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Q9BQ50

- TREX2_HUMAN

UniProt

Q9BQ50 - TREX2_HUMAN

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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

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.

pH dependencei

Optimum pH is 7.5-8.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi57 – 571Magnesium 1 By similarity
Metal bindingi57 – 571Magnesium 2 By similarity
Metal bindingi59 – 591Magnesium 1 By similarity
Binding sitei165 – 1651Substrate By similarity
Active sitei231 – 2311Proton donor/acceptor By similarity
Metal bindingi236 – 2361Magnesium 1 By similarity
Binding sitei236 – 2361Substrate By 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
Complete GO annotation...

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 Inferred

GO - Cellular componenti

  1. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

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.2 Publications

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.

Miscellaneous databases

EvolutionaryTraceiQ9BQ50.

Family & Domainsi

Region

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

Sequence similaritiesi

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. VSP_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]
ENST00000402951; ENSP00000386078; ENSG00000183479. [Q9BQ50-1]
ENST00000594277; ENSP00000470833; ENSG00000269342. [Q9BQ50-1]
ENST00000595172; ENSP00000469920; ENSG00000269342. [Q9BQ50-1]
ENST00000595261; ENSP00000472690; ENSG00000269342. [Q9BQ50-1]
ENST00000596566; ENSP00000473145; ENSG00000269342. [Q9BQ50-2]
ENST00000596889; ENSP00000469756; ENSG00000269342. [Q9BQ50-2]
ENST00000597970; ENSP00000469016; ENSG00000269342. [Q9BQ50-2]
ENST00000600040; ENSP00000469764; ENSG00000269342. [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 ]
ENST00000402951 ; ENSP00000386078 ; ENSG00000183479 . [Q9BQ50-1 ]
ENST00000594277 ; ENSP00000470833 ; ENSG00000269342 . [Q9BQ50-1 ]
ENST00000595172 ; ENSP00000469920 ; ENSG00000269342 . [Q9BQ50-1 ]
ENST00000595261 ; ENSP00000472690 ; ENSG00000269342 . [Q9BQ50-1 ]
ENST00000596566 ; ENSP00000473145 ; ENSG00000269342 . [Q9BQ50-2 ]
ENST00000596889 ; ENSP00000469756 ; ENSG00000269342 . [Q9BQ50-2 ]
ENST00000597970 ; ENSP00000469016 ; ENSG00000269342 . [Q9BQ50-2 ]
ENST00000600040 ; ENSP00000469764 ; ENSG00000269342 . [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: July 9, 2014
This is version 105 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.

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

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