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Q7Z2E3

- APTX_HUMAN

UniProt

Q7Z2E3 - APTX_HUMAN

Protein

Aprataxin

Gene

APTX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    DNA-binding protein involved in single-strand DNA break repair, double-strand DNA break repair and base excision repair. Resolves abortive DNA ligation intermediates formed either at base excision sites, or when DNA ligases attempt to repair non-ligatable breaks induced by reactive oxygen species. Catalyzes the release of adenylate groups covalently linked to 5'-phosphate termini, resulting in the production of 5'-phosphate termini that can be efficiently rejoined. Also able to hydrolyze adenosine 5'-monophosphoramidate (AMP-NH2) and diadenosine tetraphosphate (AppppA), but with lower catalytic activity.5 Publications

    Kineticsi

    1. KM=18 µM for AppppA
    2. KM=837.5 µM for AMP-NH2

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei274 – 2741Tele-AMP-histidine intermediateCurated

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri331 – 35323C2H2-typeAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. damaged DNA binding Source: UniProtKB
    3. DNA 5'-adenosine monophosphate hydrolase activity Source: UniProtKB
    4. double-stranded DNA binding Source: UniProtKB
    5. double-stranded RNA binding Source: UniProtKB
    6. metal ion binding Source: UniProtKB-KW
    7. phosphoglycolate phosphatase activity Source: UniProtKB
    8. phosphoprotein binding Source: UniProtKB
    9. polynucleotide 3'-phosphatase activity Source: UniProtKB
    10. protein binding Source: UniProtKB
    11. protein N-terminus binding Source: UniProtKB

    GO - Biological processi

    1. cell death Source: UniProtKB-KW
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. dephosphorylation Source: GOC
    4. DNA catabolic process, exonucleolytic Source: GOC
    5. DNA ligation Source: Ensembl
    6. double-strand break repair Source: UniProtKB
    7. polynucleotide 3' dephosphorylation Source: GOC
    8. regulation of protein stability Source: UniProtKB
    9. response to hydrogen peroxide Source: UniProtKB
    10. single strand break repair Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKQ7Z2E3.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aprataxin (EC:3.-.-.-)
    Alternative name(s):
    Forkhead-associated domain histidine triad-like protein
    Short name:
    FHA-HIT
    Gene namesi
    Name:APTX
    Synonyms:AXA1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:15984. APTX.

    Subcellular locationi

    Nucleusnucleoplasm. Nucleusnucleolus
    Note: Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage. Colocalizes with MDC1 at sites of DNA double-strand breaks. Interaction with NCL is required for nucleolar localization.

    GO - Cellular componenti

    1. chromatin Source: UniProtKB
    2. cytoplasm Source: UniProtKB-SubCell
    3. nucleolus Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Ataxia-oculomotor apraxia syndrome (AOA) [MIM:208920]: An autosomal recessive syndrome characterized by early-onset cerebellar ataxia, oculomotor apraxia, early areflexia and late peripheral neuropathy.7 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti211 – 2111K → Q in AOA; it probably does not greatly affect the protein; heterozygous. 1 Publication
    VAR_018794
    Natural varianti212 – 2121A → V in AOA; heterozygous. 1 Publication
    VAR_018795
    Natural varianti213 – 2131R → H in AOA. 1 Publication
    Corresponds to variant rs150886026 [ dbSNP | Ensembl ].
    VAR_018796
    Natural varianti215 – 2151H → R in AOA. 1 Publication
    VAR_018797
    Natural varianti220 – 2201P → L in AOA. 2 Publications
    VAR_018798
    Natural varianti237 – 2371L → P in AOA. 1 Publication
    VAR_025365
    Natural varianti277 – 2771V → G in AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A. 2 Publications
    VAR_018799
    Natural varianti281 – 2811D → G in AOA; heterozygous.
    VAR_018800
    Natural varianti293 – 2931W → R in AOA; heterozygous. 1 Publication
    VAR_018801

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi43 – 431R → A: Impairs interaction with XRCC1 and XRCC4. Abolishes localization at sites of DNA double-strand breaks. Loss of interaction with MDC1. 2 Publications
    Mutagenesisi52 – 521K → A: Impairs interaction with MDC1 and localization at sites of DNA double-strand breaks. 1 Publication
    Mutagenesisi274 – 2741H → A: Abolishes enzyme activity. 2 Publications
    Mutagenesisi333 – 3331C → A: Abolishes DNA-binding and enzyme activity; when associated with A-336. 1 Publication
    Mutagenesisi336 – 3361C → A: Abolishes DNA-binding and enzyme activity; when associated with A-333. 1 Publication

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    MIMi208920. phenotype.
    Orphaneti1168. Ataxia - oculomotor apraxia type 1.
    PharmGKBiPA24915.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 356356AprataxinPRO_0000109838Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei132 – 1321Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ7Z2E3.
    PaxDbiQ7Z2E3.
    PRIDEiQ7Z2E3.

    PTM databases

    PhosphoSiteiQ7Z2E3.

    Expressioni

    Tissue specificityi

    Widely expressed. In brain, it is expressed in the posterior cortex, cerebellum, hippocampus and olfactory bulb. Isoform 1 is highly expressed in the cerebral cortex and cerebellum, compared to isoform 2.3 Publications

    Gene expression databases

    ArrayExpressiQ7Z2E3.
    BgeeiQ7Z2E3.
    CleanExiHS_APTX.
    GenevestigatoriQ7Z2E3.

    Organism-specific databases

    HPAiHPA055545.

    Interactioni

    Subunit structurei

    Interacts with single-strand break repair proteins XRCC1, XRCC4, ADPRT and p53/TP53. Interacts with NCL. Interacts (via FHA-like domain) with MDC1 (phosphorylated).5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PARP1P098748EBI-847814,EBI-355676
    XRCC1P1888711EBI-847814,EBI-947466
    XRCC4Q134263EBI-847814,EBI-717592

    Protein-protein interaction databases

    BioGridi120191. 22 interactions.
    IntActiQ7Z2E3. 16 interactions.
    MINTiMINT-1205251.

    Structurei

    Secondary structure

    1
    356
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi18 – 236
    Beta strandi30 – 323
    Beta strandi38 – 414
    Turni45 – 473
    Beta strandi59 – 646
    Turni65 – 684
    Beta strandi69 – 746
    Beta strandi76 – 783
    Beta strandi92 – 954
    Beta strandi101 – 1044
    Beta strandi107 – 1159
    Helixi181 – 1833
    Helixi184 – 1885
    Turni192 – 1943
    Beta strandi195 – 1984
    Beta strandi200 – 2067
    Beta strandi211 – 22212
    Helixi227 – 2293
    Helixi232 – 2343
    Helixi235 – 25319
    Helixi254 – 2563
    Beta strandi260 – 2678
    Beta strandi269 – 2724
    Beta strandi275 – 2795
    Helixi290 – 2978
    Beta strandi301 – 3033
    Helixi304 – 31411
    Helixi323 – 3264
    Turni334 – 3363
    Beta strandi339 – 3424
    Helixi343 – 3508
    Helixi351 – 3533

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3KT9X-ray1.65A15-116[»]
    4NDFX-ray1.94A/B179-356[»]
    4NDGX-ray2.54A/B179-356[»]
    4NDHX-ray1.85A/B179-356[»]
    4NDIX-ray1.90A/B179-356[»]
    ProteinModelPortaliQ7Z2E3.
    SMRiQ7Z2E3. Positions 15-116, 178-354.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7Z2E3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini38 – 8750FHA-likeAdd
    BLAST
    Domaini182 – 287106HITPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 110110Interactions with ADPRT and NCLAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi126 – 1316Nuclear localization signalCurated
    Motifi272 – 2765Histidine triad motif

    Domaini

    The histidine triad, also called HIT motif, forms part of the binding loop for the alpha-phosphate of purine mononucleotide.By similarity
    The FHA-like domain mediates interaction with NCL; XRCC1 and XRCC4.
    The HIT domain is required for enzymatic activity.
    The C2H2-type zinc finger mediates DNA-binding.

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.Curated
    Contains 1 FHA-like domain.Curated
    Contains 1 HIT domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri331 – 35323C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG278510.
    HOGENOMiHOG000248858.
    HOVERGENiHBG050555.
    InParanoidiQ7Z2E3.
    KOiK10863.
    OMAiPGQVLHM.
    OrthoDBiEOG786H3J.
    PhylomeDBiQ7Z2E3.
    TreeFamiTF313308.

    Family and domain databases

    Gene3Di2.60.200.20. 2 hits.
    3.30.428.10. 1 hit.
    InterProiIPR026963. Aprataxin.
    IPR000253. FHA_dom.
    IPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    IPR008984. SMAD_FHA_domain.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view]
    PANTHERiPTHR12486. PTHR12486. 1 hit.
    PTHR12486:SF4. PTHR12486:SF4. 1 hit.
    SMARTiSM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    SUPFAMiSSF49879. SSF49879. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEiPS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view]

    Sequences (13)i

    Sequence statusi: Complete.

