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Protein

DNA-(apurinic or apyrimidinic site) lyase 2

Gene

apn2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. Provides the majority of the AP-endonuclease (APE) activity. Repairs phleomycin D1-induced DNA damage. Plays a role in oxidative damage repair.2 Publications

Catalytic activityi

The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.PROSITE-ProRule annotation1 Publication

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Probably binds two magnesium or manganese ions per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi42 – 421Magnesium 1By similarity
Active sitei151 – 1511By similarity
Active sitei191 – 1911Proton donor/acceptorBy similarity
Metal bindingi191 – 1911Magnesium 2By similarity
Metal bindingi193 – 1931Magnesium 2By similarity
Sitei193 – 1931Transition state stabilizerBy similarity
Sitei269 – 2691Important for catalytic activityBy similarity
Metal bindingi294 – 2941Magnesium 1By similarity
Sitei295 – 2951Interaction with DNA substrateBy similarity

GO - Molecular functioni

  • DNA-(apurinic or apyrimidinic site) lyase activity Source: PomBase
  • DNA binding Source: InterPro
  • double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: PomBase
  • metal ion binding Source: UniProtKB-KW
  • phosphodiesterase I activity Source: PomBase

GO - Biological processi

  • base-excision repair Source: GO_Central
  • cellular response to reactive oxygen species Source: PomBase
  • nucleic acid phosphodiester bond hydrolysis Source: GOC
  • positive regulation of DNA N-glycosylase activity Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

Magnesium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-(apurinic or apyrimidinic site) lyase 2 (EC:4.2.99.18)
Alternative name(s):
AP endonuclease 2
Apurinic-apyrimidinic endonuclease 2
Gene namesi
Name:apn2
ORF Names:SPBC3D6.10
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC3D6.10.
PomBaseiSPBC3D6.10. apn2.

Subcellular locationi

  • Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi402 – 4021F → A: No change in activity; when associated with A-403. 1 Publication
Mutagenesisi403 – 4031F → A: No change in activity; when associated with A-402. 1 Publication
Mutagenesisi456 – 4561P → A: No change in activity; when associated with A-457 and A-458. 1 Publication
Mutagenesisi457 – 4571L → A: No change in activity; when associated with A-456 and A-458. 1 Publication
Mutagenesisi458 – 4581C → A: No change in activity; when associated with A-456 and A-457. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 523523DNA-(apurinic or apyrimidinic site) lyase 2PRO_0000200019Add
BLAST

Proteomic databases

MaxQBiP87175.

Interactioni

Protein-protein interaction databases

BioGridi277204. 25 interactions.

Structurei

3D structure databases

ProteinModelPortaliP87175.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DNA repair enzymes AP/ExoA family.Curated

Phylogenomic databases

eggNOGiCOG0708.
InParanoidiP87175.
KOiK10772.
OMAiPPLCSKY.
OrthoDBiEOG7TTQJT.
PhylomeDBiP87175.

Family and domain databases

Gene3Di3.60.10.10. 2 hits.
InterProiIPR004808. AP_endonuc_1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR22748. PTHR22748. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 2 hits.
TIGRFAMsiTIGR00633. xth. 1 hit.
PROSITEiPS00726. AP_NUCLEASE_F1_1. 1 hit.
PS00727. AP_NUCLEASE_F1_2. 1 hit.
PS51435. AP_NUCLEASE_F1_4. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P87175-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF
60 70 80 90 100
PQQYAVVEGF DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV
110 120 130 140 150
RGQKYSYSEA PEHEKIGFFP KDIDRKTANW IDSEGRCILL DFQMFILIGV
160 170 180 190 200
YCPVNSGENR LEYRRAFYKA LRERIERLIK EGNRKIILVG DVNILCNPID
210 220 230 240 250
TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR IQHPTRKGMF
260 270 280 290 300
TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL
310 320 330 340 350
DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK
360 370 380 390 400
NKNNSPTQSE NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL
410 420 430 440 450
SFFAKQKEEK EETNKTEDVS IEVLDNNNES DIGLTVKKKV ENGNAWKQIF
460 470 480 490 500
SERAPPLCEG HKEPCKYLTV RKPGINYGRK FWICARPVGE LIKNSNAVSE
510 520
EDTQPFQCRF FIWDSDWRAN SKD
Length:523
Mass (Da):60,313
Last modified:July 1, 1997 - v1
Checksum:iB2A79AE61579FA1C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY483158 mRNA. Translation: AAR83752.1.
CU329671 Genomic DNA. Translation: CAB09119.1.
PIRiT40370.
RefSeqiNP_595522.1. NM_001021431.2.

Genome annotation databases

EnsemblFungiiSPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
GeneIDi2540679.
KEGGispo:SPBC3D6.10.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY483158 mRNA. Translation: AAR83752.1.
CU329671 Genomic DNA. Translation: CAB09119.1.
PIRiT40370.
RefSeqiNP_595522.1. NM_001021431.2.

3D structure databases

ProteinModelPortaliP87175.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277204. 25 interactions.

Proteomic databases

MaxQBiP87175.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
GeneIDi2540679.
KEGGispo:SPBC3D6.10.

Organism-specific databases

EuPathDBiFungiDB:SPBC3D6.10.
PomBaseiSPBC3D6.10. apn2.

Phylogenomic databases

eggNOGiCOG0708.
InParanoidiP87175.
KOiK10772.
OMAiPPLCSKY.
OrthoDBiEOG7TTQJT.
PhylomeDBiP87175.

Miscellaneous databases

NextBioi20801803.
PROiP87175.

Family and domain databases

Gene3Di3.60.10.10. 2 hits.
InterProiIPR004808. AP_endonuc_1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERiPTHR22748. PTHR22748. 1 hit.
PfamiPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMiSSF56219. SSF56219. 2 hits.
TIGRFAMsiTIGR00633. xth. 1 hit.
PROSITEiPS00726. AP_NUCLEASE_F1_1. 1 hit.
PS00727. AP_NUCLEASE_F1_2. 1 hit.
PS51435. AP_NUCLEASE_F1_4. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The major role of human AP-endonuclease homolog Apn2 in repair of abasic sites in Schizosaccharomyces pombe."
    Ribar B., Izumi T., Mitra S.
    Nucleic Acids Res. 32:115-126(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF PHE-402; PHE-403; PRO-456; LEU-457 AND CYS-458.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Fission yeast Uve1 and Apn2 function in distinct oxidative damage repair pathways in vivo."
    Fraser J.L.A., Neill E., Davey S.
    DNA Repair 2:1253-1267(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiAPN2_SCHPO
AccessioniPrimary (citable) accession number: P87175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: July 1, 1997
Last modified: July 22, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.