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P87175 (APN2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
DNA-(apurinic or apyrimidinic site) lyase 2

EC=4.2.99.18
Alternative name(s):
AP endonuclease 2
Apurinic-apyrimidinic endonuclease 2
Gene names
Name:apn2
ORF Names:SPBC3D6.10
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length523 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.3

Catalytic activity

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. Ref.1

Cofactor

Magnesium. Can also utilize manganese. Probably binds two magnesium or manganese ions per subunit By similarity.

Subcellular location

Nucleus By similarity UniProtKB P38207.

Sequence similarities

Belongs to the DNA repair enzymes AP/ExoA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 523523DNA-(apurinic or apyrimidinic site) lyase 2
PRO_0000200019

Sites

Active site1511 By similarity
Active site1911Proton donor/acceptor By similarity
Metal binding421Magnesium 1 By similarity
Metal binding1911Magnesium 2 By similarity
Metal binding1931Magnesium 2 By similarity
Metal binding2941Magnesium 1 By similarity
Site1931Transition state stabilizer By similarity
Site2691Important for catalytic activity By similarity
Site2951Interaction with DNA substrate By similarity

Experimental info

Mutagenesis4021F → A: No change in activity; when associated with A-403. Ref.1
Mutagenesis4031F → A: No change in activity; when associated with A-402. Ref.1
Mutagenesis4561P → A: No change in activity; when associated with A-457 and A-458. Ref.1
Mutagenesis4571L → A: No change in activity; when associated with A-456 and A-458. Ref.1
Mutagenesis4581C → A: No change in activity; when associated with A-456 and A-457. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P87175 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: B2A79AE61579FA1C

FASTA52360,313
        10         20         30         40         50         60 
MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF PQQYAVVEGF 

        70         80         90        100        110        120 
DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV RGQKYSYSEA PEHEKIGFFP 

       130        140        150        160        170        180 
KDIDRKTANW IDSEGRCILL DFQMFILIGV YCPVNSGENR LEYRRAFYKA LRERIERLIK 

       190        200        210        220        230        240 
EGNRKIILVG DVNILCNPID TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR 

       250        260        270        280        290        300 
IQHPTRKGMF TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL 

       310        320        330        340        350        360 
DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK NKNNSPTQSE 

       370        380        390        400        410        420 
NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL SFFAKQKEEK EETNKTEDVS 

       430        440        450        460        470        480 
IEVLDNNNES DIGLTVKKKV ENGNAWKQIF SERAPPLCEG HKEPCKYLTV RKPGINYGRK 

       490        500        510        520 
FWICARPVGE LIKNSNAVSE EDTQPFQCRF FIWDSDWRAN SKD 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY483158 mRNA. Translation: AAR83752.1.
CU329671 Genomic DNA. Translation: CAB09119.1.
PIRT40370.
RefSeqNP_595522.1. NM_001021431.2.

3D structure databases

ProteinModelPortalP87175.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid277204. 24 interactions.
STRING4896.SPBC3D6.10-1.

Proteomic databases

MaxQBP87175.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC3D6.10.1; SPBC3D6.10.1:pep; SPBC3D6.10.
GeneID2540679.
KEGGspo:SPBC3D6.10.

Organism-specific databases

PomBaseSPBC3D6.10.

Phylogenomic databases

eggNOGCOG0708.
KOK10772.
OMAGRKFWIC.
OrthoDBEOG7TTQJT.
PhylomeDBP87175.

Family and domain databases

Gene3D3.60.10.10. 2 hits.
InterProIPR004808. AP_endonuc_1.
IPR020847. AP_endonuclease_F1_BS.
IPR020848. AP_endonuclease_F1_CS.
IPR005135. Endo/exonuclease/phosphatase.
[Graphical view]
PANTHERPTHR22748. PTHR22748. 1 hit.
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF56219. SSF56219. 2 hits.
TIGRFAMsTIGR00633. xth. 1 hit.
PROSITEPS00726. AP_NUCLEASE_F1_1. 1 hit.
PS00727. AP_NUCLEASE_F1_2. 1 hit.
PS51435. AP_NUCLEASE_F1_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20801803.
PROP87175.

Entry information

Entry nameAPN2_SCHPO
AccessionPrimary (citable) accession number: P87175
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names