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Q9BQ50

- TREX2_HUMAN

UniProt

Q9BQ50 - TREX2_HUMAN

Protein

Three prime repair exonuclease 2

Gene

TREX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair.1 Publication

    Catalytic activityi

    Exonucleolytic cleavage in the 3'- to 5'-direction to yield nucleoside 5'-phosphates.

    Cofactori

    Binds 2 Mg2+ per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn2+ results in partial activity By similarity.By similarity

    pH dependencei

    Optimum pH is 7.5-8.0.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi57 – 571Magnesium 1By similarity
    Metal bindingi57 – 571Magnesium 2By similarity
    Metal bindingi59 – 591Magnesium 1By similarity
    Binding sitei165 – 1651SubstrateBy similarity
    Active sitei231 – 2311Proton donor/acceptorBy similarity
    Metal bindingi236 – 2361Magnesium 1By similarity
    Binding sitei236 – 2361SubstrateBy similarity

    GO - Molecular functioni

    1. 3'-5'-exodeoxyribonuclease activity Source: UniProtKB
    2. exodeoxyribonuclease III activity Source: UniProtKB-EC
    3. magnesium ion binding Source: UniProtKB
    4. nucleic acid binding Source: InterPro
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. DNA catabolic process, exonucleolytic Source: GOC
    2. DNA metabolic process Source: UniProtKB
    3. DNA repair Source: ProtInc

    Keywords - Molecular functioni

    Exonuclease, Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Three prime repair exonuclease 2 (EC:3.1.11.2)
    Alternative name(s):
    3'-5' exonuclease TREX2
    Gene namesi
    Name:TREX2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:12270. TREX2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi57 – 571D → A: Loss of enzyme activity; when associated with A-59. Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi59 – 591E → A: Loss of enzyme activity; when associated with A-57. Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi166 – 1661D → A: Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi206 – 2061R → A: Strongly reduces DNA-binding; when associated with A-208 and A-210. 1 Publication
    Mutagenesisi208 – 2081R → A: Strongly reduces DNA-binding; when associated with A-206 and A-210. 1 Publication
    Mutagenesisi210 – 2101R → A: Strongly reduces DNA-binding; when associated with A-208 and A-208. 1 Publication
    Mutagenesisi231 – 2311H → A: Loss of enzyme activity; when associated with A-236. Almost abolishes enzyme activity. 1 Publication
    Mutagenesisi236 – 2361D → A: Loss of enzyme activity; when associated with A-231. Almost abolishes enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA36950.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 279279Three prime repair exonuclease 2PRO_0000109870Add
    BLAST

    Proteomic databases

    PaxDbiQ9BQ50.
    PRIDEiQ9BQ50.

    PTM databases

    PhosphoSiteiQ9BQ50.

    Expressioni

    Tissue specificityi

    Detected in heart, breast, prostate, skeletal muscle, testis, uterus, bone marrow, colon, small intestine, stomach and thymus.1 Publication

    Gene expression databases

    ArrayExpressiQ9BQ50.
    BgeeiQ9BQ50.
    CleanExiHS_TREX2.
    GenevestigatoriQ9BQ50.

    Organism-specific databases

    HPAiHPA054060.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi116388. 3 interactions.
    MINTiMINT-1440359.
    STRINGi9606.ENSP00000333441.

    Structurei

    Secondary structure

    1
    279
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi51 – 6212
    Helixi64 – 663
    Beta strandi70 – 7910
    Helixi80 – 834
    Beta strandi101 – 1066
    Helixi115 – 1217
    Helixi125 – 1306
    Helixi138 – 14811
    Beta strandi153 – 1597
    Turni160 – 1656
    Helixi166 – 17611
    Beta strandi186 – 1894
    Helixi190 – 20011
    Helixi215 – 2239
    Helixi233 – 24614
    Helixi248 – 25811
    Helixi262 – 2643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y97X-ray2.50A/B44-279[»]
    ProteinModelPortaliQ9BQ50.
    SMRiQ9BQ50. Positions 46-271.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BQ50.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni59 – 602Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the exonuclease superfamily. TREX family.Curated

    Phylogenomic databases

    eggNOGiNOG293314.
    HOGENOMiHOG000118119.
    HOVERGENiHBG079278.
    InParanoidiQ9BQ50.
    KOiK10791.
    OMAiLARCRKA.
    PhylomeDBiQ9BQ50.
    TreeFamiTF323333.

    Family and domain databases

    Gene3Di3.30.420.10. 2 hits.
    InterProiIPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR012337. RNaseH-like_dom.
    [Graphical view]
    PfamiPF00929. RNase_T. 1 hit.
    [Graphical view]
    SMARTiSM00479. EXOIII. 1 hit.
    [Graphical view]
    SUPFAMiSSF53098. SSF53098. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BQ50-1) [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

    MGRAGSPLPR SSWPRMDDCG SRSRCSPTLC SSLRTCYPRG NITMSEAPRA    50
    ETFVFLDLEA TGLPSVEPEI AELSLFAVHR SSLENPEHDE SGALVLPRVL 100
    DKLTLCMCPE RPFTAKASEI TGLSSEGLAR CRKAGFDGAV VRTLQAFLSR 150
    QAGPICLVAH NGFDYDFPLL CAELRRLGAR LPRDTVCLDT LPALRGLDRA 200
    HSHGTRARGR QGYSLGSLFH RYFRAEPSAA HSAEGDVHTL LLIFLHRAAE 250
    LLAWADEQAR GWAHIEPMYL PPDDPSLEA 279
    Length:279
    Mass (Da):30,621
    Last modified:June 1, 2001 - v1
    Checksum:i91387E045960C1EA
    GO
    Isoform 2 (identifier: Q9BQ50-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.

    Show »
    Length:236
    Mass (Da):25,922
    Checksum:i3363BE40CFCC2300
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti180 – 1801R → C.1 Publication
    Corresponds to variant rs35132777 [ dbSNP | Ensembl ].
    VAR_025211

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343Missing in isoform 2. 1 PublicationVSP_010447Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151107 mRNA. Translation: AAD48776.1.
    AF319570 mRNA. Translation: AAK07617.1.
    AF319571 mRNA. Translation: AAK07618.1.
    AF319572 mRNA. Translation: AAK07619.1.
    AF319573 mRNA. Translation: AAK07620.1.
    DQ145722 Genomic DNA. Translation: AAZ38719.1.
    CCDSiCCDS35437.1. [Q9BQ50-2]
    RefSeqiNP_542432.2. NM_080701.3. [Q9BQ50-2]
    UniGeneiHs.644635.

    Genome annotation databases

    EnsembliENST00000330912; ENSP00000333441; ENSG00000183479. [Q9BQ50-2]
    ENST00000334497; ENSP00000334993; ENSG00000183479. [Q9BQ50-1]
    ENST00000338525; ENSP00000345218; ENSG00000183479. [Q9BQ50-2]
    ENST00000370231; ENSP00000359251; ENSG00000183479. [Q9BQ50-2]
    ENST00000370232; ENSP00000359252; ENSG00000183479. [Q9BQ50-1]
    ENST00000393862; ENSP00000377442; ENSG00000183479. [Q9BQ50-2]
    GeneIDi11219.
    KEGGihsa:11219.
    UCSCiuc010nud.2. human. [Q9BQ50-1]

    Polymorphism databases

    DMDMi47606206.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF151107 mRNA. Translation: AAD48776.1 .
    AF319570 mRNA. Translation: AAK07617.1 .
    AF319571 mRNA. Translation: AAK07618.1 .
    AF319572 mRNA. Translation: AAK07619.1 .
    AF319573 mRNA. Translation: AAK07620.1 .
    DQ145722 Genomic DNA. Translation: AAZ38719.1 .
    CCDSi CCDS35437.1. [Q9BQ50-2 ]
    RefSeqi NP_542432.2. NM_080701.3. [Q9BQ50-2 ]
    UniGenei Hs.644635.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1Y97 X-ray 2.50 A/B 44-279 [» ]
    ProteinModelPortali Q9BQ50.
    SMRi Q9BQ50. Positions 46-271.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116388. 3 interactions.
    MINTi MINT-1440359.
    STRINGi 9606.ENSP00000333441.

    PTM databases

    PhosphoSitei Q9BQ50.

    Polymorphism databases

    DMDMi 47606206.

    Proteomic databases

    PaxDbi Q9BQ50.
    PRIDEi Q9BQ50.

    Protocols and materials databases

    DNASUi 11219.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000330912 ; ENSP00000333441 ; ENSG00000183479 . [Q9BQ50-2 ]
    ENST00000334497 ; ENSP00000334993 ; ENSG00000183479 . [Q9BQ50-1 ]
    ENST00000338525 ; ENSP00000345218 ; ENSG00000183479 . [Q9BQ50-2 ]
    ENST00000370231 ; ENSP00000359251 ; ENSG00000183479 . [Q9BQ50-2 ]
    ENST00000370232 ; ENSP00000359252 ; ENSG00000183479 . [Q9BQ50-1 ]
    ENST00000393862 ; ENSP00000377442 ; ENSG00000183479 . [Q9BQ50-2 ]
    GeneIDi 11219.
    KEGGi hsa:11219.
    UCSCi uc010nud.2. human. [Q9BQ50-1 ]

    Organism-specific databases

    CTDi 11219.
    GeneCardsi GC0XM152710.
    H-InvDB HIX0017129.
    HGNCi HGNC:12270. TREX2.
    HPAi HPA054060.
    MIMi 300370. gene.
    neXtProti NX_Q9BQ50.
    PharmGKBi PA36950.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG293314.
    HOGENOMi HOG000118119.
    HOVERGENi HBG079278.
    InParanoidi Q9BQ50.
    KOi K10791.
    OMAi LARCRKA.
    PhylomeDBi Q9BQ50.
    TreeFami TF323333.

    Miscellaneous databases

    EvolutionaryTracei Q9BQ50.
    GeneWikii TREX2.
    GenomeRNAii 11219.
    NextBioi 42703.
    PROi Q9BQ50.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BQ50.
    Bgeei Q9BQ50.
    CleanExi HS_TREX2.
    Genevestigatori Q9BQ50.

    Family and domain databases

    Gene3Di 3.30.420.10. 2 hits.
    InterProi IPR006055. Exonuclease.
    IPR013520. Exonuclease_RNaseT/DNA_pol3.
    IPR012337. RNaseH-like_dom.
    [Graphical view ]
    Pfami PF00929. RNase_T. 1 hit.
    [Graphical view ]
    SMARTi SM00479. EXOIII. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53098. SSF53098. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases."
      Mazur D.J., Perrino F.W.
      J. Biol. Chem. 274:19655-19660(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
    2. NIEHS SNPs program
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-180.
    3. "Structure and expression of the TREX1 and TREX2 3'-->5' exonuclease genes."
      Mazur D.J., Perrino F.W.
      J. Biol. Chem. 276:14718-14727(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    4. "Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins."
      Mazur D.J., Perrino F.W.
      J. Biol. Chem. 276:17022-17029(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION, HOMODIMERIZATION.
    5. "The human TREX2 3' ->5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis."
      Perrino F.W., Harvey S., McMillin S., Hollis T.
      J. Biol. Chem. 280:15212-15218(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-279, SUBUNIT, MUTAGENESIS OF ASP-57; GLU-59; ASP-166; ARG-206; ARG-208; ARG-210; HIS-231 AND ASP-236.

    Entry informationi

    Entry nameiTREX2_HUMAN
    AccessioniPrimary (citable) accession number: Q9BQ50
    Secondary accession number(s): Q45F08, Q9UN77
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 24, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 106 of the entry and version 1 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

    Caution

    The gene for this protein is either identical to or adjacent to that of UCHL5IP. Most mRNAs that encode UCHL5IP also include the N-terminal part of TREX2.Curated

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome X
      Human chromosome X: 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