Q7Z2E3

PR
Gene name
APTX (AXA1)
Protein name
Aprataxin
Names
Forkhead-associated domain histidine triad-like protein, FHA-HIT
Species
Homo sapiens (Human)
KEGG Pathway
hsa:54840
EC number
3.6.1.71: In phosphorus-containing anhydrides
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

92-173 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

12 structures for Q7Z2E3

Entry ID Method Resolution Chain Position Source
3KT9 X-ray 165 A A 15-116 PDB
4NDF X-ray 194 A A/B 179-356 PDB
4NDG X-ray 254 A A/B 179-356 PDB
4NDH X-ray 185 A A/B 179-356 PDB
4NDI X-ray 190 A A/B 179-356 PDB
6CVO X-ray 240 A A/B 179-356 PDB
6CVP X-ray 200 A A/B 179-356 PDB
6CVQ X-ray 165 A A/B 179-354 PDB
6CVR X-ray 188 A A/B 179-356 PDB
6CVS X-ray 211 A A/B 179-356 PDB
6CVT X-ray 294 A A/B 179-356 PDB
AF-Q7Z2E3-F1 Predicted AlphaFoldDB

9 variants for Q7Z2E3

Variant ID(s) Position Change Description Diseaes Association Provenance
VAR_018794 211 K>Q AOA; impairs binding to adenosine-5'-diphospho-5'-(DNA) and deadenylation activity [UniProt] Yes UniProt
VAR_018795
rs748165574
 212 A>V AOA; heterozygous [UniProt] Yes UniProt
dbSNP
rs150886026
VAR_018796
 213 R>H AOA [UniProt] Yes UniProt
dbSNP
rs121908133
VAR_018797
 215 H>R AOA [UniProt] Yes UniProt
dbSNP
rs121908131
VAR_018798
 220 P>L AOA [UniProt] Yes UniProt
dbSNP
rs267606665
VAR_025365
 237 L>P AOA [UniProt] Yes UniProt
dbSNP
VAR_018799
rs121908132
 277 V>G AOA; abolishes DNA-binding and enzymatic activity towards Ap(4)A [UniProt] Yes UniProt
dbSNP
VAR_018800 281 D>G AOA; heterozygous [UniProt] Yes UniProt
rs773393618
VAR_018801
 293 W>R AOA; heterozygous [UniProt] Yes UniProt
dbSNP

No associated diseases with Q7Z2E3

No regional properties for Q7Z2E3

Type Name Position InterPro Accession
No domain, repeats, and functional sites for Q7Z2E3

Functions

Description
EC Number 3.6.1.71 In phosphorus-containing anhydrides
Subcellular Localization
  • Nucleus, nucleoplasm
  • Nucleus, nucleolus
  • Upon genotoxic stress, colocalizes with XRCC1 at sites of DNA damage (PubMed:15380105)
  • Colocalizes with MDC1 at sites of DNA double-strand breaks (PubMed:20008512)
  • Interaction with NCL is required for nucleolar localization (PubMed:16777843)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 GO annotations of cellular component

Name Definition
chromatin The ordered and organized complex of DNA, protein, and sometimes RNA, that forms the chromosome.
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
nucleolus A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.
nucleus A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent.

14 GO annotations of molecular function

Name Definition
chromatin binding Binding to chromatin, the network of fibers of DNA, protein, and sometimes RNA, that make up the chromosomes of the eukaryotic nucleus during interphase.
damaged DNA binding Binding to damaged DNA.
DNA 5'-adenosine monophosphate hydrolase activity Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus.
DNA-3'-diphospho-5'-guanosine diphosphatase Catalysis of the reaction: (DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate + GMP.
double-stranded DNA binding Binding to double-stranded DNA.
double-stranded RNA binding Binding to double-stranded RNA.
metal ion binding Binding to a metal ion.
mismatched DNA binding Binding to a double-stranded DNA region containing one or more mismatches.
phosphoglycolate phosphatase activity Catalysis of the reaction: 2-phosphoglycolate + H(2)O = glycolate + phosphate.
phosphoprotein binding Binding to a phosphorylated protein.
polynucleotide 3'-phosphatase activity Catalysis of the reaction: 3'-phosphopolynucleotide + H2O = a polynucleotide + phosphate. Hydrolyzes the free 3'-phosphate resulting from single strand breaks in DNA due to oxidative damage.
protein N-terminus binding Binding to a protein N-terminus, the end of any peptide chain at which the 2-amino (or 2-imino) function of a constituent amino acid is not attached in peptide linkage to another amino-acid residue.
single-strand break-containing DNA binding Binding to damaged DNA containing single-strand breaks (SSBs).
single-stranded DNA binding Binding to single-stranded DNA.

6 GO annotations of biological process

Name Definition
cellular response to DNA damage stimulus Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
DNA ligation The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase.
double-strand break repair The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
response to hydrogen peroxide Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a hydrogen peroxide (H2O2) stimulus.
single strand break repair The repair of single strand breaks in DNA. Repair of such breaks is mediated by the same enzyme systems as are used in base excision repair.

7 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7YRZ2 APTX Aprataxin Bos taurus (Bovine) PR
Q96T60 PNKP Bifunctional polynucleotide phosphatase/kinase Homo sapiens (Human) PR
Q9NQE9 HINT3 Adenosine 5'-monophosphoramidase HINT3 Homo sapiens (Human) PR
Q9JLV6 Pnkp Bifunctional polynucleotide phosphatase/kinase Mus musculus (Mouse) PR
Q7TQC5 Aptx Aprataxin Mus musculus (Mouse) PR
Q7YRZ1 APTX Aprataxin Sus scrofa (Pig) PR
Q19683 F21D5.5 Uncharacterized protein F21D5.5 Caenorhabditis elegans PR
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