SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q7Z2E3

- APTX_HUMAN

UniProt

Q7Z2E3 - APTX_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Aprataxin
Gene
APTX, AXA1
Organism
Homo sapiens (Human)
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.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 intermediate Inferred

Regions

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

GO - Molecular functioni

  1. DNA 5'-adenosine monophosphate hydrolase activity Source: UniProtKB
  2. chromatin binding Source: UniProtKB
  3. damaged DNA binding 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 N-terminus binding Source: UniProtKB
  11. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA catabolic process, exonucleolytic Source: GOC
  2. DNA ligation Source: Ensembl
  3. cell death Source: UniProtKB-KW
  4. cellular response to DNA damage stimulus Source: UniProtKB
  5. dephosphorylation Source: GOC
  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
Complete GO annotation...

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.6 Publications
Isoform 12 : Cytoplasm 6 Publications

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.7 Publications
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. 3 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 – 356356Aprataxin
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ7Z2E3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini38 – 8750FHA-like
Add
BLAST
Domaini182 – 287106HIT
Add
BLAST

Region

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi126 – 1316Nuclear localization signal Inferred
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 FHA-like domain.
Contains 1 HIT domain.

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. 3 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.
VSP_010534Add
BLAST
Alternative sequencei1 – 188188Missing in isoform 2.
VSP_010535Add
BLAST
Alternative sequencei1 – 102102Missing in isoform 4.
VSP_010536Add
BLAST
Alternative sequencei1 – 1414Missing in isoform 5, isoform 7, isoform 9, isoform 12 and isoform 13.
VSP_010537Add
BLAST
Alternative sequencei59 – 11254Missing in isoform 5 and isoform 10.
VSP_010538Add
BLAST
Alternative sequencei60 – 634QLKA → ESRV in isoform 12.
VSP_044091
Alternative sequencei64 – 356293Missing in isoform 12.
VSP_044092Add
BLAST
Alternative sequencei104 – 17572Missing in isoform 3.
VSP_010539Add
BLAST
Alternative sequencei175 – 19319Missing in isoform 8.
VSP_010540Add
BLAST
Alternative sequencei196 – 356161VYKDE…KHWTQ → PCTSSCDQPGF in isoform 13.
VSP_044093Add
BLAST
Alternative sequencei306 – 35651AVIEM…KHWTQ → E in isoform 6, isoform 9 and isoform 11.
VSP_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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 120 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

Similar proteinsi