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Q86WJ1

- CHD1L_HUMAN

UniProt

Q86WJ1 - CHD1L_HUMAN

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Protein

Chromodomain-helicase-DNA-binding protein 1-like

Gene
CHD1L, ALC1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 788ATP By similarity

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. nucleotide binding Source: UniProtKB
  6. 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
Complete GO annotation...

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

GO - Cellular componenti

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

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini58 – 223166Helicase ATP-bindingAdd
BLAST
Domaini351 – 513163Helicase C-terminalAdd
BLAST
Domaini704 – 897194MacroAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili638 – 67538 Reviewed predictionAdd
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

Contains 1 Macro domain.

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.

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.1 Publication
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. VSP_055675Add
BLAST
Alternative sequencei1 – 113113Missing in isoform 4. VSP_033340Add
BLAST
Alternative sequencei43 – 246204Missing in isoform 3. VSP_033341Add
BLAST
Alternative sequencei331 – 42494Missing in isoform 2. VSP_033342Add
BLAST

Sequence conflict

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

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

EnsembliENST00000369258; ENSP00000358262; ENSG00000131778. [Q86WJ1-1]
ENST00000369259; ENSP00000358263; ENSG00000131778. [Q86WJ1-3]
ENST00000431239; ENSP00000389031; ENSG00000131778. [Q86WJ1-2]
ENST00000579763; ENSP00000463454; ENSG00000264980.
ENST00000583055; ENSP00000464521; ENSG00000264980.
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 ENST00000369258 ; ENSP00000358262 ; ENSG00000131778 . [Q86WJ1-1 ]
ENST00000369259 ; ENSP00000358263 ; ENSG00000131778 . [Q86WJ1-3 ]
ENST00000431239 ; ENSP00000389031 ; ENSG00000131778 . [Q86WJ1-2 ]
ENST00000579763 ; ENSP00000463454 ; ENSG00000264980 .
ENST00000583055 ; ENSP00000464521 ; ENSG00000264980 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 104 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

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