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TREX2

Protein FULL name:

three prime repair exonuclease 2 isoform a; expressed-Xq28STS protein; 26S proteasome-associated UCH interacting protein 1; 3'-5' exonuclease; Xq28, 2000bp sequence contg. ORF [Homo sapiens].


TREX2 (Homo sapiens) is product of expression of TREX2 gene.






FUNCTION: Exonuclease with a preference for double stranded DNA with mismatched 3' termini. May play a role in DNA repair.

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

COFACTOR: Magnesium. Required for activity. Substitution with Mn(2+) results in partial activity.

BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0;

SUBUNIT: Homodimer.

SUBCELLULAR LOCATION: Nucleus (Probable).

TISSUE SPECIFICITY: Detected in heart, breast, prostate, skeletal muscle, testis, uterus, bone marrow, colon, small intestine, stomach and thymus.

SIMILARITY: 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.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 6005918
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q9BQ50 Q9BQ50
PFAM: - Q9BQ50 (Link - using uniprot id)
InterPro: - Q9BQ50 (Link - using uniprot id)
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MSEAPRAETFVFLDLEATGLPSVEPEIAELSLFAVHRSSLENPEHDESGA
LVLPRVLDKLTLCMCPERPFTAKASEITGLSSEGLARCRKAGFDGAVVRT
LQAFLSRQAGPICLVAHNGFDYDFPLLCAELRRLGARLPRDTVCLDTLPA
LRGLDRAHSHGTRARGRQGYSLGSLFHRYFRAEPSAAHSAEGDVHTLLLI
FLHRAAELLAWADEQARGWAHIEPMYLPPDDPSLEA

TREX2 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
Identification and expression of the TREX1 and TREX2 cDNA sequences encoding mammalian 3'-->5' exonucleases. Mazur DJ, Perrino FW J Biol Chem July 9, 1999
Structure and expression of the TREX1 and TREX2 3' --> 5' exonuclease genes. Mazur DJ, Perrino FW J Biol Chem May 4, 2001
Excision of 3' termini by the Trex1 and TREX2 3'-->5' exonucleases. Characterization of the recombinant proteins. Mazur DJ, Perrino FW J Biol Chem May 18, 2001
The human TREX2 3' -> 5'-exonuclease structure suggests a mechanism for efficient nonprocessive DNA catalysis. Perrino FW, Harvey S, McMillin S, Hollis T J Biol Chem April 15, 2005


Last modification of this entry: Oct. 11, 2010.

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