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Q86US8

- EST1A_HUMAN

UniProt

Q86US8 - EST1A_HUMAN

Protein

Telomerase-binding protein EST1A

Gene

SMG6

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 123 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      Previous versions | rss
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    Functioni

    Component of the telomerase ribonucleoprotein (RNP) complex that is essential for the replication of chromosome termini. May have a general role in telomere regulation. Promotes in vitro the ability of TERT to elongate telomeres. Overexpression induces telomere uncapping, chromosomal end-to-end fusions (telomeric DNA persists at the fusion points) and did not perturb TRF2 telomeric localization. Binds to the single-stranded 5'-(GTGTGG)4GTGT-3' telomeric DNA, but not to a telomerase RNA template component (TER).
    Plays a role in nonsense-mediated mRNA decay. 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. Degrades single-stranded RNA (ssRNA), but not ssDNA or dsRNA.

    Cofactori

    Manganese.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1251 – 12511Manganese; catalyticCurated
    Metal bindingi1353 – 13531Manganese; catalyticCurated
    Metal bindingi1392 – 13921Manganese; catalyticCurated

    GO - Molecular functioni

    1. endoribonuclease activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB
    4. telomeric DNA binding Source: HGNC

    GO - Biological processi

    1. gene expression Source: Reactome
    2. mRNA export from nucleus Source: HGNC
    3. mRNA metabolic process Source: Reactome
    4. nuclear-transcribed mRNA catabolic process, nonsense-mediated decay Source: UniProtKB
    5. regulation of dephosphorylation Source: HGNC
    6. RNA metabolic process Source: Reactome
    7. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    8. telomere maintenance Source: HGNC

    Keywords - Molecular functioni

    Endonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    Nonsense-mediated mRNA decay

    Keywords - Ligandi

    DNA-binding, Manganese, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Telomerase-binding protein EST1A (EC:3.1.-.-)
    Alternative name(s):
    EST1-like protein A
    Ever shorter telomeres 1A
    Smg-6 homolog
    Telomerase subunit EST1A
    hSmg5/7a
    Gene namesi
    Name:SMG6
    Synonyms:C17orf31, EST1A, KIAA0732
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:17809. SMG6.

    Subcellular locationi

    Nucleusnucleolus. Chromosometelomere Curated. Cytoplasmcytosol
    Note: Particularly enriched in the nucleolus.

    GO - Cellular componenti

    1. chromosome, telomeric region Source: UniProtKB-SubCell
    2. cytoplasm Source: HGNC
    3. cytosol Source: UniProtKB
    4. nucleolus Source: HPA
    5. nucleus Source: HGNC
    6. telomerase holoenzyme complex Source: HGNC

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Nucleus, Telomere

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi46 – 527RPDLEIY → EPDLEIE: Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 140-E--E-146. 1 Publication
    Mutagenesisi140 – 1467KPDLQIY → EPDLQIE: Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 46-E--E-52. 1 Publication
    Mutagenesisi1251 – 12511D → A: Impaired nonsense-mediated RNA decay. 3 Publications
    Mutagenesisi1251 – 12511D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1392. 3 Publications
    Mutagenesisi1353 – 13531D → A: Abolishes RNase activity. 3 Publications
    Mutagenesisi1392 – 13921D → A: Impaired nonsense-mediated RNA decay; when associated with A-1251. 3 Publications
    Mutagenesisi1392 – 13921D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1251. 3 Publications

    Organism-specific databases

    PharmGKBiPA25584.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 14191419Telomerase-binding protein EST1APRO_0000087069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei332 – 3321PhosphoserineBy similarity
    Modified residuei479 – 4791Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86US8.
    PaxDbiQ86US8.
    PRIDEiQ86US8.

    PTM databases

    PhosphoSiteiQ86US8.

    Expressioni

    Tissue specificityi

    Ubiquitous.2 Publications

    Gene expression databases

    ArrayExpressiQ86US8.
    BgeeiQ86US8.
    CleanExiHS_SMG6.
    GenevestigatoriQ86US8.

    Organism-specific databases

    HPAiHPA042932.

    Interactioni

    Subunit structurei

    May form homooligomers. Component of the telomerase holoenzyme complex at least composed of TERT, DKC1, WRAP53/TCAB1, NOP10, NHP2, GAR1, TEP1, EST1A, POT1 and a telomerase RNA template component (TERC). Interacts with TERT, independently of the telomerase RNA. Interacts with SMG1, SMG5, SMG7, UPF1, UPF2, UPF3B and the PP2A catalytic subunits. 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.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    UPF1Q92900-22EBI-3232100,EBI-373492

    Protein-protein interaction databases

    BioGridi116888. 9 interactions.
    IntActiQ86US8. 5 interactions.
    STRINGi9606.ENSP00000263073.

    Structurei

    Secondary structure

    1
    1419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1240 – 125011
    Helixi1252 – 126817
    Beta strandi1270 – 12767
    Helixi1277 – 128711
    Helixi1298 – 131922
    Beta strandi1325 – 13284
    Beta strandi1334 – 13363
    Helixi1352 – 136110
    Helixi1368 – 13714
    Beta strandi1381 – 13899
    Helixi1393 – 14019
    Helixi1409 – 14168

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DOKX-ray1.80A/B1239-1419[»]
    2HWWX-ray1.80A/B/C1239-1419[»]
    2HWXX-ray1.90A1239-1419[»]
    ProteinModelPortaliQ86US8.
    SMRiQ86US8. Positions 616-823, 1239-1417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ86US8.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1246 – 1397152PINcAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni39 – 5921EJC-binding motif 1; mediates interaction with the EJCAdd
    BLAST
    Regioni114 – 503390Interaction with telomeric DNAAdd
    BLAST
    Regioni133 – 15321EJC-binding motif 2; mediates interaction with the EJCAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili163 – 19331Sequence AnalysisAdd
    BLAST
    Coiled coili567 – 62559Sequence AnalysisAdd
    BLAST
    Coiled coili1197 – 123943Sequence AnalysisAdd
    BLAST

    Domaini

    The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion.2 Publications

    Sequence similaritiesi

    Contains 1 PINc domain.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG313444.
    HOGENOMiHOG000112402.
    HOVERGENiHBG051511.
    InParanoidiQ86US8.
    KOiK11124.
    OMAiDAETMNK.
    OrthoDBiEOG70PBWS.
    PhylomeDBiQ86US8.
    TreeFamiTF327119.

    Family and domain databases

    Gene3Di1.25.40.10. 1 hit.
    3.40.50.1010. 2 hits.
    InterProiIPR018834. DNA/RNA-bd_Est1-type.
    IPR019458. EST1.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF10374. EST1. 1 hit.
    PF10373. EST1_DNA_bind. 1 hit.
    PF13638. PIN_4. 1 hit.
    [Graphical view]
    SMARTiSM00670. PINc. 1 hit.
    [Graphical view]
    SUPFAMiSSF88723. SSF88723. 2 hits.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86US8-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAEGLERVRI SASELRGILA TLAPQAGSRE NMKELKEARP RKDNRRPDLE     50
    IYKPGLSRLR NKPKIKEPPG SEEFKDEIVN DRDCSAVENG TQPVKDVCKE 100
    LNNQEQNGPI DPENNRGQES FPRTAGQEDR SLKIIKRTKK PDLQIYQPGR 150
    RLQTVSKESA SRVEEEEVLN QVEQLRVEED ECRGNVAKEE VANKPDRAEI 200
    EKSPGGGRVG AAKGEKGKRM GKGEGVRETH DDPARGRPGS AKRYSRSDKR 250
    RNRYRTRSTS SAGSNNSAEG AGLTDNGCRR RRQDRTKERP RLKKQVSVSS 300
    TDSLDEDRID EPDGLGPRRS SERKRHLERN WSGRGEGEQK NSAKEYRGTL 350
    RVTFDAEAMN KESPMVRSAR DDMDRGKPDK GLSSGGKGSE KQESKNPKQE 400
    LRGRGRGILI LPAHTTLSVN SAGSPESAPL GPRLLFGSGS KGSRSWGRGG 450
    TTRRLWDPNN PDQKPALKTQ TPQLHFLDTD DEVSPTSWGD SRQAQASYYK 500
    FQNSDNPYYY PRTPGPASQY PYTGYNPLQY PVGPTNGVYP GPYYPGYPTP 550
    SGQYVCSPLP TSTMSPEEVE QHMRNLQQQE LHRLLRVADN QELQLSNLLS 600
    RDRISPEGLE KMAQLRAELL QLYERCILLD IEFSDNQNVD QILWKNAFYQ 650
    VIEKFRQLVK DPNVENPEQI RNRLLELLDE GSDFFDSLLQ KLQVTYKFKL 700
    EDYMDGLAIR SKPLRKTVKY ALISAQRCMI CQGDIARYRE QASDTANYGK 750
    ARSWYLKAQH IAPKNGRPYN QLALLAVYTR RKLDAVYYYM RSLAASNPIL 800
    TAKESLMSLF EETKRKAEQM EKKQHEEFDL SPDQWRKGKK STFRHVGDDT 850
    TRLEIWIHPS HPRSSQGTES GKDSEQENGL GSLSPSDLNK RFILSFLHAH 900
    GKLFTRIGME TFPAVAEKVL KEFQVLLQHS PSPIGSTRML QLMTINMFAV 950
    HNSQLKDCFS EECRSVIQEQ AAALGLAMFS LLVRRCTCLL KESAKAQLSS 1000
    PEDQDDQDDI KVSSFVPDLK ELLPSVKVWS DWMLGYPDTW NPPPTSLDLP 1050
    SHVAVDVWST LADFCNILTA VNQSEVPLYK DPDDDLTLLI LEEDRLLSGF 1100
    VPLLAAPQDP CYVEKTSDKV IAADCKRVTV LKYFLEALCG QEEPLLAFKG 1150
    GKYVSVAPVP DTMGKEMGSQ EGTRLEDEEE DVVIEDFEED SEAEGSGGED 1200
    DIRELRAKKL ALARKIAEQQ RRQEKIQAVL EDHSQMRQME LEIRPLFLVP 1250
    DTNGFIDHLA SLARLLESRK YILVVPLIVI NELDGLAKGQ ETDHRAGGYA 1300
    RVVQEKARKS IEFLEQRFES RDSCLRALTS RGNELESIAF RSEDITGQLG 1350
    NNDDLILSCC LHYCKDKAKD FMPASKEEPI RLLREVVLLT DDRNLRVKAL 1400
    TRNVPVRDIP AFLTWAQVG 1419
    Length:1,419
    Mass (Da):160,462
    Last modified:March 7, 2006 - v2
    Checksum:i93FC7DDA68BD218C
    GO
    Isoform 2 (identifier: Q86US8-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1089: Missing.
         1090-1119: ILEEDRLLSGFVPLLAAPQDPCYVEKTSDK → MRFRLCHQRGCCPHERENTCTCKMIISSLQ

    Show »
    Length:330
    Mass (Da):37,465
    Checksum:i11E6E60AC32D4F88
    GO
    Isoform 3 (identifier: Q86US8-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-908: Missing.

    Show »
    Length:511
    Mass (Da):57,455
    Checksum:i15650F8E808B11F4
    GO

    Sequence cautioni

    The sequence AAH64916.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAA34452.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti291 – 2911R → P.1 Publication
    Corresponds to variant rs1885986 [ dbSNP | Ensembl ].
    VAR_018499
    Natural varianti294 – 2941K → Q.
    Corresponds to variant rs216195 [ dbSNP | Ensembl ].
    VAR_018500
    Natural varianti341 – 3411N → T.2 Publications
    Corresponds to variant rs1885987 [ dbSNP | Ensembl ].
    VAR_018501
    Natural varianti575 – 5751N → S.
    Corresponds to variant rs34047637 [ dbSNP | Ensembl ].
    VAR_050978
    Natural varianti972 – 9721A → T.
    Corresponds to variant rs903160 [ dbSNP | Ensembl ].
    VAR_018502
    Natural varianti984 – 9841R → C.
    Corresponds to variant rs35173108 [ dbSNP | Ensembl ].
    VAR_050979
    Natural varianti1189 – 11891E → K.
    Corresponds to variant rs58801957 [ dbSNP | Ensembl ].
    VAR_061648
    Natural varianti1233 – 12331H → R.
    Corresponds to variant rs2273980 [ dbSNP | Ensembl ].
    VAR_018503

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 10891089Missing in isoform 2. 1 PublicationVSP_010360Add
    BLAST
    Alternative sequencei1 – 908908Missing in isoform 3. 1 PublicationVSP_047157Add
    BLAST
    Alternative sequencei1090 – 111930ILEED…KTSDK → MRFRLCHQRGCCPHERENTC TCKMIISSLQ in isoform 2. 1 PublicationVSP_010361Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145883 mRNA. Translation: AAN46114.1.
    AB018275 mRNA. Translation: BAA34452.2. Different initiation.
    AL133597 mRNA. Translation: CAB63733.1.
    AY168921 mRNA. Translation: AAO17581.1.
    AK302964 mRNA. Translation: BAH13860.1.
    AC090617 Genomic DNA. No translation available.
    AL450226 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90559.1.
    BC064916 mRNA. Translation: AAH64916.1. Different initiation.
    CCDSiCCDS11016.1. [Q86US8-1]
    CCDS58498.1. [Q86US8-3]
    PIRiT43475.
    RefSeqiNP_001243756.1. NM_001256827.1. [Q86US8-3]
    NP_001243757.1. NM_001256828.1. [Q86US8-3]
    NP_001269255.1. NM_001282326.1. [Q86US8-2]
    NP_060045.4. NM_017575.4. [Q86US8-1]
    XP_005256626.1. XM_005256569.1.
    XP_005256628.1. XM_005256571.2. [Q86US8-3]
    UniGeneiHs.448342.

    Genome annotation databases

    EnsembliENST00000263073; ENSP00000263073; ENSG00000070366. [Q86US8-1]
    ENST00000354901; ENSP00000346977; ENSG00000070366. [Q86US8-3]
    ENST00000536871; ENSP00000440283; ENSG00000070366. [Q86US8-3]
    GeneIDi23293.
    KEGGihsa:23293.
    UCSCiuc002fub.1. human. [Q86US8-1]
    uc010vqv.1. human.
    uc031qxw.1. human. [Q86US8-2]

    Polymorphism databases

    DMDMi91771922.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY145883 mRNA. Translation: AAN46114.1 .
    AB018275 mRNA. Translation: BAA34452.2 . Different initiation.
    AL133597 mRNA. Translation: CAB63733.1 .
    AY168921 mRNA. Translation: AAO17581.1 .
    AK302964 mRNA. Translation: BAH13860.1 .
    AC090617 Genomic DNA. No translation available.
    AL450226 Genomic DNA. No translation available.
    CH471108 Genomic DNA. Translation: EAW90559.1 .
    BC064916 mRNA. Translation: AAH64916.1 . Different initiation.
    CCDSi CCDS11016.1. [Q86US8-1 ]
    CCDS58498.1. [Q86US8-3 ]
    PIRi T43475.
    RefSeqi NP_001243756.1. NM_001256827.1. [Q86US8-3 ]
    NP_001243757.1. NM_001256828.1. [Q86US8-3 ]
    NP_001269255.1. NM_001282326.1. [Q86US8-2 ]
    NP_060045.4. NM_017575.4. [Q86US8-1 ]
    XP_005256626.1. XM_005256569.1.
    XP_005256628.1. XM_005256571.2. [Q86US8-3 ]
    UniGenei Hs.448342.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DOK X-ray 1.80 A/B 1239-1419 [» ]
    2HWW X-ray 1.80 A/B/C 1239-1419 [» ]
    2HWX X-ray 1.90 A 1239-1419 [» ]
    ProteinModelPortali Q86US8.
    SMRi Q86US8. Positions 616-823, 1239-1417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116888. 9 interactions.
    IntActi Q86US8. 5 interactions.
    STRINGi 9606.ENSP00000263073.

    PTM databases

    PhosphoSitei Q86US8.

    Polymorphism databases

    DMDMi 91771922.

    Proteomic databases

    MaxQBi Q86US8.
    PaxDbi Q86US8.
    PRIDEi Q86US8.

    Protocols and materials databases

    DNASUi 23293.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263073 ; ENSP00000263073 ; ENSG00000070366 . [Q86US8-1 ]
    ENST00000354901 ; ENSP00000346977 ; ENSG00000070366 . [Q86US8-3 ]
    ENST00000536871 ; ENSP00000440283 ; ENSG00000070366 . [Q86US8-3 ]
    GeneIDi 23293.
    KEGGi hsa:23293.
    UCSCi uc002fub.1. human. [Q86US8-1 ]
    uc010vqv.1. human.
    uc031qxw.1. human. [Q86US8-2 ]

    Organism-specific databases

    CTDi 23293.
    GeneCardsi GC17M001963.
    H-InvDB HIX0013415.
    HGNCi HGNC:17809. SMG6.
    HPAi HPA042932.
    MIMi 610963. gene.
    neXtProti NX_Q86US8.
    PharmGKBi PA25584.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG313444.
    HOGENOMi HOG000112402.
    HOVERGENi HBG051511.
    InParanoidi Q86US8.
    KOi K11124.
    OMAi DAETMNK.
    OrthoDBi EOG70PBWS.
    PhylomeDBi Q86US8.
    TreeFami TF327119.

    Enzyme and pathway databases

    Reactomei REACT_75822. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).

    Miscellaneous databases

    ChiTaRSi SMG6. human.
    EvolutionaryTracei Q86US8.
    GeneWikii SMG6.
    GenomeRNAii 23293.
    NextBioi 45116.
    PROi Q86US8.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86US8.
    Bgeei Q86US8.
    CleanExi HS_SMG6.
    Genevestigatori Q86US8.

