 3 | EBI-3232100, EBI-5280197 | |
BINARY | Q86US8 | RAN P62826 | 3 | EBI-3232100, EBI-286642 | |
BINARY | Q86US8 | UPF1 Q92900-2 | 2 | EBI-3232100, EBI-373492 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-79 | Disordered | ||||
Sequence: QAGSRENMKELKEARPRKDNRRPDLEIYKPGLSRLRNKPKIKEPPGSEEFKDEIV | ||||||
Compositional bias | 30-79 | Basic and acidic residues | ||||
Sequence: ENMKELKEARPRKDNRRPDLEIYKPGLSRLRNKPKIKEPPGSEEFKDEIV | ||||||
Region | 39-59 | EJC-binding motif 1; mediates interaction with the EJC | ||||
Sequence: RPRKDNRRPDLEIYKPGLSRL | ||||||
Compositional bias | 99-125 | Polar residues | ||||
Sequence: KELNNQEQNGPIDPENNRGQESFPRTA | ||||||
Region | 99-165 | Disordered | ||||
Sequence: KELNNQEQNGPIDPENNRGQESFPRTAGQEDRSLKIIKRTKKPDLQIYQPGRRLQTVSKESASRVEE | ||||||
Region | 114-503 | Interaction with telomeric DNA | ||||
Sequence: NNRGQESFPRTAGQEDRSLKIIKRTKKPDLQIYQPGRRLQTVSKESASRVEEEEVLNQVEQLRVEEDECRGNVAKEEVANKPDRAEIEKSPGGGRVGAAKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYSRSDKRRNRYRTRSTSSAGSNNSAEGAGLTDNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKEYRGTLRVTFDAEAMNKESPMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELRGRGRGILILPAHTTLSVNSAGSPESAPLGPRLLFGSGSKGSRSWGRGGTTRRLWDPNNPDQKPALKTQTPQLHFLDTDDEVSPTSWGDSRQAQASYYKFQN | ||||||
Compositional bias | 129-144 | Basic and acidic residues | ||||
Sequence: DRSLKIIKRTKKPDLQ | ||||||
Region | 133-153 | EJC-binding motif 2; mediates interaction with the EJC | ||||
Sequence: KIIKRTKKPDLQIYQPGRRLQ | ||||||
Coiled coil | 163-193 | |||||
Sequence: VEEEEVLNQVEQLRVEEDECRGNVAKEEVAN | ||||||
Compositional bias | 177-203 | Basic and acidic residues | ||||
Sequence: VEEDECRGNVAKEEVANKPDRAEIEKS | ||||||
Region | 177-405 | Disordered | ||||
Sequence: VEEDECRGNVAKEEVANKPDRAEIEKSPGGGRVGAAKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYSRSDKRRNRYRTRSTSSAGSNNSAEGAGLTDNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKEYRGTLRVTFDAEAMNKESPMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELRGRG | ||||||
Compositional bias | 212-245 | Basic and acidic residues | ||||
Sequence: AKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYS | ||||||
Compositional bias | 257-272 | Polar residues | ||||
Sequence: RSTSSAGSNNSAEGAG | ||||||
Compositional bias | 275-345 | Basic and acidic residues | ||||
Sequence: DNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKE | ||||||
Compositional bias | 364-402 | Basic and acidic residues | ||||
Sequence: PMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELR | ||||||
Region | 419-472 | Disordered | ||||
Sequence: VNSAGSPESAPLGPRLLFGSGSKGSRSWGRGGTTRRLWDPNNPDQKPALKTQTP | ||||||
Coiled coil | 567-625 | |||||
Sequence: EEVEQHMRNLQQQELHRLLRVADNQELQLSNLLSRDRISPEGLEKMAQLRAELLQLYER | ||||||
Region | 854-883 | Disordered | ||||
Sequence: EIWIHPSHPRSSQGTESGKDSEQENGLGSL | ||||||
Compositional bias | 861-883 | Polar residues | ||||
