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Q9BQ50 (TREX2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Three prime repair exonuclease 2

EC=3.1.11.2
Alternative name(s):
3'-5' exonuclease TREX2
Gene names
Name:TREX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Exonuclease with a preference for double-stranded DNA with mismatched 3' termini. May play a role in DNA repair. Ref.4

Catalytic activity

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

Cofactor

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

Subunit structure

Homodimer. Ref.4 Ref.5

Subcellular location

Nucleus Probable.

Tissue specificity

Detected in heart, breast, prostate, skeletal muscle, testis, uterus, bone marrow, colon, small intestine, stomach and thymus. Ref.3

Sequence similarities

Belongs to the exonuclease superfamily. TREX family.

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.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.5-8.0.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BQ50-1)

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: Q9BQ50-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 279279Three prime repair exonuclease 2
PRO_0000109870

Regions

Region59 – 602Substrate binding By similarity

Sites

Active site2311Proton donor/acceptor By similarity
Metal binding571Magnesium 1 By similarity
Metal binding571Magnesium 2 By similarity
Metal binding591Magnesium 1 By similarity
Metal binding2361Magnesium 1 By similarity
Binding site1651Substrate By similarity
Binding site2361Substrate By similarity

Natural variations

Alternative sequence1 – 4343Missing in isoform 2.
VSP_010447
Natural variant1801R → C. Ref.2
Corresponds to variant rs35132777 [ dbSNP | Ensembl ].
VAR_025211

Experimental info

Mutagenesis571D → A: Loss of enzyme activity; when associated with A-59. Almost abolishes enzyme activity. Ref.5
Mutagenesis591E → A: Loss of enzyme activity; when associated with A-57. Almost abolishes enzyme activity. Ref.5
Mutagenesis1661D → A: Almost abolishes enzyme activity. Ref.5
Mutagenesis2061R → A: Strongly reduces DNA-binding; when associated with A-208 and A-210. Ref.5
Mutagenesis2081R → A: Strongly reduces DNA-binding; when associated with A-206 and A-210. Ref.5
Mutagenesis2101R → A: Strongly reduces DNA-binding; when associated with A-208 and A-208. Ref.5
Mutagenesis2311H → A: Loss of enzyme activity; when associated with A-236. Almost abolishes enzyme activity. Ref.5
Mutagenesis2361D → A: Loss of enzyme activity; when associated with A-231. Almost abolishes enzyme activity. Ref.5

Secondary structure

............................... 279
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 91387E045960C1EA

FASTA27930,621
        10         20         30         40         50         60 
MGRAGSPLPR SSWPRMDDCG SRSRCSPTLC SSLRTCYPRG NITMSEAPRA ETFVFLDLEA 

        70         80         90        100        110        120 
TGLPSVEPEI AELSLFAVHR SSLENPEHDE SGALVLPRVL DKLTLCMCPE RPFTAKASEI 

       130        140        150        160        170        180 
TGLSSEGLAR CRKAGFDGAV VRTLQAFLSR QAGPICLVAH NGFDYDFPLL CAELRRLGAR 

       190        200        210        220        230        240 
LPRDTVCLDT LPALRGLDRA HSHGTRARGR QGYSLGSLFH RYFRAEPSAA HSAEGDVHTL 

       250        260        270 
LLIFLHRAAE LLAWADEQAR GWAHIEPMYL PPDDPSLEA 

« Hide

Isoform 2 [UniParc].

Checksum: 3363BE40CFCC2300
Show »

FASTA23625,922

References

[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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_542432.2. NM_080701.3.
UniGeneHs.644635.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y97X-ray2.50A/B44-279[»]
ProteinModelPortalQ9BQ50.
SMRQ9BQ50. Positions 46-271.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116388. 3 interactions.
MINTMINT-1440359.
STRING9606.ENSP00000333441.

PTM databases

PhosphoSiteQ9BQ50.

Polymorphism databases

DMDM47606206.

Proteomic databases

PaxDbQ9BQ50.
PRIDEQ9BQ50.

Protocols and materials databases

DNASU11219.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000330912; 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]
GeneID11219.
KEGGhsa:11219.
UCSCuc010nud.2. human. [Q9BQ50-1]

Organism-specific databases

CTD11219.
GeneCardsGC0XM152710.
H-InvDBHIX0017129.
HGNCHGNC:12270. TREX2.
HPAHPA054060.
MIM300370. gene.
neXtProtNX_Q9BQ50.
PharmGKBPA36950.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG293314.
HOGENOMHOG000118119.
HOVERGENHBG079278.
InParanoidQ9BQ50.
KOK10791.
OMALARCRKA.
PhylomeDBQ9BQ50.
TreeFamTF323333.

Gene expression databases

ArrayExpressQ9BQ50.
BgeeQ9BQ50.
CleanExHS_TREX2.
GenevestigatorQ9BQ50.

Family and domain databases

Gene3D3.30.420.10. 2 hits.
InterProIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9BQ50.
GeneWikiTREX2.
GenomeRNAi11219.
NextBio42703.
PROQ9BQ50.
SOURCESearch...

Entry information

Entry nameTREX2_HUMAN
AccessionPrimary (citable) accession number: Q9BQ50
Secondary accession number(s): Q45F08, Q9UN77
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 103 of the entry and version 1 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 X

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