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Q86WJ1

- CHD1L_HUMAN

UniProt

Q86WJ1 - CHD1L_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 1-like

Gene

CHD1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (02 Nov 2010)
      Previous versions | rss
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    Functioni

    DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding.2 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi71 – 788ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATPase activity Source: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent DNA helicase activity Source: UniProtKB
    4. DNA binding Source: InterPro
    5. helicase activity Source: InterPro
    6. nucleic acid binding Source: InterPro
    7. nucleotide binding Source: UniProtKB
    8. protein binding Source: UniProtKB

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to DNA damage stimulus Source: UniProtKB
    3. chromatin remodeling Source: UniProtKB
    4. DNA duplex unwinding Source: GOC
    5. DNA repair Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromodomain-helicase-DNA-binding protein 1-like (EC:3.6.4.12)
    Alternative name(s):
    Amplified in liver cancer protein 1
    Gene namesi
    Name:CHD1L
    Synonyms:ALC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:1916. CHD1L.

    Subcellular locationi

    Nucleus 1 Publication
    Note: Localizes at sites of DNA damage. Probably recruited to DNA damage sites by PARylated PARP1.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. nucleus Source: UniProtKB
    3. plasma membrane Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi77 – 771K → R: Abolishes ATPase activity. 1 Publication
    Mutagenesisi723 – 7231D → A: Strongly reduces poly(ADP-ribose)-binding but not ATPase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA26452.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 897897Chromodomain-helicase-DNA-binding protein 1-likePRO_0000332141Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei636 – 6361Phosphoserine1 Publication
    Modified residuei891 – 8911Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ86WJ1.
    PaxDbiQ86WJ1.
    PRIDEiQ86WJ1.

    PTM databases

    PhosphoSiteiQ86WJ1.

    Expressioni

    Tissue specificityi

    Frequently overexpressed in hepatomacellular carcinomas.1 Publication

    Gene expression databases

    ArrayExpressiQ86WJ1.
    BgeeiQ86WJ1.
    CleanExiHS_CHD1L.
    GenevestigatoriQ86WJ1.

    Organism-specific databases

    HPAiHPA027789.
    HPA028670.

    Interactioni

    Subunit structurei

    Interacts with PARP1; interacts only when PARP1 is poly-ADP-ribosylated (PARylated).1 Publication

    Protein-protein interaction databases

    BioGridi114929. 29 interactions.
    DIPiDIP-48933N.
    IntActiQ86WJ1. 7 interactions.
    MINTiMINT-7944527.

    Structurei

    3D structure databases

    ProteinModelPortaliQ86WJ1.
    SMRiQ86WJ1. Positions 41-547, 719-873.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini58 – 223166Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini351 – 513163Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini704 – 897194MacroPROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili638 – 67538Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi174 – 1774DEAH box

    Domaini

    The macro domain mediates non-covalent poly(ADP-ribose)-binding and recruitment to DNA damage sites.1 Publication

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation
    Contains 1 Macro domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG0553.
    HOVERGENiHBG077542.
    InParanoidiQ86WJ1.
    OMAiRAFEINP.
    PhylomeDBiQ86WJ1.
    TreeFamiTF333326.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR002589. Macro_dom.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51154. MACRO. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q86WJ1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MERAGATSRG GQAPGFLLRL HTEGRAEAAR VQEQDLRQWG LTGIHLRSYQ    50
    LEGVNWLAQR FHCQNGCILG DEMGLGKTCQ TIALFIYLAG RLNDEGPFLI 100
    LCPLSVLSNW KEEMQRFAPG LSCVTYAGDK EERACLQQDL KQESRFHVLL 150
    TTYEICLKDA SFLKSFPWSV LVVDEAHRLK NQSSLLHKTL SEFSVVFSLL 200
    LTGTPIQNSL QELYSLLSFV EPDLFSKEEV GDFIQRYQDI EKESESASEL 250
    HKLLQPFLLR RVKAEVATEL PKKTEVVIYH GMSALQKKYY KAILMKDLDA 300
    FENETAKKVK LQNILSQLRK CVDHPYLFDG VEPEPFEVGD HLTEASGKLH 350
    LLDKLLAFLY SGGHRVLLFS QMTQMLDILQ DYMDYRGYSY ERVDGSVRGE 400
    ERHLAIKNFG QQPIFVFLLS TRAGGVGMNL TAADTVIFVD SDFNPQNDLQ 450
    AAARAHRIGQ NKSVKVIRLI GRDTVEEIVY RKAASKLQLT NMIIEGGHFT 500
    LGAQKPAADA DLQLSEILKF GLDKLLASEG STMDEIDLES ILGETKDGQW 550
    VSDALPAAEG GSRDQEEGKN HMYLFEGKDY SKEPSKEDRK SFEQLVNLQK 600
    TLLEKASQEG RSLRNKGSVL IPGLVEGSTK RKRVLSPEEL EDRQKKRQEA 650
    AAKRRRLIEE KKRQKEEAEH KKKMAWWESN NYQSFCLPSE ESEPEDLENG 700
    EESSAELDYQ DPDATSLKYV SGDVTHPQAG AEDALIVHCV DDSGHWGRGG 750
    LFTALEKRSA EPRKIYELAG KMKDLSLGGV LLFPVDDKES RNKGQDLLAL 800
    IVAQHRDRSN VLSGIKMAAL EEGLKKIFLA AKKKKASVHL PRIGHATKGF 850
    NWYGTERLIR KHLAARGIPT YIYYFPRSKS AVLHAQSSSS SSRQLVP 897
    Length:897
    Mass (Da):100,984
    Last modified:November 2, 2010 - v2
    Checksum:i226A1F8A5272F9FE
    GO
    Isoform 2 (identifier: Q86WJ1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         331-424: Missing.

    Show »
    Length:803
    Mass (Da):90,239
    Checksum:i946382BEB5C3FE59
    GO
    Isoform 3 (identifier: Q86WJ1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         43-246: Missing.

    Show »
    Length:693
    Mass (Da):77,739
    Checksum:i06F3DA517A960C94
    GO
    Isoform 4 (identifier: Q86WJ1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-113: Missing.

    Show »
    Length:784
    Mass (Da):88,403
    Checksum:i76E431268F87A9D1
    GO
    Isoform 5 (identifier: Q86WJ1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-281: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:616
    Mass (Da):69,139
    Checksum:i34C571CA478C4FC5
    GO

    Sequence cautioni

    The sequence BAB55248.1 differs from that shown. Reason: Frameshift at position 597.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921E → EVFE in ABQ59048. (PubMed:17974005)Curated
    Sequence conflicti295 – 2951M → T in BAG56702. (PubMed:14702039)Curated
    Sequence conflicti379 – 3791L → P in BAB55248. (PubMed:14702039)Curated
    Sequence conflicti447 – 4471N → D in BAD97216. 1 PublicationCurated
    Sequence conflicti597 – 5971N → S in BAD97216. 1 PublicationCurated
    Sequence conflicti674 – 6741M → V in BAA91637. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti25 – 251R → P.1 Publication
    Corresponds to variant rs11588753 [ dbSNP | Ensembl ].
    VAR_042954
    Natural varianti350 – 3501H → Q.1 Publication
    Corresponds to variant rs17356233 [ dbSNP | Ensembl ].
    VAR_042955
    Natural varianti649 – 6491E → A.
    Corresponds to variant rs13374920 [ dbSNP | Ensembl ].
    VAR_042956
    Natural varianti743 – 7431S → C.2 Publications
    Corresponds to variant rs2275249 [ dbSNP | Ensembl ].
    VAR_042957
    Natural varianti885 – 8851A → S.6 Publications
    Corresponds to variant rs4950394 [ dbSNP | Ensembl ].
    VAR_042958

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 281281Missing in isoform 5. 1 PublicationVSP_055675Add
    BLAST
    Alternative sequencei1 – 113113Missing in isoform 4. 1 PublicationVSP_033340Add
    BLAST
    Alternative sequencei43 – 246204Missing in isoform 3. 1 PublicationVSP_033341Add
    BLAST
    Alternative sequencei331 – 42494Missing in isoform 2. 1 PublicationVSP_033342Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537213 mRNA. Translation: AAO49505.1.
    AK001342 mRNA. Translation: BAA91637.1.
    AK027631 mRNA. Translation: BAB55248.1. Frameshift.
    AK293157 mRNA. Translation: BAG56702.1.
    EF560738 mRNA. Translation: ABQ59048.1.
    AL356378 Genomic DNA. Translation: CAH72650.1.
    BC001171 mRNA. Translation: AAH01171.1.
    BC005038 mRNA. Translation: AAH05038.1.
    BC008649 mRNA. Translation: AAH08649.1.
    BC043501 mRNA. Translation: AAH43501.1.
    BC077717 mRNA. Translation: AAH77717.1.
    AK223496 mRNA. Translation: BAD97216.1.
    CCDSiCCDS58021.1. [Q86WJ1-3]
    CCDS927.1. [Q86WJ1-1]
    RefSeqiNP_001243265.1. NM_001256336.1.
    NP_001243266.1. NM_001256337.1.
    NP_001243267.1. NM_001256338.1.
    NP_004275.4. NM_004284.4.
    NP_078844.2. NM_024568.2.
    UniGeneiHs.191164.

    Genome annotation databases

    EnsembliENST00000361293; ENSP00000355100; ENSG00000131778. [Q86WJ1-5]
    ENST00000369258; ENSP00000358262; ENSG00000131778. [Q86WJ1-1]
    ENST00000369259; ENSP00000358263; ENSG00000131778. [Q86WJ1-3]
    ENST00000431239; ENSP00000389031; ENSG00000131778. [Q86WJ1-2]
    GeneIDi9557.
    KEGGihsa:9557.
    UCSCiuc001epm.5. human. [Q86WJ1-1]
    uc001epo.5. human. [Q86WJ1-3]
    uc009wjh.4. human. [Q86WJ1-2]

    Polymorphism databases

    DMDMi311033359.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF537213 mRNA. Translation: AAO49505.1 .
    AK001342 mRNA. Translation: BAA91637.1 .
    AK027631 mRNA. Translation: BAB55248.1 . Frameshift.
    AK293157 mRNA. Translation: BAG56702.1 .
    EF560738 mRNA. Translation: ABQ59048.1 .
    AL356378 Genomic DNA. Translation: CAH72650.1 .
    BC001171 mRNA. Translation: AAH01171.1 .
    BC005038 mRNA. Translation: AAH05038.1 .
    BC008649 mRNA. Translation: AAH08649.1 .
    BC043501 mRNA. Translation: AAH43501.1 .
    BC077717 mRNA. Translation: AAH77717.1 .
    AK223496 mRNA. Translation: BAD97216.1 .
    CCDSi CCDS58021.1. [Q86WJ1-3 ]
    CCDS927.1. [Q86WJ1-1 ]
    RefSeqi NP_001243265.1. NM_001256336.1.
    NP_001243266.1. NM_001256337.1.
    NP_001243267.1. NM_001256338.1.
    NP_004275.4. NM_004284.4.
    NP_078844.2. NM_024568.2.
    UniGenei Hs.191164.

    3D structure databases

    ProteinModelPortali Q86WJ1.
    SMRi Q86WJ1. Positions 41-547, 719-873.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114929. 29 interactions.
    DIPi DIP-48933N.
    IntActi Q86WJ1. 7 interactions.
    MINTi MINT-7944527.

    PTM databases

    PhosphoSitei Q86WJ1.

    Polymorphism databases

    DMDMi 311033359.

    Proteomic databases

    MaxQBi Q86WJ1.
    PaxDbi Q86WJ1.
    PRIDEi Q86WJ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361293 ; ENSP00000355100 ; ENSG00000131778 . [Q86WJ1-5 ]
    ENST00000369258 ; ENSP00000358262 ; ENSG00000131778 . [Q86WJ1-1 ]
    ENST00000369259 ; ENSP00000358263 ; ENSG00000131778 . [Q86WJ1-3 ]
    ENST00000431239 ; ENSP00000389031 ; ENSG00000131778 . [Q86WJ1-2 ]
    GeneIDi 9557.
    KEGGi hsa:9557.
    UCSCi uc001epm.5. human. [Q86WJ1-1 ]
    uc001epo.5. human. [Q86WJ1-3 ]
    uc009wjh.4. human. [Q86WJ1-2 ]

    Organism-specific databases

    CTDi 9557.
    GeneCardsi GC01P146717.
    H-InvDB HIX0000988.
    HIX0028745.
    HGNCi HGNC:1916. CHD1L.
    HPAi HPA027789.
    HPA028670.
    MIMi 613039. gene.
    neXtProti NX_Q86WJ1.
    PharmGKBi PA26452.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOVERGENi HBG077542.
    InParanoidi Q86WJ1.
    OMAi RAFEINP.
    PhylomeDBi Q86WJ1.
    TreeFami TF333326.

    Miscellaneous databases

    ChiTaRSi CHD1L. human.
    GeneWikii CHD1L.
    GenomeRNAii 9557.
    NextBioi 35849.
    PROi Q86WJ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q86WJ1.
    Bgeei Q86WJ1.
    CleanExi HS_CHD1L.
    Genevestigatori Q86WJ1.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR002589. Macro_dom.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    PS51154. MACRO. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Isolation and characterization of a novel oncogene, amplified in liver cancer 1, within a commonly amplified region at 1q21 in hepatocellular carcinoma."
      Ma N.-F., Hu L., Fung J.-M., Xie D., Zheng B.-J., Chen L., Tang D.-J., Fu L., Wu Z., Chen M., Fang Y., Guan X.-Y.
      Hepatology 47:503-510(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, VARIANT SER-885.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5), VARIANTS CYS-743 AND SER-885.
      Tissue: Neuron.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS GLN-350 AND SER-885.
      Tissue: Retina.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-897 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 15-897 (ISOFORM 2), VARIANTS PRO-25; CYS-743 AND SER-885.
      Tissue: Brain, Eye, Prostate and Skin.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 97-798.
      Tissue: Hepatocyte.
    7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891, VARIANT [LARGE SCALE ANALYSIS] SER-885, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    8. "Poly(ADP-ribose)-dependent regulation of DNA repair by the chromatin remodeling enzyme ALC1."
      Ahel D., Horejsi Z., Wiechens N., Polo S.E., Garcia-Wilson E., Ahel I., Flynn H., Skehel M., West S.C., Jackson S.P., Owen-Hughes T., Boulton S.J.
      Science 325:1240-1243(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN MACRO, ADP-RIBOSE-BINDING, INTERACTION WITH PARP1, MUTAGENESIS OF LYS-77 AND ASP-723.
    9. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-636, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: VARIANT [LARGE SCALE ANALYSIS] SER-885, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCHD1L_HUMAN
    AccessioniPrimary (citable) accession number: Q86WJ1
    Secondary accession number(s): A5YM64
    , B4DDE1, B5MDZ7, Q53EZ3, Q5VXX7, Q6DD94, Q6PK83, Q86XH3, Q96HF7, Q96SP3, Q9BVJ1, Q9NVV8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 29, 2008
    Last sequence update: November 2, 2010
    Last modified: October 1, 2014
    This is version 105 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3