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P50525

- APN1_SCHPO

UniProt

P50525 - APN1_SCHPO

Protein

DNA-(apurinic or apyrimidinic site) lyase 1

Gene

apn1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein uncertaini
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 3 (07 Jun 2004)
      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 back-up AP endonuclease (APE) activity to apn2 together with uve1.1 Publication

    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.

    Cofactori

    Binds 3 zinc ions.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi61 – 611Zinc 1By similarity
    Metal bindingi136 – 1361Zinc 1By similarity
    Metal bindingi136 – 1361Zinc 2By similarity
    Metal bindingi170 – 1701Zinc 2By similarity
    Metal bindingi173 – 1731Zinc 3By similarity
    Metal bindingi207 – 2071Zinc 2By similarity
    Metal bindingi220 – 2201Zinc 3By similarity
    Metal bindingi222 – 2221Zinc 3By similarity
    Metal bindingi252 – 2521Zinc 2By similarity

    GO - Molecular functioni

    1. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB-EC
    2. DNA binding Source: InterPro
    3. zinc ion binding Source: InterPro

    GO - Biological processi

    1. DNA repair Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase 1 (EC:4.2.99.18)
    Alternative name(s):
    Apurinic-apyrimidinic endonuclease 1
    Short name:
    AP endonuclease 1
    Gene namesi
    Name:apn1
    ORF Names:SPCC622.17
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome III

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342DNA-(apurinic or apyrimidinic site) lyase 1PRO_0000190897Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    BioGridi275375. 9 interactions.
    MINTiMINT-4690690.
    STRINGi4896.SPCC622.17-1.

    Structurei

    3D structure databases

    ProteinModelPortaliP50525.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AP endonuclease 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0648.
    HOGENOMiHOG000224893.
    OMAiDEINWIN.
    OrthoDBiEOG71VT48.
    PhylomeDBiP50525.

    Family and domain databases

    Gene3Di3.20.20.150. 1 hit.
    HAMAPiMF_00152. Nfo.
    InterProiIPR001719. AP_endonuc_2.
    IPR018246. AP_endonuc_F2_Zn_BS.
    IPR013022. Xyl_isomerase-like_TIM-brl.
    [Graphical view]
    PANTHERiPTHR21445. PTHR21445. 1 hit.
    PfamiPF01261. AP_endonuc_2. 1 hit.
    [Graphical view]
    SMARTiSM00518. AP2Ec. 1 hit.
    [Graphical view]
    SUPFAMiSSF51658. SSF51658. 1 hit.
    TIGRFAMsiTIGR00587. nfo. 1 hit.
    PROSITEiPS00729. AP_NUCLEASE_F2_1. 1 hit.
    PS00730. AP_NUCLEASE_F2_2. 1 hit.
    PS00731. AP_NUCLEASE_F2_3. 1 hit.
    PS51432. AP_NUCLEASE_F2_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P50525-1 [UniParc]FASTAAdd to Basket

    « Hide

    MCAINKAYLL TKFYISANSC AFFVKSQRKW TSPDLSEDVA QKFLETASEM    50
    KFDASKQVLV HGSYLINMAN ADEQKREQAF NCFVDDLKRC ERLGVGLYNF 100
    HPGSTASCTK EEGINNLAEC INRAHEETKS VIIVTENMAG QGNCLGGTFD 150
    DFAALKSKIK NLDRWRVCLD TCHTFAAGYD IRTEESYKKV IDEFDEKVGA 200
    KYVSGWHLND SKAPLGSNRD LHENIGLGFL GLEPFRLIMN DSRWDGIPLV 250
    LETPAKSPEQ WKKEVELLRF MVGKSSDDVE LMKESARLSN LGAASRKEHL 300
    NKFEKKEAKK DRKKKSKDGD QTTLLLRKKQ KLGNAEVKSL DE 342
    Length:342
    Mass (Da):38,657
    Last modified:June 7, 2004 - v3
    Checksum:iC6711EC23691C51D
    GO

    Sequence cautioni

    The sequence AAC28163.1 differs from that shown. Reason: Intron retention.
    The sequence AAC28163.1 differs from that shown. Reason: Frameshift at position 298.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY483157 mRNA. Translation: AAR83751.1.
    CU329672 Genomic DNA. No translation available.
    U33625 mRNA. Translation: AAC28163.1. Sequence problems.
    PIRiT52563.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY483157 mRNA. Translation: AAR83751.1 .
    CU329672 Genomic DNA. No translation available.
    U33625 mRNA. Translation: AAC28163.1 . Sequence problems.
    PIRi T52563.

    3D structure databases

    ProteinModelPortali P50525.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 275375. 9 interactions.
    MINTi MINT-4690690.
    STRINGi 4896.SPCC622.17-1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    eggNOGi COG0648.
    HOGENOMi HOG000224893.
    OMAi DEINWIN.
    OrthoDBi EOG71VT48.
    PhylomeDBi P50525.

    Miscellaneous databases

    NextBioi 20799976.
    PROi P50525.

    Family and domain databases

    Gene3Di 3.20.20.150. 1 hit.
    HAMAPi MF_00152. Nfo.
    InterProi IPR001719. AP_endonuc_2.
    IPR018246. AP_endonuc_F2_Zn_BS.
    IPR013022. Xyl_isomerase-like_TIM-brl.
    [Graphical view ]
    PANTHERi PTHR21445. PTHR21445. 1 hit.
    Pfami PF01261. AP_endonuc_2. 1 hit.
    [Graphical view ]
    SMARTi SM00518. AP2Ec. 1 hit.
    [Graphical view ]
    SUPFAMi SSF51658. SSF51658. 1 hit.
    TIGRFAMsi TIGR00587. nfo. 1 hit.
    PROSITEi PS00729. AP_NUCLEASE_F2_1. 1 hit.
    PS00730. AP_NUCLEASE_F2_2. 1 hit.
    PS00731. AP_NUCLEASE_F2_3. 1 hit.
    PS51432. AP_NUCLEASE_F2_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.
    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. Seeger K., Harris D., Lyne M., Rajandream M.A., Barrell B.G.
      Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    4. "Schizosaccharomyces pombe apn1 encodes a homologue of the Escherichia coli endonuclease IV family of DNA repair proteins."
      Ramotar D., Vadnais J., Masson J.Y., Tremblay S.
      Biochim. Biophys. Acta 1396:15-20(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-319.
    5. "Schizosaccharomyces pombe encodes a mutated AP endonuclease 1."
      Laerdahl J.K., Korvald H., Nilsen L., Dahl-Michelsen K., Rognes T., Bjoras M., Alseth I.
      DNA Repair 10:296-305(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: LACK OF FUNCTION.

    Entry informationi

    Entry nameiAPN1_SCHPO
    AccessioniPrimary (citable) accession number: P50525
    Secondary accession number(s): Q9USI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 108 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Caution

    Could be the product of a pseudogene. This is a truncated version of AP endonuclease 1. In strain 972 and its derivative FY527, this gene has a stop codon in position 5, which disrupts the gene coding for this protein. PubMed:21193357 shows that the truncated protein is not functional. A full sequence for apn1 can be found in strains SPK19802 (S.pombe var. kambucha), NCYC 132, NCYC 683, NCYC 936 and NCYC 2722 (PubMed:21193357).1 Publication

    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