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Q7TQC5

- APTX_MOUSE

UniProt

Q7TQC5 - APTX_MOUSE

Protein

Aprataxin

Gene

Aptx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (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.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei260 – 2601Tele-AMP-histidine intermediateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri317 – 33923C2H2-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: Ensembl
    2. damaged DNA binding Source: Ensembl
    3. DNA 5'-adenosine monophosphate hydrolase activity Source: UniProtKB
    4. double-stranded DNA binding Source: Ensembl
    5. double-stranded RNA binding Source: Ensembl
    6. metal ion binding Source: MGI
    7. phosphoglycolate phosphatase activity Source: Ensembl
    8. polynucleotide 3'-phosphatase activity Source: Ensembl

    GO - Biological processi

    1. DNA catabolic process, exonucleolytic Source: GOC
    2. DNA ligation Source: MGI
    3. double-strand break repair Source: Ensembl
    4. regulation of protein stability Source: Ensembl
    5. response to hydrogen peroxide Source: Ensembl
    6. single strand break repair Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1913658. Aptx.

    Subcellular locationi

    Nucleusnucleoplasm By similarity. Nucleusnucleolus By similarity
    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 By similarity.By similarity

    GO - Cellular componenti

    1. nuclear chromatin Source: Ensembl
    2. nucleolus Source: UniProtKB-SubCell
    3. nucleoplasm Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 342342AprataxinPRO_0000109840Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei123 – 1231PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiQ7TQC5.

    PTM databases

    PhosphoSiteiQ7TQC5.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in heart, liver, kidney, spleen, lung, muscle, brain stem, spinal cord, cerebellum and brain.1 Publication

    Gene expression databases

    BgeeiQ7TQC5.
    CleanExiMM_APTX.
    GenevestigatoriQ7TQC5.

    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) By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ7TQC5.
    SMRiQ7TQC5. Positions 8-108, 164-340.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 7950FHA-likeAdd
    BLAST
    Domaini168 – 273106HITPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 102102Interactions with ADPRT and NCLBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi118 – 1225Nuclear localization signalBy similarity
    Motifi258 – 2625Histidine 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.By similarity
    The HIT domain is required for enzymatic activity.By similarity
    The C2H2-type zinc finger mediates DNA-binding.By similarity

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri317 – 33923C2H2-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiNOG278510.
    GeneTreeiENSGT00570000079163.
    HOGENOMiHOG000248858.
    HOVERGENiHBG050555.
    KOiK10863.
    OMAiPGQVLHM.
    OrthoDBiEOG786H3J.
    PhylomeDBiQ7TQC5.
    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.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q7TQC5-1) [UniParc]FASTAAdd to Basket

    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

    MPEAVAKMRV CWLVRQDSRH QRIKLPHLEA VVIGRSPETK ITDKKCSRQQ    50
    VQLKAECNKG YVKVQQMGVN PTSIDSGVIG KDQEKKLLPG QVLHMVNGLY 100
    PYIVEFEEVA ESPNLTQRKR KRSDCDSEEM EAESGTGLAP GSSPSQCSVS 150
    PKKDKNGATK KESLGHWSQG LKMSMKDPKM QVYKDDQVVV IKDKYPKARH 200
    HWLVLPWASI SSLKVVTSEH LELLKHMHAV GEKVIADFAG SSKLRFRLGY 250
    HAIPSMSHVH LHVISQDFDS PCLKNKKHWN SFNTEYFLES QAVIKMVQEA 300
    GRVTVKDGTC ELLKLPLRCH ECQQLLPSIP QLKEHLRKHW GG 342
    Length:342
    Mass (Da):38,723
    Last modified:June 7, 2004 - v2
    Checksum:iA8D77F2F4B362F03
    GO
    Isoform 2 (identifier: Q7TQC5-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-66: Missing.

    Show »
    Length:276
    Mass (Da):31,069
    Checksum:i702802B5C6C13764
    GO
    Isoform 3 (identifier: Q7TQC5-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: Missing.

    Show »
    Length:335
    Mass (Da):37,996
    Checksum:iB952BC82C02F6F54
    GO
    Isoform 4 (identifier: Q7TQC5-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-7: Missing.
         67-161: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:240
    Mass (Da):27,776
    Checksum:i4E2AD21F447B2E87
    GO

