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Q7Z2E3 (APTX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Synonyms:AXA1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length356 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.12 Ref.14 Ref.16 Ref.17 Ref.18

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). Ref.12 Ref.13 Ref.14 Ref.15 Ref.20

Subcellular location

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. Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.20

Isoform 12: Cytoplasm Ref.1 Ref.12 Ref.13 Ref.14 Ref.15 Ref.20.

Tissue specificity

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. Ref.10 Ref.11 Ref.12

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.

The HIT domain is required for enzymatic activity.

The C2H2-type zinc finger mediates DNA-binding.

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 FHA-like domain.

Contains 1 HIT domain.

Biophysicochemical properties

Kinetic parameters:

KM=18 µM for AppppA

KM=837.5 µM for AMP-NH2

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
Neurodegeneration
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, exonucleolytic

Inferred from direct assay Ref.16Ref.17Ref.18PubMed 17519253. Source: GOC

DNA ligation

Inferred from electronic annotation. Source: Ensembl

cell death

Inferred from electronic annotation. Source: UniProtKB-KW

cellular response to DNA damage stimulus

Inferred from mutant phenotype Ref.14. Source: UniProtKB

dephosphorylation

Inferred from direct assay PubMed 17519253. Source: GOC

double-strand break repair

Inferred from direct assay PubMed 17519253. Source: UniProtKB

polynucleotide 3' dephosphorylation

Inferred from direct assay PubMed 17519253. Source: GOC

regulation of protein stability

Inferred from mutant phenotype Ref.15. Source: UniProtKB

response to hydrogen peroxide

Inferred from direct assay Ref.14. Source: UniProtKB

single strand break repair

Inferred from direct assay PubMed 17519253Ref.12. Source: UniProtKB

   Cellular_componentchromatin

Inferred from direct assay Ref.14. Source: UniProtKB

cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleolus

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.14Ref.15. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

   Molecular_functionDNA 5'-adenosine monophosphate hydrolase activity

Inferred from direct assay Ref.16Ref.17Ref.18PubMed 17519253. Source: UniProtKB

chromatin binding

Inferred from direct assay Ref.14. Source: UniProtKB

damaged DNA binding

Inferred from direct assay Ref.12. Source: UniProtKB

double-stranded DNA binding

Inferred from direct assay Ref.16Ref.18. Source: UniProtKB

double-stranded RNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycolate phosphatase activity

Inferred from direct assay PubMed 17519253. Source: UniProtKB

phosphoprotein binding

Inferred from physical interaction Ref.20. Source: UniProtKB

polynucleotide 3'-phosphatase activity

Inferred from direct assay PubMed 17519253. Source: UniProtKB

protein N-terminus binding

Inferred from physical interaction Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 13 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q7Z2E3-1)

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.
Note: Major form.
Isoform 2 (identifier: Q7Z2E3-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-188: Missing.
Note: Minor form.
Isoform 3 (identifier: Q7Z2E3-3)

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.
Isoform 4 (identifier: Q7Z2E3-4)

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.
Isoform 5 (identifier: Q7Z2E3-5)

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.
Isoform 6 (identifier: Q7Z2E3-6)

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.
Isoform 7 (identifier: Q7Z2E3-7)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
Isoform 8 (identifier: Q7Z2E3-8)

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.
Isoform 9 (identifier: Q7Z2E3-9)

The sequence of this isoform differs from the canonical sequence as follows:
     1-14: Missing.
     306-356: AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ → E
Note: No experimental confirmation available.
Isoform 10 (identifier: Q7Z2E3-10)

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.
Isoform 11 (identifier: Q7Z2E3-11)

The sequence of this isoform differs from the canonical sequence as follows:
     306-356: AVIEMVQEAGRVTVRDGMPELLKLPLRCHECQQLLPSIPQLKEHLRKHWTQ → E
Note: No experimental confirmation available.
Isoform 12 (identifier: Q7Z2E3-12)

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.
Isoform 13 (identifier: Q7Z2E3-13)

Also known as: LE5;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 356356Aprataxin
PRO_0000109838

Regions

Domain38 – 8750FHA-like
Domain182 – 287106HIT
Zinc finger331 – 35323C2H2-type
Region1 – 110110Interactions with ADPRT and NCL
Motif126 – 1316Nuclear localization signal Probable
Motif272 – 2765Histidine triad motif

Sites

Active site2741Tele-AMP-histidine intermediate Probable

Amino acid modifications

Modified residue1321Phosphoserine Ref.19

Natural variations

Alternative sequence1 – 193193Missing in isoform 6.
VSP_010534
Alternative sequence1 – 188188Missing in isoform 2.
VSP_010535
Alternative sequence1 – 102102Missing in isoform 4.
VSP_010536
Alternative sequence1 – 1414Missing in isoform 5, isoform 7, isoform 9, isoform 12 and isoform 13.
VSP_010537
Alternative sequence59 – 11254Missing in isoform 5 and isoform 10.
VSP_010538
Alternative sequence60 – 634QLKA → ESRV in isoform 12.
VSP_044091
Alternative sequence64 – 356293Missing in isoform 12.
VSP_044092
Alternative sequence104 – 17572Missing in isoform 3.
VSP_010539
Alternative sequence175 – 19319Missing in isoform 8.
VSP_010540
Alternative sequence196 – 356161VYKDE…KHWTQ → PCTSSCDQPGF in isoform 13.
VSP_044093
Alternative sequence306 – 35651AVIEM…KHWTQ → E in isoform 6, isoform 9 and isoform 11.
VSP_010541
Natural variant2111K → Q in AOA; it probably does not greatly affect the protein; heterozygous. Ref.22
VAR_018794
Natural variant2121A → V in AOA; heterozygous. Ref.23
VAR_018795
Natural variant2131R → H in AOA. Ref.11
Corresponds to variant rs150886026 [ dbSNP | Ensembl ].
VAR_018796
Natural variant2151H → R in AOA. Ref.21
VAR_018797
Natural variant2201P → L in AOA. Ref.10 Ref.11
VAR_018798
Natural variant2371L → P in AOA. Ref.24
VAR_025365
Natural variant2771V → G in AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A. Ref.10 Ref.16 Ref.23
VAR_018799
Natural variant2811D → G in AOA; heterozygous.
VAR_018800
Natural variant2931W → R in AOA; heterozygous. Ref.23
VAR_018801

Experimental info

Mutagenesis431R → A: Impairs interaction with XRCC1 and XRCC4. Abolishes localization at sites of DNA double-strand breaks. Loss of interaction with MDC1. Ref.13 Ref.20
Mutagenesis521K → A: Impairs interaction with MDC1 and localization at sites of DNA double-strand breaks. Ref.20
Mutagenesis2741H → A: Abolishes enzyme activity. Ref.17 Ref.18
Mutagenesis3331C → A: Abolishes DNA-binding and enzyme activity; when associated with A-336. Ref.18
Mutagenesis3361C → A: Abolishes DNA-binding and enzyme activity; when associated with A-333. Ref.18

Secondary structure

........................................................ 356
Helix Strand Turn

Details...

Sequences

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

Last modified June 7, 2004. Version 2.
Checksum: 5B338490E35EC8E4

FASTA35640,740
        10         20         30         40         50         60 
MSNVNLSVSD FWRVMMRVCW LVRQDSRHQR IRLPHLEAVV IGRGPETKIT DKKCSRQQVQ 

        70         80         90        100        110        120 
LKAECNKGYV KVKQVGVNPT SIDSVVIGKD QEVKLQPGQV LHMVNELYPY IVEFEEEAKN 

       130        140        150        160        170        180 
PGLETHRKRK RSGNSDSIER DAAQEAEAGT GLEPGSNSGQ CSVPLKKGKD APIKKESLGH 

       190        200        210        220        230        240 
WSQGLKISMQ DPKMQVYKDE QVVVIKDKYP KARYHWLVLP WTSISSLKAV AREHLELLKH 

       250        260        270        280        290        300 
MHTVGEKVIV DFAGSSKLRF RLGYHAIPSM SHVHLHVISQ DFDSPCLKNK KHWNSFNTEY 

       310        320        330        340        350 
FLESQAVIEM VQEAGRVTVR DGMPELLKLP LRCHECQQLL PSIPQLKEHL RKHWTQ 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 2AF4F98B97C0A76B
Show »

FASTA16819,715
Isoform 3 [UniParc].

Checksum: 4213615369B997A5
Show »

FASTA28432,901
Isoform 4 [UniParc].

Checksum: B2338C3B2822B710
Show »

FASTA25429,108
Isoform 5 [UniParc].

Checksum: AD5D2BD20A81EBD6
Show »

FASTA28833,125
Isoform 6 [UniParc].

Checksum: 5583AA4F55EDF41B
Show »

FASTA11313,305
Isoform 7 [UniParc].

Checksum: C0D4FAEBF89ABA74
Show »

FASTA34239,104
Isoform 8 [UniParc].

Checksum: DC2FF196087D3ADB
Show »

FASTA33738,589
Isoform 9 [UniParc].

