Gene Symbol | CHD1L |
Entrez ID | 9557 |
Uniprot ID | Q86WJ1 |
Description | chromodomain helicase DNA binding protein 1-like |
Chromosomal Location | chr1: 147,242,641-147,295,766 |
Ontology | GO ID | GO Term | Definition | Evidence |
---|---|---|---|---|
BP |
GO:0000717 |
nucleotide-excision repair, DNA duplex unwinding |
The unwinding, or local denaturation, of the DNA duplex to create a bubble around the site of the DNA damage. |
TAS |
BP |
GO:0006281 |
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. |
TAS |
BP |
GO:0006293 |
nucleotide-excision repair, preincision complex stabilization |
The stabilization of the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage as well as the unwound DNA. The stabilization of the protein-DNA complex ensures proper positioning of the preincision complex before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage. |
TAS |
BP |
GO:0006294 |
nucleotide-excision repair, preincision complex assembly |
The aggregation, arrangement and bonding together of proteins on DNA to form the multiprotein complex involved in damage recognition, DNA helix unwinding, and endonucleolytic cleavage at the site of DNA damage. This assembly occurs before the phosphodiester backbone of the damaged strand is cleaved 3' and 5' of the site of DNA damage. |
TAS |
BP |
GO:0006295 |
nucleotide-excision repair, DNA incision, 3'-to lesion |
The endonucleolytic cleavage of the damaged strand of DNA 3' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision precedes the incision formed 5' to the site of damage. |
TAS |
BP |
GO:0006296 |
nucleotide-excision repair, DNA incision, 5'-to lesion |
The endonucleolytic cleavage of the damaged strand of DNA 5' to the site of damage. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. The incision follows the incision formed 3' to the site of damage. |
TAS |
BP |
GO:0006338 |
chromatin remodeling |
Dynamic structural changes to eukaryotic chromatin occurring throughout the cell division cycle. These changes range from the local changes necessary for transcriptional regulation to global changes necessary for chromosome segregation. |
IDA |
BP |
GO:0006974 |
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. |
IDA |
BP |
GO:0033683 |
nucleotide-excision repair, DNA incision |
A process that results in the endonucleolytic cleavage of the damaged strand of DNA. The incision occurs at the junction of single-stranded DNA and double-stranded DNA that is formed when the DNA duplex is unwound. |
TAS |
BP |
GO:0070911 |
global genome nucleotide-excision repair |
The nucleotide-excision repair process in which DNA lesions are removed from nontranscribed strands and from transcriptionally silent regions over the entire genome. |
TAS |
CC |
GO:0005634 |
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. |
IDA |
CC |
GO:0005654 |
nucleoplasm |
That part of the nuclear content other than the chromosomes or the nucleolus. |
IDA|TAS |
CC |
GO:0005737 |
cytoplasm |
All of the contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
IDA |
CC |
GO:0005886 |
plasma membrane |
The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
IDA |
MF |
GO:0000166 |
nucleotide binding |
Interacting selectively and non-covalently with a nucleotide, any compound consisting of a nucleoside that is esterified with (ortho)phosphate or an oligophosphate at any hydroxyl group on the ribose or deoxyribose. |
IDA |
MF |
GO:0003676 |
nucleic acid binding |
Interacting selectively and non-covalently with any nucleic acid. |
IEA |
MF |
GO:0004003 |
ATP-dependent DNA helicase activity |
Catalysis of the reaction: ATP + H2O = ADP + phosphate; this reaction drives the unwinding of the DNA helix. |
TAS |
MF |
GO:0005515 |
protein binding |
Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). |
IPI |
MF |
GO:0005524 |
ATP binding |
