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Protein

Three-prime repair exonuclease 1

Gene

Trex1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Major cellular 3'-to-5' DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3' termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the processing of aberrant DNA replication intermediates. Inefficiently degrades oxidized DNA, such as that generated upon antimicrobial reactive oxygen production or upon absorption of UV light. During GZMA-mediated cell death, contributes to DNA damage in concert with NME1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair.10 Publications

Catalytic activityi

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

Cofactori

Mg2+4 PublicationsNote: Binds 2 Mg2+ per subunit. The second magnesium ion interacts with only one residue. Substitution with Mn2+ results in partial activity.4 Publications

Enzyme regulationi

Calcium, lithium and sodium inhibit the exonuclease activity but not the DNA binding.1 Publication

pH dependencei

Optimum pH is 7.5-8.0.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi18 – 181Magnesium 1
Metal bindingi18 – 181Magnesium 2
Metal bindingi20 – 201Magnesium 1
Binding sitei129 – 1291Substrate
Active sitei195 – 1951Proton donor/acceptor1 Publication
Metal bindingi200 – 2001Magnesium 1
Binding sitei200 – 2001Substrate

GO - Molecular functioni

  • 3'-5'-exodeoxyribonuclease activity Source: UniProtKB
  • 3'-5' exonuclease activity Source: UniProtKB
  • adenyl deoxyribonucleotide binding Source: MGI
  • double-stranded DNA binding Source: MGI
  • exodeoxyribonuclease III activity Source: UniProtKB-EC
  • metal ion binding Source: UniProtKB-KW
  • MutLalpha complex binding Source: MGI
  • MutSalpha complex binding Source: MGI
  • protein homodimerization activity Source: UniProtKB
  • single-stranded DNA binding Source: MGI

GO - Biological processi

  • cellular response to interferon-beta Source: MGI
  • DNA metabolic process Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Three-prime repair exonuclease 1 (EC:3.1.11.2)
Alternative name(s):
3'-5' exonuclease TREX1
DNase III
Gene namesi
Name:Trex1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:1328317. Trex1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Mutant animals exhibit a dramatically reduced survival after weaning, with 50% of survival at 9 weeks (PubMed:18724932) or 17 weeks (PubMed:15254239). In 6-8 week old animals, multiple organs show extensive inflammation. The most severe diffuse lymphocytic infiltration occurs in the heart, followed by the lung, the liver, the smooth muscle of the uterus and the salivary gland with periductal infiltration. Other tissues exhibit only minimal to mild lymphocytic infiltration (PubMed:24218451). The heart phenotype includes inflammatory myocarditis leading to progressive, often dilated, cardiomyopathy and circulatory failure. Enlargement of the spleen and lymph nodes is observed in less than 10% of old mice (over 1 year of age) (PubMed:15254239). Mutant animals have a reduced 3'-exonuclease activity. They accumulate ssDNA from endogenous retroelements and produce high levels of autoantibodies. Do not show an increase in spontaneous mutation frequency or cancer incidence. Double knockout of TREX1 and either IRF3, IFNAR1 or RAG2 fully rescues the TREX1 single knockout phenotype (PubMed:18724932).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi114 – 1141R → H: Reduces activity. Loss of endogenous retroelement metabolization. 2 Publications
Mutagenesisi124 – 1241H → A: Strongly reduces activity. 1 Publication
Mutagenesisi195 – 1951H → A: Loss of activity. Loss of endogenous retroelement metabolization. 3 Publications
Mutagenesisi200 – 2001D → N: Reduces activity. Loss of endogenous retroelement metabolization. 1 Publication
Mutagenesisi201 – 2011V → D: Reduces activity. Loss of endogenous retroelement metabolization. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 314314Three-prime repair exonuclease 1PRO_0000109869Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei78 – 781PhosphoserineBy similarity
Modified residuei167 – 1671PhosphoserineBy similarity
Modified residuei261 – 2611PhosphoserineBy similarity

Post-translational modificationi

Ubiquitinated, but not targeted to proteasomal degradation. Ubiquitination may be important for interaction with UBQLN1 (By similarity).By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ91XB0.
MaxQBiQ91XB0.
PaxDbiQ91XB0.
PRIDEiQ91XB0.

PTM databases

iPTMnetiQ91XB0.
PhosphoSiteiQ91XB0.

Expressioni

Tissue specificityi

Widely expressed with high expression levels detected in spleen, thymus and uterus.1 Publication

Inductioni

Induced by cytosolic DNA. Induced by inflammatory stimuli in a cell-specific fashion. Up-regulated by IFN-alpha and IFN-gamma in B-cells and by LPS and viral and bacterial DNA (via Toll-like receptor signaling) in dendritic cells and macrophages.2 Publications

Gene expression databases

CleanExiMM_TREX1.
GenevisibleiQ91XB0. MM.

Interactioni

Subunit structurei

Homodimer. Interacts (via proline-rich region) with TCERG1/CA150 (via the second WW domain). Component of the SET complex, composed of at least ANP32A, APEX1, HMGB2, NME1, SET and TREX1. Within this complex, directly interacts with SET; this interaction does not result in TREX1 inhibition. Also interacts with NME1, but only following translocation to the nucleus. Directly interacts with UBQLN1 (via ubiquitin-like domain); the interaction may control TREX1 subcellular location.3 Publications

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204312. 1 interaction.
STRINGi10090.ENSMUSP00000050971.

Structurei

Secondary structure

1
314
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 2312Combined sources
Helixi25 – 273Combined sources
Beta strandi31 – 4010Combined sources
Helixi41 – 455Combined sources
Beta strandi52 – 543Combined sources
Beta strandi65 – 706Combined sources
Helixi79 – 857Combined sources
Helixi89 – 946Combined sources
Helixi102 – 11312Combined sources
Beta strandi117 – 1237Combined sources
Turni124 – 1296Combined sources
Helixi130 – 13910Combined sources
Beta strandi141 – 1433Combined sources
Turni146 – 1494Combined sources
Beta strandi151 – 1544Combined sources
Helixi155 – 16612Combined sources
Helixi179 – 1879Combined sources
Beta strandi194 – 1963Combined sources
Helixi197 – 20812Combined sources
Helixi212 – 22211Combined sources
Helixi226 – 2283Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IOCX-ray2.10A/B1-242[»]
2O4GX-ray2.35A/B/C/D9-245[»]
2O4IX-ray3.50A/B9-245[»]
2OA8X-ray2.10A/B5-234[»]
3B6OX-ray2.10A/B/C/D9-245[»]
3B6PX-ray2.30A/B/C/D9-245[»]
3MXIX-ray2.55A/B1-242[»]
3MXJX-ray1.95A/B1-242[»]
3MXMX-ray1.75A/B1-242[»]
3U3YX-ray2.28A/B1-314[»]
3U6FX-ray2.30A/B1-314[»]
4YNQX-ray2.80A/B/C/D1-235[»]
ProteinModelPortaliQ91XB0.
SMRiQ91XB0. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ91XB0.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 212Substrate binding
Regioni54 – 6310Proline-rich region
Regioni236 – 31479Necessary for endoplasmic reticulum localizationAdd
BLAST
Regioni244 – 31471Interaction with UBQLN1By similarityAdd
BLAST
Regioni281 – 31434Necessary for cytoplasmic retentionAdd
BLAST

Sequence similaritiesi

Belongs to the exonuclease superfamily. TREX family.Curated

Phylogenomic databases

eggNOGiKOG4793. Eukaryota.
ENOG4111YSP. LUCA.
GeneTreeiENSGT00390000012715.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ91XB0.
KOiK10790.
OMAiLAVHRCA.
OrthoDBiEOG7DC26B.
PhylomeDBiQ91XB0.
TreeFamiTF323333.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.

Sequencei

Sequence statusi: Complete.

Q91XB0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGSQTLPHGH MQTLIFLDLE ATGLPSSRPE VTELCLLAVH RRALENTSIS
60 70 80 90 100
QGHPPPVPRP PRVVDKLSLC IAPGKACSPG ASEITGLSKA ELEVQGRQRF
110 120 130 140 150
DDNLAILLRA FLQRQPQPCC LVAHNGDRYD FPLLQTELAR LSTPSPLDGT
160 170 180 190 200
FCVDSIAALK ALEQASSPSG NGSRKSYSLG SIYTRLYWQA PTDSHTAEGD
210 220 230 240 250
VLTLLSICQW KPQALLQWVD EHARPFSTVK PMYGTPATTG TTNLRPHAAT
260 270 280 290 300
ATTPLATANG SPSNGRSRRP KSPPPEKVPE APSQEGLLAP LSLLTLLTLA
310
IATLYGLFLA SPGQ
Length:314
Mass (Da):33,675
Last modified:May 24, 2004 - v2
Checksum:i52C4F63A23214A7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti53 – 531H → L in AAH11133 (PubMed:15489334).Curated
Sequence conflicti269 – 2691R → G in AAH11133 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151106 mRNA. Translation: AAD48775.2.
AF319574 mRNA. Translation: AAK07621.1.
AK009899 mRNA. Translation: BAB26571.2.
AK087832 mRNA. Translation: BAC40020.1.
AK171916 mRNA. Translation: BAE42731.1.
BC011133 mRNA. Translation: AAH11133.1.
CCDSiCCDS23544.1.
RefSeqiNP_001012236.1. NM_001012236.1.
NP_035767.4. NM_011637.6.
UniGeneiMm.439964.

Genome annotation databases

EnsembliENSMUST00000061973; ENSMUSP00000050971; ENSMUSG00000049734.
ENSMUST00000112053; ENSMUSP00000107684; ENSMUSG00000049734.
GeneIDi22040.
KEGGimmu:22040.
UCSCiuc009rrr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF151106 mRNA. Translation: AAD48775.2.
AF319574 mRNA. Translation: AAK07621.1.
AK009899 mRNA. Translation: BAB26571.2.
AK087832 mRNA. Translation: BAC40020.1.
AK171916 mRNA. Translation: BAE42731.1.
BC011133 mRNA. Translation: AAH11133.1.
CCDSiCCDS23544.1.
RefSeqiNP_001012236.1. NM_001012236.1.
NP_035767.4. NM_011637.6.
UniGeneiMm.439964.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2IOCX-ray2.10A/B1-242[»]
2O4GX-ray2.35A/B/C/D9-245[»]
2O4IX-ray3.50A/B9-245[»]
2OA8X-ray2.10A/B5-234[»]
3B6OX-ray2.10A/B/C/D9-245[»]
3B6PX-ray2.30A/B/C/D9-245[»]
3MXIX-ray2.55A/B1-242[»]
3MXJX-ray1.95A/B1-242[»]
3MXMX-ray1.75A/B1-242[»]
3U3YX-ray2.28A/B1-314[»]
3U6FX-ray2.30A/B1-314[»]
4YNQX-ray2.80A/B/C/D1-235[»]
ProteinModelPortaliQ91XB0.
SMRiQ91XB0. Positions 6-234.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204312. 1 interaction.
STRINGi10090.ENSMUSP00000050971.

PTM databases

iPTMnetiQ91XB0.
PhosphoSiteiQ91XB0.

Proteomic databases

EPDiQ91XB0.
MaxQBiQ91XB0.
PaxDbiQ91XB0.
PRIDEiQ91XB0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000061973; ENSMUSP00000050971; ENSMUSG00000049734.
ENSMUST00000112053; ENSMUSP00000107684; ENSMUSG00000049734.
GeneIDi22040.
KEGGimmu:22040.
UCSCiuc009rrr.1. mouse.

Organism-specific databases

CTDi11277.
MGIiMGI:1328317. Trex1.

Phylogenomic databases

eggNOGiKOG4793. Eukaryota.
ENOG4111YSP. LUCA.
GeneTreeiENSGT00390000012715.
HOGENOMiHOG000118119.
HOVERGENiHBG079278.
InParanoidiQ91XB0.
KOiK10790.
OMAiLAVHRCA.
OrthoDBiEOG7DC26B.
PhylomeDBiQ91XB0.
TreeFamiTF323333.

Miscellaneous databases

EvolutionaryTraceiQ91XB0.
PROiQ91XB0.
SOURCEiSearch...

Gene expression databases

CleanExiMM_TREX1.
GenevisibleiQ91XB0. MM.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], FUNCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Spleen and Tongue.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  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: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, HOMODIMERIZATION.
  5. "Gene-targeted mice lacking the Trex1 (DNase III) 3'-->5' DNA exonuclease develop inflammatory myocarditis."
    Morita M., Stamp G., Robins P., Dulic A., Rosewell I., Hrivnak G., Daly G., Lindahl T., Barnes D.E.
    Mol. Cell. Biol. 24:6719-6727(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INFLAMMATION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
  6. "Trex1 exonuclease degrades ssDNA to prevent chronic checkpoint activation and autoimmune disease."
    Yang Y.G., Lindahl T., Barnes D.E.
    Cell 131:873-886(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CELL CYCLE REGULATION, SUBCELLULAR LOCATION.
  7. "Trex1 prevents cell-intrinsic initiation of autoimmunity."
    Stetson D.B., Ko J.S., Heidmann T., Medzhitov R.
    Cell 134:587-598(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS REGULATOR OF IFN RESPONSE, SUBCELLULAR LOCATION, INDUCTION BY CYTOSOLIC DNA, DISRUPTION PHENOTYPE, MUTAGENESIS OF ARG-114; HIS-195; ASP-200 AND VAL-201.
  8. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Spleen.
  10. "Oxidative damage of DNA confers resistance to cytosolic nuclease TREX1 degradation and potentiates STING-dependent immune sensing."
    Gehrke N., Mertens C., Zillinger T., Wenzel J., Bald T., Zahn S., Tueting T., Hartmann G., Barchet W.
    Immunity 39:482-495(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN OXIDIZED DNA DEGRADATION.
  11. "The exonuclease trex1 restrains macrophage proinflammatory activation."
    Pereira-Lopes S., Celhar T., Sans-Fons G., Serra M., Fairhurst A.M., Lloberas J., Celada A.
    J. Immunol. 191:6128-6135(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN INNATE IMMUNE SYSTEM REGULATION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE, INDUCTION BY INFLAMMATORY STIMULI.
  12. "The crystal structure of TREX1 explains the 3' nucleotide specificity and reveals a polyproline II helix for protein partnering."
    de Silva U., Choudhury S., Bailey S.L., Harvey S., Perrino F.W., Hollis T.
    J. Biol. Chem. 282:10537-10543(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1-242 IN COMPLEXES WITH DNA; AMP; CALCIUM AND MANGANESE IONS, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, MUTAGENESIS OF ARG-114 AND VAL-201.
  13. "Structure of the dimeric exonuclease TREX1 in complex with DNA displays a proline-rich binding site for WW Domains."
    Brucet M., Querol-Audi J., Serra M., Ramirez-Espain X., Bertlik K., Ruiz L., Lloberas J., Macias M.J., Fita I., Celada A.
    J. Biol. Chem. 282:14547-14557(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 9-245 AND MUTANT ALA-195 IN COMPLEXES WITH DNA AND MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, DNA-BINDING, SUBUNIT, INTERACTION WITH TCERG1, SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-195.
  14. "Structural and biochemical studies of TREX1 inhibition by metals. Identification of a new active histidine conserved in DEDDh exonucleases."
    Brucet M., Querol-Audi J., Bertlik K., Lloberas J., Fita I., Celada A.
    Protein Sci. 17:2059-2069(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 9-245 IN COMPLEXES WITH TMP; LITHIUM; SODIUM AND ZINC IONS, FUNCTION, CATALYTIC ACTIVITY, DNA-BINDING, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-124 AND HIS-195.
  15. "Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease."
    Bailey S.L., Harvey S., Perrino F.W., Hollis T.
    DNA Repair 11:65-73(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 1-142 AND MUTANTS ASN-18; HIS-200; ASN-200 AND ASP-201 IN COMPLEXES WITH DNA; CALCIUM AND MAGNESIUM IONS, COFACTOR, SUBUNIT.

Entry informationi

Entry nameiTREX1_MOUSE
AccessioniPrimary (citable) accession number: Q91XB0
Secondary accession number(s): Q3TAD7, Q9D6W2, Q9R1B0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: May 24, 2004
Last modified: June 8, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.