Sequence: HPRSSQGTESGKDSEQENGLGSL | ||||||
Coiled coil | 1197-1239 | |||||
Sequence: GGEDDIRELRAKKLALARKIAEQQRRQEKIQAVLEDHSQMRQM | ||||||
Domain | 1246-1397 | PINc | ||||
Sequence: LFLVPDTNGFIDHLASLARLLESRKYILVVPLIVINELDGLAKGQETDHRAGGYARVVQEKARKSIEFLEQRFESRDSCLRALTSRGNELESIAFRSEDITGQLGNNDDLILSCCLHYCKDKAKDFMPASKEEPIRLLREVVLLTDDRNLRV |
Domain
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q86US8-1
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
- Length1,419
- Mass (Da)160,462
- Last updated2006-03-07 v2
- Checksum93FC7DDA68BD218C
Q86US8-2
- Name2
- Differences from canonical
- 1-1089: Missing
- 1090-1119: ILEEDRLLSGFVPLLAAPQDPCYVEKTSDK → MRFRLCHQRGCCPHERENTCTCKMIISSLQ
Q86US8-3
- Name3
- Differences from canonical
- 1-908: Missing
Computationally mapped potential isoform sequences
There are 9 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_047157 | 1-908 | in isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_010360 | 1-1089 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 30-79 | Basic and acidic residues | ||||
Sequence: ENMKELKEARPRKDNRRPDLEIYKPGLSRLRNKPKIKEPPGSEEFKDEIV | ||||||
Compositional bias | 99-125 | Polar residues | ||||
Sequence: KELNNQEQNGPIDPENNRGQESFPRTA | ||||||
Compositional bias | 129-144 | Basic and acidic residues | ||||
Sequence: DRSLKIIKRTKKPDLQ | ||||||
Compositional bias | 177-203 | Basic and acidic residues | ||||
Sequence: VEEDECRGNVAKEEVANKPDRAEIEKS | ||||||
Compositional bias | 212-245 | Basic and acidic residues | ||||
Sequence: AKGEKGKRMGKGEGVRETHDDPARGRPGSAKRYS | ||||||
Compositional bias | 257-272 | Polar residues | ||||
Sequence: RSTSSAGSNNSAEGAG | ||||||
Compositional bias | 275-345 | Basic and acidic residues | ||||
Sequence: DNGCRRRRQDRTKERPRLKKQVSVSSTDSLDEDRIDEPDGLGPRRSSERKRHLERNWSGRGEGEQKNSAKE | ||||||
Compositional bias | 364-402 | Basic and acidic residues | ||||
Sequence: PMVRSARDDMDRGKPDKGLSSGGKGSEKQESKNPKQELR | ||||||
Compositional bias | 861-883 | Polar residues | ||||
Sequence: HPRSSQGTESGKDSEQENGLGSL | ||||||
Alternative sequence | VSP_010361 | 1090-1119 | in isoform 2 | |||
Sequence: ILEEDRLLSGFVPLLAAPQDPCYVEKTSDK → MRFRLCHQRGCCPHERENTCTCKMIISSLQ |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY145883 EMBL· GenBank· DDBJ | AAN46114.1 EMBL· GenBank· DDBJ | mRNA | ||
AB018275 EMBL· GenBank· DDBJ | BAA34452.2 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL133597 EMBL· GenBank· DDBJ | CAB63733.1 EMBL· GenBank· DDBJ | mRNA | ||
AY168921 EMBL· GenBank· DDBJ | AAO17581.1 EMBL· GenBank· DDBJ | mRNA | ||
AK302964 EMBL· GenBank· DDBJ | BAH13860.1 EMBL· GenBank· DDBJ | mRNA | ||
AC090617 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL450226 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471108 EMBL· GenBank· DDBJ | EAW90559.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC064916 EMBL· GenBank· DDBJ | AAH64916.1 EMBL· GenBank· DDBJ | mRNA | Different initiation |