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Protein

Exonuclease 1

Gene

EXO1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

5'->3' double-stranded DNA exonuclease which may also possess a cryptic 3'->5' double-stranded DNA exonuclease activity. Functions in DNA mismatch repair (MMR) to excise mismatch-containing DNA tracts directed by strand breaks located either 5' or 3' to the mismatch. Also exhibits endonuclease activity against 5'-overhanging flap structures similar to those generated by displacement synthesis when DNA polymerase encounters the 5'-end of a downstream Okazaki fragment. Required for somatic hypermutation (SHM) and class switch recombination (CSR) of immunoglobulin genes. Essential for male and female meiosis.12 Publications

Cofactori

Mg2+By similarityNote: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi30Magnesium 1By similarity1
Metal bindingi78Magnesium 1By similarity1
Metal bindingi150Magnesium 1By similarity1
Metal bindingi152Magnesium 1By similarity1
Metal bindingi171Magnesium 2By similarity1
Metal bindingi173Magnesium 2By similarity1
Metal bindingi225Magnesium 2By similarity1

GO - Molecular functioni

  • 5'-3' exodeoxyribonuclease activity Source: UniProtKB
  • 5'-3' exonuclease activity Source: UniProtKB
  • chromatin binding Source: Ensembl
  • DNA binding Source: UniProtKB
  • double-stranded DNA 5'-3' exodeoxyribonuclease activity Source: UniProtKB
  • exonuclease activity Source: ProtInc
  • flap endonuclease activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • RNA-DNA hybrid ribonuclease activity Source: ProtInc
  • single-stranded DNA 5'-3' exodeoxyribonuclease activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Excision nuclease, Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA excision, DNA repair, Immunity, Meiosis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS10792-MONOMER.
BRENDAi3.1.11.1. 2681.
ReactomeiR-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ9UQ84.

Names & Taxonomyi

Protein namesi
Recommended name:
Exonuclease 1 (EC:3.1.-.-)
Short name:
hExo1
Alternative name(s):
Exonuclease I
Short name:
hExoI
Gene namesi
Name:EXO1
Synonyms:EXOI, HEX1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:3511. EXO1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi78D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also reduces DNA-binding to 5'-overhanging flap structures. 1 Publication1
Mutagenesisi173D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. No effect on DNA-binding to 5'-overhanging flap structures. 2 Publications1
Mutagenesisi225D → A: Abrogates double-stranded DNA exonuclease activity and endonuclease activity against 5'-overhanging flap structures. Also enhances DNA-binding to 5'-overhanging flap structures. 1 Publication1
Mutagenesisi418K → A or T: Complete loss of nuclear localization. 1 Publication1
Mutagenesisi419R → A: Complete loss of nuclear localization. 1 Publication1
Mutagenesisi454S → A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-621 and A-714. 1 Publication1
Mutagenesisi621T → A: No rescue of HU-induced degradation. No rescue of HU-induced degradation; when associated with A-714. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-714. 1 Publication1
Mutagenesisi714S → A: No rescue of HU-induced degradation and loss of HU-induced increase of phosphorylation. No rescue of HU-induced degradation; when associated with A-621. No rescue of HU-induced degradation; when associated with A-454. Loss of HU-sensitivity and resistance to HU-induced degradation; when associated with A-454 and A-621. 1 Publication1

Organism-specific databases

DisGeNETi9156.
OpenTargetsiENSG00000174371.
PharmGKBiPA27923.

Polymorphism and mutation databases

BioMutaiEXO1.
DMDMi85700954.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001540391 – 846Exonuclease 1Add BLAST846

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei376Phosphoserine1 Publication1
Modified residuei422PhosphoserineCombined sources1 Publication1
Modified residuei454Phosphoserine1 Publication1
Modified residuei482N6-acetyllysine1 Publication1
Modified residuei581Phosphothreonine1 Publication1
Modified residuei598PhosphoserineCombined sources1 Publication1
Modified residuei610PhosphoserineCombined sources1
Modified residuei621Phosphothreonine1 Publication1
Modified residuei623PhosphoserineCombined sources1 Publication1
Modified residuei639Phosphoserine1 Publication1
Modified residuei660Phosphoserine1 Publication1
Modified residuei674Phosphoserine1 Publication1
Modified residuei714Phosphoserine; by ATR1 Publication1
Modified residuei746Phosphoserine1 Publication1

Post-translational modificationi

Phosphorylated upon DNA damage and in response to agents stalling DNA replication, probably by ATM or ATR. Phosphorylation at Ser-454, Thr-621 and Ser-714 is induced upon DNA-damage caused by treatment with hydroxyurea (HU) but not upon IR treatment. The HU-induced EXO1 triple phosphorylation facilitates destabilisation/degradation of the protein.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9UQ84.
PaxDbiQ9UQ84.
PeptideAtlasiQ9UQ84.
PRIDEiQ9UQ84.

PTM databases

iPTMnetiQ9UQ84.
PhosphoSitePlusiQ9UQ84.

Expressioni

Tissue specificityi

Highly expressed in bone marrow, testis and thymus. Expressed at lower levels in colon, lymph nodes, ovary, placenta, prostate, small intestine, spleen and stomach.4 Publications

Developmental stagei

Highly expressed in fetal liver and at lower levels in fetal brain, heart, kidney, spleen and thymus.1 Publication

Gene expression databases

BgeeiENSG00000174371.
CleanExiHS_EXO1.
ExpressionAtlasiQ9UQ84. baseline and differential.
GenevisibleiQ9UQ84. HS.

Organism-specific databases

HPAiHPA053079.
HPA060554.

Interactioni

Subunit structurei

Interacts with the MLH1-PMS2 heterodimer via MLH1. Interacts with MSH3. Interacts with the MSH2-MSH6 heterodimer via MSH2, and this interaction may increase the processivity of the 5'->3' exonuclease activity. Interacts with PCNA, and this interaction may both stimulate the cryptic 3'->5' exonuclease activity and suppress the 5'->3' exonuclease activity. Interacts with WRN, and this interaction stimulates both the 5'->3' exonuclease activity and cleavage of 5'-overhanging flap structures. Interacts with RECQL/RECQ1, and this interaction stimulates cleavage of 5'-overhanging flap structures.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MSH2P432463EBI-944694,EBI-355888
RBBP8Q997083EBI-944667,EBI-745715

Protein-protein interaction databases

BioGridi114602. 26 interactors.
DIPiDIP-36701N.
IntActiQ9UQ84. 14 interactors.
MINTiMINT-84735.
STRINGi9606.ENSP00000311873.

Structurei

Secondary structure

1846
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi6 – 9Combined sources4
Turni10 – 12Combined sources3
Beta strandi13 – 18Combined sources6
Helixi19 – 22Combined sources4
Beta strandi25 – 30Combined sources6
Helixi32 – 41Combined sources10
Helixi43 – 47Combined sources5
Helixi54 – 68Combined sources15
Beta strandi72 – 77Combined sources6
Turni83 – 85Combined sources3
Helixi86 – 106Combined sources21
Turni107 – 109Combined sources3
Helixi113 – 119Combined sources7
Helixi120 – 122Combined sources3
Helixi127 – 139Combined sources13
Beta strandi143 – 146Combined sources4
Helixi151 – 160Combined sources10
Beta strandi165 – 168Combined sources4
Helixi172 – 177Combined sources6
Beta strandi180 – 185Combined sources6
Beta strandi190 – 196Combined sources7
Helixi197 – 200Combined sources4
Turni204 – 208Combined sources5
Helixi212 – 222Combined sources11
Beta strandi225 – 227Combined sources3
Helixi235 – 244Combined sources10
Helixi250 – 254Combined sources5
Helixi257 – 261Combined sources5
Helixi269 – 284Combined sources16
Beta strandi286 – 289Combined sources4
Turni290 – 293Combined sources4
Beta strandi294 – 299Combined sources6
Helixi307 – 309Combined sources3
Helixi311 – 313Combined sources3
Helixi319 – 326Combined sources8
Turni332 – 334Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QE9X-ray2.51Y/Z1-352[»]
3QEAX-ray3.10Z1-352[»]
3QEBX-ray3.00Z1-352[»]
ProteinModelPortaliQ9UQ84.
SMRiQ9UQ84.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UQ84.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 99N-domainAdd BLAST99
Regioni129 – 387Interaction with MSH31 PublicationAdd BLAST259
Regioni138 – 229I-domainAdd BLAST92
Regioni388 – 490Interaction with MLH1Add BLAST103
Regioni600 – 846Interaction with MSH2Add BLAST247
Regioni787 – 846Interaction with MLH1Add BLAST60

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi418 – 421Nuclear localization signal4

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG2518. Eukaryota.
COG0258. LUCA.
GeneTreeiENSGT00510000047676.
HOVERGENiHBG081488.
InParanoidiQ9UQ84.
KOiK10746.
OMAiEPIHVRK.
OrthoDBiEOG091G06DK.
PhylomeDBiQ9UQ84.
TreeFamiTF314997.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR020045. 5-3_exonuclease_C.
IPR032641. Exo1.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERiPTHR11081. PTHR11081. 1 hit.
PTHR11081:SF8. PTHR11081:SF8. 1 hit.
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UQ84-1) [UniParc]FASTAAdd to basket
Also known as: B

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
MGIQGLLQFI KEASEPIHVR KYKGQVVAVD TYCWLHKGAI ACAEKLAKGE
60 70 80 90 100
PTDRYVGFCM KFVNMLLSHG IKPILVFDGC TLPSKKEVER SRRERRQANL
110 120 130 140 150
LKGKQLLREG KVSEARECFT RSINITHAMA HKVIKAARSQ GVDCLVAPYE
160 170 180 190 200
ADAQLAYLNK AGIVQAIITE DSDLLAFGCK KVILKMDQFG NGLEIDQARL
210 220 230 240 250
GMCRQLGDVF TEEKFRYMCI LSGCDYLSSL RGIGLAKACK VLRLANNPDI
260 270 280 290 300
VKVIKKIGHY LKMNITVPED YINGFIRANN TFLYQLVFDP IKRKLIPLNA
310 320 330 340 350
YEDDVDPETL SYAGQYVDDS IALQIALGNK DINTFEQIDD YNPDTAMPAH
360 370 380 390 400
SRSHSWDDKT CQKSANVSSI WHRNYSPRPE SGTVSDAPQL KENPSTVGVE
410 420 430 440 450
RVISTKGLNL PRKSSIVKRP RSAELSEDDL LSQYSLSFTK KTKKNSSEGN
460 470 480 490 500
KSLSFSEVFV PDLVNGPTNK KSVSTPPRTR NKFATFLQRK NEESGAVVVP
510 520 530 540 550
GTRSRFFCSS DSTDCVSNKV SIQPLDETAV TDKENNLHES EYGDQEGKRL
560 570 580 590 600
VDTDVARNSS DDIPNNHIPG DHIPDKATVF TDEESYSFES SKFTRTISPP
610 620 630 640 650
TLGTLRSCFS WSGGLGDFSR TPSPSPSTAL QQFRRKSDSP TSLPENNMSD
660 670 680 690 700
VSQLKSEESS DDESHPLREE ACSSQSQESG EFSLQSSNAS KLSQCSSKDS
710 720 730 740 750
DSEESDCNIK LLDSQSDQTS KLRLSHFSKK DTPLRNKVPG LYKSSSADSL
760 770 780 790 800
STTKIKPLGP ARASGLSKKP ASIQKRKHHN AENKPGLQIK LNELWKNFGF
810 820 830 840
KKDSEKLPPC KKPLSPVRDN IQLTPEAEED IFNKPECGRV QRAIFQ
Length:846
Mass (Da):94,103
Last modified:January 24, 2006 - v2
Checksum:i850BC21CA9790D08
GO
Isoform 2 (identifier: Q9UQ84-4) [UniParc]FASTAAdd to basket
Also known as: A

The sequence of this isoform differs from the canonical sequence as follows:
     803-803: D → F
     804-846: Missing.

Show »
Length:803
Mass (Da):89,231
Checksum:i1EDC61DB5D70A0B6
GO

Sequence cautioni

The sequence AAC33874 differs from that shown. Reason: Frameshift at position 793.Curated

Polymorphismi

Most naturally occurring variants in this protein are not associated with familial disposition to hereditary non-polyposis colorectal cancer (HNPCC) (PubMed:12517792). Furthermore, germline deletions involving this locus are not associated with clinically manifested colorectal tumors (PubMed:14623461).2 Publications

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02496627V → A.1 Publication1
Natural variantiVAR_02496776V → I.1 PublicationCorresponds to variant rs4149864dbSNPEnsembl.1
Natural variantiVAR_02496893R → G.1 PublicationCorresponds to variant rs4149865dbSNPEnsembl.1
Natural variantiVAR_024969109E → K Abrogates exonuclease activity. 2 PublicationsCorresponds to variant rs143546023dbSNPEnsembl.1
Natural variantiVAR_024970137A → S.1 PublicationCorresponds to variant rs147663824dbSNPEnsembl.1
Natural variantiVAR_024971279N → S.1 PublicationCorresponds to variant rs4149909dbSNPEnsembl.1
Natural variantiVAR_024972299N → S.1 PublicationCorresponds to variant rs4149910dbSNPEnsembl.1
Natural variantiVAR_024973354H → R.5 PublicationsCorresponds to variant rs735943dbSNPEnsembl.1
Natural variantiVAR_024974410L → R Abrogates exonuclease activity. 3 PublicationsCorresponds to variant rs571928768dbSNPEnsembl.1
Natural variantiVAR_024975428D → N.1 PublicationCorresponds to variant rs4149962dbSNPEnsembl.1
Natural variantiVAR_024976438F → C.1 Publication1
Natural variantiVAR_024977439T → M May be associated with an increased risk of colorectal cancer. 3 PublicationsCorresponds to variant rs4149963dbSNPEnsembl.1
Natural variantiVAR_024978456S → Y.1 PublicationCorresponds to variant rs4149964dbSNPEnsembl.1
Natural variantiVAR_024979458V → M.1 PublicationCorresponds to variant rs4149965dbSNPEnsembl.1
Natural variantiVAR_024980460V → L.1 PublicationCorresponds to variant rs4149966dbSNPEnsembl.1
Natural variantiVAR_024981503R → T.1 PublicationCorresponds to variant rs4149967dbSNPEnsembl.1
Natural variantiVAR_024982589E → K.6 PublicationsCorresponds to variant rs1047840dbSNPEnsembl.1
Natural variantiVAR_024983610S → G.2 PublicationsCorresponds to variant rs12122770dbSNPEnsembl.1
Natural variantiVAR_024984634R → Q.1 PublicationCorresponds to variant rs4149978dbSNPEnsembl.1
Natural variantiVAR_024985640P → A.2 PublicationsCorresponds to variant rs61736331dbSNPEnsembl.1
Natural variantiVAR_024986640P → S Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770. 3 PublicationsCorresponds to variant rs61736331dbSNPEnsembl.1
Natural variantiVAR_024987670E → G.8 PublicationsCorresponds to variant rs1776148dbSNPEnsembl.1
Natural variantiVAR_024988723R → C.7 PublicationsCorresponds to variant rs1635498dbSNPEnsembl.1
Natural variantiVAR_024989726H → P.1 Publication1
Natural variantiVAR_024990757P → L May be associated with a reduced risk of colorectal cancer. 4 PublicationsCorresponds to variant rs9350dbSNPEnsembl.1
Natural variantiVAR_024991759G → E Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with L-770. 4 PublicationsCorresponds to variant rs4150001dbSNPEnsembl.1
Natural variantiVAR_024992770P → L Reduces interaction with MSH2; abrogates interaction with MSH2; when associated with S-640 or E-759. 2 PublicationsCorresponds to variant rs200622305dbSNPEnsembl.1
Natural variantiVAR_024993827A → V.1 PublicationCorresponds to variant rs145975455dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_017029803D → F in isoform 2. 1 Publication1
Alternative sequenceiVSP_017030804 – 846Missing in isoform 2. 1 PublicationAdd BLAST43

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084974 mRNA. Translation: AAD13754.1.
AF091740 mRNA. Translation: AAC63043.1.
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA. Translation: AAC69879.1.
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA. Translation: AAC69880.1.
AF042282 mRNA. Translation: AAC32259.1.
AC004783 Genomic DNA. Translation: AAC32424.1.
AF060479 mRNA. Translation: AAC33874.1. Frameshift.
AF549168 Genomic DNA. Translation: AAN39382.1.
AL365366 Genomic DNA. Translation: CAI15658.1.
BC007491 mRNA. Translation: AAH07491.1.
AL080139 mRNA. Translation: CAB45733.1.
CCDSiCCDS1620.1. [Q9UQ84-1]
CCDS44336.1. [Q9UQ84-4]
PIRiT12524.
RefSeqiNP_003677.4. NM_003686.4. [Q9UQ84-4]
NP_006018.4. NM_006027.4. [Q9UQ84-1]
NP_569082.2. NM_130398.3. [Q9UQ84-1]
XP_006711903.1. XM_006711840.2. [Q9UQ84-1]
XP_011542623.1. XM_011544321.1. [Q9UQ84-1]
XP_011542624.1. XM_011544322.1. [Q9UQ84-1]
UniGeneiHs.498248.

Genome annotation databases

EnsembliENST00000348581; ENSP00000311873; ENSG00000174371. [Q9UQ84-1]
ENST00000366548; ENSP00000355506; ENSG00000174371. [Q9UQ84-1]
ENST00000518483; ENSP00000430251; ENSG00000174371. [Q9UQ84-4]
GeneIDi9156.
KEGGihsa:9156.
UCSCiuc001hzh.4. human. [Q9UQ84-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF084974 mRNA. Translation: AAD13754.1.
AF091740 mRNA. Translation: AAC63043.1.
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA. Translation: AAC69879.1.
AF091754
, AF091742, AF091743, AF091744, AF091745, AF091746, AF091747, AF091748, AF091749, AF091750, AF091751, AF091752, AF091753 Genomic DNA. Translation: AAC69880.1.
AF042282 mRNA. Translation: AAC32259.1.
AC004783 Genomic DNA. Translation: AAC32424.1.
AF060479 mRNA. Translation: AAC33874.1. Frameshift.
AF549168 Genomic DNA. Translation: AAN39382.1.
AL365366 Genomic DNA. Translation: CAI15658.1.
BC007491 mRNA. Translation: AAH07491.1.
AL080139 mRNA. Translation: CAB45733.1.
CCDSiCCDS1620.1. [Q9UQ84-1]
CCDS44336.1. [Q9UQ84-4]
PIRiT12524.
RefSeqiNP_003677.4. NM_003686.4. [Q9UQ84-4]
NP_006018.4. NM_006027.4. [Q9UQ84-1]
NP_569082.2. NM_130398.3. [Q9UQ84-1]
XP_006711903.1. XM_006711840.2. [Q9UQ84-1]
XP_011542623.1. XM_011544321.1. [Q9UQ84-1]
XP_011542624.1. XM_011544322.1. [Q9UQ84-1]
UniGeneiHs.498248.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QE9X-ray2.51Y/Z1-352[»]
3QEAX-ray3.10Z1-352[»]
3QEBX-ray3.00Z1-352[»]
ProteinModelPortaliQ9UQ84.
SMRiQ9UQ84.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114602. 26 interactors.
DIPiDIP-36701N.
IntActiQ9UQ84. 14 interactors.
MINTiMINT-84735.
STRINGi9606.ENSP00000311873.

PTM databases

iPTMnetiQ9UQ84.
PhosphoSitePlusiQ9UQ84.

Polymorphism and mutation databases

BioMutaiEXO1.
DMDMi85700954.

Proteomic databases

EPDiQ9UQ84.
PaxDbiQ9UQ84.
PeptideAtlasiQ9UQ84.
PRIDEiQ9UQ84.

Protocols and materials databases

DNASUi9156.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000348581; ENSP00000311873; ENSG00000174371. [Q9UQ84-1]
ENST00000366548; ENSP00000355506; ENSG00000174371. [Q9UQ84-1]
ENST00000518483; ENSP00000430251; ENSG00000174371. [Q9UQ84-4]
GeneIDi9156.
KEGGihsa:9156.
UCSCiuc001hzh.4. human. [Q9UQ84-1]

Organism-specific databases

CTDi9156.
DisGeNETi9156.
GeneCardsiEXO1.
H-InvDBHIX0022634.
HGNCiHGNC:3511. EXO1.
HPAiHPA053079.
HPA060554.
MIMi606063. gene.
neXtProtiNX_Q9UQ84.
OpenTargetsiENSG00000174371.
PharmGKBiPA27923.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2518. Eukaryota.
COG0258. LUCA.
GeneTreeiENSGT00510000047676.
HOVERGENiHBG081488.
InParanoidiQ9UQ84.
KOiK10746.
OMAiEPIHVRK.
OrthoDBiEOG091G06DK.
PhylomeDBiQ9UQ84.
TreeFamiTF314997.

Enzyme and pathway databases

BioCyciZFISH:HS10792-MONOMER.
BRENDAi3.1.11.1. 2681.
ReactomeiR-HSA-5358565. Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha).
R-HSA-5358606. Mismatch repair (MMR) directed by MSH2:MSH3 (MutSbeta).
R-HSA-5685938. HDR through Single Strand Annealing (SSA).
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5693554. Resolution of D-loop Structures through Synthesis-Dependent Strand Annealing (SDSA).
R-HSA-5693568. Resolution of D-loop Structures through Holliday Junction Intermediates.
R-HSA-5693579. Homologous DNA Pairing and Strand Exchange.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5693616. Presynaptic phase of homologous DNA pairing and strand exchange.
R-HSA-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-69473. G2/M DNA damage checkpoint.
SIGNORiQ9UQ84.

Miscellaneous databases

EvolutionaryTraceiQ9UQ84.
GeneWikiiExonuclease_1.
GenomeRNAii9156.
PROiQ9UQ84.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000174371.
CleanExiHS_EXO1.
ExpressionAtlasiQ9UQ84. baseline and differential.
GenevisibleiQ9UQ84. HS.

Family and domain databases

Gene3Di3.40.50.1010. 1 hit.
InterProiIPR020045. 5-3_exonuclease_C.
IPR032641. Exo1.
IPR008918. HhH2.
IPR029060. PIN_domain-like.
IPR006086. XPG-I_dom.
IPR006084. XPG/Rad2.
IPR019974. XPG_CS.
IPR006085. XPG_DNA_repair_N.
[Graphical view]
PANTHERiPTHR11081. PTHR11081. 1 hit.
PTHR11081:SF8. PTHR11081:SF8. 1 hit.
PfamiPF00867. XPG_I. 1 hit.
PF00752. XPG_N. 1 hit.
[Graphical view]
PRINTSiPR00853. XPGRADSUPER.
SMARTiSM00279. HhH2. 1 hit.
SM00484. XPGI. 1 hit.
SM00485. XPGN. 1 hit.
[Graphical view]
SUPFAMiSSF47807. SSF47807. 1 hit.
SSF88723. SSF88723. 1 hit.
PROSITEiPS00841. XPG_1. 1 hit.
PS00842. XPG_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiEXO1_HUMAN
AccessioniPrimary (citable) accession number: Q9UQ84
Secondary accession number(s): O60545
, O75214, O75466, Q5T396, Q96IJ1, Q9UG38, Q9UNW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: January 24, 2006
Last modified: November 2, 2016
This is version 148 of the entry and version 2 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 1
    Human chromosome 1: 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

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.