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Q7TQC5 (APTX_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aprataxin

EC=3.-.-.-
Alternative name(s):
Forkhead-associated domain histidine triad-like protein
Short name=FHA-HIT
Gene names
Name:Aptx
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6

Subunit structure

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.

Subcellular location

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.

Tissue specificity

Widely expressed. Expressed in heart, liver, kidney, spleen, lung, muscle, brain stem, spinal cord, cerebellum and brain. Ref.5

Domain

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 similarities

Contains 1 C2H2-type zinc finger.

Contains 1 FHA-like domain.

Contains 1 HIT domain.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, exonucleolytic

Inferred from mutant phenotype Ref.6. Source: GOC

DNA ligation

Inferred from direct assay Ref.6. Source: MGI

double-strand break repair

Inferred from electronic annotation. Source: Ensembl

regulation of protein stability

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

single strand break repair

Inferred from mutant phenotype Ref.6. Source: UniProtKB

   Cellular_componentnuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement Ref.5. Source: MGI

   Molecular_functionDNA 5'-adenosine monophosphate hydrolase activity

Inferred from mutant phenotype Ref.6. Source: UniProtKB

chromatin binding

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

double-stranded RNA binding

Inferred from electronic annotation. Source: Ensembl

metal ion binding

Traceable author statement Ref.5. Source: MGI

phosphoglycolate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

polynucleotide 3'-phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7TQC5-1)

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.
Isoform 2 (identifier: Q7TQC5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.
Isoform 3 (identifier: Q7TQC5-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
Isoform 4 (identifier: Q7TQC5-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-7: Missing.
     67-161: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Aprataxin
PRO_0000109840

Regions

Domain30 – 7950FHA-like
Domain168 – 273106HIT
Zinc finger317 – 33923C2H2-type
Region1 – 102102Interactions with ADPRT and NCL By similarity
Motif118 – 1225Nuclear localization signal By similarity
Motif258 – 2625Histidine triad motif

Sites

Active site2601Tele-AMP-histidine intermediate By similarity

Amino acid modifications

Modified residue1231Phosphoserine By similarity

Natural variations

Alternative sequence1 – 6666Missing in isoform 2.
VSP_010542
Alternative sequence1 – 77Missing in isoform 3 and isoform 4.
VSP_010543
Alternative sequence67 – 16195Missing in isoform 4.
VSP_010544

Experimental info

Sequence conflict861K → L in AAH21872. Ref.4
Sequence conflict2371D → E in AAH21872. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: A8D77F2F4B362F03

FASTA34238,723
        10         20         30         40         50         60 
MPEAVAKMRV CWLVRQDSRH QRIKLPHLEA VVIGRSPETK ITDKKCSRQQ VQLKAECNKG 

        70         80         90        100        110        120 
YVKVQQMGVN PTSIDSGVIG KDQEKKLLPG QVLHMVNGLY PYIVEFEEVA ESPNLTQRKR 

       130        140        150        160        170        180 
KRSDCDSEEM EAESGTGLAP GSSPSQCSVS PKKDKNGATK KESLGHWSQG LKMSMKDPKM 

       190        200        210        220        230        240 
QVYKDDQVVV IKDKYPKARH HWLVLPWASI SSLKVVTSEH LELLKHMHAV GEKVIADFAG 

       250        260        270        280        290        300 
SSKLRFRLGY HAIPSMSHVH LHVISQDFDS PCLKNKKHWN SFNTEYFLES QAVIKMVQEA 

       310        320        330        340 
GRVTVKDGTC ELLKLPLRCH ECQQLLPSIP QLKEHLRKHW GG 

« Hide

Isoform 2 [UniParc].

Checksum: 702802B5C6C13764
Show »

FASTA27631,069
Isoform 3 [UniParc].

Checksum: B952BC82C02F6F54
Show »

FASTA33537,996
Isoform 4 [UniParc].

Checksum: 4E2AD21F447B2E87
Show »

FASTA24027,776

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The gene mutated in ataxia-ocular apraxia 1 encodes the new HIT/Zn-finger protein aprataxin."
Moreira M.-C., Barbot C., Tachi N., Kozuka N., Uchida E., Gibson T., Mendonca P., Costa M., Barros J., Yanagisawa T., Watanabe M., Ikeda Y., Aoki M., Nagata T., Coutinho P., Sequeiros J., Koenig M.
Nat. Genet. 29:189-193(2001) [PubMed] [Europe PMC] [Abstract]
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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001020615.1. NM_001025444.3.
NP_001020616.1. NM_001025445.2.
NP_079821.3. NM_025545.4.
XP_006538229.1. XM_006538166.1.
XP_006538230.1. XM_006538167.1.
XP_006538231.1. XM_006538168.1.
XP_006538232.1. XM_006538169.1.
XP_006538233.1. XM_006538170.1.
XP_006538234.1. XM_006538171.1.
UniGeneMm.430710.

3D structure databases

ProteinModelPortalQ7TQC5.
SMRQ7TQC5. Positions 8-108, 171-340.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ7TQC5.

Proteomic databases

PRIDEQ7TQC5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000030119; ENSMUSP00000030119; ENSMUSG00000028411. [Q7TQC5-3]
ENSMUST00000068125; ENSMUSP00000124264; ENSMUSG00000028411. [Q7TQC5-1]
ENSMUST00000108103; ENSMUSP00000103738; ENSMUSG00000028411. [Q7TQC5-4]
GeneID66408.
KEGGmmu:66408.
UCSCuc008sho.1. mouse. [Q7TQC5-1]

Organism-specific databases

CTD54840.
MGIMGI:1913658. Aptx.

Phylogenomic databases

eggNOGNOG278510.
GeneTreeENSGT00570000079163.
HOGENOMHOG000248858.
HOVERGENHBG050555.
KOK10863.
OMAPGQVLHM.
OrthoDBEOG786H3J.
PhylomeDBQ7TQC5.
TreeFamTF313308.

Gene expression databases

BgeeQ7TQC5.
CleanExMM_APTX.
GenevestigatorQ7TQC5.

Family and domain databases

Gene3D2.60.200.20. 2 hits.
3.30.428.10. 1 hit.
InterProIPR000253. 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]
PANTHERPTHR12486. PTHR12486. 1 hit.
SMARTSM00355. ZnF_C2H2. 1 hit.
[Graphical view]
SUPFAMSSF49879. SSF49879. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEPS00892. 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]
ProtoNetSearch...

Other

NextBio321599.
PROQ7TQC5.
SOURCESearch...

Entry information

Entry nameAPTX_MOUSE
AccessionPrimary (citable) accession number: Q7TQC5
Secondary accession number(s): Q8BPA7 expand/collapse secondary AC list , Q8C2B5, Q8K3D1, Q9CQ59
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot