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Reviewed, UniProtKB/Swiss-Prot Q9BQ50 (TREX2_HUMAN)

Last modified November 3, 2009. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length279 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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

Magnesium. Required for activity. Substitution with Mn2+ results in partial activity.

Subunit structure

Homodimer. Ref.4

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
   Molecular functionExonuclease
Hydrolase
Nuclease
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processDNA repair Ref.1

Traceable author statement. Source: ProtInc

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3'-5'-exodeoxyribonuclease activity Ref.1

Traceable author statement. Source: ProtInc

exodeoxyribonuclease III activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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

Natural variations

Alternative sequence1 – 4343Missing in isoform 2.
VSP_010447
Natural variant1801R → C
VAR_025211

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.

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: 10391904] [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: 11278605] [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: 11279105] [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: 15661738] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 44-279.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

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.
IPIIPI00383247.
IPI00939474.
RefSeqNP_542432.2.
UniGeneHs.644635

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1Y97X-ray2.50A/B44-279[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ9BQ50.

Proteomic databases

PRIDEQ9BQ50.

Genome annotation databases

EnsemblENST00000330912; ENSP00000333441; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000334497; ENSP00000334993; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000338525; ENSP00000345218; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000370231; ENSP00000359251; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000370232; ENSP00000359252; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000393862; ENSP00000377442; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000402951; ENSP00000386078; ENSG00000183479; Homo sapiens. [Genome view]
ENST00000414588; ENSP00000401692; ENSG00000183479; Homo sapiens. [Genome view]
GeneID11219.
KEGGhsa:11219.
UCSCuc004fhj.1. human.

Organism-specific databases

CTD11219.
GeneCardsGC0XM152363.
H-InvDBHIX0017129.
HGNCHGNC:12270. TREX2.
MIM300370. gene.
PharmGKBPA36950.
GenAtlasSearch...

Phylogenomic databases

HOVERGENQ9BQ50.
OMAAETFVFL.

Enzyme and pathway databases

BRENDA3.1.11.2. 247.

Gene expression databases

ArrayExpressQ9BQ50.
BgeeQ9BQ50.
CleanExHS_TREX2.
GenevestigatorQ9BQ50.
GermOnlineENSG00000183479. Homo sapiens.

Family and domain databases

InterProIPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
[Graphical view]
PfamPF00929. Exonuc_X-T. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42703.
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: November 3, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome X

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

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents