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P43138

- APEX1_RAT

UniProt

P43138 - APEX1_RAT

Protein

DNA-(apurinic or apyrimidinic site) lyase

Gene

Apex1

Organism
Rattus norvegicus (Rat)
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, 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.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.PROSITE-ProRule annotation

    Cofactori

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

    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
    Sitei30 – 312Cleavage; by granzyme ABy similarity
    Metal bindingi69 – 691Magnesium 1By similarity
    Metal bindingi95 – 951Magnesium 1By similarity
    Active sitei170 – 1701By similarity
    Active sitei209 – 2091Proton donor/acceptorBy similarity
    Metal bindingi209 – 2091Magnesium 2By similarity
    Metal bindingi211 – 2111Magnesium 2By similarity
    Sitei211 – 2111Transition state stabilizerBy similarity
    Sitei282 – 2821Important for catalytic activityBy similarity
    Metal bindingi307 – 3071Magnesium 1By similarity
    Sitei308 – 3081Interaction 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: UniProtKB
    6. double-stranded DNA 3'-5' exodeoxyribonuclease activity Source: RefGenome
    7. endoribonuclease activity Source: RGD
    8. metal ion binding Source: UniProtKB
    9. NF-kappaB binding Source: RGD
    10. oxidoreductase activity Source: UniProtKB
    11. phosphoric diester hydrolase activity Source: Ensembl
    12. protein binding Source: RGD
    13. protein complex binding Source: RGD
    14. RNA binding Source: UniProtKB-KW
    15. site-specific endodeoxyribonuclease activity, specific for altered base Source: UniProtKB
    16. transcription coactivator activity Source: UniProtKB

    GO - Biological processi

    1. aging Source: RGD
    2. base-excision repair Source: RefGenome
    3. cell redox homeostasis Source: Ensembl
    4. cellular response to cAMP Source: RGD
    5. cellular response to hydrogen peroxide Source: RGD
    6. cellular response to organonitrogen compound Source: RGD
    7. cellular response to peptide hormone stimulus Source: RGD
    8. DNA catabolic process, endonucleolytic Source: GOC
    9. DNA catabolic process, exonucleolytic Source: GOC
    10. DNA demethylation Source: UniProtKB
    11. DNA recombination Source: UniProtKB-KW
    12. DNA repair Source: UniProtKB
    13. negative regulation of smooth muscle cell migration Source: RGD
    14. nucleic acid phosphodiester bond hydrolysis Source: GOC
    15. positive regulation of DNA repair Source: UniProtKB
    16. positive regulation of G1/S transition of mitotic cell cycle Source: RGD
    17. regulation of mRNA stability Source: UniProtKB
    18. regulation of transcription, DNA-templated Source: UniProtKB-KW
    19. response to drug Source: RGD
    20. response to organonitrogen compound Source: RGD
    21. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
    22. 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

    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, Ref1
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 15

    Organism-specific databases

    RGDi2126. Apex1.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Nucleusnucleolus By similarity. Nucleus speckle PROSITE-ProRule annotation. Endoplasmic reticulum By similarity. Cytoplasm PROSITE-ProRule annotation
    Note: 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 63-79). S-nitrosylation at Cys-92 and Cys-309 regulates its nuclear-cytosolic shuttling. Detected in the cytoplasm of B cells stimulated to switch. Ubiquitinated form is localized predominantly in the cytoplasm By similarity.By similarity
    Chain DNA-(apurinic or apyrimidinic site) lyase, mitochondrial : Mitochondrion
    Note: The cleaved APEX2 is only detected in mitochondria. 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.By similarity

    GO - Cellular componenti

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

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum, Mitochondrion, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 317316DNA-(apurinic or apyrimidinic site) lyasePRO_0000200012Add
    BLAST
    Chaini31 – 317287DNA-(apurinic or apyrimidinic site) lyase, mitochondrialBy similarityPRO_0000402574Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei6 – 61N6-acetyllysine; by EP300By similarity
    Modified residuei26 – 261N6-acetyllysineBy similarity
    Modified residuei30 – 301N6-acetyllysineBy similarity
    Modified residuei31 – 311N6-acetyllysineBy similarity
    Modified residuei34 – 341N6-acetyllysineBy similarity
    Disulfide bondi64 ↔ 92AlternateBy similarity
    Modified residuei64 – 641S-nitrosocysteine; alternateBy similarity
    Modified residuei92 – 921S-nitrosocysteine; alternateBy similarity
    Modified residuei196 – 1961N6-acetyllysineBy similarity
    Modified residuei232 – 2321Phosphothreonine; by CDK5By similarity
    Modified residuei309 – 3091S-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-232 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. 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 is deacetylated by SIRT1 By similarity.By similarity
    Cleaved at Lys-30 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-64 and Cys-92 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

    PaxDbiP43138.
    PRIDEiP43138.

    PTM databases

    PhosphoSiteiP43138.

    Expressioni

    Gene expression databases

    GenevestigatoriP43138.

    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. 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

    Structurei

    3D structure databases

    ProteinModelPortaliP43138.
    SMRiP43138. Positions 39-317.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 3231Necessary 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 – 125Nuclear localization signal (NLS)By similarity
    Regioni22 – 3211Necessary for interaction with NPM1 and for efficient rRNA bindingBy similarityAdd
    BLAST
    Regioni63 – 7917Nuclear export signal (NES)By similarityAdd
    BLAST
    Regioni288 – 31730Mitochondrial 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.
    InParanoidiP43138.
    KOiK10771.
    OMAiTYDKRWS.
    OrthoDBiEOG7C8GJ6.
    PhylomeDBiP43138.
    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.