    Sequence cautioni

    The sequence AAP86334.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti86 – 861K → L in AAH21872. (PubMed:15489334)Curated
    Sequence conflicti237 – 2371D → E in AAH21872. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6666Missing in isoform 2. 1 PublicationVSP_010542Add
    BLAST
    Alternative sequencei1 – 77Missing in isoform 3 and isoform 4. 2 PublicationsVSP_010543
    Alternative sequencei67 – 16195Missing in isoform 4. 1 PublicationVSP_010544Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040780 mRNA. Translation: AAK91771.1.
    AY040782 Genomic DNA. Translation: AAK91773.1.
    AY208844 mRNA. Translation: AAP86334.1. Different initiation.
    AK005286 mRNA. Translation: BAB23933.2.
    AK010516 mRNA. Translation: BAB26998.2.
    AK077351 mRNA. Translation: BAC36763.1.
    AK088928 mRNA. Translation: BAC40657.1.
    BC021872 mRNA. Translation: AAH21872.2.
    CCDSiCCDS38711.1. [Q7TQC5-1]
    CCDS38712.1. [Q7TQC5-3]
    RefSeqiNP_001020615.1. NM_001025444.3. [Q7TQC5-3]
    NP_001020616.1. NM_001025445.2. [Q7TQC5-2]
    NP_079821.3. NM_025545.4. [Q7TQC5-1]
    XP_006538229.1. XM_006538166.1. [Q7TQC5-3]
    XP_006538230.1. XM_006538167.1. [Q7TQC5-3]
    XP_006538231.1. XM_006538168.1. [Q7TQC5-3]
    XP_006538232.1. XM_006538169.1. [Q7TQC5-3]
    XP_006538233.1. XM_006538170.1. [Q7TQC5-3]
    XP_006538234.1. XM_006538171.1. [Q7TQC5-2]
    UniGeneiMm.430710.

    Genome annotation databases

    EnsembliENSMUST00000030119; ENSMUSP00000030119; ENSMUSG00000028411. [Q7TQC5-3]
    ENSMUST00000068125; ENSMUSP00000124264; ENSMUSG00000028411. [Q7TQC5-1]
    ENSMUST00000108103; ENSMUSP00000103738; ENSMUSG00000028411. [Q7TQC5-4]
    GeneIDi66408.
    KEGGimmu:66408.
    UCSCiuc008sho.1. mouse. [Q7TQC5-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040780 mRNA. Translation: AAK91771.1 .
    AY040782 Genomic DNA. Translation: AAK91773.1 .
    AY208844 mRNA. Translation: AAP86334.1 . Different initiation.
    AK005286 mRNA. Translation: BAB23933.2 .
    AK010516 mRNA. Translation: BAB26998.2 .
    AK077351 mRNA. Translation: BAC36763.1 .
    AK088928 mRNA. Translation: BAC40657.1 .
    BC021872 mRNA. Translation: AAH21872.2 .
    CCDSi CCDS38711.1. [Q7TQC5-1 ]
    CCDS38712.1. [Q7TQC5-3 ]
    RefSeqi NP_001020615.1. NM_001025444.3. [Q7TQC5-3 ]
    NP_001020616.1. NM_001025445.2. [Q7TQC5-2 ]
    NP_079821.3. NM_025545.4. [Q7TQC5-1 ]
    XP_006538229.1. XM_006538166.1. [Q7TQC5-3 ]
    XP_006538230.1. XM_006538167.1. [Q7TQC5-3 ]
    XP_006538231.1. XM_006538168.1. [Q7TQC5-3 ]
    XP_006538232.1. XM_006538169.1. [Q7TQC5-3 ]
    XP_006538233.1. XM_006538170.1. [Q7TQC5-3 ]
    XP_006538234.1. XM_006538171.1. [Q7TQC5-2 ]
    UniGenei Mm.430710.

    3D structure databases

    ProteinModelPortali Q7TQC5.
    SMRi Q7TQC5. Positions 8-108, 164-340.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q7TQC5.

    Proteomic databases

    PRIDEi Q7TQC5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030119 ; ENSMUSP00000030119 ; ENSMUSG00000028411 . [Q7TQC5-3 ]
    ENSMUST00000068125 ; ENSMUSP00000124264 ; ENSMUSG00000028411 . [Q7TQC5-1 ]
    ENSMUST00000108103 ; ENSMUSP00000103738 ; ENSMUSG00000028411 . [Q7TQC5-4 ]
    GeneIDi 66408.
    KEGGi mmu:66408.
    UCSCi uc008sho.1. mouse. [Q7TQC5-1 ]

    Organism-specific databases

    CTDi 54840.
    MGIi MGI:1913658. Aptx.

    Phylogenomic databases

    eggNOGi NOG278510.
    GeneTreei ENSGT00570000079163.
    HOGENOMi HOG000248858.
    HOVERGENi HBG050555.
    KOi K10863.
    OMAi PGQVLHM.
    OrthoDBi EOG786H3J.
    PhylomeDBi Q7TQC5.
    TreeFami TF313308.

    Miscellaneous databases

    NextBioi 321599.
    PROi Q7TQC5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q7TQC5.
    CleanExi MM_APTX.
    Genevestigatori Q7TQC5.

    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.
    PS50157. ZINC_FINGER_C2H2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 [GENOMIC DNA / MRNA] (ISOFORM 1).
      Strain: BALB/c and C57BL/6J.
    2. "Differential polyadenylation of mouse FHA-HIT transcript."
      Chen Y., Huang C.-H.
      Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
      Strain: C57BL/6J and NOD.
      Tissue: Cerebellum, Embryonic stem cell, Pituitary and Thymus.
    4. "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] (ISOFORM 3).
      Strain: Czech II.
      Tissue: Mammary tumor.
    5. Cited for: TISSUE SPECIFICITY.
    6. "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.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiAPTX_MOUSE
    AccessioniPrimary (citable) accession number: Q7TQC5
    Secondary accession number(s): Q8BPA7
    , Q8C2B5, Q8K3D1, Q9CQ59
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 99 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3