    Family and domain databases

    Gene3Di 1.25.40.10. 1 hit.
    3.40.50.1010. 2 hits.
    InterProi IPR018834. DNA/RNA-bd_Est1-type.
    IPR019458. EST1.
    IPR002716. PIN_dom.
    IPR029060. PIN_domain-like.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF10374. EST1. 1 hit.
    PF10373. EST1_DNA_bind. 1 hit.
    PF13638. PIN_4. 1 hit.
    [Graphical view ]
    SMARTi SM00670. PINc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF88723. SSF88723. 2 hits.
    ProtoNeti Search...

    Publicationsi

    1. "A human homolog of yeast est1 associates with telomerase and uncaps chromosome ends when overexpressed."
      Reichenbach P., Hoess M., Azzalin C.M., Nabholz M., Bucher P., Lingner J.
      Curr. Biol. 13:568-574(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-341, FUNCTION IN TELOMERE REGULATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE TELOMERASE RIBONUCLEOPROTEIN COMPLEX.
      Tissue: Cervix carcinoma.
    2. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
      Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS PRO-291 AND THR-341.
      Tissue: Brain.
    3. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
      Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
      DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SEQUENCE REVISION.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Testis.
    5. "Functional conservation of the telomerase protein Est1p in humans."
      Snow B.E., Erdmann N., Cruickshank J., Goldman H., Gill R.M., Robinson M.O., Harrington L.
      Curr. Biol. 13:698-704(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 32-1419 (ISOFORM 1), FUNCTION IN TELOMERE REGULATION, TISSUE SPECIFICITY, SINGLE-STRANDED TELOMERE DNA-BINDING, IDENTIFICATION IN THE TELOMERASE RIBONUCLEOPROTEIN COMPLEX, INTERACTION WITH TERT.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
      Tissue: Testis.
    7. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 888-1419 (ISOFORM 1).
      Tissue: Testis.
    10. "Characterization of human Smg5/7a: a protein with similarities to Caenorhabditis elegans SMG5 and SMG7 that functions in the dephosphorylation of Upf1."
      Chiu S.-Y., Serin G., Ohara O., Maquat L.E.
      RNA 9:77-87(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PP2A CATALYTIC SUBUNITS; SMG1; UPF1; UPF2 AND UPF3B.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "SMG6 is the catalytic endonuclease that cleaves mRNAs containing nonsense codons in metazoan."
      Huntzinger E., Kashima I., Fauser M., Sauliere J., Izaurralde E.
      RNA 14:2609-2617(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, CATALYTIC ACTIVITY, DOMAIN, MUTAGENESIS OF ASP-1251 AND ASP-1392.
    13. "SMG6 promotes endonucleolytic cleavage of nonsense mRNA in human cells."
      Eberle A.B., Lykke-Andersen S., Muhlemann O., Jensen T.H.
      Nat. Struct. Mol. Biol. 16:49-55(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, CATALYTIC ACTIVITY, DOMAIN, SUBCELLULAR LOCATION, INTERACTION WITH UPF1, MUTAGENESIS OF ASP-1251; ASP-1353 AND ASP-1392.
    14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-479, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    15. "A human telomerase holoenzyme protein required for Cajal body localization and telomere synthesis."
      Venteicher A.S., Abreu E.B., Meng Z., McCann K.E., Terns R.M., Veenstra T.D., Terns M.P., Artandi S.E.
      Science 323:644-648(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE TELOMERASE HOLOENZYME COMPLEX.
    16. "SMG6 interacts with the exon junction complex via two conserved EJC-binding motifs (EBMs) required for nonsense-mediated mRNA decay."
      Kashima I., Jonas S., Jayachandran U., Buchwald G., Conti E., Lupas A.N., Izaurralde E.
      Genes Dev. 24:2440-2450(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN NONSENSE-MEDIATED MRNA DECAY, HOMOOLIGOMERIZATION, INTERACTION WITH UPF1; UPF2; UPF3B; SMG5; SMG7 AND THE EXON JUNCTION COMPLEX, MUTAGENESIS OF 46-ARG--TYR-52 AND 140-LYS--TYR-146.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Structures of the PIN domains of SMG6 and SMG5 reveal a nuclease within the mRNA surveillance complex."
      Glavan F., Behm-Ansmant I., Izaurralde E., Conti E.
      EMBO J. 25:5117-5125(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1239-1419, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-1353.
    19. "Crystal structure of the PIN domain of human telomerase-associated protein EST1A."
      Takeshita D., Zenno S., Lee W.C., Saigo K., Tanokura M.
      Proteins 68:980-989(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1239-1419.

    Entry informationi

    Entry nameiEST1A_HUMAN
    AccessioniPrimary (citable) accession number: Q86US8
    Secondary accession number(s): B7Z874
    , O94837, Q86VH6, Q9UF60
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 123 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3