CHD1L
entrez
9557
canonical
uniprot
Q86WJ1
canonical
ensembl
ENSG00000131778
resolver
ensp
ENSP00000355100
resolver
ensp
ENSP00000358262
resolver
ensp
ENSP00000358263
resolver
ensp
ENSP00000389031
resolver
ensp
ENSP00000498899
resolver
ensp
ENSP00000587513
resolver
enst
ENST00000361293
resolver
enst
ENST00000431239
resolver
genesymbol
CHD1L
resolver
genesymbol_syn
ALC1
resolver
hgnc
HGNC:1916
resolver
uniprot
A0A0A0MRH8
resolver
uniprot
A0A0A0MSH9
resolver
uniprot
A5YM64
resolver
uniprot
B4DDE1
resolver
uniprot
B5MDZ7
resolver
uniprot
Q53EZ3
resolver
uniprot
Q5VXX7
resolver
uniprot
Q6DD94
resolver
uniprot
Q6PK83
resolver
uniprot
Q86XH3
resolver
uniprot
Q96HF7
resolver
uniprot
Q96SP3
resolver
uniprot
Q9BVJ1
resolver
uniprot
Q9NVV8
resolver
uniprot_entry
A0A0A0MRH8_HUMAN
resolver
uniprot_entry
A0A0A0MSH9_HUMAN
resolver
uniprot_entry
CHD1L_HUMAN
resolver
uniprot_sec
A5YM64
resolver
uniprot_sec
B4DDE1
resolver
uniprot_sec
B5MDZ7
resolver
uniprot_sec
Q53EZ3
resolver
uniprot_sec
Q5VXX7
resolver
uniprot_sec
Q6DD94
resolver
uniprot_sec
Q6PK83
resolver
uniprot_sec
Q86XH3
resolver
uniprot_sec
Q96HF7
resolver
uniprot_sec
Q96SP3
resolver
uniprot_sec
Q9BVJ1
resolver
uniprot_sec
Q9NVV8
resolver
activity_regulation
ACTIVITY REGULATION: Adopts an inactive conformation in absence of DNA damage (PubMed:33357431, PubMed:34486521, PubMed:34874266). Binding to poly-ADP-ribosylated histones activates the ATP-dependent chromatin remodeler activity (PubMed:34486521, PubMed:34874266). {ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}.
uniprot
proteins
amino_acid_sequence
MERAGATSRGGQAPGFLLRLHTEGRAEAARVQEQDLRQWGLTGIHLRSYQLEGVNWLAQRFHCQNGCILGDEMGLGKTCQTIALFIYLAGRLNDEGPFLILCPLSVLSNWKEEMQRFAPGLSCVTYAGDKEERACLQQDLKQESRFHVLLTTYEICLKDASFLKSFPWSVLVVDEAHRLKNQSSLLHKTLSEFSVVFSLLLTGTPIQNSLQELYSLLSFVEPDLFSKEEVGDFIQRYQDIEKESESASELHKLLQPFLLRRVKAEVATELPKKTEVVIYHGMSALQKKYYKAILMKDLDAFENETAKKVKLQNILSQLRKCVDHPYLFDGVEPEPFEVGDHLTEASGKLHLLDKLLAFLYSGGHRVLLFSQMTQMLDILQDYMDYRGYSYERVDGSVRGEERHLAIKNFGQQPIFVFLLSTRAGGVGMNLTAADTVIFVDSDFNPQNDLQAAARAHRIGQNKSVKVIRLIGRDTVEEIVYRKAASKLQLTNMIIEGGHFTLGAQKPAADADLQLSEILKFGLDKLLASEGSTMDEIDLESILGETKDGQWVSDALPAAEGGSRDQEEGKNHMYLFEGKDYSKEPSKEDRKSFEQLVNLQKTLLEKASQEGRSLRNKGSVLIPGLVEGSTKRKRVLSPEELEDRQKKRQEAAAKRRRLIEEKKRQKEEAEHKKKMAWWESNNYQSFCLPSEESEPEDLENGEESSAELDYQDPDATSLKYVSGDVTHPQAGAEDALIVHCVDDSGHWGRGGLFTALEKRSAEPRKIYELAGKMKDLSLGGVLLFPVDDKESRNKGQDLLALIVAQHRDRSNVLSGIKMAALEEGLKKIFLAAKKKKASVHLPRIGHATKGFNWYGTERLIRKHLAARGIPTYIYYFPRSKSAVLHSQSSSSSSRQLVP
uniprot
proteins
ec_number
3.6.4.-
uniprot
proteins
function
FUNCTION: ATP-dependent chromatin remodeler that mediates chromatin-remodeling following DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:33357431, PubMed:34210977, PubMed:34486521, PubMed:34874266). Recruited to DNA damage sites through interaction with poly-ADP-ribose: specifically recognizes and binds histones that are poly-ADP-ribosylated on serine residues in response to DNA damage (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Poly-ADP-ribose-binding activates the ATP-dependent chromatin remodeler activity, thereby regulating chromatin during DNA repair (PubMed:19661379, PubMed:29220652, PubMed:29220653, PubMed:34486521, PubMed:34874266). Catalyzes nucleosome sliding away from DNA breaks in an ATP-dependent manner (PubMed:19661379, PubMed:29220652, PubMed:29220653). Chromatin remodeling activity promotes PARP2 removal from chromatin (PubMed:33275888). {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:33275888, ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34210977, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}.
uniprot
proteins
mass_dalton
101000
uniprot
proteins
mutagenesis
MUTAGEN 77; /note="K->R: Abolishes ATPase activity."; /evidence="ECO:0000269|PubMed:19661379"; MUTAGEN 175; /note="E->Q: Abrogates chromatin remodeling activity. Prevents PARP2 removal from chromatin."; /evidence="ECO:0000269|PubMed:29220653, ECO:0000269|PubMed:33275888"; MUTAGEN 307..308; /note="KK->EE: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-398 and E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 319..320; /note="RK->EE: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-407; E-422 and E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 332..337; /note="EPEPFE->APAPAA: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 381; /note="D->A: Decreased interaction with nucleosomes."; /evidence="ECO:0000269|PubMed:34210977"; MUTAGEN 398; /note="R->E: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-307, E-308 and E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 407; /note="K->E: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-319, E-320, E-422 and E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 420; /note="S->A: Does not reduce interaction of the macro domain with the N-terminal ATPase module; when associated with E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 422; /note="R->E: Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-319, E-320, E-407 and E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 457; /note="R->H: Abolished ATP-dependent chromatin remodeler activity."; /evidence="ECO:0000269|PubMed:34210977"; MUTAGEN 611..612; /note="RS->AA: Strongly reduced interaction with the acidic patch of histones."; /evidence="ECO:0000269|PubMed:33357431, ECO:0000269|PubMed:34486521"; MUTAGEN 611; /note="R->E: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:34210977"; MUTAGEN 614; /note="R->E: Reduced interaction with histones."; /evidence="ECO:0000269|PubMed:34210977"; MUTAGEN 653..656; /note="KRRR->AAAA: Does not reduce interaction of the macro domain with the N-terminal ATPase module; when associated with E-750."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 723; /note="D->A: Strongly reduces poly(ADP-ribose)-binding but not ATPase activity."; /evidence="ECO:0000269|PubMed:19661379"; MUTAGEN 750; /note="G->E: Disrupts interaction with PARP1. Abolishes the release from auto-inhibition through macro domain binding to the N-terminal ATPase module. Reduces interaction of the macro domain with the N-terminal ATPase module; when associated with E-307, E-308 and E-398; E-319, E-320, E-407 and E-422."; /evidence="ECO:0000269|PubMed:29220653"; MUTAGEN 857; /note="R->E: Loss of auto-inhibition, leading to constitutive ATP-dependent chromatin remodeler activity."; /evidence="ECO:0000269|PubMed:29220652
uniprot
proteins
protein_family
SNF2/RAD54 helicase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16710414
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18023026
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19661379
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23891004
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
29220652
uniprot
proteins
pubmed
29220653
uniprot
proteins
pubmed
29320706
uniprot
proteins
pubmed
33275888
uniprot
proteins
pubmed
33357431
uniprot
proteins
pubmed
34210977
uniprot
proteins
pubmed
34465625
uniprot
proteins
pubmed
34486521
uniprot
proteins
pubmed
34874266
uniprot
proteins
sequence_length
897
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19661379}. Chromosome {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220652, ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}. Note=Localizes at sites of DNA damage; recruited by histones H2B and H3 poly-ADP-ribosylated on 'Ser-6' and 'Ser-10', respectively (H2BS6ADPr and H3S10ADPr) by PARP1 or PARP2. {ECO:0000269|PubMed:34486521, ECO:0000269|PubMed:34874266}.
uniprot
proteins