Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9H790

- EXO5_HUMAN

UniProt

Q9H790 - EXO5_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Exonuclease V

Gene

EXO5

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

Functioni

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.1 Publication

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] cluster1 PublicationNote: Binds 1 [4Fe-4S] cluster.1 Publication
  • Mg2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi92 – 921Iron-sulfur (4Fe-4S)
Metal bindingi343 – 3431Iron-sulfur (4Fe-4S)
Metal bindingi346 – 3461Iron-sulfur (4Fe-4S)
Metal bindingi352 – 3521Iron-sulfur (4Fe-4S)

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB
  2. DNA binding Source: UniProtKB-KW
  3. metal ion binding Source: UniProtKB-KW
  4. protein homodimerization activity Source: UniProtKB
  5. single-stranded DNA 3'-5' exodeoxyribonuclease activity Source: UniProtKB
  6. single-stranded DNA 5'-3' exodeoxyribonuclease activity Source: UniProtKB

GO - Biological processi

  1. DNA catabolic process, exonucleolytic Source: GOC
  2. interstrand cross-link repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

4Fe-4S, DNA-binding, Iron, Iron-sulfur, Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Exonuclease V (EC:3.1.-.-)
Short name:
Exo V
Short name:
hExo5
Alternative name(s):
Defects in morphology protein 1 homolog
Gene namesi
Name:EXO5
Synonyms:C1orf176, DEM1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:26115. EXO5.

Subcellular locationi

Nucleus 1 Publication. Cytoplasmcytosol 1 Publication
Note: Localizes to repair foci in response to DNA damage.

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi196 – 1961E → A: Nearly abolishes exonuclease activity. 1 Publication
Mutagenesisi343 – 3431C → A: Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-346. 1 Publication
Mutagenesisi346 – 3461C → A: Abolishes iron-sulfur-binding and affects exonuclease activity; when associated with A-343. 1 Publication

Organism-specific databases

PharmGKBiPA164718736.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 373373Exonuclease VPRO_0000307320Add
BLAST

Proteomic databases

MaxQBiQ9H790.
PaxDbiQ9H790.
PRIDEiQ9H790.

PTM databases

PhosphoSiteiQ9H790.

Expressioni

Gene expression databases

BgeeiQ9H790.
CleanExiHS_DEM1.
ExpressionAtlasiQ9H790. baseline and differential.
GenevestigatoriQ9H790.

Organism-specific databases

HPAiHPA028429.

Interactioni

Subunit structurei

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.1 Publication

Protein-protein interaction databases

BioGridi122299. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliQ9H790.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the EXO5 family.Curated

Phylogenomic databases

eggNOGiNOG331822.
GeneTreeiENSGT00390000015205.
HOVERGENiHBG095898.
InParanoidiQ9H790.
KOiK17815.
OMAiIFDAMVQ.
OrthoDBiEOG761BTW.
PhylomeDBiQ9H790.
TreeFamiTF332529.

Family and domain databases

InterProiIPR019190. EXOV.
[Graphical view]
PfamiPF09810. Exo5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9H790-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAETREEETV SAEASGFSDL SDSEFLEFLD LEDAQESKAL VNMPGPSSES
60 70 80 90 100
LGKDDKPISL QNWKRGLDIL SPMERFHLKY LYVTDLATQN WCELQTAYGK
110 120 130 140 150
ELPGFLAPEK AAVLDTGASI HLARELELHD LVTVPVTTKE DAWAIKFLNI
160 170 180 190 200
LLLIPTLQSE GHIREFPVFG EGEGVLLVGV IDELHYTAKG ELELAELKTR
210 220 230 240 250
RRPMLPLEAQ KKKDCFQVSL YKYIFDAMVQ GKVTPASLIH HTKLCLEKPL
260 270 280 290 300
GPSVLRHAQQ GGFSVKSLGD LMELVFLSLT LSDLPVIDIL KIEYIHQETA
310 320 330 340 350
TVLGTEIVAF KEKEVRAKVQ HYMAYWMGHR EPQGVDVEEA WKCRTCTYAD
360 370
ICEWRKGSGV LSSTLAPQVK KAK
Length:373
Mass (Da):41,816
Last modified:March 1, 2001 - v1
Checksum:iEAFB31099EA40FAD
GO

Sequence cautioni

The sequence CAI16298.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16299.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16300.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16301.1 differs from that shown. Reason: Erroneous gene model prediction. Curated
The sequence CAI16302.1 differs from that shown. Reason: Erroneous gene model prediction. Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti115 – 1151D → N Polymorphism that does not affect exonuclease activity.
Corresponds to variant rs1134586 [ dbSNP | Ensembl ].
VAR_035407
Natural varianti172 – 1721G → V Polymorphism that does not affect exonuclease activity. 1 Publication
Corresponds to variant rs11208299 [ dbSNP | Ensembl ].
VAR_035408

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS453.1.
RefSeqiNP_073611.1. NM_022774.1.
XP_005271182.1. XM_005271125.1.
XP_005271183.1. XM_005271126.1.
XP_005271185.1. XM_005271128.1.
UniGeneiHs.59584.

Genome annotation databases

EnsembliENST00000296380; ENSP00000296380; ENSG00000164002.
ENST00000358527; ENSP00000351328; ENSG00000164002.
ENST00000372703; ENSP00000361788; ENSG00000164002.
GeneIDi64789.
KEGGihsa:64789.
UCSCiuc001cfp.3. human.

Polymorphism databases

DMDMi74752706.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS453.1.
RefSeqi NP_073611.1. NM_022774.1.
XP_005271182.1. XM_005271125.1.
XP_005271183.1. XM_005271126.1.
XP_005271185.1. XM_005271128.1.
UniGenei Hs.59584.

3D structure databases

ProteinModelPortali Q9H790.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122299. 3 interactions.

PTM databases

PhosphoSitei Q9H790.

Polymorphism databases

DMDMi 74752706.

Proteomic databases

MaxQBi Q9H790.
PaxDbi Q9H790.
PRIDEi Q9H790.

Protocols and materials databases

DNASUi 64789.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000296380 ; ENSP00000296380 ; ENSG00000164002 .
ENST00000358527 ; ENSP00000351328 ; ENSG00000164002 .
ENST00000372703 ; ENSP00000361788 ; ENSG00000164002 .
GeneIDi 64789.
KEGGi hsa:64789.
UCSCi uc001cfp.3. human.

Organism-specific databases

CTDi 64789.
GeneCardsi GC01P040975.
HGNCi HGNC:26115. EXO5.
HPAi HPA028429.
neXtProti NX_Q9H790.
PharmGKBi PA164718736.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG331822.
GeneTreei ENSGT00390000015205.
HOVERGENi HBG095898.
InParanoidi Q9H790.
KOi K17815.
OMAi IFDAMVQ.
OrthoDBi EOG761BTW.
PhylomeDBi Q9H790.
TreeFami TF332529.

Miscellaneous databases

GenomeRNAii 64789.
NextBioi 66850.
PROi Q9H790.

Gene expression databases

Bgeei Q9H790.
CleanExi HS_DEM1.
ExpressionAtlasi Q9H790. baseline and differential.
Genevestigatori Q9H790.

Family and domain databases

InterProi IPR019190. EXOV.
[Graphical view ]
Pfami PF09810. Exo5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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.

Entry informationi

Entry nameiEXO5_HUMAN
AccessioniPrimary (citable) accession number: Q9H790
Secondary accession number(s): D3DPV4
, Q5SWM7, Q5SWM8, Q5SWM9, Q5SWN0, Q5SWN1, Q8WTW9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: March 1, 2001
Last modified: November 26, 2014
This is version 83 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

Keywords - Technical termi

Complete proteome, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3