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Q7TQC5

- APTX_MOUSE

UniProt

Q7TQC5 - APTX_MOUSE

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Protein

Aprataxin

Gene

Aptx

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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: Ensembl
  3. nucleoplasm Source: MGI
Complete GO annotation...

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

MaxQBiQ7TQC5.
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.
ExpressionAtlasiQ7TQC5. baseline and differential.
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.
InParanoidiQ7TQC5.
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

        10         20         30         40         50
MPEAVAKMRV CWLVRQDSRH QRIKLPHLEA VVIGRSPETK ITDKKCSRQQ
60 70 80 90 100
VQLKAECNKG YVKVQQMGVN PTSIDSGVIG KDQEKKLLPG QVLHMVNGLY
110 120 130 140 150
PYIVEFEEVA ESPNLTQRKR KRSDCDSEEM EAESGTGLAP GSSPSQCSVS
160 170 180 190 200
PKKDKNGATK KESLGHWSQG LKMSMKDPKM QVYKDDQVVV IKDKYPKARH
210 220 230 240 250
HWLVLPWASI SSLKVVTSEH LELLKHMHAV GEKVIADFAG SSKLRFRLGY
260 270 280 290 300
HAIPSMSHVH LHVISQDFDS PCLKNKKHWN SFNTEYFLES QAVIKMVQEA
310 320 330 340
GRVTVKDGTC ELLKLPLRCH ECQQLLPSIP QLKEHLRKHW GG
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. Curated

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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

MaxQBi Q7TQC5.
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.
InParanoidi Q7TQC5.
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.
ExpressionAtlasi Q7TQC5. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 100 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