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Index > Protein center > ERI1(Gene name) > Human
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  • ERI1 (Gene name),
  • 3'-5' exoribonuclease 1 (Protein name ),  ERI1_HUMAN from NCBI database.
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  • General Annotation
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  • Antigen Annotation
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  • Predicted Eptitope
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  • Gene name:
    ERI1(3'EXO;THEX1);
    Protein name:
    3'-5' exoribonuclease 1;
    Alternative:
    Eri-1 homolog;3'-5' exonuclease ERI1;Histone mRNA 3'-exonuclease 1;Histone mRNA 3'-end-specific exoribonuclease;Protein 3'hExo(HEXO);
    Organism:
    Human (Homo sapiens). 
    General Annotation
    Sub Unit:
    Identified in a histone pre-mRNA complex, at least composed of ERI1, LSM11, SLBP, SNRPB, SYNCRIP and YBX1. Interacts in a cooperative manner with SLBP to the mature 3'-end of histone mRNAs (By similarity). Binds to 40S and 60S ribosomal subunits and to 80S assembled ribosomes. Found in a ternary complex with SLBP and the stem-loop structure of the 3'-end of histone mRNAs.
    Function:
    RNA exonuclease that binds to the 3'-end of histone mRNAs and degrades them, suggesting that it plays an essential role in histone mRNA decay after replication. A 2' and 3'-hydroxyl groups at the last nucleotide of the histone 3'-end is required for efficient degradation of RNA substrates. Also able to degrade the 3'-overhangs of short interfering RNAs (siRNAs) in vitro, suggesting a possible role as regulator of RNA interference (RNAi). Requires for binding the 5'-ACCCA-3' sequence present in stem-loop structure. Able to bind other mRNAs. Required for 5.8S rRNA 3'-end processing. Also binds to 5.8s ribosomal RNA. Binds with high affinity to the stem-loop structure of replication-dependent histone pre-mRNAs.
    Subcellular Location:
    Cytoplasm Nucleus Nucleus nucleolus
    Protein Attributes:
    Sequence length:
    349
    Sequence:
    50:
    MEDPQSKEPA | GEAVALALLE | SPRPEGGEEP | PRPSPEETQQ | CKFDGQETKG | 
    100:
    SKFITSSASD | FSDPVYKEIA | ITNGCINRMS | KEELRAKLSE | FKLETRGVKD | 
    150:
    VLKKRLKNYY | KKQKLMLKES | NFADSYYDYI | CIIDFEATCE | EGNPPEFVHE | 
    200:
    IIEFPVVLLN | THTLEIEDTF | QQYVRPEINT | QLSDFCISLT | GITQDQVDRA | 
    250:
    DTFPQVLKKV | IDWMKLKELG | TKYKYSLLTD | GSWDMSKFLN | IQCQLSRLKY | 
    300:
    PPFAKKWINI | RKSYGNFYKV | PRSQTKLTIM | LEKLGMDYDG | RPHCGLDDSK | 
    349:
    NIARIAVRML | QDGCELRINE | KMHAGQLMSV | SSSLPIEGTP | PPQMPHFRK
    3D Structure:
    N/A
    Predicted Eptitope:
    Please Sign in.
    EIAab Sequence  Vaild Sequence:
    Please Sign in.
    Related Databases
    SMR:
    UniGene:
    MIM:
    String:
    KEGG:
    Pfam:
    Uniprot:
     
    FOR
    ELISA Kit for Human 3'-5' exoribonuclease 1
    ELISA Kit for Human 3'-5' exoribonuclease 1
    ELISA Kit for Human 3'-5' exoribonuclease 1
    CLIA Kit for Human 3'-5' exoribonuclease 1
    CLIA Kit for Human 3'-5' exoribonuclease 1
    CLIA Kit for Human 3'-5' exoribonuclease 1
    Polyclonal Antibody for Human 3'-5' exoribonuclease 1
    Polyclonal Antibody for Human 3'-5' exoribonuclease 1
    Polyclonal Antibody for Human 3'-5' exoribonuclease 1
    Monoclonal Antibody for Human 3'-5' exoribonuclease 1
    Monoclonal Antibody for Human 3'-5' exoribonuclease 1
    Monoclonal Antibody for Human 3'-5' exoribonuclease 1
    Protein for Human 3'-5' exoribonuclease 1
    Protein for Human 3'-5' exoribonuclease 1
    Protein for Human 3'-5' exoribonuclease 1

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    Precision
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    Linearity
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    References
    1. 1.
      "A 3' exonuclease that specifically interacts with the 3' end of histone mRNA."
      Dominski Z. , Yang X.-C. , Kaygun H. , Dadlez M. , Marzluff W.F.
      Mol. Cell12:295-305(2003) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [MRNA];PROTEIN SEQUENCE OF 2-23; 43-48; 53-67; 161-172; 200-208; 225-237; 263-269 AND 284-291;FUNCTION;ENZYME REGULATION;ENZYME ACTIVITY;RNA-BINDING
    2. 2.
      "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. , more...
      Nat. Genet.36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA];VARIANT PRO-16
    3. 3.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
      tissue: Testis.
    4. 4.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]
    5. 5.
      "A conserved siRNA-degrading RNase negatively regulates RNA interference in C. elegans."
      Kennedy S. , Wang D. , Ruvkun G.
      Nature427:645-649(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: ENZYME ACTIVITY IN VITRO
    6. 6.
      "Characterization of 3'hExo, a 3' exonuclease specifically interacting with the 3' end of histone mRNA."
      Yang X.-C. , Purdy M. , Marzluff W.F. , Dominski Z.
      J. Biol. Chem.281:30447-30454(2006) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: FUNCTION;IDENTIFICATION IN A TERNARY COMPLEX;ENZYME ACTIVITY;SUBCELLULAR LOCATION;MUTAGENESIS OF LYS-92; ARG-96; LYS-99; LYS-104; ARG-105; THY-109; THY-110; LYS-111; LYS-112; ASP-234; MET-235 AND ASP-298;RNA-BINDING
    7. 7.
      "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]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
      tissue: Leukemic T-cell.
    8. 8.
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
    9. 9.
      "Crystallographic structure of the nuclease domain of 3'hExo, a DEDDh family member, bound to rAMP."
      Cheng Y. , Patel D.J.
      J. Mol. Biol.343:305-312(2004) [PubMed] [Europe PMC] [Abstract]
      [15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s) Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 123-322 IN COMPLEX WITH MAGNESIUM IONS AND AMP
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