SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CXF7

- CHD1L_MOUSE

UniProt

Q9CXF7 - CHD1L_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Chromodomain-helicase-DNA-binding protein 1-like
Gene
Chd1l
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at transcript 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 By similarity.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi65 – 728ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATPase activity Source: UniProtKB
  3. DNA binding Source: InterPro
  4. helicase activity Source: UniProtKB-KW
  5. nucleotide binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. chromatin remodeling 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)
Gene namesi
Name:Chd1l
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1915308. Chd1l.

Subcellular locationi

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 900900Chromodomain-helicase-DNA-binding protein 1-like
PRO_0000332142Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei641 – 6411Phosphoserine By similarity
Modified residuei894 – 8941Phosphoserine By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ9CXF7.
PRIDEiQ9CXF7.

PTM databases

PhosphoSiteiQ9CXF7.

Expressioni

Gene expression databases

BgeeiQ9CXF7.
GenevestigatoriQ9CXF7.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi212634. 1 interaction.
DIPiDIP-58953N.
STRINGi10090.ENSMUSP00000029730.

Structurei

3D structure databases

ProteinModelPortaliQ9CXF7.
SMRiQ9CXF7. Positions 22-547, 722-878.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini52 – 217166Helicase ATP-binding
Add
BLAST
Domaini345 – 507163Helicase C-terminal
Add
BLAST
Domaini709 – 900192Macro
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili643 – 68038 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi168 – 1714DEAH box

Domaini

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

Sequence similaritiesi

Contains 1 Macro domain.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00680000100002.
HOGENOMiHOG000030789.
HOVERGENiHBG077542.
InParanoidiQ9CXF7.
OMAiNWKEEME.
OrthoDBiEOG72G16M.
PhylomeDBiQ9CXF7.
TreeFamiTF333326.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR014001. 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.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51154. MACRO. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9CXF7-1) [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

MASGLPRFLQ ALPAEHGPEP LRTRVQEPDL QQWGLTGIRL RSYQLEGVNW    50
LVQCFHCQNG CILGDEMGLG KTCQTIALLI YLVGRLNDEG PFLVLCPLSV 100
LSNWKEEMER FAPGLSCVTY TGDKEERARL QQDLRQESGF HVLLTTYEIC 150
LKDASFLKSF SWSVLAVDEA HRLKNQSSLL HRTLSEFSAV FRLLLTGTPI 200
QNSLRELYSL LCVVEPDLFC REQVEDFVQR YQDIEKESKS ASELHRLLQP 250
FLLRRVKAQV ATELPKKTEV VVYHGMSALQ KKYYKAILMK DLDAFENETA 300
KKVKLQNILT QLRKCVDHPY LFDGVEPEPF EVGEHLIEAS GKLHLLDRLL 350
AFLYSGGHRV LLFSQMTHML DILQDYMDYR GYSYERVDGS VRGEERHLAI 400
KNFGNQPIFV FLLSTRAGGV GMNLTAADTV IFVDSDFNPQ NDLQAAARAH 450
RIGQNKSVKV IRLIGRDTVE EIVYRKAASK LQLTNMVIEG GHFTPGAQKP 500
SAEADFQLSE ILKFGLDKLL SSEGSSMEDI DLKSILGETK DGQWTPDALP 550
AAAAAGGGSL EPEEGSELES RSYENHMYLF EGRDYSKEPS KEDRKSFEQL 600
VNLQKTLLEK TSHGGRTLRN KGSVLIPGLA EGPIKRKKIL SPEELEDRRK 650
KRQEAAAKRK RLMEEKRKEK EEAEHRKKMA WWESNGYQSF CLSSEDSELE 700
DLEGGDESSA ELAYEDLDST SINYVSGDVT HPQAGEEDAV IVHCVDDSGR 750
WGRGGLFTAL EVRSAEPRKI YELAGKMEDL SLGDVLLFPI DDKESRDKGQ 800
DLLALVVAQH RDRTNVLSGI KMAALEEGLK KIFLAAKKKK ASVHLPRIGH 850
ATKGFNWYGT ERLIRKHLAT RGIPTYIYYF PRSKARHSQP ASSSSAPLVP 900
Length:900
Mass (Da):101,438
Last modified:June 1, 2001 - v1
Checksum:i89FEE484E71BBE09
GO
Isoform 2 (identifier: Q9CXF7-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     877-900: IYYFPRSKARHSQPASSSSAPLVP → MYPSVV

Show »
Length:882
Mass (Da):99,485
Checksum:i3109C6228FD48C9E
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei877 – 90024IYYFP…APLVP → MYPSVV in isoform 2.
VSP_033343Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti300 – 3001A → S in AAH62966. 1 Publication
Sequence conflicti300 – 3001A → S in AAH57567. 1 Publication
Sequence conflicti558 – 5581G → GG in BAE38319. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK014473 mRNA. Translation: BAB29376.1.
AK165656 mRNA. Translation: BAE38319.1.
BC052385 mRNA. Translation: AAH52385.1.
BC057567 mRNA. Translation: AAH57567.1.
BC062966 mRNA. Translation: AAH62966.1.
CCDSiCCDS38561.1. [Q9CXF7-1]
RefSeqiNP_080815.1. NM_026539.2. [Q9CXF7-1]
UniGeneiMm.41447.

Genome annotation databases

EnsembliENSMUST00000029730; ENSMUSP00000029730; ENSMUSG00000028089. [Q9CXF7-1]
GeneIDi68058.
KEGGimmu:68058.
UCSCiuc008qow.1. mouse. [Q9CXF7-1]
uc008qox.1. mouse. [Q9CXF7-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK014473 mRNA. Translation: BAB29376.1 .
AK165656 mRNA. Translation: BAE38319.1 .
BC052385 mRNA. Translation: AAH52385.1 .
BC057567 mRNA. Translation: AAH57567.1 .
BC062966 mRNA. Translation: AAH62966.1 .
CCDSi CCDS38561.1. [Q9CXF7-1 ]
RefSeqi NP_080815.1. NM_026539.2. [Q9CXF7-1 ]
UniGenei Mm.41447.

3D structure databases

ProteinModelPortali Q9CXF7.
SMRi Q9CXF7. Positions 22-547, 722-878.
ModBasei Search...

Protein-protein interaction databases

BioGridi 212634. 1 interaction.
DIPi DIP-58953N.
STRINGi 10090.ENSMUSP00000029730.

PTM databases

PhosphoSitei Q9CXF7.

Proteomic databases

PaxDbi Q9CXF7.
PRIDEi Q9CXF7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000029730 ; ENSMUSP00000029730 ; ENSMUSG00000028089 . [Q9CXF7-1 ]
GeneIDi 68058.
KEGGi mmu:68058.
UCSCi uc008qow.1. mouse. [Q9CXF7-1 ]
uc008qox.1. mouse. [Q9CXF7-2 ]

Organism-specific databases

CTDi 9557.
MGIi MGI:1915308. Chd1l.

Phylogenomic databases

eggNOGi COG0553.
GeneTreei ENSGT00680000100002.
HOGENOMi HOG000030789.
HOVERGENi HBG077542.
InParanoidi Q9CXF7.
OMAi NWKEEME.
OrthoDBi EOG72G16M.
PhylomeDBi Q9CXF7.
TreeFami TF333326.

Miscellaneous databases

ChiTaRSi CHD1L. mouse.
NextBioi 326336.
PROi Q9CXF7.
SOURCEi Search...

Gene expression databases

Bgeei Q9CXF7.
Genevestigatori Q9CXF7.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi 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 PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51154. MACRO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6J.
    Tissue: Kidney and Liver.
  2. "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 1).
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiCHD1L_MOUSE
AccessioniPrimary (citable) accession number: Q9CXF7
Secondary accession number(s): Q3TMX1, Q6P5C0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 29, 2008
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi