CHD1L_HUMAN
ID CHD1L_HUMAN Reviewed; 897 AA.
AC Q86WJ1; A5YM64; B4DDE1; B5MDZ7; Q53EZ3; Q5VXX7; Q6DD94; Q6PK83; Q86XH3;
AC Q96HF7; Q96SP3; Q9BVJ1; Q9NVV8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-SEP-2018, sequence version 3.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:29220653};
DE AltName: Full=Amplified in liver cancer protein 1 {ECO:0000303|PubMed:18023026};
GN Name=CHD1L {ECO:0000312|HGNC:HGNC:1916};
GN Synonyms=ALC1 {ECO:0000303|PubMed:18023026};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=18023026; DOI=10.1002/hep.22072;
RA Ma N.-F., Hu L., Fung J.-M., Xie D., Zheng B.-J., Chen L., Tang D.-J.,
RA Fu L., Wu Z., Chen M., Fang Y., Guan X.-Y.;
RT "Isolation and characterization of a novel oncogene, amplified in liver
RT cancer 1, within a commonly amplified region at 1q21 in hepatocellular
RT carcinoma.";
RL Hepatology 47:503-510(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), AND VARIANT
RP CYS-743.
RC TISSUE=Neuron;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLN-350.
RC TISSUE=Retina;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-885.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 2-897 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 15-897 (ISOFORM 2), AND VARIANTS PRO-25 AND CYS-743.
RC TISSUE=Brain, Eye, Prostate, and Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-798.
RC TISSUE=Hepatocyte;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN MACRO, ADP-RIBOSE-BINDING,
RP INTERACTION WITH PARP1, AND MUTAGENESIS OF LYS-77 AND ASP-723.
RX PubMed=19661379; DOI=10.1126/science.1177321;
RA Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I.,
RA Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.;
RT "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin
RT remodeling enzyme ALC1.";
RL Science 325:1240-1243(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-607; SER-618; SER-628 AND
RP SER-636, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-540, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP INTERACTION WITH CIAO1.
RX PubMed=23891004; DOI=10.1016/j.cmet.2013.06.015;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B integrate iron homeostasis and
RT maturation of different subsets of cytosolic-nuclear iron-sulfur
RT proteins.";
RL Cell Metab. 18:187-198(2013).
RN [15]
RP ERRATUM OF PUBMED:23891004.
RX PubMed=29320706; DOI=10.1016/j.cmet.2017.12.009;
RA Stehling O., Mascarenhas J., Vashisht A.A., Sheftel A.D., Niggemeyer B.,
RA Roesser R., Pierik A.J., Wohlschlegel J.A., Lill R.;
RT "Human CIA2A-FAM96A and CIA2B-FAM96B Integrate Iron Homeostasis and
RT Maturation of Different Subsets of Cytosolic-Nuclear Iron-Sulfur
RT Proteins.";
RL Cell Metab. 27:263-263(2018).
RN [16]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH PARP1, DOMAIN MACRO,
RP ADP-RIBOSE-BINDING, AND MUTAGENESIS OF GLU-175; 307-LYS-LYS-308;
RP 319-ARG-LYS-320; 332-GLU--GLU-337; ARG-398; LYS-407; SER-420; ARG-422;
RP 653-LYS--ARG-656; GLY-750; ARG-842; ARG-857 AND ARG-860.
RX PubMed=29220653; DOI=10.1016/j.molcel.2017.11.019;
RA Singh H.R., Nardozza A.P., Moeller I.R., Knobloch G., Kistemaker H.A.V.,
RA Hassler M., Harrer N., Blessing C., Eustermann S., Kotthoff C., Huet S.,
RA Mueller-Planitz F., Filippov D.V., Timinszky G., Rand K.D., Ladurner A.G.;
RT "A Poly-ADP-Ribose trigger releases the auto-inhibition of a chromatin
RT remodeling oncogene.";
RL Mol. Cell 68:860-871(2017).
CC -!- FUNCTION: DNA helicase which plays a role in chromatin-remodeling
CC following DNA damage (PubMed:19661379, PubMed:29220653). Targeted to
CC sites of DNA damage through interaction with poly(ADP-ribose) and
CC functions to regulate chromatin during DNA repair (PubMed:19661379).
