Descriptions

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

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

11 structures for Q9JLV6

Entry ID Method Resolution Chain Position Source
1UJX NMR - A 1-106 PDB
1YJ5 X-ray 280 A PDB
1YJM X-ray 220 A A/B/C 1-110 PDB
3U7E X-ray 170 A B 142-522 PDB
3U7F X-ray 180 A B 142-522 PDB
3U7G X-ray 210 A A 144-522 PDB
3U7H X-ray 200 A B 142-522 PDB
3ZVL X-ray 165 A A 111-522 PDB
3ZVM X-ray 200 A A/B 111-522 PDB
3ZVN X-ray 215 A A 111-522 PDB
AF-Q9JLV6-F1 Predicted AlphaFoldDB

No variants for Q9JLV6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q9JLV6

No associated diseases with Q9JLV6

1 regional properties for Q9JLV6

Type Name Position InterPro Accession
domain YqgF/RNase H-like domain 4 - 104 IPR006641

Functions

Description
EC Number 2.7.1.78 Phosphotransferases with an alcohol group as acceptor
Subcellular Localization
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.
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.
SCF ubiquitin ligase complex A ubiquitin ligase complex in which a cullin from the Cul1 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 adaptor and an F-box protein. SCF complexes are involved in targeting proteins for degradation by the proteasome. The best characterized complexes are those from yeast and mammals (with core subunits named Cdc53/Cul1, Rbx1/Hrt1/Roc1).
site of double-strand break A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix.

5 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
double-stranded DNA binding Binding to double-stranded DNA.
polydeoxyribonucleotide 5'-hydroxyl-kinase activity Catalysis of the reaction: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA.
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.
ubiquitin ligase-substrate adaptor activity The binding activity of a molecule that brings together a ubiquitin ligase and its substrate. Usually mediated by F-box BTB/POZ domain proteins.

12 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 involved in DNA repair The re-formation of a broken phosphodiester bond in the DNA backbone, carried out by DNA ligase, that contributes to DNA repair.
DNA repair The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway.
double-strand break repair via nonhomologous end joining The repair of a double-strand break in DNA in which the two broken ends are rejoined with little or no sequence complementarity. Information at the DNA ends may be lost due to the modification of broken DNA ends. This term covers instances of separate pathways, called classical (or canonical) and alternative nonhomologous end joining (C-NHEJ and A-NHEJ). These in turn may further branch into sub-pathways, but evidence is still unclear.
negative regulation of protein ADP-ribosylation Any process that decreases the frequency, rate or extent of protein ADP-ribosylation. Protein ADP-ribosylation is the transfer, from NAD, of ADP-ribose to protein amino acids.
nucleotide phosphorylation The process of introducing one or more phosphate groups into a nucleotide to produce a phosphorylated nucleoside.
positive regulation of double-strand break repair via nonhomologous end joining Any process that activates or increases the frequency, rate or extent of double-strand break repair via nonhomologous end joining.
positive regulation of telomerase activity Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
positive regulation of telomere capping Any process that activates or increases the frequency, rate or extent of telomere capping.
positive regulation of telomere maintenance via telomerase Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase.
protein K63-linked ubiquitination A protein ubiquitination process in which a polymer of ubiquitin, formed by linkages between lysine residues at position 63 of the ubiquitin monomers, is added to a protein. K63-linked ubiquitination does not target the substrate protein for degradation, but is involved in several pathways, notably as a signal to promote error-free DNA postreplication repair.
response to oxidative stress 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

6 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q7YRZ2 APTX Aprataxin Bos taurus (Bovine) PR
Q7Z2E3 APTX Aprataxin Homo sapiens (Human) PR
Q96T60 PNKP Bifunctional polynucleotide phosphatase/kinase Homo sapiens (Human) 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
MSQLGSRGRL WLQSPTGGPP PIFLPSDGQA LVLGRGPLTQ VTDRKCSRNQ VELIADPESR
70 80 90 100 110 120
TVAVKQLGVN PSTVGVHELK PGLSGSLSLG DVLYLVNGLY PLTLRWEELS TSGSQPDAPP
130 140 150 160 170 180
DTPGDPEEGE DTEPQKKRVR KSSLGWESLK KLLVFTASGV KPQGKVAAFD LDGTLITTRS
190 200 210 220 230 240
GKVFPTSPSD WRILYPEIPK KLQELAAEGY KLVIFTNQMG IGRGKLPAEV FKGKVEAVLE
250 260 270 280 290 300
KLGVPFQVLV ATHAGLNRKP VSGMWDHLQE QANEGIPISV EDSVFVGDAA GRLANWAPGR
310 320 330 340 350 360
KKKDFSCADR LFALNVGLPF ATPEEFFLKW PAARFELPAF DPRTISSAGP LYLPESSSLL
370 380 390 400 410 420
SPNPEVVVAV GFPGAGKSTF IQEHLVSAGY VHVNRDTLGS WQRCVSSCQA ALRQGKRVVI
430 440 450 460 470 480
DNTNPDVPSR ARYIQCAKDA GVPCRCFNFC ATIEQARHNN RFREMTDPSH APVSDMVMFS
490 500 510 520
YRKQFEPPTL AEGFLEILEI PFRLQEHLDP ALQRLYRQFS EG