    This entry describes 13 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7Z2E3-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MSNVNLSVSD FWRVMMRVCW LVRQDSRHQR IRLPHLEAVV IGRGPETKIT    50
    DKKCSRQQVQ LKAECNKGYV KVKQVGVNPT SIDSVVIGKD QEVKLQPGQV 100
    LHMVNELYPY IVEFEEEAKN PGLETHRKRK RSGNSDSIER DAAQEAEAGT 150
    GLEPGSNSGQ CSVPLKKGKD APIKKESLGH WSQGLKISMQ DPKMQVYKDE 200
    QVVVIKDKYP KARYHWLVLP WTSISSLKAV AREHLELLKH MHTVGEKVIV 250
    DFAGSSKLRF RLGYHAIPSM SHVHLHVISQ DFDSPCLKNK KHWNSFNTEY 300
    FLESQAVIEM VQEAGRVTVR DGMPELLKLP LRCHECQQLL PSIPQLKEHL 350
    RKHWTQ 356

    Note: Major form.

    Length:356
    Mass (Da):40,740
    Last modified:June 7, 2004 - v2
    Checksum:i5B338490E35EC8E4
    GO
    Isoform 2 (identifier: Q7Z2E3-2) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-188: Missing.

    Note: Minor form.

    Show »
    Length:168
    Mass (Da):19,715
    Checksum:i2AF4F98B97C0A76B
    GO
    Isoform 3 (identifier: Q7Z2E3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         104-175: Missing.

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:284
    Mass (Da):32,901
    Checksum:i4213615369B997A5
    GO
    Isoform 4 (identifier: Q7Z2E3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-102: Missing.

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:254
    Mass (Da):29,108
    Checksum:iB2338C3B2822B710
    GO
    Isoform 5 (identifier: Q7Z2E3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         59-112: Missing.

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:288
    Mass (Da):33,125
    Checksum:iAD5D2BD20A81EBD6
    GO
    Isoform 6 (identifier: Q7Z2E3-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-193: Missing.
         306-356: AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ → E

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:113
    Mass (Da):13,305
    Checksum:i5583AA4F55EDF41B
    GO
    Isoform 7 (identifier: Q7Z2E3-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.

    Show »
    Length:342
    Mass (Da):39,104
    Checksum:iC0D4FAEBF89ABA74
    GO
    Isoform 8 (identifier: Q7Z2E3-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         175-193: Missing.

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:337
    Mass (Da):38,589
    Checksum:iDC2FF196087D3ADB
    GO
    Isoform 9 (identifier: Q7Z2E3-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         306-356: AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ → E

    Note: No experimental confirmation available.

    Show »
    Length:292
    Mass (Da):33,294
    Checksum:i5802EE9F37B07600
    GO
    Isoform 10 (identifier: Q7Z2E3-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         59-112: Missing.

    Note: May be an aberrant isoform present in cancer cell lines.

    Show »
    Length:302
    Mass (Da):34,761
    Checksum:i4CAFA4C9BB2399EC
    GO
    Isoform 11 (identifier: Q7Z2E3-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         306-356: AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ → E

    Note: No experimental confirmation available.

    Show »
    Length:306
    Mass (Da):34,930
    Checksum:iAC5FCCDC3642F91B
    GO
    Isoform 12 (identifier: Q7Z2E3-12) [UniParc]FASTAAdd to Basket

    Also known as: LP2, LP2E5, LP2P3, LP2P3E5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         60-63: QLKA → ESRV
         64-356: Missing.

    Show »
    Length:49
    Mass (Da):5,828
    Checksum:iF731A5E3CB6C1C8A
    GO
    Isoform 13 (identifier: Q7Z2E3-13) [UniParc]FASTAAdd to Basket

    Also known as: LE5

    The sequence of this isoform differs from the canonical sequence as follows:
         1-14: Missing.
         196-356: VYKDEQVVVI...KEHLRKHWTQ → PCTSSCDQPGF

    Show »
    Length:192
    Mass (Da):21,389
    Checksum:i80F7BD34425AAA69
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti211 – 2111K → Q in AOA; it probably does not greatly affect the protein; heterozygous. 1 Publication
    VAR_018794
    Natural varianti212 – 2121A → V in AOA; heterozygous. 1 Publication
    VAR_018795
    Natural varianti213 – 2131R → H in AOA. 1 Publication
    Corresponds to variant rs150886026 [ dbSNP | Ensembl ].
    VAR_018796
    Natural varianti215 – 2151H → R in AOA. 1 Publication
    VAR_018797
    Natural varianti220 – 2201P → L in AOA. 2 Publications
    VAR_018798
    Natural varianti237 – 2371L → P in AOA. 1 Publication
    VAR_025365
    Natural varianti277 – 2771V → G in AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A. 2 Publications
    VAR_018799
    Natural varianti281 – 2811D → G in AOA; heterozygous.
    VAR_018800
    Natural varianti293 – 2931W → R in AOA; heterozygous. 1 Publication
    VAR_018801