CC Able to catalyze nucleosome sliding in an ATP-dependent manner
CC (PubMed:19661379). Helicase activity is strongly stimulated upon
CC poly(ADP-ribose)-binding (PubMed:19661379, PubMed:29220653).
CC {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:29220653}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:29220653};
CC -!- SUBUNIT: Interacts (via macro domain) with PARP1; interacts only when
CC PARP1 is poly-ADP-ribosylated (PARylated) (PubMed:19661379,
CC PubMed:29220653). Interacts with CIAO1 (PubMed:23891004).
CC {ECO:0000269|PubMed:19661379, ECO:0000269|PubMed:23891004,
CC ECO:0000269|PubMed:29220653}.
CC -!- INTERACTION:
CC Q86WJ1-1; P09874: PARP1; NbExp=3; IntAct=EBI-15797018, EBI-355676;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19661379}.
CC Note=Localizes at sites of DNA damage. Probably recruited to DNA damage
CC sites by PARylated PARP1. {ECO:0000269|PubMed:19661379}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q86WJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86WJ1-2; Sequence=VSP_033342;
CC Name=3;
CC IsoId=Q86WJ1-3; Sequence=VSP_033341;
CC Name=4;
CC IsoId=Q86WJ1-4; Sequence=VSP_033340;
CC Name=5;
CC IsoId=Q86WJ1-5; Sequence=VSP_055675;
CC -!- TISSUE SPECIFICITY: Frequently overexpressed in hepatomacellular
CC carcinomas. {ECO:0000269|PubMed:18023026}.
CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding
CC and recruitment to DNA damage sites (PubMed:19661379, PubMed:29220653).
CC Mediates auto-inhibition of ATPase activity by interacting with the N-
CC terminal ATPase module, encompassing the helicase ATP-binding domain
CC and helicase C-terminal domain (PubMed:29220653). PARP1 activation upon
CC DNA damage and poly(ADP-ribose)-binding release the auto-inhibition by
CC the macro domain and trigger ATPase activity (PubMed:29220653). Does
CC not bind monomeric ADP-ribose and mono-ADP-ribose fails to release the
CC auto-inhibition of the ATPase module by the macro domain
CC (PubMed:29220653). {ECO:0000269|PubMed:19661379,
CC ECO:0000269|PubMed:29220653}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55248.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF537213; AAO49505.1; -; mRNA.
DR EMBL; AK001342; BAA91637.1; -; mRNA.
DR EMBL; AK027631; BAB55248.1; ALT_FRAME; mRNA.
DR EMBL; AK293157; BAG56702.1; -; mRNA.
DR EMBL; EF560738; ABQ59048.1; -; mRNA.
DR EMBL; AC242426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356378; CAH72650.1; -; Genomic_DNA.
DR EMBL; BC001171; AAH01171.1; -; mRNA.
DR EMBL; BC005038; AAH05038.1; -; mRNA.
DR EMBL; BC008649; AAH08649.1; -; mRNA.
DR EMBL; BC043501; AAH43501.1; -; mRNA.
DR EMBL; BC077717; AAH77717.1; -; mRNA.
DR EMBL; AK223496; BAD97216.1; -; mRNA.
DR CCDS; CCDS58021.1; -. [Q86WJ1-3]
DR CCDS; CCDS58022.1; -. [Q86WJ1-5]
DR CCDS; CCDS927.1; -. [Q86WJ1-1]
DR RefSeq; NP_001243266.1; NM_001256337.2. [Q86WJ1-5]
DR RefSeq; NP_001243267.1; NM_001256338.2. [Q86WJ1-3]
DR RefSeq; NP_001335382.1; NM_001348453.1. [Q86WJ1-4]
DR RefSeq; NP_001335385.1; NM_001348456.1. [Q86WJ1-5]
DR RefSeq; NP_001335386.1; NM_001348457.1. [Q86WJ1-5]
DR RefSeq; NP_001335387.1; NM_001348458.1. [Q86WJ1-5]
DR RefSeq; NP_001335388.1; NM_001348459.1. [Q86WJ1-5]
DR RefSeq; NP_001335389.1; NM_001348460.1. [Q86WJ1-5]
DR RefSeq; NP_001335390.1; NM_001348461.1. [Q86WJ1-5]
DR RefSeq; NP_001335391.1; NM_001348462.1. [Q86WJ1-5]
DR RefSeq; NP_001335392.1; NM_001348463.1. [Q86WJ1-5]
DR RefSeq; NP_001335393.1; NM_001348464.1. [Q86WJ1-5]
DR RefSeq; NP_001335394.1; NM_001348465.1. [Q86WJ1-5]
DR RefSeq; NP_001335395.1; NM_001348466.1. [Q86WJ1-5]
DR RefSeq; NP_004275.4; NM_004284.5. [Q86WJ1-1]
DR RefSeq; NP_078844.2; NM_024568.3. [Q86WJ1-4]
DR PDB; 6ZHX; EM; 2.50 A; K/L=604-639.
DR PDB; 6ZHY; EM; 3.00 A; K=604-639.
DR PDB; 7ENN; EM; 2.80 A; K=1-897.
DR PDB; 7EPU; X-ray; 3.50 A; B=1-880.
DR PDB; 7OTQ; EM; 4.80 A; K=16-879.
DR PDBsum; 6ZHX; -.
DR PDBsum; 6ZHY; -.
DR PDBsum; 7ENN; -.
DR PDBsum; 7EPU; -.
DR PDBsum; 7OTQ; -.
DR AlphaFoldDB; Q86WJ1; -.
DR SMR; Q86WJ1; -.
DR BioGRID; 114929; 94.
DR DIP; DIP-48933N; -.
DR IntAct; Q86WJ1; 49.
DR MINT; Q86WJ1; -.
DR STRING; 9606.ENSP00000358262; -.
DR GlyGen; Q86WJ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q86WJ1; -.
DR PhosphoSitePlus; Q86WJ1; -.
DR BioMuta; CHD1L; -.
DR DMDM; 311033359; -.
DR EPD; Q86WJ1; -.
DR jPOST; Q86WJ1; -.
DR MassIVE; Q86WJ1; -.
DR MaxQB; Q86WJ1; -.
DR PaxDb; Q86WJ1; -.
DR PeptideAtlas; Q86WJ1; -.
DR PRIDE; Q86WJ1; -.
DR ProteomicsDB; 6203; -.
DR ProteomicsDB; 70174; -. [Q86WJ1-1]
DR ProteomicsDB; 70175; -. [Q86WJ1-2]
DR ProteomicsDB; 70176; -. [Q86WJ1-3]
DR ProteomicsDB; 70177; -. [Q86WJ1-4]
DR ABCD; Q86WJ1; 1 sequenced antibody.
DR Antibodypedia; 20241; 204 antibodies from 30 providers.
DR DNASU; 9557; -.
DR Ensembl; ENST00000369258.8; ENSP00000358262.4; ENSG00000131778.20. [Q86WJ1-1]
DR Ensembl; ENST00000369259.4; ENSP00000358263.3; ENSG00000131778.20. [Q86WJ1-3]
DR GeneID; 9557; -.
DR KEGG; hsa:9557; -.
DR MANE-Select; ENST00000369258.8; ENSP00000358262.4; NM_004284.6; NP_004275.4.
DR UCSC; uc001epm.6; human. [Q86WJ1-1]
DR CTD; 9557; -.
DR DisGeNET; 9557; -.
DR GeneCards; CHD1L; -.
DR HGNC; HGNC:1916; CHD1L.
DR HPA; ENSG00000131778; Low tissue specificity.
DR MIM; 613039; gene.
DR neXtProt; NX_Q86WJ1; -.
DR OpenTargets; ENSG00000131778; -.
DR PharmGKB; PA26452; -.
DR VEuPathDB; HostDB:ENSG00000131778; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000159402; -.
DR InParanoid; Q86WJ1; -.
DR OMA; FIVHCVD; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q86WJ1; -.
DR TreeFam; TF333326; -.
DR PathwayCommons; Q86WJ1; -.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR SignaLink; Q86WJ1; -.
DR BioGRID-ORCS; 9557; 14 hits in 1095 CRISPR screens.
DR ChiTaRS; CHD1L; human.
DR GeneWiki; CHD1L; -.
DR GenomeRNAi; 9557; -.
DR Pharos; Q86WJ1; Tbio.
DR PRO; PR:Q86WJ1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q86WJ1; protein.
DR Bgee; ENSG00000131778; Expressed in C1 segment of cervical spinal cord and 158 other tissues.
DR ExpressionAtlas; Q86WJ1; baseline and differential.
DR Genevisible; Q86WJ1; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IMP:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; TAS:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
DR Gene3D; 3.40.220.10; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR031053; ALC1.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR002589; Macro_dom.
DR InterPro; IPR043472; Macro_dom-like.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR47157; PTHR47157; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF52949; SSF52949; 1.
DR PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Coiled coil; DNA damage;
KW DNA repair; Helicase; Hydrolase; Methylation; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..897
FT /note="Chromodomain-helicase-DNA-binding protein 1-like"
FT /id="PRO_0000332141"
FT DOMAIN 58..223
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 351..513
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 704..897
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 615..673
FT /note="Required for helicase activity"
FT /evidence="ECO:0000269|PubMed:29220653"
FT REGION 628..654
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..711
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 638..675
FT /evidence="ECO:0000255"
FT MOTIF 174..177
FT /note="DEAH box"
FT COMPBIAS 631..654
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 691..708
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 71..78
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 9
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 618
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 628
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 636
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT VAR_SEQ 1..281
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055675"
FT VAR_SEQ 1..113
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_033340"
FT VAR_SEQ 43..246
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033341"
FT VAR_SEQ 331..424
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033342"
FT VARIANT 25
FT /note="R -> P (in dbSNP:rs11588753)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_042954"
FT VARIANT 350
FT /note="H -> Q (in dbSNP:rs17356233)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_042955"
FT VARIANT 649
FT /note="E -> A (in dbSNP:rs13374920)"
FT /id="VAR_042956"
FT VARIANT 743
FT /note="S -> C (in dbSNP:rs2275249)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_042957"
FT VARIANT 885
FT /note="S -> A (in dbSNP:rs4950394)"
FT /evidence="ECO:0000269|PubMed:16710414"
FT /id="VAR_042958"
FT MUTAGEN 77
FT /note="K->R: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:19661379"
FT MUTAGEN 175
FT /note="E->Q: Abrogates chromatin remodeling activity."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 307..308
FT /note="KK->EE: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-398
FT and Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 319..320
FT /note="RK->EE: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-407;
FT Glu-422 and Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 332..337
FT /note="EPEPFE->APAPAA: Reduces interaction of the macro
FT domain with the N-terminal ATPase module; when associated
FT with Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 398
FT /note="R->E: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-307,
FT Glu-308 and Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 407
FT /note="K->E: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-319,
FT Glu-320, Glu-422 and Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 420
FT /note="S->A: Does not reduce interaction of the macro
FT domain with the N-terminal ATPase module; when associated
FT with Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 422
FT /note="R->E: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-319,
FT Glu-320, Glu-407 and Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 653..656
FT /note="KRRR->AAAA: Does not reduce interaction of the macro
FT domain with the N-terminal ATPase module; when associated
FT with Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 723
FT /note="D->A: Strongly reduces poly(ADP-ribose)-binding but
FT not ATPase activity."
FT /evidence="ECO:0000269|PubMed:19661379"
FT MUTAGEN 750
FT /note="G->E: Disrupts interaction with PARP1. Abolishes the
FT release from auto-inhibition through macro domain binding
FT to the N-terminal ATPase module. Reduces interaction of the
FT macro domain with the N-terminal ATPase module; when
FT associated with Glu-307, Glu-308 and Glu-398; Glu-319, Glu-
FT 320, Glu-407 and Glu-422; His-842 and Trp-860 or with Gln-
FT 857."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 842
FT /note="R->H: Loss of auto-inhibition; when associated with
FT Trp-860. Reduces interaction of the macro domain with the
FT N-terminal ATPase module; when associated with Trp-860 and
FT Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 857
FT /note="R->E,Q: Reduces interaction of the macro domain with
FT the N-terminal ATPase module; when associated with Glu-
FT 750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 857
FT /note="R->Q: Loss of auto-inhibition."
FT /evidence="ECO:0000269|PubMed:29220653"
FT MUTAGEN 860
FT /note="R->W: Loss of auto-inhibition; when associated with
FT His-842. Reduces interaction of the macro domain with the
FT N-terminal ATPase module; when associated with His-842 and
FT Glu-750."
FT /evidence="ECO:0000269|PubMed:29220653"
FT CONFLICT 192
FT /note="E -> EVFE (in Ref. 3; ABQ59048)"
FT /evidence="ECO:0000305"
FT CONFLICT 295
FT /note="M -> T (in Ref. 2; BAG56702)"
FT /evidence="ECO:0000305"
FT CONFLICT 379
FT /note="L -> P (in Ref. 2; BAB55248)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="N -> D (in Ref. 6; BAD97216)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="N -> S (in Ref. 6; BAD97216)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="M -> V (in Ref. 2; BAA91637)"
FT /evidence="ECO:0000305"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 48..63
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 77..90
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 107..117
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 123..125
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 130..137
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 210..220
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 254..257
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 263..266
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 284..295
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 301..306
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 325..327
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 341..345
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 347..362
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 366..371
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 373..386
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 400..411
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 416..420
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 435..439
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 445..453
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 475..487
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 490..497
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 517..519
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 537..544
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 549..552
FT /evidence="ECO:0007829|PDB:7ENN"
FT STRAND 569..573
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 587..598
FT /evidence="ECO:0007829|PDB:7ENN"
FT TURN 614..616
FT /evidence="ECO:0007829|PDB:7ENN"
FT HELIX 641..666
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 718..722
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 734..736
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 738..740
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 750..757
FT /evidence="ECO:0007829|PDB:7EPU"
FT TURN 758..760
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 761..771
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 800..802
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 808..810
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 818..834
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 837..840
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 845..847
FT /evidence="ECO:0007829|PDB:7EPU"
FT HELIX 849..862
FT /evidence="ECO:0007829|PDB:7EPU"
FT TURN 863..867
FT /evidence="ECO:0007829|PDB:7EPU"
FT STRAND 870..874
FT /evidence="ECO:0007829|PDB:7EPU"
SQ SEQUENCE 897 AA; 101000 MW; 226A1F8A44A8F9FE CRC64;
MERAGATSRG GQAPGFLLRL HTEGRAEAAR VQEQDLRQWG LTGIHLRSYQ LEGVNWLAQR
FHCQNGCILG DEMGLGKTCQ TIALFIYLAG RLNDEGPFLI LCPLSVLSNW KEEMQRFAPG
LSCVTYAGDK EERACLQQDL KQESRFHVLL TTYEICLKDA SFLKSFPWSV LVVDEAHRLK
NQSSLLHKTL SEFSVVFSLL LTGTPIQNSL QELYSLLSFV EPDLFSKEEV GDFIQRYQDI
EKESESASEL HKLLQPFLLR RVKAEVATEL PKKTEVVIYH GMSALQKKYY KAILMKDLDA
FENETAKKVK LQNILSQLRK CVDHPYLFDG VEPEPFEVGD HLTEASGKLH LLDKLLAFLY
SGGHRVLLFS QMTQMLDILQ DYMDYRGYSY ERVDGSVRGE ERHLAIKNFG QQPIFVFLLS
TRAGGVGMNL TAADTVIFVD SDFNPQNDLQ AAARAHRIGQ NKSVKVIRLI GRDTVEEIVY
RKAASKLQLT NMIIEGGHFT LGAQKPAADA DLQLSEILKF GLDKLLASEG STMDEIDLES
ILGETKDGQW VSDALPAAEG GSRDQEEGKN HMYLFEGKDY SKEPSKEDRK SFEQLVNLQK
TLLEKASQEG RSLRNKGSVL IPGLVEGSTK RKRVLSPEEL EDRQKKRQEA AAKRRRLIEE
KKRQKEEAEH KKKMAWWESN NYQSFCLPSE ESEPEDLENG EESSAELDYQ DPDATSLKYV
SGDVTHPQAG AEDALIVHCV DDSGHWGRGG LFTALEKRSA EPRKIYELAG KMKDLSLGGV
LLFPVDDKES RNKGQDLLAL IVAQHRDRSN VLSGIKMAAL EEGLKKIFLA AKKKKASVHL
PRIGHATKGF NWYGTERLIR KHLAARGIPT YIYYFPRSKS AVLHSQSSSS SSRQLVP
