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Protein

Three prime repair exonuclease 2

Gene

TREX2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

Mg2+By similarityNote: Binds 2 Mg(2+) 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 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

  • 3'-5'-exodeoxyribonuclease activity Source: UniProtKB
  • exodeoxyribonuclease III activity Source: UniProtKB-EC
  • magnesium ion binding Source: UniProtKB
  • nucleic acid binding Source: InterPro
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • DNA catabolic process, exonucleolytic Source: GO_Central
  • DNA metabolic process Source: UniProtKB
  • 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 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:12270. TREX2.

Subcellular locationi

GO - Cellular componenti

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.

Polymorphism and mutation databases

BioMutaiTREX2.
DMDMi47606206.

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

BgeeiQ9BQ50.
CleanExiHS_TREX2.
ExpressionAtlasiQ9BQ50. baseline and differential.
GenevisibleiQ9BQ50. HS.

Organism-specific databases

HPAiHPA054060.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi116388. 7 interactions.
MINTiMINT-1440359.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00390000012715.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ9BQ50.
KOiK10791.
OMAiDVHTLLM.
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. AlignAdd to basket

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

        10         20         30         40         50
MGRAGSPLPR SSWPRMDDCG SRSRCSPTLC SSLRTCYPRG NITMSEAPRA
60 70 80 90 100
ETFVFLDLEA TGLPSVEPEI AELSLFAVHR SSLENPEHDE SGALVLPRVL
110 120 130 140 150
DKLTLCMCPE RPFTAKASEI TGLSSEGLAR CRKAGFDGAV VRTLQAFLSR
160 170 180 190 200
QAGPICLVAH NGFDYDFPLL CAELRRLGAR LPRDTVCLDT LPALRGLDRA
210 220 230 240 250
HSHGTRARGR QGYSLGSLFH RYFRAEPSAA HSAEGDVHTL LLIFLHRAAE
260 270
LLAWADEQAR GWAHIEPMYL PPDDPSLEA
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:
EMBLi
GenBanki
DDBJi
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]
ENST00000370212; ENSP00000359231; ENSG00000183479. [Q9BQ50-1]
ENST00000370231; ENSP00000359251; ENSG00000183479. [Q9BQ50-2]
ENST00000370232; ENSP00000359252; ENSG00000183479. [Q9BQ50-1]
ENST00000393862; ENSP00000377442; ENSG00000183479. [Q9BQ50-2]
GeneIDi11219.
KEGGihsa:11219.
UCSCiuc010nud.2. human. [Q9BQ50-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi116388. 7 interactions.
MINTiMINT-1440359.

PTM databases

PhosphoSiteiQ9BQ50.

Polymorphism and mutation databases

BioMutaiTREX2.
DMDMi47606206.

Proteomic databases

PaxDbiQ9BQ50.
PRIDEiQ9BQ50.

Protocols and materials databases

DNASUi11219.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000330912; ENSP00000333441; ENSG00000183479. [Q9BQ50-2]
ENST00000334497; ENSP00000334993; ENSG00000183479. [Q9BQ50-1]
ENST00000338525; ENSP00000345218; ENSG00000183479. [Q9BQ50-2]
ENST00000370212; ENSP00000359231; ENSG00000183479. [Q9BQ50-1]
ENST00000370231; ENSP00000359251; ENSG00000183479. [Q9BQ50-2]
ENST00000370232; ENSP00000359252; ENSG00000183479. [Q9BQ50-1]
ENST00000393862; ENSP00000377442; ENSG00000183479. [Q9BQ50-2]
GeneIDi11219.
KEGGihsa:11219.
UCSCiuc010nud.2. human. [Q9BQ50-1]

Organism-specific databases

CTDi11219.
GeneCardsiGC0XM152710.
H-InvDBHIX0017129.
HGNCiHGNC:12270. TREX2.
HPAiHPA054060.
MIMi300370. gene.
neXtProtiNX_Q9BQ50.
PharmGKBiPA36950.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG293314.
GeneTreeiENSGT00390000012715.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ9BQ50.
KOiK10791.
OMAiDVHTLLM.
PhylomeDBiQ9BQ50.
TreeFamiTF323333.

Miscellaneous databases

ChiTaRSiTREX2. human.
EvolutionaryTraceiQ9BQ50.
GeneWikiiTREX2.
GenomeRNAii11219.
NextBioi42703.
PROiQ9BQ50.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BQ50.
CleanExiHS_TREX2.
ExpressionAtlasiQ9BQ50. baseline and differential.
GenevisibleiQ9BQ50. HS.

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.
ProtoNetiSearch...

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: June 24, 2015
This is version 112 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.