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P23196

- APEX1_BOVIN

UniProt

P23196 - APEX1_BOVIN

Protein

DNA-(apurinic or apyrimidinic site) lyase

Gene

APEX1

Organism
Bos taurus (Bovine)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Multifunctional protein that plays a central role in the cellular response to oxidative stress. The two major activities of APEX1 in DNA repair and redox regulation of transcriptional factors. Functions as a apurinic/apyrimidinic (AP) endodeoxyribonuclease in the DNA base excision repair (BER) pathway of DNA lesions induced by oxidative and alkylating agents. Initiates repair of AP sites in DNA by catalyzing hydrolytic incision of the phosphodiester backbone immediately adjacent to the damage, generating a single-strand break with 5'-deoxyribose phosphate and 3'-hydroxyl ends. Does also incise at AP sites in the DNA strand of DNA/RNA hybrids, single-stranded DNA regions of R-loop structures, and single-stranded RNA molecules. Has a 3'-5' exoribonuclease activity on mismatched deoxyribonucleotides at the 3' termini of nicked or gapped DNA molecules during short-patch BER. Possesses a DNA 3' phosphodiesterase activity capable of removing lesions (such as phosphoglycolate) blocking the 3' side of DNA strand breaks. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation. Acts as a loading factor for POLB onto non-incised AP sites in DNA and stimulates the 5'-terminal deoxyribose 5'-phosphate (dRp) excision activity of POLB. Plays a role in the protection from granzymes-mediated cellular repair leading to cell death. Also involved in the DNA cleavage step of class switch recombination (CSR). On the other hand, APEX1 also exerts reversible nuclear redox activity to regulate DNA binding affinity and transcriptional activity of transcriptional factors by controlling the redox status of their DNA-binding domain, such as the FOS/JUN AP-1 complex after exposure to IR. Involved in calcium-dependent down-regulation of parathyroid hormone (PTH) expression by binding to negative calcium response elements (nCaREs). Together with HNRNPL or the dimer XRCC5/XRCC6, associates with nCaRE, acting as an activator of transcriptional repression. Stimulates the YBX1-mediated MDR1 promoter activity, when acetylated at Lys-6 and Lys-7, leading to drug resistance. Acts also as an endoribonuclease involved in the control of single-stranded RNA metabolism. Plays a role in regulating MYC mRNA turnover by preferentially cleaving in between UA and CA dinucleotides of the MYC coding region determinant (CRD). In association with NMD1, plays a role in the rRNA quality control process during cell cycle progression. Associates, together with YBX1, on the MDR1 promoter. Together with NPM1, associates with rRNA. Binds DNA and RNA By similarity.By similarity

    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 annotation

    Enzyme regulationi

    NPM1 stimulates endodeoxyribonuclease activity on double-stranded DNA with AP sites, but inhibits endoribonuclease activity on single-stranded RNA containing AP sites.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei31 – 322Cleavage; by granzyme ABy similarity
    Metal bindingi70 – 701Magnesium 1By similarity
    Metal bindingi96 – 961Magnesium 1By similarity
    Active sitei171 – 1711By similarity
    Active sitei210 – 2101Proton donor/acceptorBy similarity
    Metal bindingi210 – 2101Magnesium 2By similarity
    Metal bindingi212 – 2121Magnesium 2By similarity
    Sitei212 – 2121Transition state stabilizerBy similarity
    Sitei283 – 2831Important for catalytic activityBy similarity
    Metal bindingi308 – 3081Magnesium 1By similarity
    Sitei309 – 3091Interaction with DNA substrateBy similarity

    GO - Molecular functioni

    1. 3'-5' exonuclease activity Source: UniProtKB
    2. chromatin DNA binding Source: UniProtKB
    3. damaged DNA binding Source: UniProtKB
    4. DNA-(apurinic or apyrimidinic site) lyase activity Source: UniProtKB
    5. DNA binding Source: AgBase
    6. double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: RefGenome
    7. metal ion binding Source: AgBase
    8. oxidoreductase activity Source: UniProtKB
    9. phosphoric diester hydrolase activity Source: AgBase
    10. RNA binding Source: UniProtKB-KW
    11. site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB
    12. transcription coactivator activity Source: AgBase

    GO - Biological processi

    1. base-excision repair Source: RefGenome
    2. cell redox homeostasis Source: AgBase
    3. DNA catabolic process, endonucleolytic Source: GOC
    4. DNA catabolic process, exonucleolytic Source: GOC
    5. DNA demethylation Source: UniProtKB
    6. DNA recombination Source: UniProtKB-KW
    7. DNA repair Source: UniProtKB
    8. nucleic acid phosphodiester bond hydrolysis Source: GOC
    9. positive regulation of DNA repair Source: UniProtKB
    10. regulation of mRNA stability Source: UniProtKB
    11. regulation of transcription, DNA-templated Source: UniProtKB-KW
    12. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Activator, Endonuclease, Exonuclease, Hydrolase, Lyase, Nuclease, Repressor

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding, RNA-binding

    Enzyme and pathway databases

    BRENDAi4.2.99.18. 908.
    ReactomeiREACT_203635. Displacement of DNA glycosylase by APE1.
    REACT_218453. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_218762. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_227100. Removal of DNA patch containing abasic residue.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA-(apurinic or apyrimidinic site) lyase (EC:3.1.-.-, EC:4.2.99.18)
    Alternative name(s):
    APEX nuclease
    Short name:
    APEN
    Apurinic-apyrimidinic endonuclease 1
    Short name:
    AP endonuclease 1
    REF-1
    Redox factor-1
    Cleaved into the following chain:
    Gene namesi
    Name:APEX1
    Synonyms:APE, APEX, BAP1, REF1
    OrganismiBos taurus (Bovine)
    Taxonomic identifieri9913 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
    ProteomesiUP000009136: Chromosome 10

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Nucleusnucleolus By similarity. Nucleus speckle PROSITE-ProRule annotation. Endoplasmic reticulum By similarity. Cytoplasm PROSITE-ProRule annotation
    Note: Detected in the cytoplasm of B-cells stimulated to switch. Colocalized with SIRT1 in the nucleus. Colocalized with YBX1 in nuclear speckles after genotoxic stress. Together with OGG1 is recruited to nuclear speckles in UVA-irradiated cells. Colocalized with nucleolin and NPM1 in the nucleolus. Its nucleolar localization is cell cycle dependent and requires active rRNA transcription. Colocalized with calreticulin in the endoplasmic reticulum. Translocation from the nucleus to the cytoplasm is stimulated in presence of nitric oxide (NO) and function in a CRM1-dependent manner, possibly as a consequence of demasking a nuclear export signal (amino acid position 64-80). S-nitrosylation at Cys-93 and Cys-310 regulates its nuclear-cytosolic shuttling. Ubiquitinated form is localized predominantly in the cytoplasm.
    Chain DNA-(apurinic or apyrimidinic site) lyase, mitochondrial : Mitochondrion
    Note: Translocation from the cytoplasm to the mitochondria is mediated by ROS signaling and cleavage mediated by granzyme A. Tom20-dependent translocated mitochondrial APEX1 level is significantly increased after genotoxic stress By similarity. The cleaved APEX2 is only detected in mitochondria.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB-SubCell
    4. mitochondrion Source: UniProtKB
    5. nuclear speck Source: UniProtKB
    6. nucleolus Source: UniProtKB
    7. nucleoplasm Source: UniProtKB
    8. nucleus Source: UniProtKB
    9. perinuclear region of cytoplasm Source: AgBase

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed2 Publications
    Chaini2 – 318317DNA-(apurinic or apyrimidinic site) lyasePRO_0000200009Add
    BLAST
    Chaini32 – 318287DNA-(apurinic or apyrimidinic site) lyase, mitochondrialPRO_0000402571Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61N6-acetyllysine; by EP300By similarity
    Modified residuei7 – 71N6-acetyllysine; by EP300By similarity
    Modified residuei27 – 271N6-acetyllysineBy similarity
    Modified residuei31 – 311N6-acetyllysineBy similarity
    Modified residuei32 – 321N6-acetyllysineBy similarity
    Modified residuei35 – 351N6-acetyllysineBy similarity
    Disulfide bondi65 ↔ 93AlternateBy similarity
    Modified residuei65 – 651S-nitrosocysteine; alternateBy similarity
    Modified residuei93 – 931S-nitrosocysteine; alternateBy similarity
    Modified residuei197 – 1971N6-acetyllysineBy similarity
    Modified residuei233 – 2331Phosphothreonine; by CDK5By similarity
    Modified residuei310 – 3101S-nitrosocysteineBy similarity

    Post-translational modificationi

    Phosphorylated. Phosphorylation by kinase PKC or casein kinase CK2 results in enhanced redox activity that stimulates binding of the FOS/JUN AP-1 complex to its cognate binding site. AP-endodeoxyribonuclease activity is not affected by CK2-mediated phosphorylation. Phosphorylation of Thr-233 by CDK5 in response to MPP+/MPTP (1-methyl-4-phenylpyridinium) reduces AP-endodeoxyribonuclease activity resulting in accumulation of DNA damage and contributing to neuronal death By similarity.By similarity
    Acetylated on Lys-6 and Lys-7. Acetylation is increased by the transcriptional coactivator EP300 acetyltransferase, genotoxic agents like H2O2 and methyl methanesulfonate (MMS). Acetylation increases its binding affinity to the negative calcium response element (nCaRE) DNA promoter. The acetylated form induces a stronger binding of YBX1 to the Y-box sequence in the MDR1 promoter than the unacetylated form. Deacetylated on lysines. Lys-6 and Lys-7 are deacetylated by SIRT1 By similarity.By similarity
    Cleaved at Lys-31 by granzyme A to create the mitochondrial form; leading in reduction of binding to DNA, AP endodeoxyribonuclease activity, redox activation of transcription factors and to enhanced cell death. Cleaved by granzyme K; leading to intracellular ROS accumulation and enhanced cell death after oxidative stress By similarity.By similarity
    Cys-69 and Cys-93 are nitrosylated in response to nitric oxide (NO) and lead to the exposure of the nuclear export signal (NES).By similarity
    Ubiquitinated by MDM2; leading to translocation to the cytoplasm and proteasomal degradation.By similarity

    Keywords - PTMi

    Acetylation, Cleavage on pair of basic residues, Disulfide bond, Phosphoprotein, S-nitrosylation, Ubl conjugation

    Proteomic databases

    PaxDbiP23196.
    PRIDEiP23196.

    Expressioni

    Tissue specificityi

    The mitochondrial form is expressed in liver (at protein level). Thymus.1 Publication

    Inductioni

    By several DNA damaging agents.

    Interactioni

    Subunit structurei

    Monomer. Homodimer; disulfide-linked. Component of the SET complex, composed of at least APEX1, SET, ANP32A, HMGB2, NME1 and TREX1. Associates with the dimer XRCC5/XRCC6 in a DNA-dependent manner. Interacts with SIRT1; the interaction is increased in the context of genotoxic stress. Interacts with HDAC1, HDAC2 and HDAC3; the interactions are not dependent on the APEX1 acetylation status. Interacts with XRCC1; the interaction is induced by SIRT1 and increased with the APEX1 acetylated form. Interacts with NPM1 (via N-terminal domain); the interaction is RNA-dependent and decreases in hydrogen peroxide-damaged cells. Interacts (via N-terminus) with YBX1 (via C-terminus); the interaction is increased in presence of APEX1 acetylated at Lys-6 and Lys-7. Interacts with HNRNPL; the interaction is DNA-dependent. Interacts (via N-terminus) with KPNA1 and KPNA2. Interacts with TXN; the interaction stimulates the FOS/JUN AP-1 complex DNA-binding activity in a redox-dependent manner. Interacts with GZMA, KRT8, MDM2, POLB, PRDX6, PRPF19, RPLP0, TOMM20 and WDR77. Binds to CDK5 By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9913.ENSBTAP00000003559.

    Structurei

    Secondary structure

    1
    318
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi54 – 563
    Beta strandi61 – 677
    Helixi71 – 766
    Helixi79 – 868
    Beta strandi89 – 946
    Helixi105 – 1084
    Helixi111 – 1133
    Beta strandi115 – 1195
    Beta strandi121 – 1233
    Beta strandi130 – 1367
    Beta strandi139 – 1446
    Helixi148 – 1503
    Beta strandi151 – 1533
    Beta strandi156 – 1605
    Beta strandi165 – 1706
    Helixi181 – 20121
    Beta strandi204 – 2096
    Helixi216 – 2183
    Turni222 – 2276
    Helixi233 – 24513
    Helixi251 – 2555
    Turni268 – 2714
    Helixi272 – 2754
    Beta strandi282 – 2865
    Helixi288 – 2936
    Beta strandi294 – 2996
    Beta strandi305 – 3084
    Beta strandi311 – 3155

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LYRmodel-A40-318[»]
    1XZRmodel-A40-318[»]
    1XZSmodel-A40-318[»]
    1XZTmodel-A40-318[»]
    ProteinModelPortaliP23196.
    SMRiP23196. Positions 40-318.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 3332Necessary for interaction with YBX1, binding to RNA, association together with NPM1 to rRNA, endoribonuclease activity on abasic RNA and localization in the nucleoliBy similarityAdd
    BLAST
    Regioni8 – 136Nuclear localization signal (NLS)By similarity
    Regioni23 – 3311Necessary for interaction with NPM1 and for efficient rRNA bindingBy similarityAdd
    BLAST
    Regioni64 – 8017Nuclear export signal (NES)By similarityAdd
    BLAST
    Regioni289 – 31830Mitochondrial targeting sequence (MTS)By similarityAdd
    BLAST

    Domaini

    The N-terminus contains the redox activity while the C-terminus exerts the DNA AP-endodeoxyribonuclease activity; both function are independent in their actions. An unconventional mitochondrial targeting sequence (MTS) is harbored within the C-terminus, that appears to be masked by the N-terminal sequence containing the nuclear localization signal (NLS), that probably blocks the interaction between the MTS and Tom proteins By similarity.By similarity

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0708.
    GeneTreeiENSGT00530000063540.
    HOGENOMiHOG000034586.
    HOVERGENiHBG050531.
    InParanoidiP23196.
    KOiK10771.
    OrthoDBiEOG7C8GJ6.
    TreeFamiTF315048.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    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. 1 hit.
    TIGRFAMsiTIGR00633. xth. 1 hit.
    PROSITEiPS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS00727. AP_NUCLEASE_F1_2. 1 hit.
    PS00728. AP_NUCLEASE_F1_3. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P23196-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRGKKGAV VEDAEEPKTE PEAKKSKAGA KKNEKEAVGE GAVLYEDPPD    50
    QKTSPSGKSA TLKICSWNVD GLRAWIKKKG LDWVKEEAPD ILCLQETKCS 100
    ENKLPVELQE LSGLSHQYWS APSDKEGYSG VGLLSRQCPL KVSYGIGEEE 150
    HDQEGRVIVA EYDAFVLVTA YVPNAGRGLV RLEYRQRWDE AFRKFLKGLA 200
    SRKPLVLCGD LNVAHEEIDL RNPKGNKKNA GFTPQERQGF GELLQAVPLT 250
    DSFRHLYPNT AYAYTFWTYM MNARSKNVGW RLDYFLLSQS VLPALCDSKI 300
    RSKALGSDHC PITLYLAL 318
    Length:318
    Mass (Da):35,570
    Last modified:January 23, 2007 - v2
    Checksum:i40C733FBA2EA738D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti21 – 222PE → LP AA sequence (PubMed:2441359)Curated
    Sequence conflicti291 – 2911V → L in AAI22611. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56685 mRNA. Translation: CAA40014.1.
    BC122610 mRNA. Translation: AAI22611.1.
    PIRiS26830.
    RefSeqiNP_788782.2. NM_176609.3.
    UniGeneiBt.1302.

    Genome annotation databases

    EnsembliENSBTAT00000003559; ENSBTAP00000003559; ENSBTAG00000002745.
    GeneIDi281630.
    KEGGibta:281630.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X56685 mRNA. Translation: CAA40014.1 .
    BC122610 mRNA. Translation: AAI22611.1 .
    PIRi S26830.
    RefSeqi NP_788782.2. NM_176609.3.
    UniGenei Bt.1302.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LYR model - A 40-318 [» ]
    1XZR model - A 40-318 [» ]
    1XZS model - A 40-318 [» ]
    1XZT model - A 40-318 [» ]
    ProteinModelPortali P23196.
    SMRi P23196. Positions 40-318.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9913.ENSBTAP00000003559.

    Proteomic databases

    PaxDbi P23196.
    PRIDEi P23196.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSBTAT00000003559 ; ENSBTAP00000003559 ; ENSBTAG00000002745 .
    GeneIDi 281630.
    KEGGi bta:281630.

    Organism-specific databases

    CTDi 328.

    Phylogenomic databases

    eggNOGi COG0708.
    GeneTreei ENSGT00530000063540.
    HOGENOMi HOG000034586.
    HOVERGENi HBG050531.
    InParanoidi P23196.
    KOi K10771.
    OrthoDBi EOG7C8GJ6.
    TreeFami TF315048.

    Enzyme and pathway databases

    BRENDAi 4.2.99.18. 908.
    Reactomei REACT_203635. Displacement of DNA glycosylase by APE1.
    REACT_218453. Resolution of AP sites via the multiple-nucleotide patch replacement pathway.
    REACT_218762. Base-free sugar-phosphate removal via the single-nucleotide replacement pathway.
    REACT_227100. Removal of DNA patch containing abasic residue.

    Miscellaneous databases

    NextBioi 20805567.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    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. 1 hit.
    TIGRFAMsi TIGR00633. xth. 1 hit.
    PROSITEi PS00726. AP_NUCLEASE_F1_1. 1 hit.
    PS00727. AP_NUCLEASE_F1_2. 1 hit.
    PS00728. AP_NUCLEASE_F1_3. 1 hit.
    PS51435. AP_NUCLEASE_F1_4. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation of cDNA clones encoding an enzyme from bovine cells that repairs oxidative DNA damage in vitro: homology with bacterial repair enzymes."
      Robson C.N., Milne A.M., Pappin D.J.C., Hickson I.D.
      Nucleic Acids Res. 19:1087-1092(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-19.
      Tissue: Thymus.
    2. NIH - Mammalian Gene Collection (MGC) project
      Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Hereford.
      Tissue: Basal ganglia.
    3. "Purification and amino-terminal amino acid sequence of an apurinic/apyrimidinic endonuclease from calf thymus."
      Henner W.D., Kiker N.P., Jorgensen T.J., Munck J.-N.
      Nucleic Acids Res. 15:5529-5544(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-23.
      Tissue: Thymus.
    4. "Identification and characterization of mitochondrial abasic (AP)-endonuclease in mammalian cells."
      Chattopadhyay R., Wiederhold L., Szczesny B., Boldogh I., Hazra T.K., Izumi T., Mitra S.
      Nucleic Acids Res. 34:2067-2076(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 34-38, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    5. "Three-dimensional structure prediction of bovine AP lyase, BAP1: prediction of interaction with DNA and alterations as a result of Arg176->Ala, Asp282->Ala, and His308->Asn mutations."
      Khurshid R., Salim A., Abbasi A.
      Biochem. Biophys. Res. Commun. 326:711-717(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 40-318.

    Entry informationi

    Entry nameiAPEX1_BOVIN
    AccessioniPrimary (citable) accession number: P23196
    Secondary accession number(s): Q0IIJ5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1991
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    The specific activity of the cleaved mitochondrial endodeoxyribonuclease appeared to be about 3-fold higher than of the full-length form. Extract of mitochondria, but not of nuclei or cytosol, cleaves recombinant APEX1 to generate a mitochondrial APEX1-sized product.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3