Interacting selectively and non-covalently with ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
IEA |
MF |
GO:0016887 |
ATPase activity |
Catalysis of the reaction: ATP + H2O = ADP + phosphate + 2 H+. May or may not be coupled to another reaction. |
IMP |
Domain ID | Description |
---|---|
IPR000330 |
SNF2-related, N-terminal domain |
IPR001650 |
Helicase, C-terminal |
IPR002464 |
DNA/RNA helicase, ATP-dependent, DEAH-box type, conserved site |
IPR002589 |
Macro domain |
IPR014001 |
Helicase superfamily 1/2, ATP-binding domain |
IPR027417 |
P-loop containing nucleoside triphosphate hydrolase |
IPR031053 |
Chromodomain-helicase-DNA-binding protein 1-like |
UMLS CUI | UMLS Term |
---|---|
C0236969 |
Substance-Related Disorders |
Tissue | Cell Type |
---|---|
adrenal gland |
glandular cells |
bone marrow |
hematopoietic cells |
breast |
glandular cells |
bronchus |
respiratory epithelial cells |
cerebellum |
Purkinje cells |
colon |
glandular cells |
duodenum |
glandular cells |
epididymis |
glandular cells |
esophagus |
squamous epithelial cells |
fallopian tube |
glandular cells |
gallbladder |
glandular cells |
kidney |
cells in glomeruli |
kidney |
cells in tubules |
lymph node |
germinal center cells |
lymph node |
non-germinal center cells |
nasopharynx |
respiratory epithelial cells |
oral mucosa |
squamous epithelial cells |
ovary |
follicle cells |
pancreas |
islets of Langerhans |
placenta |
decidual cells |
rectum |
glandular cells |
salivary gland |
glandular cells |
skin |
keratinocytes |
stomach |
glandular cells |
testis |
cells in seminiferous ducts |
thyroid gland |
glandular cells |
tonsil |
non-germinal center cells |
urinary bladder |
urothelial cells |
vagina |
squamous epithelial cells |
Pubmed ID | Author | Year | Title |
---|---|---|---|
22951915 |
Haozi et al. |
2012 |
Altered gene expression profile in cumulus cells of mature MII oocytes from patients with polycystic ovary syndrome |
Gene Symbol | Entrez ID | Uniprot ID | Score |
---|---|---|---|
EIF4A1 |
1973 |
P60842 |
0.63 |
H2AFX |
3014 |
P16104 |
0.63 |
H2AFZ |
3015 |
P0C0S5 |
0.63 |
HIST1H2BB |
3018 |
P33778 |
0.63 |
NR4A1 |
3164 |
P22736 |
0.63 |
RFC2 |
5982 |
P35250 |
0.63 |
RPA1 |
6117 |
P27694 |
0.63 |
RPA3 |
6119 |
P35244 |
0.63 |
XRCC1 |
7515 |
P18887 |
0.63 |
HIST2H2BE |
8349 |
Q16778 |
0.63 |
API5 |
8539 |
Q9BZZ5 |
0.63 |
CHD1L |
9557 |
Q86WJ1 |
0.63 |
PARP2 |
10038 |
Q9UGN5 |
0.63 |
CTCF |
10664 |
P49711 |
0.63 |
CBX1 |
10951 |
P83916 |
0.63 |
SUPT16H |
11198 |
Q9Y5B9 |
0.63 |
CBX3 |
11335 |
Q13185 |
0.63 |
CBX5 |
23468 |
P45973 |
0.63 |
SCYL1 |
57410 |
Q96KG9 |
0.63 |
UBE2O |
63893 |
Q9C0C9 |
0.63 |
HIST1H2BK |
85236 |
O60814 |
0.63 |
HIST3H2A |
92815 |
Q7L7L0 |
0.63 |
H3F3AP6 |
644914 |
N/A |
0.63 |
HIST2H2AA3; HIST2H2AA4 |
723790 |
Q6FI13 |
0.63 |
TRIM33 |
51592 |
Q9UPN9 |
0.65 |
PRKDC |
5591 |
P78527 |
0.73 |
RPA2 |
6118 |
P15927 |
0.73 |
XRCC5 |
7520 |
P13010 |
0.73 |
PARP1 |
142 |
P09874 |
0.74 |
XRCC6 |
2547 |
P12956 |
0.74 |
APLF |
200558 |
Q8IW19 |
0.74 |
HIST1H2BC; HIST1H2BE; HIST1H2BF; HIST1H2BG; HIST1H2BI |
8339 |
P62807 |
0.49 |
SRPK2 |
6733 |
P78362 |
0.52 |
FAS |
355 |
P25445 |
0.63 |
ART3 |
419 |
Q13508 |
0.63 |
CDC5L |
988 |
Q99459 |
0.63 |
EEF1G |
1937 |
P26641 |
0.63 |
NT5E |
4907 |
P21589 |
0.63 |
NTRK1 |
4914 |
P04629 |
0.63 |
SUMO2 |
6613 |
P61956 |
0.63 |
CIAO1 |
9391 |
O76071 |
0.63 |
TGOLN2 |
10618 |
O43493 |
0.63 |
KLK11 |
11012 |
Q9UBX7 |
0.63 |
SNW1 |
22938 |
Q13573 |
0.63 |
KLK5 |
25818 |
Q9Y337 |
0.63 |
RNF146 |
81847 |
Q9NTX7 |
0.63 |
RNF166 |
115992 |
Q96A37 |
0.63 |
HIST1H2BA |
255626 |
Q96A08 |
0.63 |
KIR2DS2 |
100132285 |
P43631 |
0.63 |
FOXL1 |
2300 |
Q12952 |
0.72 |
ID1 |
3397 |
P41134 |
0.72 |
PLK1 |
5347 |
P53350 |
0.72 |
TEAD2 |
8463 |
Q15562 |
0.72 |
FOXB1 |
27023 |
Q99853 |
0.72 |
FOXP1 |
27086 |
Q9H334 |
0.72 |
FAM134A |
79137 |
Q8NC44 |
0.72 |
LRRK2 |
120892 |
Q5S007 |
0.72 |
SGO1 |
151648 |
Q5FBB7 |
0.72 |