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O14646

- CHD1_HUMAN

UniProt

O14646 - CHD1_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 1

Gene

CHD1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 137 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    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. Is also associated with histone deacetylase (HDAC) activity By similarity. 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. Required for maintaining open chromatin and pluripotency in embryonic stem cells.By similarity1 Publication

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi506 – 5138ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent DNA helicase activity Source: ProtInc
    3. DNA binding Source: UniProtKB-KW
    4. methylated histone binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. chromatin remodeling Source: Ensembl
    2. DNA duplex unwinding Source: GOC
    3. regulation of transcription from RNA polymerase II promoter Source: ProtInc
    4. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Chromatin regulator, Helicase, Hydrolase

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, DNA-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromodomain-helicase-DNA-binding protein 1 (EC:3.6.4.12)
    Short name:
    CHD-1
    Alternative name(s):
    ATP-dependent helicase CHD1
    Gene namesi
    Name:CHD1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 5

    Organism-specific databases

    HGNCiHGNC:1915. CHD1.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26451.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 17101710Chromodomain-helicase-DNA-binding protein 1PRO_0000080224Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei215 – 2151Phosphoserine1 Publication
    Modified residuei216 – 2161Phosphoserine1 Publication
    Modified residuei237 – 2371Phosphothreonine1 Publication
    Modified residuei241 – 2411Phosphoserine1 Publication
    Modified residuei250 – 2501Phosphothreonine1 Publication
    Modified residuei252 – 2521Phosphoserine1 Publication
    Modified residuei1025 – 10251Phosphoserine1 Publication
    Modified residuei1040 – 10401Phosphoserine3 Publications
    Modified residuei1081 – 10811Phosphoserine1 Publication
    Modified residuei1096 – 10961Phosphoserine2 Publications
    Modified residuei1098 – 10981Phosphoserine2 Publications
    Modified residuei1100 – 11001Phosphoserine2 Publications
    Modified residuei1102 – 11021Phosphoserine1 Publication
    Modified residuei1353 – 13531Phosphoserine1 Publication
    Modified residuei1355 – 13551Phosphoserine1 Publication
    Modified residuei1356 – 13561Phosphoserine1 Publication
    Modified residuei1360 – 13601Phosphoserine1 Publication
    Modified residuei1363 – 13631Phosphoserine1 Publication
    Modified residuei1371 – 13711Phosphoserine1 Publication
    Modified residuei1677 – 16771Phosphoserine3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO14646.
    PaxDbiO14646.
    PRIDEiO14646.

    PTM databases

    PhosphoSiteiO14646.

    Expressioni

    Gene expression databases

    ArrayExpressiO14646.
    BgeeiO14646.
    CleanExiHS_CHD1.
    GenevestigatoriO14646.

    Organism-specific databases

    HPAiHPA022236.

    Interactioni

    Subunit structurei

    Component of the SAGA complex By similarity. Interacts with BCLAF1, NCoR, SRP20 and SAFB 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 similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    NS1B2BUF13EBI-1560858,EBI-4291940From a different organism.

    Protein-protein interaction databases

    BioGridi107530. 19 interactions.
    DIPiDIP-38922N.
    IntActiO14646. 1 interaction.
    STRINGi9606.ENSP00000284049.

    Structurei

    Secondary structure

    1
    1710
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi273 – 28412
    Helixi289 – 2924
    Helixi294 – 3007
    Turni303 – 3064
    Turni309 – 3113
    Beta strandi314 – 3229
    Helixi327 – 3293
    Beta strandi331 – 3333
    Helixi335 – 3406
    Helixi347 – 36418
    Helixi368 – 38720
    Beta strandi390 – 3978
    Beta strandi408 – 4136
    Helixi418 – 4203
    Beta strandi422 – 4254
    Helixi426 – 4327
    Helixi434 – 4418
    Helixi1128 – 113811
    Helixi1144 – 11463
    Helixi1148 – 11547
    Helixi1162 – 118019
    Beta strandi1201 – 12044
    Beta strandi1207 – 12104
    Helixi1211 – 122717
    Helixi1232 – 12365
    Beta strandi1249 – 12513
    Helixi1255 – 126814
    Helixi1273 – 12786
    Beta strandi1280 – 12834
    Turni1285 – 12873
    Helixi1299 – 132426

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2B2TX-ray2.45A/B268-443[»]
    C268-373[»]
    2B2UX-ray2.95A/B268-443[»]
    C268-373[»]
    2B2VX-ray2.65A/B268-443[»]
    C268-373[»]
    2B2WX-ray2.40A/B268-443[»]
    C268-373[»]
    2B2YX-ray2.35A/B268-443[»]
    C268-373[»]
    4B4CX-ray1.62A1119-1327[»]
    4NW2X-ray1.90A/C268-443[»]
    4O42X-ray1.87A268-443[»]
    ProteinModelPortaliO14646.
    SMRiO14646. Positions 270-1020, 1124-1327.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO14646.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini272 – 36493Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini389 – 45264Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini493 – 663171Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini792 – 943152Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST
    Repeati1628 – 163251
    Repeati1634 – 163852
    Repeati1640 – 164453

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1628 – 1644173 X 5 AA repeats of H-S-D-H-RAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi614 – 6174DEAH box

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1 – 7070Ser-richAdd
    BLAST
    Compositional biasi117 – 13721Ser-richAdd
    BLAST

    Domaini

    The 2 chromodomains are involved in the binding to the histone H3 methyllysine at position 4 (H3K4me3).1 Publication

    Sequence similaritiesi

    Belongs to the SNF2/RAD54 helicase family.Curated
    Contains 2 chromo domains.PROSITE-ProRule annotation
    Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
    Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0553.
    HOGENOMiHOG000207917.
    HOVERGENiHBG005325.
    InParanoidiO14646.
    KOiK11367.
    OMAiMDHRASS.
    OrthoDBiEOG7NPFSB.
    PhylomeDBiO14646.
    TreeFamiTF313461.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR023780. 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]
    PfamiPF00385. Chromo. 2 hits.
    PF13907. DUF4208. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEiPS00598. CHROMO_1. 2 hits.
    PS50013. CHROMO_2. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O14646-1) [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

    MNGHSDEESV RNSSGESSQS DDDSGSASGS GSGSSSGSSS DGSSSQSGSS     50
    DSDSGSESGS QSESESDTSR ENKVQAKPPK VDGAEFWKSS PSILAVQRSA 100
    ILKKQQQQQQ QQQHQASSNS GSEEDSSSSE DSDDSSSEVK RKKHKDEDWQ 150
    MSGSGSPSQS GSDSESEEER EKSSCDETES DYEPKNKVKS RKPQNRSKSK 200
    NGKKILGQKK RQIDSSEEDD DEEDYDNDKR SSRRQATVNV SYKEDEEMKT 250
    DSDDLLEVCG EDVPQPEEEE FETIERFMDC RIGRKGATGA TTTIYAVEAD 300
    GDPNAGFEKN KEPGEIQYLI KWKGWSHIHN TWETEETLKQ QNVRGMKKLD 350
    NYKKKDQETK RWLKNASPED VEYYNCQQEL TDDLHKQYQI VERIIAHSNQ 400
    KSAAGYPDYY CKWQGLPYSE CSWEDGALIS KKFQACIDEY FSRNQSKTTP 450
    FKDCKVLKQR PRFVALKKQP SYIGGHEGLE LRDYQLNGLN WLAHSWCKGN 500
    SCILADEMGL GKTIQTISFL NYLFHEHQLY GPFLLVVPLS TLTSWQREIQ 550
    TWASQMNAVV YLGDINSRNM IRTHEWTHHQ TKRLKFNILL TTYEILLKDK 600
    AFLGGLNWAF IGVDEAHRLK NDDSLLYKTL IDFKSNHRLL ITGTPLQNSL 650
    KELWSLLHFI MPEKFSSWED FEEEHGKGRE YGYASLHKEL EPFLLRRVKK 700
    DVEKSLPAKV EQILRMEMSA LQKQYYKWIL TRNYKALSKG SKGSTSGFLN 750
    IMMELKKCCN HCYLIKPPDN NEFYNKQEAL QHLIRSSGKL ILLDKLLIRL 800
    RERGNRVLIF SQMVRMLDIL AEYLKYRQFP FQRLDGSIKG ELRKQALDHF 850
    NAEGSEDFCF LLSTRAGGLG INLASADTVV IFDSDWNPQN DLQAQARAHR 900
    IGQKKQVNIY RLVTKGSVEE DILERAKKKM VLDHLVIQRM DTTGKTVLHT 950
    GSAPSSSTPF NKEELSAILK FGAEELFKEP EGEEQEPQEM DIDEILKRAE 1000
    THENEPGPLT VGDELLSQFK VANFSNMDED DIELEPERNS KNWEEIIPED 1050
    QRRRLEEEER QKELEEIYML PRMRNCAKQI SFNGSEGRRS RSRRYSGSDS 1100
    DSISEGKRPK KRGRPRTIPR ENIKGFSDAE IRRFIKSYKK FGGPLERLDA 1150
    IARDAELVDK SETDLRRLGE LVHNGCIKAL KDSSSGTERT GGRLGKVKGP 1200
    TFRISGVQVN AKLVISHEEE LIPLHKSIPS DPEERKQYTI PCHTKAAHFD 1250
    IDWGKEDDSN LLIGIYEYGY GSWEMIKMDP DLSLTHKILP DDPDKKPQAK 1300
    QLQTRADYLI KLLSRDLAKK EALSGAGSSK RRKARAKKNK AMKSIKVKEE 1350
    IKSDSSPLPS EKSDEDDDKL SESKSDGRER SKKSSVSDAP VHITASGEPV 1400
    PISEESEELD QKTFSICKER MRPVKAALKQ LDRPEKGLSE REQLEHTRQC 1450
    LIKIGDHITE CLKEYTNPEQ IKQWRKNLWI FVSKFTEFDA RKLHKLYKHA 1500
    IKKRQESQQN SDQNSNLNPH VIRNPDVERL KENTNHDDSS RDSYSSDRHL 1550
    TQYHDHHKDR HQGDSYKKSD SRKRPYSSFS NGKDHRDWDH YKQDSRYYSD 1600
    REKHRKLDDH RSRDHRSNLE GSLKDRSHSD HRSHSDHRLH SDHRSSSEYT 1650
    HHKSSRDYRY HSDWQMDHRA SSSGPRSPLD QRSPYGSRSP FEHSVEHKST 1700
    PEHTWSSRKT 1710
    Length:1,710
    Mass (Da):196,688
    Last modified:November 24, 2009 - v2
    Checksum:iD888AAA46FDA31B1
    GO
    Isoform 2 (identifier: O14646-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1684-1684: Missing.

    Show »
    Length:1,709
    Mass (Da):196,590
    Checksum:i8B2C96C7597E55B4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti392 – 3921E → G in AAB87381. (PubMed:9326634)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti264 – 2641P → T.
    Corresponds to variant rs10062803 [ dbSNP | Ensembl ].
    VAR_055652

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1684 – 16841Missing in isoform 2. 2 PublicationsVSP_038432

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006513 mRNA. Translation: AAB87381.1.
    AC022121 Genomic DNA. No translation available.
    BC117134 mRNA. Translation: AAI17135.1.
    CCDSiCCDS34204.1. [O14646-1]
    RefSeqiNP_001261.2. NM_001270.2. [O14646-1]
    XP_005271924.1. XM_005271867.2. [O14646-1]
    UniGeneiHs.643465.

    Genome annotation databases

    EnsembliENST00000284049; ENSP00000284049; ENSG00000153922. [O14646-1]
    GeneIDi1105.
    KEGGihsa:1105.
    UCSCiuc003knf.3. human. [O14646-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF006513 mRNA. Translation: AAB87381.1 .
    AC022121 Genomic DNA. No translation available.
    BC117134 mRNA. Translation: AAI17135.1 .
    CCDSi CCDS34204.1. [O14646-1 ]
    RefSeqi NP_001261.2. NM_001270.2. [O14646-1 ]
    XP_005271924.1. XM_005271867.2. [O14646-1 ]
    UniGenei Hs.643465.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2B2T X-ray 2.45 A/B 268-443 [» ]
    C 268-373 [» ]
    2B2U X-ray 2.95 A/B 268-443 [» ]
    C 268-373 [» ]
    2B2V X-ray 2.65 A/B 268-443 [» ]
    C 268-373 [» ]
    2B2W X-ray 2.40 A/B 268-443 [» ]
    C 268-373 [» ]
    2B2Y X-ray 2.35 A/B 268-443 [» ]
    C 268-373 [» ]
    4B4C X-ray 1.62 A 1119-1327 [» ]
    4NW2 X-ray 1.90 A/C 268-443 [» ]
    4O42 X-ray 1.87 A 268-443 [» ]
    ProteinModelPortali O14646.
    SMRi O14646. Positions 270-1020, 1124-1327.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107530. 19 interactions.
    DIPi DIP-38922N.
    IntActi O14646. 1 interaction.
    STRINGi 9606.ENSP00000284049.

    Chemistry

    DrugBanki DB00445. Epirubicin.

    PTM databases

    PhosphoSitei O14646.

    Proteomic databases

    MaxQBi O14646.
    PaxDbi O14646.
    PRIDEi O14646.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000284049 ; ENSP00000284049 ; ENSG00000153922 . [O14646-1 ]
    GeneIDi 1105.
    KEGGi hsa:1105.
    UCSCi uc003knf.3. human. [O14646-1 ]

    Organism-specific databases

    CTDi 1105.
    GeneCardsi GC05M098219.
    H-InvDB HIX0005061.
    HGNCi HGNC:1915. CHD1.
    HPAi HPA022236.
    MIMi 602118. gene.
    neXtProti NX_O14646.
    PharmGKBi PA26451.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOGENOMi HOG000207917.
    HOVERGENi HBG005325.
    InParanoidi O14646.
    KOi K11367.
    OMAi MDHRASS.
    OrthoDBi EOG7NPFSB.
    PhylomeDBi O14646.
    TreeFami TF313461.

    Miscellaneous databases

    EvolutionaryTracei O14646.
    GeneWikii CHD1.
    GenomeRNAii 1105.
    NextBioi 4580.
    PROi O14646.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O14646.
    Bgeei O14646.
    CleanExi HS_CHD1.
    Genevestigatori O14646.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR023780. 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 ]
    Pfami PF00385. Chromo. 2 hits.
    PF13907. DUF4208. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEi PS00598. CHROMO_1. 2 hits.
    PS50013. CHROMO_2. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "The DNA sequence and comparative analysis of human chromosome 5."
      Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
      , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
      Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
      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] (ISOFORM 2).
      Tissue: Cerebellum.
    4. "Human but not yeast CHD1 binds directly and selectively to histone H3 methylated at lysine 4 via its tandem chromodomains."
      Sims R.J. III, Chen C.-F., Santos-Rosa H., Kouzarides T., Patel S.S., Reinberg D.
      J. Biol. Chem. 280:41789-41792(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH H3K4ME2 AND H3K4ME3.
    5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    6. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Molecular implications of evolutionary differences in CHD double chromodomains."
      Flanagan J.F., Blus B.J., Kim D., Clines K.L., Rastinejad F., Khorasanizadeh S.
      J. Mol. Biol. 369:334-342(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, INTERACTION WITH HISTONE H3K4ME3.
    8. "Recognition of trimethylated histone H3 lysine 4 facilitates the recruitment of transcription postinitiation factors and pre-mRNA splicing."
      Sims R.J. III, Millhouse S., Chen C.-F., Lewis B.A., Erdjument-Bromage H., Tempst P., Manley J.L., Reinberg D.
      Mol. Cell 28:665-676(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH H3K4ME3; PAF1; SFA3A1; SFA3A2; SFA3A3; SNF2 AND SSRP1.
    9. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1040; SER-1081 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-237; SER-241; SER-1040; SER-1096; SER-1098; SER-1100 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "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 THR-250; SER-252; SER-1025; SER-1040 AND SER-1677, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-216; SER-1096; SER-1098; SER-1100; SER-1102; SER-1353; SER-1355; SER-1356; SER-1360; SER-1363 AND SER-1371, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Double chromodomains cooperate to recognize the methylated histone H3 tail."
      Flanagan J.F., Mi L.-Z., Chruszcz M., Cymborowski M., Clines K.L., Kim Y., Minor W., Rastinejad F., Khorasanizadeh S.
      Nature 438:1181-1185(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 268-443, INTERACTION WITH HISTONE H3K4ME3.

    Entry informationi

    Entry nameiCHD1_HUMAN
    AccessioniPrimary (citable) accession number: O14646
    Secondary accession number(s): Q17RZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 137 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 5
      Human chromosome 5: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3