    P43138-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPKRGKRAAA EDGEEPKSEP ETKKSKGAAK KTEKEAAGEG PVLYEDPPDQ    50
    KTSASGKSAT LKICSWNVDG LRAWIKKKGL DWVKEEAPDI LCLQETKCSE 100
    NKLPAELQEL PGLTHQYWSA PSDKEGYSGV GLLSRQCPLK VSYGIGEEEH 150
    DQEGRVIVAE FESFILVTAY VPNAGRGLVR LEYRQRWDEA FRKFLKDLAS 200
    RKPLVLCGDL NVAHEEIDLR NPKGNKKNAG FTPQERQGFG EMLQAVPLAD 250
    SFRHLYPNTA YAYTFWTYMM NARSKNVGWR LDYFLLSHSL LPALCDSKIR 300
    SKALGSDHCP ITLYLAL 317
    Length:317
    Mass (Da):35,538
    Last modified:January 23, 2007 - v2
    Checksum:iFBA6293C739E7804
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101Missing in AAA21019. (PubMed:7510394)Curated
    Sequence conflicti236 – 2361R → A in AAA21019. (PubMed:7510394)Curated
    Sequence conflicti288 – 2881H → Q in AAA21019. (PubMed:7510394)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27076 mRNA. Translation: AAA21019.1.
    AB023065 Genomic DNA. Translation: BAA82124.1.
    D44495 mRNA. Translation: BAA07938.1.
    AF309114 mRNA. Translation: AAG40859.1.
    BC078816 mRNA. Translation: AAH78816.1.
    PIRiS42397.
    RefSeqiNP_077062.1. NM_024148.1.
    XP_006251975.1. XM_006251913.1.
    UniGeneiRn.5949.

    Genome annotation databases

    EnsembliENSRNOT00000013176; ENSRNOP00000013176; ENSRNOG00000009663.
    GeneIDi79116.
    KEGGirno:79116.
    UCSCiRGD:2126. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L27076 mRNA. Translation: AAA21019.1 .
    AB023065 Genomic DNA. Translation: BAA82124.1 .
    D44495 mRNA. Translation: BAA07938.1 .
    AF309114 mRNA. Translation: AAG40859.1 .
    BC078816 mRNA. Translation: AAH78816.1 .
    PIRi S42397.
    RefSeqi NP_077062.1. NM_024148.1.
    XP_006251975.1. XM_006251913.1.
    UniGenei Rn.5949.

    3D structure databases

    ProteinModelPortali P43138.
    SMRi P43138. Positions 39-317.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei P43138.

    Proteomic databases

    PaxDbi P43138.
    PRIDEi P43138.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000013176 ; ENSRNOP00000013176 ; ENSRNOG00000009663 .
    GeneIDi 79116.
    KEGGi rno:79116.
    UCSCi RGD:2126. rat.

    Organism-specific databases

    CTDi 328.
    RGDi 2126. Apex1.

    Phylogenomic databases

    eggNOGi COG0708.
    GeneTreei ENSGT00530000063540.
    HOGENOMi HOG000034586.
    HOVERGENi HBG050531.
    InParanoidi P43138.
    KOi K10771.
    OMAi TYDKRWS.
    OrthoDBi EOG7C8GJ6.
    PhylomeDBi P43138.
    TreeFami TF315048.

    Miscellaneous databases

    NextBioi 614526.
    PROi P43138.

    Gene expression databases

    Genevestigatori P43138.

    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. "Cloning of the multifunctional rat apurinic/apyrimidinic endonuclease (rAPEN)/redox factor from an immature T cell line."
      Wilson T.M., Carney J.P., Kelley M.R.
      Nucleic Acids Res. 22:530-531(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Testis.
    2. "Genomic structure of the rat major AP endonuclease gene (Apex) with an adjacent putative O-sialoglycoprotease gene (Prsmg1/Gcpl1) and a processed Apex pseudogene (Apexp1)."
      Yao M., Akiyama K., Tan Y., Sarker A.H., Ikeda S., Alam S.S., Tsutsui K., Yoshida M.C., Seki S.
      Acta Med. Okayama 53:245-252(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "cDNA and deduced amino acid sequence of rat APEX nuclease."
      Tan Y., Akiyama K., Seki S., Tabayashi T., Taniyama M.
      Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Sprague-Dawley.
      Tissue: Brain.
    4. "Cloning of APEX cDNA gene from PC12 cell line."
      Xie Z.H., Liu C.Z., Wang A.M., Ma C.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Pheochromocytoma.
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Kidney.
    6. Cited for: SUBCELLULAR LOCATION.
    7. "Identification of apurinic/apyrimidinic endonuclease 1 (APE1) as the endoribonuclease that cleaves c-myc mRNA."
      Barnes T., Kim W.C., Mantha A.K., Kim S.E., Izumi T., Mitra S., Lee C.H.
      Nucleic Acids Res. 37:3946-3958(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiAPEX1_RAT
    AccessioniPrimary (citable) accession number: P43138
    Secondary accession number(s): Q548N9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    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 By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3