CHD1L_MOUSE
ID CHD1L_MOUSE Reviewed; 900 AA.
AC Q9CXF7; Q3TMX1; Q6P5C0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE EC=3.6.4.12 {ECO:0000250|UniProtKB:Q86WJ1};
GN Name=Chd1l;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Liver;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: DNA helicase which plays a role in chromatin-remodeling
CC following DNA damage. Targeted to sites of DNA damage through
CC interaction with poly(ADP-ribose) and functions to regulate chromatin
CC during DNA repair. Able to catalyze nucleosome sliding in an ATP-
CC dependent manner. Helicase activity is strongly stimulated upon
CC poly(ADP-ribose)-binding. {ECO:0000250|UniProtKB:Q86WJ1}.
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:0000250|UniProtKB:Q86WJ1};
CC -!- SUBUNIT: Interacts (via macro domain) with PARP1; interacts only when
CC PARP1; interacts only when PARP1 is poly-ADP-ribosylated (PARylated)
CC (By similarity). Interacts with CIAO1 (By similarity).
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q86WJ1}.
CC Note=Localizes at sites of DNA damage. Probably recruited to DNA damage
CC sites by PARylated PARP1. {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CXF7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CXF7-2; Sequence=VSP_033343;
CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-binding
CC and recruitment to DNA damage sites (By similarity). Mediates auto-
CC inhibition of ATPase activity by interacting with the N-terminal ATPase
CC module, encompassing the helicase ATP-binding domain and helicase C-
CC terminal domain (By similarity). PARP1 activation upon DNA damage and
CC poly(ADP-ribose)-binding release the auto-inhibition by the macro
CC domain and trigger ATPase activity (By similarity).
CC {ECO:0000250|UniProtKB:Q86WJ1}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
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DR EMBL; AK014473; BAB29376.1; -; mRNA.
DR EMBL; AK165656; BAE38319.1; -; mRNA.
DR EMBL; BC052385; AAH52385.1; -; mRNA.
DR EMBL; BC057567; AAH57567.1; -; mRNA.
DR EMBL; BC062966; AAH62966.1; -; mRNA.
DR CCDS; CCDS38561.1; -. [Q9CXF7-1]
DR RefSeq; NP_080815.1; NM_026539.2. [Q9CXF7-1]
DR AlphaFoldDB; Q9CXF7; -.
DR SMR; Q9CXF7; -.
DR BioGRID; 212634; 1.
DR DIP; DIP-58953N; -.
DR IntAct; Q9CXF7; 1.
DR STRING; 10090.ENSMUSP00000029730; -.
DR iPTMnet; Q9CXF7; -.
DR PhosphoSitePlus; Q9CXF7; -.
DR EPD; Q9CXF7; -.
DR jPOST; Q9CXF7; -.
DR MaxQB; Q9CXF7; -.
DR PaxDb; Q9CXF7; -.
DR PeptideAtlas; Q9CXF7; -.
DR PRIDE; Q9CXF7; -.
DR ProteomicsDB; 283825; -. [Q9CXF7-1]
DR ProteomicsDB; 283826; -. [Q9CXF7-2]
DR Antibodypedia; 20241; 204 antibodies from 30 providers.
DR DNASU; 68058; -.
DR Ensembl; ENSMUST00000029730; ENSMUSP00000029730; ENSMUSG00000028089. [Q9CXF7-1]
DR GeneID; 68058; -.
DR KEGG; mmu:68058; -.
DR UCSC; uc008qow.1; mouse. [Q9CXF7-1]
DR UCSC; uc008qox.1; mouse. [Q9CXF7-2]
DR CTD; 9557; -.
DR MGI; MGI:1915308; Chd1l.
DR VEuPathDB; HostDB:ENSMUSG00000028089; -.
DR eggNOG; KOG0385; Eukaryota.
DR GeneTree; ENSGT00940000159402; -.
DR HOGENOM; CLU_000315_17_9_1; -.
DR InParanoid; Q9CXF7; -.
DR OMA; FIVHCVD; -.
DR OrthoDB; 61251at2759; -.
DR PhylomeDB; Q9CXF7; -.
DR TreeFam; TF333326; -.
DR Reactome; R-MMU-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-MMU-5696400; Dual Incision in GG-NER.
DR BioGRID-ORCS; 68058; 7 hits in 110 CRISPR screens.
DR ChiTaRS; Chd1l; mouse.
DR PRO; PR:Q9CXF7; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9CXF7; protein.
DR Bgee; ENSMUSG00000028089; Expressed in saccule of membranous labyrinth and 236 other tissues.
DR Genevisible; Q9CXF7; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; ISS:UniProtKB.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0000166; F:nucleotide binding; ISS:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
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; 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; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51154; MACRO; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; DNA damage; DNA repair;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..900
FT /note="Chromodomain-helicase-DNA-binding protein 1-like"
FT /id="PRO_0000332142"
FT DOMAIN 52..217
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 345..507
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 709..900
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT REGION 546..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 620..678
FT /note="Required for helicase activity"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT REGION 641..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 643..680
FT /evidence="ECO:0000255"
FT MOTIF 168..171
FT /note="DEAH box"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 534
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 612
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 623
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 641
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86WJ1"
FT VAR_SEQ 877..900
FT /note="IYYFPRSKARHSQPASSSSAPLVP -> MYPSVV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033343"
FT CONFLICT 300
FT /note="A -> S (in Ref. 2; AAH62966/AAH57567)"
FT /evidence="ECO:0000305"
FT CONFLICT 558
FT /note="G -> GG (in Ref. 1; BAE38319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 900 AA; 101438 MW; 89FEE484E71BBE09 CRC64;
MASGLPRFLQ ALPAEHGPEP LRTRVQEPDL QQWGLTGIRL RSYQLEGVNW LVQCFHCQNG
CILGDEMGLG KTCQTIALLI YLVGRLNDEG PFLVLCPLSV LSNWKEEMER FAPGLSCVTY
TGDKEERARL QQDLRQESGF HVLLTTYEIC LKDASFLKSF SWSVLAVDEA HRLKNQSSLL
HRTLSEFSAV FRLLLTGTPI QNSLRELYSL LCVVEPDLFC REQVEDFVQR YQDIEKESKS
ASELHRLLQP FLLRRVKAQV ATELPKKTEV VVYHGMSALQ KKYYKAILMK DLDAFENETA
KKVKLQNILT QLRKCVDHPY LFDGVEPEPF EVGEHLIEAS GKLHLLDRLL AFLYSGGHRV
LLFSQMTHML DILQDYMDYR GYSYERVDGS VRGEERHLAI KNFGNQPIFV FLLSTRAGGV
GMNLTAADTV IFVDSDFNPQ NDLQAAARAH RIGQNKSVKV IRLIGRDTVE EIVYRKAASK
LQLTNMVIEG GHFTPGAQKP SAEADFQLSE ILKFGLDKLL SSEGSSMEDI DLKSILGETK
DGQWTPDALP AAAAAGGGSL EPEEGSELES RSYENHMYLF EGRDYSKEPS KEDRKSFEQL
VNLQKTLLEK TSHGGRTLRN KGSVLIPGLA EGPIKRKKIL SPEELEDRRK KRQEAAAKRK
RLMEEKRKEK EEAEHRKKMA WWESNGYQSF CLSSEDSELE DLEGGDESSA ELAYEDLDST
SINYVSGDVT HPQAGEEDAV IVHCVDDSGR WGRGGLFTAL EVRSAEPRKI YELAGKMEDL
SLGDVLLFPI DDKESRDKGQ DLLALVVAQH RDRTNVLSGI KMAALEEGLK KIFLAAKKKK
ASVHLPRIGH ATKGFNWYGT ERLIRKHLAT RGIPTYIYYF PRSKARHSQP ASSSSAPLVP
