Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

P22936

- APN1_YEAST

UniProt

P22936 - APN1_YEAST

Protein

DNA-(apurinic or apyrimidinic site) lyase 1

Gene

APN1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 4 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    DNA repair enzyme that cleaves apurinic/apyrimidinic (AP) sites and removes 3'-blocking groups present at single strand breaks of damaged DNA. APN1 accounts for > 97% of both apurinic/ apyrimidinic (AP) lyase and DNA 3'-repair diesterase activities.

    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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi83 – 831Zinc 1By similarity
    Metal bindingi123 – 1231Zinc 1By similarity
    Metal bindingi158 – 1581Zinc 1By similarity
    Metal bindingi158 – 1581Zinc 2By similarity
    Metal bindingi192 – 1921Zinc 2By similarity
    Metal bindingi195 – 1951Zinc 3By similarity
    Metal bindingi229 – 2291Zinc 2By similarity
    Metal bindingi242 – 2421Zinc 3By similarity
    Metal bindingi244 – 2441Zinc 3By similarity
    Metal bindingi274 – 2741Zinc 2By similarity

    GO - Molecular functioni

    1. 3'-tyrosyl-DNA phosphodiesterase activity Source: SGD
    2. DNA-(apurinic or apyrimidinic site) lyase activity Source: SGD
    3. DNA binding Source: InterPro
    4. double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: SGD
    5. phosphoric diester hydrolase activity Source: SGD
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. base-excision repair Source: SGD
    2. DNA catabolic process, endonucleolytic Source: GOC
    3. DNA catabolic process, exonucleolytic Source: GOC

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciYEAST:G3O-31899-MONOMER.
    BRENDAi4.2.99.18. 984.

    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
    Ordered Locus Names:YKL114C
    ORF Names:YKL513
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    SGDiS000001597. APN1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: SGD
    2. nucleus Source: SGD

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 367366DNA-(apurinic or apyrimidinic site) lyase 1PRO_0000190898Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei356 – 3561Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP22936.
    PaxDbiP22936.
    PeptideAtlasiP22936.

    Expressioni

    Gene expression databases

    GenevestigatoriP22936.

    Interactioni

    Subunit structurei

    Monomer.

    Protein-protein interaction databases

    BioGridi34020. 82 interactions.
    DIPiDIP-4106N.
    IntActiP22936. 2 interactions.
    MINTiMINT-537191.
    STRINGi4932.YKL114C.

    Structurei

    3D structure databases

    ProteinModelPortaliP22936.
    SMRiP22936. Positions 18-296.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AP endonuclease 2 family.Curated

    Phylogenomic databases

    eggNOGiCOG0648.
    GeneTreeiENSGT00390000013698.
    HOGENOMiHOG000224893.
    KOiK10771.
    OMAiDEINWIN.
    OrthoDBiEOG71VT48.

    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.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P22936-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSTPSFVRS AVSKYKFGAH MSGAGGISNS VTNAFNTGCN SFAMFLKSPR    50
    KWVSPQYTQE EIDKFKKNCA TYNYNPLTDV LPHGQYFINL ANPDREKAEK 100
    SYESFMDDLN RCEQLGIGLY NLHPGSTLKG DHQLQLKQLA SYLNKAIKET 150
    KFVKIVLENM AGTGNLVGSS LVDLKEVIGM IEDKSRIGVC IDTCHTFAAG 200
    YDISTTETFN NFWKEFNDVI GFKYLSAVHL NDSKAPLGAN RDLHERLGQG 250
    YLGIDVFRMI AHSEYLQGIP IVLETPYEND EGYGNEIKLM EWLESKSESE 300
    LLEDKEYKEK NDTLQKLGAK SRKEQLDKFE VKQKKRAGGT KRKKATAEPS 350
    DNDILSQMTK KRKTKKE 367
    Length:367
    Mass (Da):41,439
    Last modified:January 23, 2007 - v4
    Checksum:i76C14935B760A6D1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti239 – 2391A → S in AAA34429. (PubMed:1693433)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33667 Genomic DNA. Translation: AAA34429.1.
    S93804 Genomic DNA. Translation: AAB22003.1.
    Z28114 Genomic DNA. Translation: CAA81954.1.
    BK006944 Genomic DNA. Translation: DAA09044.1.
    PIRiS29871.
    RefSeqiNP_012808.1. NM_001179680.1.

    Genome annotation databases

    EnsemblFungiiYKL114C; YKL114C; YKL114C.
    GeneIDi853746.
    KEGGisce:YKL114C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M33667 Genomic DNA. Translation: AAA34429.1 .
    S93804 Genomic DNA. Translation: AAB22003.1 .
    Z28114 Genomic DNA. Translation: CAA81954.1 .
    BK006944 Genomic DNA. Translation: DAA09044.1 .
    PIRi S29871.
    RefSeqi NP_012808.1. NM_001179680.1.

    3D structure databases

    ProteinModelPortali P22936.
    SMRi P22936. Positions 18-296.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34020. 82 interactions.
    DIPi DIP-4106N.
    IntActi P22936. 2 interactions.
    MINTi MINT-537191.
    STRINGi 4932.YKL114C.

    Proteomic databases

    MaxQBi P22936.
    PaxDbi P22936.
    PeptideAtlasi P22936.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKL114C ; YKL114C ; YKL114C .
    GeneIDi 853746.
    KEGGi sce:YKL114C.

    Organism-specific databases

    SGDi S000001597. APN1.

    Phylogenomic databases

    eggNOGi COG0648.
    GeneTreei ENSGT00390000013698.
    HOGENOMi HOG000224893.
    KOi K10771.
    OMAi DEINWIN.
    OrthoDBi EOG71VT48.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-31899-MONOMER.
    BRENDAi 4.2.99.18. 984.

    Miscellaneous databases

    NextBioi 974804.
    PROi P22936.

    Gene expression databases

    Genevestigatori P22936.

    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. "Yeast structural gene (APN1) for the major apurinic endonuclease: homology to Escherichia coli endonuclease IV."
      Popoff S.C., Spira A.I., Johnson A.W., Demple B.
      Proc. Natl. Acad. Sci. U.S.A. 87:4193-4197(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1 and the BAF1 loci and reveals one tRNA gene and several new open reading frames including homologs to RAD2 and kinases."
      Jacquier A., Legrain P., Dujon B.
      Yeast 8:121-132(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. "Yeast DNA diesterase for 3'-fragments of deoxyribose: purification and physical properties of a repair enzyme for oxidative DNA damage."
      Johnson A.W., Demple B.
      J. Biol. Chem. 263:18009-18016(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, PROTEIN SEQUENCE OF 2-26.
    6. "Metalloenzymes in DNA repair. Escherichia coli endonuclease IV and Saccharomyces cerevisiae Apn1."
      Levin J.D., Shapiro R., Demple B.
      J. Biol. Chem. 266:22893-22898(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: METAL-BINDING STUDIES.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-356, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAPN1_YEAST
    AccessioniPrimary (citable) accession number: P22936
    Secondary accession number(s): D6VXH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 7250 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3