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Q8K4H4 (APTX_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length329 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

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.

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA ligation

Inferred from electronic annotation. Source: Ensembl

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 electronic annotation. Source: Ensembl

   Cellular_componentnuclear chromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionDNA 5'-adenosine monophosphate hydrolase activity

Inferred from electronic annotation. Source: Ensembl

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

Inferred from electronic annotation. Source: UniProtKB-KW

phosphoglycolate phosphatase activity

Inferred from electronic annotation. Source: Ensembl

polynucleotide 3'-phosphatase activity

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 329329Aprataxin
PRO_0000109842

Regions

Domain23 – 7250FHA-like
Domain155 – 260106HIT
Zinc finger304 – 32623C2H2-type
Region1 – 9595Interactions with ADPRT and NCL By similarity
Motif111 – 1155Nuclear localization signal By similarity
Motif245 – 2495Histidine triad motif

Sites

Active site2471Tele-AMP-histidine intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8K4H4 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 636B827F661B14FD

FASTA32937,720
        10         20         30         40         50         60 
MRVCWLVRQD CWHQRIKLPH LEAVVIGRSP ETKITDKKCS RQQVQLKAEC NKRYVNVKQM 

        70         80         90        100        110        120 
GVNPTSIDEV VIGKDREMKL LPGQVLHMVN ELYPYMVEFE EVAESPNVTQ RKRKRPDCDS 

       130        140        150        160        170        180 
QEMEAEAGAS PSQCSVSPKT GKHGAAKEES LGHWSQGLKI SMKDPKMQVY KDDQVVVIKD 

       190        200        210        220        230        240 
KYPKARHHWL VLPWASISSL KVVTSEHLEL LKHMHAVGEK VIADFTGSSK LRFRLGYHAI 

       250        260        270        280        290        300 
PSMSHVHLHV ISQDFDSPCL KNKKHWNSFN TEYFLESQAV IKMVQEAGRV TVKDGTCELL 

       310        320 
KLPLRCHECQ QLLPSIPQLK EHLRKHWGG 

« Hide

References

« Hide 'large scale' references
[1]"Identification of FHA-HIT as a novel nuclear protein involved in cell-cycle regulation."
Huang C.-H., Chen H., Peng J., Chen Y.
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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].
Tissue: Testis.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF398235 mRNA. Translation: AAM90583.1.
BC078716 mRNA. Translation: AAH78716.1.
RefSeqNP_683687.1. NM_148889.2.
XP_006238089.1. XM_006238027.1.
XP_006238090.1. XM_006238028.1.
UniGeneRn.50459.

3D structure databases

ProteinModelPortalQ8K4H4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10116.ENSRNOP00000009176.

Proteomic databases

PRIDEQ8K4H4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000046463; ENSRNOP00000046400; ENSRNOG00000006582.
GeneID259271.
KEGGrno:259271.
UCSCRGD:628740. rat.

Organism-specific databases

CTD54840.
RGD628740. Aptx.

Phylogenomic databases

eggNOGNOG278510.
GeneTreeENSGT00570000079163.
HOGENOMHOG000248858.
HOVERGENHBG050555.
InParanoidQ8K4H4.
KOK10863.
OMAPGQVLHM.
OrthoDBEOG786H3J.
PhylomeDBQ8K4H4.

Gene expression databases

GenevestigatorQ8K4H4.

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

NextBio624321.

Entry information

Entry nameAPTX_RAT
AccessionPrimary (citable) accession number: Q8K4H4
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: October 1, 2002
Last modified: April 16, 2014
This is version 83 of the entry and version 1 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