Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P40201 (CHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 1

Short name=CHD-1
EC=3.6.4.12
Alternative name(s):
ATP-dependent helicase CHD1
Gene names
Name:Chd1
Synonyms:Chd-1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1711 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

ATP-dependent chromatin-remodeling factor which functions as substrate recognition component of the transcription regulatory histone acetylation (HAT) complex SAGA. Regulates polymerase II transcription. Also required for efficient transcription by RNA polymerase I, and more specifically the polymerase I transcription termination step. Regulates negatively DNA replication. Not only involved in transcription-related chromatin-remodeling, but also required to maintain a specific chromatin configuration across the genome. Required for the bridging of SNF2, the FACT complex, the PAF complex as well as the U2 snRNP complex to H3K4me3. Functions to modulate the efficiency of pre-mRNA splicing in part through physical bridging of spliceosomal components to H3K4me3 By similarity. Required for maintaining open chromatin and pluripotency in embryonic stem cells. Is also associated with histone deacetylase (HDAC) activity. Ref.6 Ref.7

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the SAGA complex By similarity. Specifically interacts with methylated H3K4me2 and H3K4me3. Interacts with the FACT complex, the PAF complex and the U2 snRNP. Interacts directly with PAF1, SFA3A1, SFA3A2, SFA3A3, SNF2 and SSRP1 By similarity. Interacts with BCLAF1, NCoR, SRP20 and SAFB. Ref.5 Ref.6 Ref.7

Subcellular location

Nucleus. Cytoplasm. Note: Is released into the cytoplasm when cells enter mitosis and is reincorporated into chromatin during telophase-cytokinesis. Ref.4 Ref.5

Tissue specificity

Abundance is higher in cells representing early stages of the B-lymphoid lineage such as pre-B and B-cells, than in cells representing mature plasmacytes or other cell lineages such as fibroblasts.

Domain

The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3) By similarity. Ref.5

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 17111711Chromodomain-helicase-DNA-binding protein 1
PRO_0000080225

Regions

Domain270 – 36293Chromo 1
Domain387 – 45064Chromo 2
Domain491 – 661171Helicase ATP-binding
Domain790 – 941152Helicase C-terminal
Repeat1629 – 163351
Repeat1635 – 163952
Repeat1641 – 164553
Nucleotide binding504 – 5118ATP Potential
Region1629 – 1645173 X 5 AA repeats of H-S-D-H-R
Motif612 – 6154DEAH box
Compositional bias1 – 7070Ser-rich
Compositional bias116 – 13621Ser-rich

Amino acid modifications

Modified residue2141Phosphoserine By similarity
Modified residue2151Phosphoserine By similarity
Modified residue2351Phosphothreonine By similarity
Modified residue2391Phosphoserine By similarity
Modified residue2481Phosphothreonine By similarity
Modified residue2501Phosphoserine By similarity
Modified residue10231Phosphoserine By similarity
Modified residue10381Phosphoserine By similarity
Modified residue10791Phosphoserine By similarity
Modified residue10941Phosphoserine By similarity
Modified residue10961Phosphoserine By similarity
Modified residue10981Phosphoserine By similarity
Modified residue11001Phosphoserine By similarity
Modified residue13531Phosphoserine By similarity
Modified residue13551Phosphoserine By similarity
Modified residue13561Phosphoserine By similarity
Modified residue13601Phosphoserine By similarity
Modified residue13631Phosphoserine By similarity
Modified residue16781Phosphoserine By similarity

Experimental info

Sequence conflict1591S → L in AAB08486. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P40201 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 51499636E943A856

FASTA1,711196,385
        10         20         30         40         50         60 
MNGHSDEESV RNGSGESSQS GDDCGSASGS GSGSSSGSSS DGSSSQSGSS DSDSGSDSGS 

        70         80         90        100        110        120 
QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA MLRKQPQQAQ QQRPASSNSG 

       130        140        150        160        170        180 
SEEDSSSSED SDDSSSGAKR KKHNDEDWQM SGSGSPSQSG SDSESEEERD KSSCDGTESD 

       190        200        210        220        230        240 
YEPKNKVRSR KPQNRSKSKN GKKILGQKKR QIDSSEDEDD EDYDNDKRSS RRQATVNVSY 

       250        260        270        280        290        300 
KEDEEMKTDS DDLLEVCGED VPQPEDEEFE TIERVMDCRV GRKGATGATT TIYAVEADGD 

       310        320        330        340        350        360 
PNAGFERNKE PGDIQYLIKW KGWSHIHNTW ETEETLKQQN VRGMKKLDNY KKKDQETKRW 

       370        380        390        400        410        420 
LKNASPEDVE YYNCQQELTD DLHKQYQIVE RIIAHSNQKS AAGLPDYYCK WQGLPYSECS 

       430        440        450        460        470        480 
WEDGALISKK FQTCIDEYFS RNQSKTTPFK DCKVLKQRPR FVALKKQPSY IGGHEGLELR 

       490        500        510        520        530        540 
DYQLNGLNWL AHSWCKGNSC ILADEMGLGK TIQTISFLNY LFHEHQLYGP FLLVVPLSTL 

       550        560        570        580        590        600 
TSWQREIQTW ASQMNAVVYL GDINSRNMIR THEWMHPQTK RLKFNILLTT YEILLKDKAF 

       610        620        630        640        650        660 
LGGLNWAFIG VDEAHRLKND DSLLYKTLID FKSNHRLLIT GTPLQNSLKE LWSLLHFIMP 

       670        680        690        700        710        720 
EKFSSWEDFE EEHGKGREYG YASLHKELEP FLLRRVKKDV EKSLPAKVEQ ILRMEMSALQ 

       730        740        750        760        770        780 
KQYYKWILTR NYKALSKGSK GSTSGFLNIM MELKKCCNHC YLIKPPDNNE FYNKQEALQH 

       790        800        810        820        830        840 
LIRSSGKLIL LDKLLIRLRE RGNRVLIFSQ MVRMLDILAE YLKYRQFPFQ RLDGSIKGEL 

       850        860        870        880        890        900 
RKQALDHFNA EGSEDFCFLL STRAGGLGIN LASADTVVIF DSDWNPQNDL QAQARAHRIG 

       910        920        930        940        950        960 
QKKQVNIYRL VTKGSVEEDI LERAKKKMVL DHLVIQRMDT TGKTVLHTGS APSSSTPFNK 

       970        980        990       1000       1010       1020 
EELSAILKFG AEELFKEPEG EEQEPQEMDI DEILKRAETH ENEPGPLSVG DELLSQFKVA 

      1030       1040       1050       1060       1070       1080 
NFSNMDEDDI ELEPERNSKN WEEIIPEEQR RRLEEEERQK ELEEIYMLPR MRNCAKQISF 

      1090       1100       1110       1120       1130       1140 
NGSEGRRSRS RRYSGSDSDS ISERKRPKKR GRPRTIPREN IKGFSDAEIR RFIKSYKKFG 

      1150       1160       1170       1180       1190       1200 
GPLERLDAIA RDAELVDKSE TDLRRLGELV HNGCVKALKD SSSGTERAGG RLGKVKGPTF 

      1210       1220       1230       1240       1250       1260 
RISGVQVNAK LVIAHEDELI PLHKSIPSDP EERKQYTIPC HTKAAHFDID WGKEDDSNLL 

      1270       1280       1290       1300       1310       1320 
IGIYEYGYGS WEMIKMDPDL SLTHKILPDD PDKKPQAKQL QTRADYLIKL LSRDLAKREA 

      1330       1340       1350       1360       1370       1380 
QRLCGAGGSK RRKTRAKKSK AMKSIKVKEE IKSDSSPLPS EKSDEDDDKL NDSKPESKDR 

      1390       1400       1410       1420       1430       1440 
SKKSVVSDAP VHITASGEPV PIAEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE 

      1450       1460       1470       1480       1490       1500 
REQLEHTRQC LIKIGDHITE CLKEYSNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA 

      1510       1520       1530       1540       1550       1560 
IKKRQESQQN SDQNSNVATT HVIRNPDMER LKENTNHDDS SRDSYSSDRH LSQYHDHHKD 

      1570       1580       1590       1600       1610       1620 
RHQGDSYKKS DSRKRPYSSF SNGKDHREWD HYRQDSRYYS DREKHRKLDD HRSREHRPSL 

      1630       1640       1650       1660       1670       1680 
EGGLKDRCHS DHRSHSDHRM HSDHRSSSEH THHKSSRDYR YLSDWQLDHR AASSGPRSPL 

      1690       1700       1710 
DQRSPYGSRS PFEHSAEHRS TPEHTWSSRK T 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian DNA-binding protein that contains a chromodomain and an SNF2/SWI2-like helicase domain."
Delmas V., Stokes D.G., Perry R.P.
Proc. Natl. Acad. Sci. U.S.A. 90:2414-2418(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"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].
[4]"DNA-binding and chromatin localization properties of CHD1."
Stokes D.G., Perry R.P.
Mol. Cell. Biol. 15:2745-2753(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DNA-BINDING.
[5]"CHD1 interacts with SSRP1 and depends on both its chromodomain and its ATPase/helicase-like domain for proper association with chromatin."
Kelley D.E., Stokes D.G., Perry R.P.
Chromosoma 108:10-25(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH SSRP1.
[6]"CHD1 associates with NCoR and histone deacetylase as well as with RNA splicing proteins."
Tai H.H., Geisterfer M., Bell J.C., Moniwa M., Davie J.R., Boucher L., McBurney M.W.
Biochem. Biophys. Res. Commun. 308:170-176(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCLAF1; NCOR; SRP20 AND SAF-B, FUNCTION.
[7]"Chd1 regulates open chromatin and pluripotency of embryonic stem cells."
Gaspar-Maia A., Alajem A., Polesso F., Sridharan R., Mason M.J., Heidersbach A., Ramalho-Santos J., McManus M.T., Plath K., Meshorer E., Ramalho-Santos M.
Nature 460:863-868(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CHROMATIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L10410 mRNA. Translation: AAB08486.1.
CH466630 Genomic DNA. Translation: EDL20454.1.
BC115822 mRNA. Translation: AAI15823.1.
PIRA47392.
RefSeqNP_031716.2. NM_007690.3.
UniGeneMm.8137.

3D structure databases

ProteinModelPortalP40201.
SMRP40201. Positions 268-441, 1122-1327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198693. 2 interactions.
IntActP40201. 2 interactions.
MINTMINT-4090783.

PTM databases

PhosphoSiteP40201.

Proteomic databases

PaxDbP40201.
PRIDEP40201.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000024627; ENSMUSP00000024627; ENSMUSG00000023852.
GeneID12648.
KEGGmmu:12648.
UCSCuc008aou.2. mouse.

Organism-specific databases

CTD1105.
MGIMGI:88393. Chd1.

Phylogenomic databases

eggNOGCOG0553.
GeneTreeENSGT00560000076896.
HOGENOMHOG000207917.
HOVERGENHBG005325.
InParanoidQ14BJ0.
KOK11367.
OMAHRKLDDH.
OrthoDBEOG7NPFSB.
TreeFamTF300674.

Gene expression databases

ArrayExpressP40201.
BgeeP40201.
CleanExMM_CHD1.
GenevestigatorP40201.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR023780. Chromo_domain.
IPR000953. Chromo_domain/shadow.
IPR016197. Chromodomain-like.
IPR023779. Chromodomain_CS.
IPR025260. DUF4208.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamPF00385. Chromo. 2 hits.
PF13907. DUF4208. 1 hit.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEPS00598. CHROMO_1. 2 hits.
PS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio281852.
PROP40201.
SOURCESearch...

Entry information

Entry nameCHD1_MOUSE
AccessionPrimary (citable) accession number: P40201
Secondary accession number(s): Q14BJ0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 116 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot