P40201 (CHD1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 109.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended 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 |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 1711 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence 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.8 |
| 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.8 |
| 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. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1711 | 1711 | Chromodomain-helicase-DNA-binding protein 1 | PRO_0000080225 | |||||
Regions | |||||||||
| Domain | 270 – 362 | 93 | Chromo 1 | ||||||
| Domain | 387 – 450 | 64 | Chromo 2 | ||||||
| Domain | 491 – 661 | 171 | Helicase ATP-binding | ||||||
| Domain | 790 – 941 | 152 | Helicase C-terminal | ||||||
| Repeat | 1629 – 1633 | 5 | 1 | ||||||
| Repeat | 1635 – 1639 | 5 | 2 | ||||||
| Repeat | 1641 – 1645 | 5 | 3 | ||||||
| Nucleotide binding | 504 – 511 | 8 | ATP Potential | ||||||
| Region | 1629 – 1645 | 17 | 3 X 5 AA repeats of H-S-D-H-R | ||||||
| Motif | 612 – 615 | 4 | DEAH box | ||||||
| Compositional bias | 1 – 70 | 70 | Ser-rich | ||||||
| Compositional bias | 116 – 136 | 21 | Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 5 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 214 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 215 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 235 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 239 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 248 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 250 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1023 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1038 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1079 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1094 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1096 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1098 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1100 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1353 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1355 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1356 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1360 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1363 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1678 | 1 | Phosphoserine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 159 | 1 | S → L in AAB08486. Ref.1 | ||||||
Sequences
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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] | "Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY. Tissue: Liver. |
| [8] | "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. |
| IPI | IPI00107999. |
| PIR | A47392. |
| RefSeq | NP_031716.2. NM_007690.3. |
| UniGene | Mm.8137. |
3D structure databases | |
| ProteinModelPortal | P40201. |
| SMR | P40201. Positions 268-441, 1122-1327. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P40201. 1 interaction. |
PTM databases | |
| PhosphoSite | P40201. |
Proteomic databases | |
| PaxDb | P40201. |
| PRIDE | P40201. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000024627; ENSMUSP00000024627; ENSMUSG00000023852. |
| GeneID | 12648. |
| KEGG | mmu:12648. |
Organism-specific databases | |
| CTD | 1105. |
| MGI | MGI:88393. Chd1. |
Phylogenomic databases | |
| eggNOG | COG0553. |
| GeneTree | ENSGT00560000076896. |
| HOGENOM | HOG000207917. |
| HOVERGEN | HBG005325. |
| InParanoid | Q14BJ0. |
| KO | K11367. |
| OMA | AETHENE. |
| OrthoDB | EOG4PG601. |
Gene expression databases | |
| ArrayExpress | P40201. |
| Bgee | P40201. |
| CleanEx | MM_CHD1. |
| Genevestigator | P40201. |
| GermOnline | ENSMUSG00000023852. Mus musculus. |
Family and domain databases | |
| InterPro | IPR023780. Chromo_domain. IPR000953. Chromo_domain/shadow. IPR016197. Chromodomain-like. IPR023779. Chromodomain_CS. IPR025260. DUF4208. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000330. SNF2_N. [Graphical view] |
| Pfam | PF00385. Chromo. 2 hits. PF13907. DUF4208. 1 hit. PF00271. Helicase_C. 1 hit. PF00176. SNF2_N. 1 hit. [Graphical view] |
| SMART | SM00298. CHROMO. 2 hits. SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view] |
| SUPFAM | SSF54160. Chromodomain-like. 2 hits. |
| PROSITE | PS00598. CHROMO_1. 2 hits. PS50013. CHROMO_2. 2 hits. PS00690. DEAH_ATP_HELICASE. False negative. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 281852. |
| SOURCE | Search... |
Entry information
| Entry name | CHD1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: P40201 Secondary accession number(s): Q14BJ0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