Checksum: 5802EE9F37B07600
Show »

FASTA29233,294
Isoform 10 [UniParc].

Checksum: 4CAFA4C9BB2399EC
Show »

FASTA30234,761
Isoform 11 [UniParc].

Checksum: AC5FCCDC3642F91B
Show »

FASTA30634,930
Isoform 12 (LP2) (LP2E5) (LP2P3) (LP2P3E5) [UniParc].

Checksum: F731A5E3CB6C1C8A
Show »

FASTA495,828
Isoform 13 (LE5) [UniParc].

Checksum: 80F7BD34425AAA69
Show »

FASTA19221,389

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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. expand/collapse author list , 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]"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: 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]"Aprataxin, a novel protein that protects against genotoxic stress."
Gueven N., Becherel O.J., Kijas A.W., Chen P., Howe O., Rudolph J.H., Gatti R., Date H., Onodera O., Taucher-Scholz G., Lavin M.F.
Hum. Mol. Genet. 13:1081-1093(2004) [PubMed] [Europe PMC] [Abstract]
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]"CK2 phosphorylation-dependent interaction between aprataxin and MDC1 in the DNA damage response."
Becherel O.J., Jakob B., Cherry A.L., Gueven N., Fusser M., Kijas A.W., Peng C., Katyal S., McKinnon P.J., Chen J., Epe B., Smerdon S.J., Taucher-Scholz G., Lavin M.F.
Nucleic Acids Res. 38:1489-1503(2010) [PubMed] [Europe PMC] [Abstract]
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]"Cerebellar ataxia with oculomotor apRAxia type 1: clinical and genetic studies."
Le Ber I., Moreira M.-C., Rivaud-Pechoux S., Chamayou C., Ochsner F., Kuntzer T., Tardieu M., Saied G., Habert M.-O., Demarquay G., Tannier C., Beis J.-M., Brice A., Koenig M., Duerr A.
Brain 126:2761-2772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AOA VAL-212; GLY-277 AND ARG-293.
[24]"Very late onset in ataxia oculomotor apraxia type I."
Criscuolo C., Mancini P., Menchise V., Sacca F., De Michele G., Banfi S., Filla A.
Ann. Neurol. 57:777-777(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001182177.1. NM_001195248.1.
NP_001182178.1. NM_001195249.1.
NP_001182179.1. NM_001195250.1.
NP_001182180.1. NM_001195251.1.
NP_001182181.1. NM_001195252.1.
NP_001182183.1. NM_001195254.1.
NP_778239.1. NM_175069.2.
NP_778243.1. NM_175073.2.
UniGeneHs.20158.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalQ7Z2E3.
SMRQ7Z2E3. Positions 15-116, 184-354.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120191. 19 interactions.
IntActQ7Z2E3. 16 interactions.
MINTMINT-1205251.

PTM databases

PhosphoSiteQ7Z2E3.

Polymorphism databases

DMDM48428038.

Proteomic databases

PaxDbQ7Z2E3.
PRIDEQ7Z2E3.

Protocols and materials databases

DNASU54840.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000309615; 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]
GeneID54840.
KEGGhsa:54840.
UCSCuc003zrj.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

CTD54840.
GeneCardsGC09M032962.
HGNCHGNC:15984. APTX.
HPAHPA055545.
MIM208920. phenotype.
606350. gene.
neXtProtNX_Q7Z2E3.
Orphanet1168. Ataxia - oculomotor apraxia type 1.
PharmGKBPA24915.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG278510.
HOGENOMHOG000248858.
HOVERGENHBG050555.
InParanoidQ7Z2E3.
KOK10863.
OMAPGQVLHM.
OrthoDBEOG786H3J.
PhylomeDBQ7Z2E3.
TreeFamTF313308.

Enzyme and pathway databases

SABIO-RKQ7Z2E3.

Gene expression databases

ArrayExpressQ7Z2E3.
BgeeQ7Z2E3.
CleanExHS_APTX.
GenevestigatorQ7Z2E3.

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.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ7Z2E3.
GeneWikiAprataxin.
GenomeRNAi54840.
NextBio57644.
PROQ7Z2E3.
SOURCESearch...

Entry information

Entry nameAPTX_HUMAN
AccessionPrimary (citable) accession number: Q7Z2E3
Secondary accession number(s): A8MTN4 expand/collapse secondary AC list , D3DRK9, D3DRL0, Q0P662, Q5T781, Q5T782, Q5T784, Q6JV81, Q6JV82, Q6JV85, Q7Z2F3, Q7Z336, Q7Z5R5, Q7Z6V7, Q7Z6V8, Q9NXM5
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: April 16, 2014
This is version 116 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM