ID CHD1L_HUMAN Reviewed; 897 AA.
AC Q86WJ1; A5YM64; Q53EZ3; Q5VXX7; Q6DD94; Q6PK83; Q86XH3; Q96HF7;
AC Q96SP3; Q9BVJ1; Q9NVV8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2010, sequence version 2.
DT 01-MAY-2013, entry version 90.
DE RecName: Full=Chromodomain-helicase-DNA-binding protein 1-like;
DE EC=3.6.4.12;
DE AltName: Full=Amplified in liver cancer protein 1;
GN Name=CHD1L; Synonyms=ALC1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP AND VARIANT SER-885.
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
RT liver cancer 1, within a commonly amplified region at 1q21 in
RT hepatocellular carcinoma.";
RL Hepatology 47:503-510(2008).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-831 (ISOFORM 1), AND VARIANT SER-885.
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 VARIANTS
RP GLN-350 AND SER-885.
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA 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.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA 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.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA 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
RP SEQUENCE [LARGE SCALE MRNA] OF 2-897 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 15-897 (ISOFORM 2), AND VARIANTS PRO-25; CYS-743
RP AND SER-885.
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
RT project: 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, VARIANT [LARGE
RP SCALE ANALYSIS] SER-885, AND MASS SPECTROMETRY.
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.,
RA Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T.,
RA 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 MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] SER-885, AND MASS SPECTROMETRY.
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
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
CC chromatin during DNA repair. Able to catalyze nucleosome sliding
CC in an ATP-dependent manner. Helicase activity is strongly
CC stimulated upon poly(ADP-ribose)-binding.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Interacts with PARP1; interacts only when PARP1 is poly-
CC ADP-ribosylated (PARylated).
CC -!- SUBCELLULAR LOCATION: Nucleus. Note=Localizes at sites of DNA
CC damage. Probably recruited to DNA damage sites by PARylated PARP1.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
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 -!- TISSUE SPECIFICITY: Frequently overexpressed in hepatomacellular
CC carcinomas.
CC -!- DOMAIN: The macro domain mediates non-covalent poly(ADP-ribose)-
CC binding and recruitment to DNA damage sites.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 Macro domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55248.1; Type=Frameshift; Positions=597;
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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; EF560738; ABQ59048.1; -; mRNA.
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 IPI; IPI00329088; -.
DR IPI; IPI00854584; -.
DR IPI; IPI00890729; -.
DR IPI; IPI00890749; -.
DR RefSeq; NP_001243265.1; NM_001256336.1.
DR RefSeq; NP_001243266.1; NM_001256337.1.
DR RefSeq; NP_001243267.1; NM_001256338.1.
DR RefSeq; NP_004275.4; NM_004284.4.
DR RefSeq; NP_078844.2; NM_024568.2.
DR RefSeq; XP_003960255.1; XM_003960206.1.
DR RefSeq; XP_003960264.1; XM_003960215.1.
DR UniGene; Hs.191164; -.
DR HSSP; Q97XQ5; 1Z63.
DR ProteinModelPortal; Q86WJ1; -.
DR SMR; Q86WJ1; 41-547, 719-873.
DR DIP; DIP-48933N; -.
DR IntAct; Q86WJ1; 4.
DR PhosphoSite; Q86WJ1; -.
DR DMDM; 311033359; -.
DR PaxDb; Q86WJ1; -.
DR PRIDE; Q86WJ1; -.
DR Ensembl; ENST00000369258; ENSP00000358262; ENSG00000131778.
DR Ensembl; ENST00000369259; ENSP00000358263; ENSG00000131778.
DR Ensembl; ENST00000431239; ENSP00000389031; ENSG00000131778.
DR Ensembl; ENST00000579763; ENSP00000463454; ENSG00000264980.
DR Ensembl; ENST00000583055; ENSP00000464521; ENSG00000264980.
DR GeneID; 101060601; -.
DR GeneID; 9557; -.
DR KEGG; hsa:101060601; -.
DR KEGG; hsa:9557; -.
DR UCSC; uc001epm.4; human.
DR UCSC; uc001epo.4; human.
DR UCSC; uc009wjh.3; human.
DR CTD; 9557; -.
DR GeneCards; GC01P146717; -.
DR H-InvDB; HIX0000988; -.
DR H-InvDB; HIX0028745; -.
DR HGNC; HGNC:1916; CHD1L.
DR HPA; HPA027789; -.
DR HPA; HPA028670; -.
DR MIM; 613039; gene.
DR neXtProt; NX_Q86WJ1; -.
DR PharmGKB; PA26452; -.
DR eggNOG; COG0553; -.
DR HOVERGEN; HBG077542; -.
DR InParanoid; Q86WJ1; -.
DR OMA; TCQTIAL; -.
DR OrthoDB; EOG4SXNBV; -.
DR PhylomeDB; Q86WJ1; -.
DR ChiTaRS; CHD1L; human.
DR NextBio; 35849; -.
DR ArrayExpress; Q86WJ1; -.
DR Bgee; Q86WJ1; -.
DR CleanEx; HS_CHD1L; -.
DR Genevestigator; Q86WJ1; -.
DR GO; GO:0005737; C:cytoplasm; 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:0004003; F:ATP-dependent DNA helicase activity; TAS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0000166; F:nucleotide binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; TAS:UniProtKB.
DR InterPro; IPR002589; A1pp.
DR InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR000330; SNF2_N.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF00176; SNF2_N; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 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 Alternative splicing; ATP-binding; Coiled coil; Complete proteome;
KW DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Polymorphism; Reference proteome.
FT CHAIN 1 897 Chromodomain-helicase-DNA-binding protein
FT 1-like.
FT /FTId=PRO_0000332141.
FT DOMAIN 58 223 Helicase ATP-binding.
FT DOMAIN 351 513 Helicase C-terminal.
FT DOMAIN 704 897 Macro.
FT NP_BIND 71 78 ATP (By similarity).
FT COILED 638 675 Potential.
FT MOTIF 174 177 DEAH box.
FT MOD_RES 636 636 Phosphoserine.
FT MOD_RES 891 891 Phosphoserine.
FT VAR_SEQ 1 113 Missing (in isoform 4).
FT /FTId=VSP_033340.
FT VAR_SEQ 43 246 Missing (in isoform 3).
FT /FTId=VSP_033341.
FT VAR_SEQ 331 424 Missing (in isoform 2).
FT /FTId=VSP_033342.
FT VARIANT 25 25 R -> P (in dbSNP:rs11588753).
FT /FTId=VAR_042954.
FT VARIANT 350 350 H -> Q (in dbSNP:rs17356233).
FT /FTId=VAR_042955.
FT VARIANT 649 649 E -> A (in dbSNP:rs13374920).
FT /FTId=VAR_042956.
FT VARIANT 743 743 S -> C (in dbSNP:rs2275249).
FT /FTId=VAR_042957.
FT VARIANT 885 885 A -> S (in dbSNP:rs4950394).
FT /FTId=VAR_042958.
FT MUTAGEN 77 77 K->R: Abolishes ATPase activity.
FT MUTAGEN 723 723 D->A: Strongly reduces poly(ADP-ribose)-
FT binding but not ATPase activity.
FT CONFLICT 192 192 E -> EVFE (in Ref. 3; ABQ59048).
FT CONFLICT 379 379 L -> P (in Ref. 2; BAB55248).
FT CONFLICT 447 447 N -> D (in Ref. 6; BAD97216).
FT CONFLICT 597 597 N -> S (in Ref. 6; BAD97216).
FT CONFLICT 674 674 M -> V (in Ref. 2; BAA91637).
SQ SEQUENCE 897 AA; 100984 MW; 226A1F8A5272F9FE 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 AVLHAQSSSS SSRQLVP
//
