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Q86US8 (EST1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:SMG6
Synonyms:C17orf31, EST1A, KIAA0732
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.5 Ref.12 Ref.13 Ref.16 Ref.18

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. Ref.1 Ref.5 Ref.12 Ref.13 Ref.16 Ref.18

Cofactor

Manganese. Ref.18

Subunit structure

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. Ref.1 Ref.5 Ref.10 Ref.13 Ref.15 Ref.16

Subcellular location

Nucleusnucleolus. Chromosometelomere Probable. Cytoplasmcytosol. Note: Particularly enriched in the nucleolus. Ref.1 Ref.13

Tissue specificity

Ubiquitous. Ref.1 Ref.5

Domain

The PINc domain confers endonuclease activity and is expected to bind the catalytic metal ion. Ref.12 Ref.13

Sequence similarities

Contains 1 PINc domain.

Sequence caution

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.

Ontologies

Keywords
   Biological processNonsense-mediated mRNA decay
   Cellular componentChromosome
Cytoplasm
Nucleus
Telomere
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
   LigandDNA-binding
Manganese
Metal-binding
   Molecular functionEndonuclease
Hydrolase
Nuclease
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA metabolic process

Traceable author statement. Source: Reactome

RNA phosphodiester bond hydrolysis, endonucleolytic

Inferred from direct assay Ref.13. Source: GOC

gene expression

Traceable author statement. Source: Reactome

mRNA export from nucleus

Traceable author statement PubMed 16488880. Source: HGNC

mRNA metabolic process

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Inferred from mutant phenotype Ref.12Ref.13Ref.16. Source: UniProtKB

regulation of dephosphorylation

Traceable author statement PubMed 15721257. Source: HGNC

telomere maintenance

Inferred from mutant phenotype Ref.5. Source: HGNC

   Cellular_componentchromosome, telomeric region

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay PubMed 14636577. Source: HGNC

cytosol

Inferred from direct assay Ref.13. Source: UniProtKB

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 14636577. Source: HGNC

telomerase holoenzyme complex

Traceable author statement Ref.5. Source: HGNC

   Molecular_functionendoribonuclease activity

Inferred from direct assay Ref.13. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

telomeric DNA binding

Inferred from direct assay Ref.5. Source: HGNC

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

UPF1Q92900-22EBI-3232100,EBI-373492

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: 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.
Isoform 2 (identifier: Q86US8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1089: Missing.
     1090-1119: ILEEDRLLSGFVPLLAAPQDPCYVEKTSDK → MRFRLCHQRGCCPHERENTCTCKMIISSLQ
Isoform 3 (identifier: Q86US8-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 14191419Telomerase-binding protein EST1A
PRO_0000087069

Regions

Domain1246 – 1397152PINc
Region39 – 5921EJC-binding motif 1; mediates interaction with the EJC
Region114 – 503390Interaction with telomeric DNA
Region133 – 15321EJC-binding motif 2; mediates interaction with the EJC
Coiled coil163 – 19331 Potential
Coiled coil567 – 62559 Potential
Coiled coil1197 – 123943 Potential

Sites

Metal binding12511Manganese; catalytic Probable
Metal binding13531Manganese; catalytic Probable
Metal binding13921Manganese; catalytic Probable

Amino acid modifications

Modified residue3321Phosphoserine By similarity
Modified residue4791Phosphothreonine Ref.14

Natural variations

Alternative sequence1 – 10891089Missing in isoform 2.
VSP_010360
Alternative sequence1 – 908908Missing in isoform 3.
VSP_047157
Alternative sequence1090 – 111930ILEED…KTSDK → MRFRLCHQRGCCPHERENTC TCKMIISSLQ in isoform 2.
VSP_010361
Natural variant2911R → P. Ref.2
Corresponds to variant rs1885986 [ dbSNP | Ensembl ].
VAR_018499
Natural variant2941K → Q.
Corresponds to variant rs216195 [ dbSNP | Ensembl ].
VAR_018500
Natural variant3411N → T. Ref.1 Ref.2
Corresponds to variant rs1885987 [ dbSNP | Ensembl ].
VAR_018501
Natural variant5751N → S.
Corresponds to variant rs34047637 [ dbSNP | Ensembl ].
VAR_050978
Natural variant9721A → T.
Corresponds to variant rs903160 [ dbSNP | Ensembl ].
VAR_018502
Natural variant9841R → C.
Corresponds to variant rs35173108 [ dbSNP | Ensembl ].
VAR_050979
Natural variant11891E → K.
Corresponds to variant rs58801957 [ dbSNP | Ensembl ].
VAR_061648
Natural variant12331H → R.
Corresponds to variant rs2273980 [ dbSNP | Ensembl ].
VAR_018503

Experimental info

Mutagenesis46 – 527RPDLEIY → EPDLEIE: Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 140-E--E-146. Ref.16
Mutagenesis140 – 1467KPDLQIY → EPDLQIE: Alters interaction with the EJC. Loss of interaction with the EJC; when associated with 46-E--E-52. Ref.16
Mutagenesis12511D → A: Impaired nonsense-mediated RNA decay. Ref.12 Ref.13
Mutagenesis12511D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1392. Ref.12 Ref.13
Mutagenesis13531D → A: Abolishes RNase activity. Ref.13 Ref.18
Mutagenesis13921D → A: Impaired nonsense-mediated RNA decay; when associated with A-1251. Ref.12 Ref.13
Mutagenesis13921D → N: Loss of endonuclease activity and nonsense-mediated RNA decay; when associated with N-1251. Ref.12 Ref.13

Secondary structure

........................ 1419
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 7, 2006. Version 2.
Checksum: 93FC7DDA68BD218C

FASTA1,419160,462
        10         20         30         40         50         60 
MAEGLERVRI SASELRGILA TLAPQAGSRE NMKELKEARP RKDNRRPDLE IYKPGLSRLR 

        70         80         90        100        110        120 
NKPKIKEPPG SEEFKDEIVN DRDCSAVENG TQPVKDVCKE LNNQEQNGPI DPENNRGQES 

       130        140        150        160        170        180 
FPRTAGQEDR SLKIIKRTKK PDLQIYQPGR RLQTVSKESA SRVEEEEVLN QVEQLRVEED 

       190        200        210        220        230        240 
ECRGNVAKEE VANKPDRAEI EKSPGGGRVG AAKGEKGKRM GKGEGVRETH DDPARGRPGS 

       250        260        270        280        290        300 
AKRYSRSDKR RNRYRTRSTS SAGSNNSAEG AGLTDNGCRR RRQDRTKERP RLKKQVSVSS 

       310        320        330        340        350        360 
TDSLDEDRID EPDGLGPRRS SERKRHLERN WSGRGEGEQK NSAKEYRGTL RVTFDAEAMN 

       370        380        390        400        410        420 
KESPMVRSAR DDMDRGKPDK GLSSGGKGSE KQESKNPKQE LRGRGRGILI LPAHTTLSVN 

       430        440        450        460        470        480 
SAGSPESAPL GPRLLFGSGS KGSRSWGRGG TTRRLWDPNN PDQKPALKTQ TPQLHFLDTD 

       490        500        510        520        530        540 
DEVSPTSWGD SRQAQASYYK FQNSDNPYYY PRTPGPASQY PYTGYNPLQY PVGPTNGVYP 

       550        560        570        580        590        600 
GPYYPGYPTP SGQYVCSPLP TSTMSPEEVE QHMRNLQQQE LHRLLRVADN QELQLSNLLS 

       610        620        630        640        650        660 
RDRISPEGLE KMAQLRAELL QLYERCILLD IEFSDNQNVD QILWKNAFYQ VIEKFRQLVK 

       670        680        690        700        710        720 
DPNVENPEQI RNRLLELLDE GSDFFDSLLQ KLQVTYKFKL EDYMDGLAIR SKPLRKTVKY 

       730        740        750        760        770        780 
ALISAQRCMI CQGDIARYRE QASDTANYGK ARSWYLKAQH IAPKNGRPYN QLALLAVYTR 

       790        800        810        820        830        840 
RKLDAVYYYM RSLAASNPIL TAKESLMSLF EETKRKAEQM EKKQHEEFDL SPDQWRKGKK 

       850        860        870        880        890        900 
STFRHVGDDT TRLEIWIHPS HPRSSQGTES GKDSEQENGL GSLSPSDLNK RFILSFLHAH 

       910        920        930        940        950        960 
GKLFTRIGME TFPAVAEKVL KEFQVLLQHS PSPIGSTRML QLMTINMFAV HNSQLKDCFS 

       970        980        990       1000       1010       1020 
EECRSVIQEQ AAALGLAMFS LLVRRCTCLL KESAKAQLSS PEDQDDQDDI KVSSFVPDLK 

      1030       1040       1050       1060       1070       1080 
ELLPSVKVWS DWMLGYPDTW NPPPTSLDLP SHVAVDVWST LADFCNILTA VNQSEVPLYK 

      1090       1100       1110       1120       1130       1140 
DPDDDLTLLI LEEDRLLSGF VPLLAAPQDP CYVEKTSDKV IAADCKRVTV LKYFLEALCG 

      1150       1160       1170       1180       1190       1200 
QEEPLLAFKG GKYVSVAPVP DTMGKEMGSQ EGTRLEDEEE DVVIEDFEED SEAEGSGGED 

      1210       1220       1230       1240       1250       1260 
DIRELRAKKL ALARKIAEQQ RRQEKIQAVL EDHSQMRQME LEIRPLFLVP DTNGFIDHLA 

      1270       1280       1290       1300       1310       1320 
SLARLLESRK YILVVPLIVI NELDGLAKGQ ETDHRAGGYA RVVQEKARKS IEFLEQRFES 

      1330       1340       1350       1360       1370       1380 
RDSCLRALTS RGNELESIAF RSEDITGQLG NNDDLILSCC LHYCKDKAKD FMPASKEEPI 

      1390       1400       1410 
RLLREVVLLT DDRNLRVKAL TRNVPVRDIP AFLTWAQVG 

« Hide

Isoform 2 [UniParc].

Checksum: 11E6E60AC32D4F88
Show »

FASTA33037,465
Isoform 3 [UniParc].

Checksum: 15650F8E808B11F4
Show »

FASTA51157,455

References

« Hide 'large scale' references
[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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT43475.
RefSeqNP_001243756.1. NM_001256827.1.
NP_001243757.1. NM_001256828.1.
NP_001269255.1. NM_001282326.1.
NP_060045.4. NM_017575.4.
XP_005256626.1. XM_005256569.1.
XP_005256628.1. XM_005256571.2.
UniGeneHs.448342.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DOKX-ray1.80A/B1239-1419[»]
2HWWX-ray1.80A/B/C1239-1419[»]
2HWXX-ray1.90A1239-1419[»]
ProteinModelPortalQ86US8.
SMRQ86US8. Positions 616-823, 1239-1417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116888. 9 interactions.
IntActQ86US8. 5 interactions.
STRING9606.ENSP00000263073.

PTM databases

PhosphoSiteQ86US8.

Polymorphism databases

DMDM91771922.

Proteomic databases

PaxDbQ86US8.
PRIDEQ86US8.

Protocols and materials databases

DNASU23293.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263073; ENSP00000263073; ENSG00000070366. [Q86US8-1]
ENST00000354901; ENSP00000346977; ENSG00000070366. [Q86US8-3]
ENST00000536871; ENSP00000440283; ENSG00000070366. [Q86US8-3]
ENST00000544865; ENSP00000443920; ENSG00000070366.
GeneID23293.
KEGGhsa:23293.
UCSCuc002fub.1. human. [Q86US8-1]
uc010vqv.1. human.
uc031qxw.1. human. [Q86US8-2]

Organism-specific databases

CTD23293.
GeneCardsGC17M001963.
H-InvDBHIX0013415.
HGNCHGNC:17809. SMG6.
HPAHPA042932.
MIM610963. gene.
neXtProtNX_Q86US8.
PharmGKBPA25584.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG313444.
HOGENOMHOG000112402.
HOVERGENHBG051511.
InParanoidQ86US8.
KOK11124.
OMADAETMNK.
OrthoDBEOG70PBWS.
PhylomeDBQ86US8.
TreeFamTF327119.

Enzyme and pathway databases

ReactomeREACT_21257. Metabolism of RNA.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ86US8.
BgeeQ86US8.
CleanExHS_SMG6.
GenevestigatorQ86US8.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR018834. DNA/RNA-bd_Est1-type.
IPR019458. EST1.
IPR002716. PIN_dom.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF10374. EST1. 1 hit.
PF10373. EST1_DNA_bind. 1 hit.
PF13638. PIN_4. 1 hit.
[Graphical view]
SMARTSM00670. PINc. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSMG6. human.
EvolutionaryTraceQ86US8.
GeneWikiSMG6.
GenomeRNAi23293.
NextBio45116.
PROQ86US8.
SOURCESearch...

Entry information

Entry nameEST1A_HUMAN
AccessionPrimary (citable) accession number: Q86US8
Secondary accession number(s): B7Z874 expand/collapse secondary AC list , O94837, Q86VH6, Q9UF60
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 7, 2006
Last modified: April 16, 2014
This is version 118 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM