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Q9H790 (EXO5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Exonuclease V

Short name=Exo V
Short name=hExo5
EC=3.1.-.-
Alternative name(s):
Defects in morphology protein 1 homolog
Gene names
Name:EXO5
Synonyms:C1orf176, DEM1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Single-stranded DNA (ssDNA) bidirectional exonuclease involved in DNA repair. Probably involved in DNA repair following ultraviolet (UV) irradiation and interstrand cross-links (ICLs) damage. Has both 5'-3' and 3'-5' exonuclease activities with a strong preference for 5'-ends. Acts as a sliding exonuclease that loads at ssDNA ends and then slides along the ssDNA prior to cutting; however the sliding and the 3'-5' exonuclease activities are abolished upon binding to the replication protein A (RPA) complex that enforces 5'-directionality activity. Ref.5

Cofactor

Binds 1 4Fe-4S cluster. Ref.5

Magnesium By similarity. Ref.5

Subunit structure

Monomer; monomeric form has weak exonuclease activity. Homodimer; homodimeric form is unsure but has much higher exonuclease activity, suggesting that it could homodimerize upon DNA-binding. Interacts with the replication protein A (RPA) complex. Ref.5

Subcellular location

Nucleus. Cytoplasmcytosol. Note: Localizes to repair foci in response to DNA damage. Ref.5

Sequence similarities

Belongs to the EXO5 family.

Sequence caution

The sequence CAI16298.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16299.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16300.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16301.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAI16302.1 differs from that shown. Reason: Erroneous gene model prediction.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 373373Exonuclease V
PRO_0000307320

Sites

Metal binding921Iron-sulfur (4Fe-4S)
Metal binding3431Iron-sulfur (4Fe-4S)
Metal binding3461Iron-sulfur (4Fe-4S)
Metal binding3521Iron-sulfur (4Fe-4S)

Natural variations

Natural variant1151D → N Polymorphism that does not affect exonuclease activity. Ref.5
Corresponds to variant rs1134586 [ dbSNP | Ensembl ].
VAR_035407
Natural variant1721G → V Polymorphism that does not affect exonuclease activity. Ref.4 Ref.5
Corresponds to variant rs11208299 [ dbSNP | Ensembl ].
VAR_035408

Experimental info

Mutagenesis1961E → A: Nearly abolishes exonuclease activity. Ref.5
Mutagenesis3431C → A: Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-346. Ref.5
Mutagenesis3461C → A: Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-343. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9H790 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: EAFB31099EA40FAD

FASTA37341,816
        10         20         30         40         50         60 
MAETREEETV SAEASGFSDL SDSEFLEFLD LEDAQESKAL VNMPGPSSES LGKDDKPISL 

        70         80         90        100        110        120 
QNWKRGLDIL SPMERFHLKY LYVTDLATQN WCELQTAYGK ELPGFLAPEK AAVLDTGASI 

       130        140        150        160        170        180 
HLARELELHD LVTVPVTTKE DAWAIKFLNI LLLIPTLQSE GHIREFPVFG EGEGVLLVGV 

       190        200        210        220        230        240 
IDELHYTAKG ELELAELKTR RRPMLPLEAQ KKKDCFQVSL YKYIFDAMVQ GKVTPASLIH 

       250        260        270        280        290        300 
HTKLCLEKPL GPSVLRHAQQ GGFSVKSLGD LMELVFLSLT LSDLPVIDIL KIEYIHQETA 

       310        320        330        340        350        360 
TVLGTEIVAF KEKEVRAKVQ HYMAYWMGHR EPQGVDVEEA WKCRTCTYAD ICEWRKGSGV 

       370 
LSSTLAPQVK KAK 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Coronary artery.
[2]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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], VARIANT VAL-172.
Tissue: Ovary.
[5]"Human exonuclease 5 is a novel sliding exonuclease required for genome stability."
Sparks J.L., Kumar R., Singh M., Wold M.S., Pandita T.K., Burgers P.M.
J. Biol. Chem. 287:42773-42783(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, COFACTOR, INTERACTION WITH THE REPLICATION PROTEIN A (RPA) COMPLEX, MUTAGENESIS OF GLU-196; CYS-343 AND CYS-346, CHARACTERIZATION OF VARIANTS ASN-115 AND VAL-172.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK024797 mRNA. Translation: BAB15008.1.
AL603839 Genomic DNA. Translation: CAI16298.1. Sequence problems.
AL603839 Genomic DNA. Translation: CAI16299.1. Sequence problems.
AL603839 Genomic DNA. Translation: CAI16300.1. Sequence problems.
AL603839 Genomic DNA. Translation: CAI16301.1. Sequence problems.
AL603839 Genomic DNA. Translation: CAI16302.1. Sequence problems.
AL603839 Genomic DNA. Translation: CAI16303.1.
CH471059 Genomic DNA. Translation: EAX07210.1.
CH471059 Genomic DNA. Translation: EAX07211.1.
CH471059 Genomic DNA. Translation: EAX07212.1.
CH471059 Genomic DNA. Translation: EAX07213.1.
CH471059 Genomic DNA. Translation: EAX07214.1.
BC021969 mRNA. Translation: AAH21969.1.
CCDSCCDS453.1.
RefSeqNP_073611.1. NM_022774.1.
XP_005271182.1. XM_005271125.1.
XP_005271183.1. XM_005271126.1.
XP_005271185.1. XM_005271128.1.
UniGeneHs.59584.

3D structure databases

ProteinModelPortalQ9H790.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid122299. 3 interactions.

PTM databases

PhosphoSiteQ9H790.

Polymorphism databases

DMDM74752706.

Proteomic databases

MaxQBQ9H790.
PaxDbQ9H790.
PRIDEQ9H790.

Protocols and materials databases

DNASU64789.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296380; ENSP00000296380; ENSG00000164002.
ENST00000358527; ENSP00000351328; ENSG00000164002.
ENST00000372703; ENSP00000361788; ENSG00000164002.
GeneID64789.
KEGGhsa:64789.
UCSCuc001cfp.3. human.

Organism-specific databases

CTD64789.
GeneCardsGC01P040975.
HGNCHGNC:26115. EXO5.
HPAHPA028429.
neXtProtNX_Q9H790.
PharmGKBPA164718736.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331822.
HOVERGENHBG095898.
InParanoidQ9H790.
KOK17815.
OMAIFDAMVQ.
OrthoDBEOG761BTW.
PhylomeDBQ9H790.
TreeFamTF332529.

Gene expression databases

BgeeQ9H790.
CleanExHS_DEM1.
GenevestigatorQ9H790.

Family and domain databases

InterProIPR019190. EXOV.
[Graphical view]
PfamPF09810. Exo5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi64789.
NextBio66850.
PROQ9H790.

Entry information

Entry nameEXO5_HUMAN
AccessionPrimary (citable) accession number: Q9H790
Secondary accession number(s): D3DPV4 expand/collapse secondary AC list , Q5SWM7, Q5SWM8, Q5SWM9, Q5SWN0, Q5SWN1, Q8WTW9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM