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P87175

- APN2_SCHPO

UniProt

P87175 - APN2_SCHPO

Protein

DNA-(apurinic or apyrimidinic site) lyase 2

Gene

apn2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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.1 PublicationPROSITE-ProRule annotation

    Cofactori

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

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

    GO - Biological processi

    1. base-excision repair Source: PomBase
    2. cellular response to reactive oxygen species Source: PomBase
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA catabolic process, exonucleolytic Source: GOC
    5. nucleic acid phosphodiester bond hydrolysis Source: GOC
    6. positive regulation of DNA N-glycosylase activity Source: PomBase

    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: Chromosome II

    Organism-specific databases

    PomBaseiSPBC3D6.10.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: PomBase

    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. 24 interactions.
    STRINGi4896.SPBC3D6.10-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP87175.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0708.
    KOiK10772.
    OMAiGRKFWIC.
    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

    MRILSWNVNG IQNPFNYFPW NKKNSYKEIF QELQADVICV QELKMQKDSF    50
    PQQYAVVEGF DSYFTFPKIR KGYSGVGFYV KKDVAIPVKA EEGITGILPV 100
    RGQKYSYSEA PEHEKIGFFP KDIDRKTANW IDSEGRCILL DFQMFILIGV 150
    YCPVNSGENR LEYRRAFYKA LRERIERLIK EGNRKIILVG DVNILCNPID 200
    TADQKDIIRE SLIPSIMESR QWIRDLLLPS RLGLLLDIGR IQHPTRKGMF 250
    TCWNTRLNTR PTNYGTRIDY TLATPDLLPW VQDADIMAEV MGSDHCPVYL 300
    DLKEEYEGKK LSNFLSHSKE PPLLSTAHHS AYRPSKNIHS MFQHFNSMKK 350
    NKNNSPTQSE NVSASASSGS SPTVSRANSV IDVDAYPPEK RRRKEQSKLL 400
    SFFAKQKEEK EETNKTEDVS IEVLDNNNES DIGLTVKKKV ENGNAWKQIF 450
    SERAPPLCEG HKEPCKYLTV RKPGINYGRK FWICARPVGE LIKNSNAVSE 500
    EDTQPFQCRF FIWDSDWRAN SKD 523
    Length:523
    Mass (Da):60,313
    Last modified:July 1, 1997 - v1
    Checksum:iB2A79AE61579FA1C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY483158 mRNA. Translation: AAR83752.1 .
    CU329671 Genomic DNA. Translation: CAB09119.1 .
    PIRi T40370.
    RefSeqi NP_595522.1. NM_001021431.2.

    3D structure databases

    ProteinModelPortali P87175.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 277204. 24 interactions.
    STRINGi 4896.SPBC3D6.10-1.

    Proteomic databases

    MaxQBi P87175.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC3D6.10.1 ; SPBC3D6.10.1:pep ; SPBC3D6.10 .
    GeneIDi 2540679.
    KEGGi spo:SPBC3D6.10.

    Organism-specific databases

    PomBasei SPBC3D6.10.

    Phylogenomic databases

    eggNOGi COG0708.
    KOi K10772.
    OMAi GRKFWIC.
    OrthoDBi EOG7TTQJT.
    PhylomeDBi P87175.

    Miscellaneous databases

    NextBioi 20801803.
    PROi P87175.

    Family and domain databases

    Gene3Di 3.60.10.10. 2 hits.
    InterProi IPR004808. AP_endonuc_1.
    IPR020847. AP_endonuclease_F1_BS.
    IPR020848. AP_endonuclease_F1_CS.
    IPR005135. Endo/exonuclease/phosphatase.
    [Graphical view ]
    PANTHERi PTHR22748. PTHR22748. 1 hit.
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56219. SSF56219. 2 hits.
    TIGRFAMsi TIGR00633. xth. 1 hit.
    PROSITEi PS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS00727. AP_NUCLEASE_F1_2. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 97 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