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 193193Missing in isoform 6. 1 PublicationVSP_010534Add
    BLAST
    Alternative sequencei1 – 188188Missing in isoform 2. 4 PublicationsVSP_010535Add
    BLAST
    Alternative sequencei1 – 102102Missing in isoform 4. 3 PublicationsVSP_010536Add
    BLAST
    Alternative sequencei1 – 1414Missing in isoform 5, isoform 7, isoform 9, isoform 12 and isoform 13. 5 PublicationsVSP_010537Add
    BLAST
    Alternative sequencei59 – 11254Missing in isoform 5 and isoform 10. 2 PublicationsVSP_010538Add
    BLAST
    Alternative sequencei60 – 634QLKA → ESRV in isoform 12. 1 PublicationVSP_044091
    Alternative sequencei64 – 356293Missing in isoform 12. 1 PublicationVSP_044092Add
    BLAST
    Alternative sequencei104 – 17572Missing in isoform 3. 1 PublicationVSP_010539Add
    BLAST
    Alternative sequencei175 – 19319Missing in isoform 8. 1 PublicationVSP_010540Add
    BLAST
    Alternative sequencei196 – 356161VYKDE…KHWTQ → PCTSSCDQPGF in isoform 13. 1 PublicationVSP_044093Add
    BLAST
    Alternative sequencei306 – 35651AVIEM…KHWTQ → E in isoform 6, isoform 9 and isoform 11. 3 PublicationsVSP_010541Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY302067 mRNA. Translation: AAQ74130.1.
    AY302068 mRNA. Translation: AAQ74131.1.
    AY302070 mRNA. Translation: AAQ74133.1.
    AY302071 mRNA. Translation: AAQ74134.1.
    AY302072 mRNA. Translation: AAQ74135.1.
    AY302074 mRNA. Translation: AAQ74137.1.
    AY040777 mRNA. Translation: AAK91768.1.
    AY208829 mRNA. Translation: AAP86319.1.
    AY208830 mRNA. Translation: AAP86320.1.
    AY208831 mRNA. Translation: AAP86321.1.
    AY208832 mRNA. Translation: AAP86322.1.
    AY208833 mRNA. Translation: AAP86323.1.
    AY208834 mRNA. Translation: AAP86324.1.
    AY208835 mRNA. Translation: AAP86325.1.
    AY208836 mRNA. Translation: AAP86326.1.
    AY208837 mRNA. Translation: AAP86327.1.
    AY208838 mRNA. Translation: AAP86328.1.
    AY208839 mRNA. Translation: AAP86329.1.
    AY208840 mRNA. Translation: AAP86330.1.
    AY208841 mRNA. Translation: AAP86331.1.
    AY208842 mRNA. Translation: AAP86332.1.
    AK000164 mRNA. Translation: BAA90985.1.
    AK055672 mRNA. Translation: BAG51552.1.
    BX538161 mRNA. Translation: CAD98041.1.
    AL162590, AL353717 Genomic DNA. Translation: CAI15549.1.
    AL162590, AL353717 Genomic DNA. Translation: CAI15551.1.
    AL353717, AL162590 Genomic DNA. Translation: CAI15728.1.
    AL353717, AL162590 Genomic DNA. Translation: CAI15730.1.
    AL353717 Genomic DNA. Translation: CAI15734.1.
    AL353717 Genomic DNA. Translation: CAI15735.1.
    CH471071 Genomic DNA. Translation: EAW58530.1.
    CH471071 Genomic DNA. Translation: EAW58529.1.
    CH471071 Genomic DNA. Translation: EAW58531.1.
    CH471071 Genomic DNA. Translation: EAW58532.1.
    CH471071 Genomic DNA. Translation: EAW58534.1.
    CH471071 Genomic DNA. Translation: EAW58535.1.
    BC001628 mRNA. Translation: AAH01628.1.
    BC032650 mRNA. Translation: AAH32650.1.
    BC104881 mRNA. Translation: AAI04882.1.
    AJ565850 mRNA. Translation: CAD92454.1.
    AJ565851 mRNA. Translation: CAD92455.1.
    AJ565852 mRNA. Translation: CAD92456.1.
    AJ565853 mRNA. Translation: CAD92457.1.
    AJ565854 mRNA. Translation: CAD92458.1.
    AJ565855 mRNA. Translation: CAD92459.1.
    AJ575566 mRNA. Translation: CAE01427.1.
    CCDSiCCDS47956.1. [Q7Z2E3-7]
    CCDS56568.1. [Q7Z2E3-10]
    CCDS6532.1. [Q7Z2E3-11]
    RefSeqiNP_001182177.1. NM_001195248.1. [Q7Z2E3-1]
    NP_001182178.1. NM_001195249.1. [Q7Z2E3-7]
    NP_001182179.1. NM_001195250.1. [Q7Z2E3-10]
    NP_001182180.1. NM_001195251.1. [Q7Z2E3-9]
    NP_001182181.1. NM_001195252.1. [Q7Z2E3-3]
    NP_001182183.1. NM_001195254.1. [Q7Z2E3-5]
    NP_778239.1. NM_175069.2. [Q7Z2E3-11]
    NP_778243.1. NM_175073.2. [Q7Z2E3-7]
    XP_006716854.1. XM_006716791.1. [Q7Z2E3-7]
    XP_006716855.1. XM_006716792.1. [Q7Z2E3-4]
    UniGeneiHs.20158.

    Genome annotation databases

    EnsembliENST00000309615; ENSP00000311547; ENSG00000137074. [Q7Z2E3-11]
    ENST00000379813; ENSP00000369141; ENSG00000137074. [Q7Z2E3-7]
    ENST00000379817; ENSP00000369145; ENSG00000137074. [Q7Z2E3-7]
    ENST00000379819; ENSP00000369147; ENSG00000137074. [Q7Z2E3-1]
    ENST00000379825; ENSP00000369153; ENSG00000137074. [Q7Z2E3-11]
    ENST00000397172; ENSP00000380357; ENSG00000137074. [Q7Z2E3-3]
    ENST00000436040; ENSP00000400806; ENSG00000137074. [Q7Z2E3-13]
    ENST00000460940; ENSP00000418311; ENSG00000137074. [Q7Z2E3-12]
    ENST00000463596; ENSP00000419846; ENSG00000137074. [Q7Z2E3-7]
    ENST00000467331; ENSP00000418733; ENSG00000137074. [Q7Z2E3-12]
    ENST00000468275; ENSP00000420263; ENSG00000137074. [Q7Z2E3-7]
    ENST00000472896; ENSP00000417804; ENSG00000137074. [Q7Z2E3-12]
    ENST00000476858; ENSP00000419042; ENSG00000137074. [Q7Z2E3-10]
    ENST00000479656; ENSP00000420071; ENSG00000137074. [Q7Z2E3-12]
    ENST00000482687; ENSP00000419289; ENSG00000137074. [Q7Z2E3-13]
    ENST00000485479; ENSP00000418144; ENSG00000137074. [Q7Z2E3-12]
    ENST00000494649; ENSP00000417634; ENSG00000137074. [Q7Z2E3-12]
    ENST00000495360; ENSP00000419623; ENSG00000137074. [Q7Z2E3-12]
    GeneIDi54840.
    KEGGihsa:54840.
    UCSCiuc003zrj.3. human. [Q7Z2E3-1]
    uc003zrl.3. human. [Q7Z2E3-2]
    uc003zrr.3. human. [Q7Z2E3-5]
    uc003zru.3. human. [Q7Z2E3-10]
    uc003zrv.3. human. [Q7Z2E3-11]
    uc003zrw.3. human. [Q7Z2E3-3]
    uc003zrx.3. human. [Q7Z2E3-9]

    Polymorphism databases

    DMDMi48428038.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY302067 mRNA. Translation: AAQ74130.1 .
    AY302068 mRNA. Translation: AAQ74131.1 .
    AY302070 mRNA. Translation: AAQ74133.1 .
    AY302071 mRNA. Translation: AAQ74134.1 .
    AY302072 mRNA. Translation: AAQ74135.1 .
    AY302074 mRNA. Translation: AAQ74137.1 .
    AY040777 mRNA. Translation: AAK91768.1 .
    AY208829 mRNA. Translation: AAP86319.1 .
    AY208830 mRNA. Translation: AAP86320.1 .
    AY208831 mRNA. Translation: AAP86321.1 .
    AY208832 mRNA. Translation: AAP86322.1 .
    AY208833 mRNA. Translation: AAP86323.1 .
    AY208834 mRNA. Translation: AAP86324.1 .
    AY208835 mRNA. Translation: AAP86325.1 .
    AY208836 mRNA. Translation: AAP86326.1 .
    AY208837 mRNA. Translation: AAP86327.1 .
    AY208838 mRNA. Translation: AAP86328.1 .
    AY208839 mRNA. Translation: AAP86329.1 .
    AY208840 mRNA. Translation: AAP86330.1 .
    AY208841 mRNA. Translation: AAP86331.1 .
    AY208842 mRNA. Translation: AAP86332.1 .
    AK000164 mRNA. Translation: BAA90985.1 .
    AK055672 mRNA. Translation: BAG51552.1 .
    BX538161 mRNA. Translation: CAD98041.1 .
    AL162590 , AL353717 Genomic DNA. Translation: CAI15549.1 .
    AL162590 , AL353717 Genomic DNA. Translation: CAI15551.1 .
    AL353717 , AL162590 Genomic DNA. Translation: CAI15728.1 .
    AL353717 , AL162590 Genomic DNA. Translation: CAI15730.1 .
    AL353717 Genomic DNA. Translation: CAI15734.1 .
    AL353717 Genomic DNA. Translation: CAI15735.1 .
    CH471071 Genomic DNA. Translation: EAW58530.1 .
    CH471071 Genomic DNA. Translation: EAW58529.1 .
    CH471071 Genomic DNA. Translation: EAW58531.1 .
    CH471071 Genomic DNA. Translation: EAW58532.1 .
    CH471071 Genomic DNA. Translation: EAW58534.1 .
    CH471071 Genomic DNA. Translation: EAW58535.1 .
    BC001628 mRNA. Translation: AAH01628.1 .
    BC032650 mRNA. Translation: AAH32650.1 .
    BC104881 mRNA. Translation: AAI04882.1 .
    AJ565850 mRNA. Translation: CAD92454.1 .
    AJ565851 mRNA. Translation: CAD92455.1 .
    AJ565852 mRNA. Translation: CAD92456.1 .
    AJ565853 mRNA. Translation: CAD92457.1 .
    AJ565854 mRNA. Translation: CAD92458.1 .
    AJ565855 mRNA. Translation: CAD92459.1 .
    AJ575566 mRNA. Translation: CAE01427.1 .
    CCDSi CCDS47956.1. [Q7Z2E3-7 ]
    CCDS56568.1. [Q7Z2E3-10 ]
    CCDS6532.1. [Q7Z2E3-11 ]
    RefSeqi NP_001182177.1. NM_001195248.1. [Q7Z2E3-1 ]
    NP_001182178.1. NM_001195249.1. [Q7Z2E3-7 ]
    NP_001182179.1. NM_001195250.1. [Q7Z2E3-10 ]
    NP_001182180.1. NM_001195251.1. [Q7Z2E3-9 ]
    NP_001182181.1. NM_001195252.1. [Q7Z2E3-3 ]
    NP_001182183.1. NM_001195254.1. [Q7Z2E3-5 ]
    NP_778239.1. NM_175069.2. [Q7Z2E3-11 ]
    NP_778243.1. NM_175073.2. [Q7Z2E3-7 ]
    XP_006716854.1. XM_006716791.1. [Q7Z2E3-7 ]
    XP_006716855.1. XM_006716792.1. [Q7Z2E3-4 ]
    UniGenei Hs.20158.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3KT9 X-ray 1.65 A 15-116 [» ]
    4NDF X-ray 1.94 A/B 179-356 [» ]
    4NDG X-ray 2.54 A/B 179-356 [» ]
    4NDH X-ray 1.85 A/B 179-356 [» ]
    4NDI X-ray 1.90 A/B 179-356 [» ]
    ProteinModelPortali Q7Z2E3.
    SMRi Q7Z2E3. Positions 15-116, 178-354.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120191. 22 interactions.
    IntActi Q7Z2E3. 16 interactions.
    MINTi MINT-1205251.

    PTM databases

    PhosphoSitei Q7Z2E3.

    Polymorphism databases

    DMDMi 48428038.

    Proteomic databases

    MaxQBi Q7Z2E3.
    PaxDbi Q7Z2E3.
    PRIDEi Q7Z2E3.

    Protocols and materials databases

    DNASUi 54840.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309615 ; ENSP00000311547 ; ENSG00000137074 . [Q7Z2E3-11 ]
    ENST00000379813 ; ENSP00000369141 ; ENSG00000137074 . [Q7Z2E3-7 ]
    ENST00000379817 ; ENSP00000369145 ; ENSG00000137074 . [Q7Z2E3-7 ]
    ENST00000379819 ; ENSP00000369147 ; ENSG00000137074 . [Q7Z2E3-1 ]
    ENST00000379825 ; ENSP00000369153 ; ENSG00000137074 . [Q7Z2E3-11 ]
    ENST00000397172 ; ENSP00000380357 ; ENSG00000137074 . [Q7Z2E3-3 ]
    ENST00000436040 ; ENSP00000400806 ; ENSG00000137074 . [Q7Z2E3-13 ]
    ENST00000460940 ; ENSP00000418311 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000463596 ; ENSP00000419846 ; ENSG00000137074 . [Q7Z2E3-7 ]
    ENST00000467331 ; ENSP00000418733 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000468275 ; ENSP00000420263 ; ENSG00000137074 . [Q7Z2E3-7 ]
    ENST00000472896 ; ENSP00000417804 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000476858 ; ENSP00000419042 ; ENSG00000137074 . [Q7Z2E3-10 ]
    ENST00000479656 ; ENSP00000420071 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000482687 ; ENSP00000419289 ; ENSG00000137074 . [Q7Z2E3-13 ]
    ENST00000485479 ; ENSP00000418144 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000494649 ; ENSP00000417634 ; ENSG00000137074 . [Q7Z2E3-12 ]
    ENST00000495360 ; ENSP00000419623 ; ENSG00000137074 . [Q7Z2E3-12 ]
    GeneIDi 54840.
    KEGGi hsa:54840.
    UCSCi uc003zrj.3. human. [Q7Z2E3-1 ]
    uc003zrl.3. human. [Q7Z2E3-2 ]
    uc003zrr.3. human. [Q7Z2E3-5 ]
    uc003zru.3. human. [Q7Z2E3-10 ]
    uc003zrv.3. human. [Q7Z2E3-11 ]
    uc003zrw.3. human. [Q7Z2E3-3 ]
    uc003zrx.3. human. [Q7Z2E3-9 ]

    Organism-specific databases

    CTDi 54840.
    GeneCardsi GC09M032962.
    GeneReviewsi APTX.
    HGNCi HGNC:15984. APTX.
    HPAi HPA055545.
    MIMi 208920. phenotype.
    606350. gene.
    neXtProti NX_Q7Z2E3.
    Orphaneti 1168. Ataxia - oculomotor apraxia type 1.
    PharmGKBi PA24915.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG278510.
    HOGENOMi HOG000248858.
    HOVERGENi HBG050555.
    InParanoidi Q7Z2E3.
    KOi K10863.
    OMAi PGQVLHM.
    OrthoDBi EOG786H3J.
    PhylomeDBi Q7Z2E3.
    TreeFami TF313308.

    Enzyme and pathway databases

    SABIO-RK Q7Z2E3.

    Miscellaneous databases

    EvolutionaryTracei Q7Z2E3.
    GeneWikii Aprataxin.
    GenomeRNAii 54840.
    NextBioi 57644.
    PROi Q7Z2E3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q7Z2E3.
    Bgeei Q7Z2E3.
    CleanExi HS_APTX.
    Genevestigatori Q7Z2E3.

    Family and domain databases

    Gene3Di 2.60.200.20. 2 hits.
    3.30.428.10. 1 hit.
    InterProi IPR026963. Aprataxin.
    IPR000253. FHA_dom.
    IPR019808. Histidine_triad_CS.
    IPR001310. Histidine_triad_HIT.
    IPR011146. HIT-like.
    IPR008984. SMAD_FHA_domain.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    [Graphical view ]
    PANTHERi PTHR12486. PTHR12486. 1 hit.
    PTHR12486:SF4. PTHR12486:SF4. 1 hit.
    SMARTi SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49879. SSF49879. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEi PS00892. HIT_1. 1 hit.
    PS51084. HIT_2. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Novel splice variants increase molecular diversity of aprataxin, the gene responsible for early-onset ataxia with ocular motor apraxia and hypoalbuminemia."
      Hirano M., Nishiwaki T., Kariya S., Furiya Y., Kawahara M., Ueno S.
      Neurosci. Lett. 366:120-125(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 12 AND 13), ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
    2. "Identification of FHA-HIT as a novel nuclear protein involved in cell-cycle regulation."
      Huang C.-H.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Chen Y., Huang C.-H.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 10).
      Tissue: Hypothalamus, Kidney, Lung adenocarcinoma, Lymphoma, Melanoma, Muscle, Retinoblastoma, Skin and Testis.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 11).
      Tissue: Colon.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 9).
      Tissue: Endometrium.
    6. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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] (ISOFORMS 2; 4 AND 7).
      Tissue: Brain, Lung and Lymph.
    9. "Mutations in the APTX gene."
      Hellenbroich Y., Habeck M.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-261 (ISOFORMS 2; 4; 5 AND 7).
      Tissue: Brain.
    10. "Early-onset ataxia with ocular motor apraxia and hypoalbuminemia is caused by mutations in a new HIT superfamily gene."
      Date H., Onodera O., Tanaka H., Iwabuchi K., Uekawa K., Igarashi S., Koike R., Hiroi T., Yuasa T., Awaya Y., Sakai T., Takahashi T., Nagatomo H., Sekijima Y., Kawachi I., Takiyama Y., Nishizawa M., Fukuhara N.
      , Saito K., Sugano S., Tsuji S.
      Nat. Genet. 29:184-188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, VARIANTS AOA LEU-220 AND GLY-277.
    11. Cited for: ALTERNATIVE SPLICING, TISSUE SPECIFICITY, VARIANTS AOA HIS-213 AND LEU-220.
    12. "Aprataxin, the causative protein for EAOH is a nuclear protein with a potential role as a DNA repair protein."
      Sano Y., Date H., Igarashi S., Onodera O., Oyake M., Takahashi T., Hayashi S., Morimatsu M., Takahashi H., Makifuchi T., Fukuhara N., Tsuji S.
      Ann. Neurol. 55:241-249(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH XRCC1.
    13. "The ataxia-oculomotor apraxia 1 gene product has a role distinct from ATM and interacts with the DNA strand break repair proteins XRCC1 and XRCC4."
      Clements P.M., Breslin C., Deeks E.D., Byrd P.J., Ju L., Bieganowski P., Brenner C., Moreira M.-C., Taylor A.M.R., Caldecott K.W.
      DNA Repair 3:1493-1502(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XRCC1 AND XRCC4, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-43.
    14. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH XRCC1; ADPRT; TP53 AND NCL.
    15. "Nucleolar localization of aprataxin is dependent on interaction with nucleolin and on active ribosomal DNA transcription."
      Becherel O.J., Gueven N., Birrell G.W., Schreiber V., Suraweera A., Jakob B., Taucher-Scholz G., Lavin M.F.
      Hum. Mol. Genet. 15:2239-2249(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH XRCC1 AND NCL.
    16. "Aprataxin forms a discrete branch in the HIT (histidine triad) superfamily of proteins with both DNA/RNA binding and nucleotide hydrolase activities."
      Kijas A.W., Harris J.L., Harris J.M., Lavin M.F.
      J. Biol. Chem. 281:13939-13948(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING, CHARACTERIZATION OF VARIANT GLY-277.
    17. "The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates."
      Ahel I., Rass U., El-Khamisy S.F., Katyal S., Clements P.M., McKinnon P.J., Caldecott K.W., West S.C.
      Nature 443:713-716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-274.
    18. "Actions of aprataxin in multiple DNA repair pathways."
      Rass U., Ahel I., West S.C.
      J. Biol. Chem. 282:9469-9474(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-274; CYS-333 AND CYS-336.
    19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 15-116, SUBCELLULAR LOCATION, INTERACTION WITH MDC1, MUTAGENESIS OF ARG-43 AND LYS-52.
    21. "Early-onset ataxia with ocular motor apraxia and hypoalbuminemia: the aprataxin gene mutations."
      Shimazaki H., Takiyama Y., Sakoe K., Ikeguchi K., Niijima K., Kaneko J., Namekawa M., Ogawa T., Date H., Tsuji S., Nakano I., Nishizawa M.
      Neurology 59:590-595(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AOA ARG-215.
    22. "Phenotypic variability of aprataxin gene mutations."
      Tranchant C., Fleury M., Moreira M.-C., Koenig M., Warter J.-M.
      Neurology 60:868-870(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT AOA GLN-211.
    23. Cited for: VARIANTS AOA VAL-212; GLY-277 AND ARG-293.
    24. Cited for: VARIANT AOA PRO-237.
    25. "Coenzyme Q deficiency and cerebellar ataxia associated with an aprataxin mutation."
      Quinzii C.M., Kattah A.G., Naini A., Akman H.O., Mootha V.K., DiMauro S., Hirano M.
      Neurology 64:539-541(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN AOA.

    Entry informationi

    Entry nameiAPTX_HUMAN
    AccessioniPrimary (citable) accession number: Q7Z2E3
    Secondary accession number(s): A8MTN4
    , D3DRK9, D3DRL0, Q0P662, Q5T781, Q5T782, Q5T784, Q6JV81, Q6JV82, Q6JV85, Q7Z2F3, Q7Z336, Q7Z5R5, Q7Z6V7, Q7Z6V8, Q9NXM5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 121 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3