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Q3L8U1

- CHD9_HUMAN

UniProt

Q3L8U1 - CHD9_HUMAN

Protein

Chromodomain-helicase-DNA-binding protein 9

Gene

CHD9

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 2 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional coactivator for PPARA and possibly other nuclear receptors. Proposed to be a ATP-dependent chromatin remodeling protein. Has DNA-dependent ATPase activity and binds to A/T-rich DNA. Associates with A/T-rich regulatory regions in promoters of genes that participate in the differentiation of progenitors during osteogenesis By similarity.By similarity

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi885 – 8928ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA binding Source: UniProtKB-KW
    3. helicase activity Source: UniProtKB-KW
    4. protein binding Source: IntAct

    GO - Biological processi

    1. cellular lipid metabolic process Source: Reactome
    2. chromatin modification Source: UniProtKB-KW
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. small molecule metabolic process Source: Reactome
    5. 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

    Enzyme and pathway databases

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chromodomain-helicase-DNA-binding protein 9 (EC:3.6.4.12)
    Short name:
    CHD-9
    Alternative name(s):
    ATP-dependent helicase CHD9
    Chromatin-related mesenchymal modulator
    Short name:
    CReMM
    Chromatin-remodeling factor CHROM1
    Kismet homolog 2
    PPAR-alpha-interacting complex protein 320 kDa
    Peroxisomal proliferator-activated receptor A-interacting complex 320 kDa protein
    Gene namesi
    Name:CHD9
    Synonyms:KIAA0308, KISH2, PRIC320
    ORF Names:AD-013, x0008
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:25701. CHD9.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleoplasm Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA128394727.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 28972897Chromodomain-helicase-DNA-binding protein 9PRO_0000233172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei499 – 4991N6-acetyllysine1 Publication
    Modified residuei550 – 5501Phosphoserine4 Publications
    Modified residuei611 – 6111Phosphoserine2 Publications
    Modified residuei1468 – 14681Phosphoserine3 Publications
    Modified residuei1472 – 14721Phosphoserine3 Publications
    Modified residuei2026 – 20261Phosphoserine2 Publications
    Modified residuei2058 – 20581Phosphoserine2 Publications
    Modified residuei2059 – 20591Phosphoserine2 Publications

    Post-translational modificationi

    Phosphorylated on serine and tyrosine residues.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ3L8U1.
    PaxDbiQ3L8U1.
    PRIDEiQ3L8U1.

    PTM databases

    PhosphoSiteiQ3L8U1.

    Expressioni

    Tissue specificityi

    Widely expressed at low levels. In bone marrow, expression is restricted to osteoprogenitor cells adjacent to mature osteoblasts.2 Publications

    Gene expression databases

    ArrayExpressiQ3L8U1.
    BgeeiQ3L8U1.
    CleanExiHS_CHD9.
    GenevestigatoriQ3L8U1.

    Organism-specific databases

    HPAiHPA042053.
    HPA049420.

    Interactioni

    Subunit structurei

    Interacts with PPARA. Probably interacts with ESR1 and NR1I3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPARAQ078692EBI-960730,EBI-78615

    Protein-protein interaction databases

    BioGridi123174. 7 interactions.
    IntActiQ3L8U1. 5 interactions.
    STRINGi9606.ENSP00000381522.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3L8U1.
    SMRiQ3L8U1. Positions 715-1403, 2482-2529, 2545-2626.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini690 – 76172Chromo 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini773 – 83967Chromo 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini872 – 1046175Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini1186 – 1337152Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2332 – 2481150Binds A/T-rich DNAAdd
    BLAST
    Regioni2429 – 24368A.T hook-like

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi868 – 8725LXXLL motif 1
    Motifi997 – 10004DEAH box
    Motifi1036 – 10405LXXLL motif 2
    Motifi2031 – 20355LXXLL motif 3
    Motifi2721 – 27255LXXLL motif 4
    Motifi2793 – 27986LXXLL motif 5

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi220 – 31293Ser-richAdd
    BLAST
    Compositional biasi562 – 666105Lys-richAdd
    BLAST
    Compositional biasi2128 – 219871Ser-richAdd
    BLAST
    Compositional biasi2639 – 265012Poly-AlaAdd
    BLAST
    Compositional biasi2785 – 27884Poly-Ala
    Compositional biasi2878 – 288811Poly-SerAdd
    BLAST

    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.
    HOVERGENiHBG081150.
    InParanoidiQ3L8U1.
    KOiK14438.
    OMAiQEDKGGT.
    OrthoDBiEOG7NSB1C.
    PhylomeDBiQ3L8U1.
    TreeFamiTF313572.

    Family and domain databases

    Gene3Di3.40.50.300. 2 hits.
    InterProiIPR006576. BRK_domain.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view]
    PfamiPF07533. BRK. 2 hits.
    PF00385. Chromo. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view]
    SMARTiSM00592. BRK. 2 hits.
    SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEiPS50013. CHROMO_2. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q3L8U1-1) [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

    MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI     50
    DSLNHVQGTP THQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF 100
    NCSPIHPQNQ PNGLFPDVSD GSPMWGHQTA TTISNQNGSP FHQQGHSHSM 150
    HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ QNRNNLNPGQ NSLSQSKNFM 200
    NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH FHKCSSHQEG 250
    NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLASNHTNQ 300
    TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS 350
    NSKLSPVHMN FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP 400
    FTGLDPEDLL QEGLLPHFDE STFGQDNSSH ILDHDLDRQF TSHLVTRPSD 450
    MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC LQRQPPSSKK SDGSGTYTKL 500
    QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER GERNIPRVMS 550
    PENFPTASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT 600
    LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDIE 650
    GKQSEEEVKG SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRT 700
    VKKEISPGVM IDTEEFFVKY KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK 750
    LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE VSFCEDKDTG EPVIYYLVKW 800
    CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP PSNIWKKIDQ 850
    SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY 900
    EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ 950
    YEMYFRDSQG RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH 1000
    RLKNKNCKLL EGLKLMNLEH KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS 1050
    ESTFMQEFGD LKTEEQVQKL QAILKPMMLR RLKEDVEKKL APKEETIIEV 1100
    ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL RKCCNHPYLI 1150
    KGAEEKILGE FRDTYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK 1200
    VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD 1250
    RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA 1300
    VKVYRLVTRN SYEREMFDRA SLKLGLDKAV LQSMSGRESN VGGIQQLSKK 1350
    EIEDLLRRGA YGAIMEEEDE GSKFCEEDID QILLRRTKTI TIESEGRGST 1400
    FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR NSLVIDTPRI 1450
    RKQTRPFSAT KDELAELSEA ESEGDEKPKL RRPCDRSNGY GRTECFRVEK 1500
    NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK 1550
    GFIWDLITPT EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE 1600
    WLRKYNPEQL LQDEGYKKHI KHHCNKVLLR VRMLYYLKQE VIGNECQKVF 1650
    DGVDASDIDV WVPEPDHSEV PAEWWDFDAD KSLLIGVFKH GYEKYNTIRA 1700
    DPALCFLERV GKPDEKAVAA EQRANDYMDG DVEDPEYKPA PAIFKDDIED 1750
    DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ 1800
    IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV 1850
    STFGVVFDPD RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL 1900
    PSKEELVDPN IFIQPITEER ASRTLYRIEL LRKVREQALR HPQLFERLKL 1950
    CHPNPDLPVW WECGPHDRDL LIGAAKHGVS RTDYHILRDP ELSFMAAQRN 2000
    YSQSKMAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI ILEEMKVKSE 2050
    NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKCET 2100
    DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS 2150
    SSSSSCSHSR SGSSSSSSSS CSSASSSSSS STSSSSSSSS SSSEESDSDE 2200
    EEAQKRESTT HMKAYDEESV ASLSTTQDET QDSFQMNNGT PESAYILQGG 2250
    YMLAASYWPK DRVMINRLDS ICQTVLKGKW PSARRSYDAN TVASFYTTKL 2300
    LDSPGAATEY SDPSVPTPPG AGVKEEHDQS TQMSKVKKHV REKEFTVKIK 2350
    DEGGLKLTFQ KQGLAQKRPF DGEDGALGQQ QYLTRLRELQ SASETSLVNF 2400
    PKSIPVSGTS IQPTLGANGV ILDNQPIVKK RRGRRKNVEG VDIFFFNRNK 2450
    PPNHVSLGLT SSQISTGINP ALSYTQPQGI PDTESPVPVI NLKDGTRLAG 2500
    DDAPKRKDLE KWLKEHPGYV EDLGAFIPRM QLHEGRPKQK RHRCRNPNKL 2550
    DVNSLTGEER VQLINRRNAR KVGGAFAPPL KDLCRFLKEN SEYGVAPEWG 2600
    DVVKQSGFLP ESMYERILTG PVVREEVSRR GRRPKSGIAK ATAAAAAASA 2650
    TSVSGNPLLA NGLLPGVDLT TLQALQQNLQ NLQSLQVTAG LMGMPTGLPS 2700
    GGEAKNMAAM FPMLLSGMAG LPNLLGMGGL LTKPTESGTE DKKGSDSKES 2750
    EGKTERTESQ SSENGGENSV SSSPSTSSTA ALNTAAAANP LALNPLLLSN 2800
    ILYPGMLLTP GLNLHIPTLS QSNTFDVQNK NSDLGSSKSV EVKEEDSRIK 2850
    DQEDKGGTEP SPLNENSTDE GSEKADASSG SDSTSSSSED SDSSNED 2897
    Length:2,897
    Mass (Da):326,022
    Last modified:November 25, 2008 - v2
    Checksum:i91884A5E2F8ED183
    GO
    Isoform 2 (identifier: Q3L8U1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2336-2351: Missing.

    Show »
    Length:2,881
    Mass (Da):324,055
    Checksum:i5D325328A88F5E4E
    GO
    Isoform 3 (identifier: Q3L8U1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         2206-2206: R → RA
         2336-2351: Missing.

    Show »
    Length:2,882
    Mass (Da):324,127
    Checksum:iE5E272E36C779BB6
    GO

    Sequence cautioni

    The sequence BAB14112.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti98 – 1003SQF → PQL in AAT66509. 1 PublicationCurated
    Sequence conflicti119 – 1191S → P in AAT66509. 1 PublicationCurated
    Sequence conflicti208 – 2081V → A in AAT66509. 1 PublicationCurated
    Sequence conflicti473 – 4731L → I in AAT66509. 1 PublicationCurated
    Sequence conflicti836 – 8361R → C in ABD24032. (PubMed:16554032)Curated
    Sequence conflicti836 – 8361R → C in BAA20767. (PubMed:9205841)Curated
    Sequence conflicti1072 – 10721A → V in ABD24032. (PubMed:16554032)Curated
    Sequence conflicti1072 – 10721A → V in BAB14112. (PubMed:14702039)Curated
    Sequence conflicti1122 – 11221S → F in AAT66509. 1 PublicationCurated
    Sequence conflicti1372 – 13721S → P in AAT66509. 1 PublicationCurated
    Sequence conflicti1442 – 14421S → G in ABD24032. (PubMed:16554032)Curated
    Sequence conflicti1442 – 14421S → G in BAB14112. (PubMed:14702039)Curated
    Sequence conflicti1724 – 17241A → T in AAT66509. 1 PublicationCurated
    Sequence conflicti1754 – 17541S → L in AAT66509. 1 PublicationCurated
    Sequence conflicti1867 – 18671T → A in AAT66509. 1 PublicationCurated
    Sequence conflicti2025 – 20251A → V in AAT66509. 1 PublicationCurated
    Sequence conflicti2069 – 20691T → A in AAT66509. 1 PublicationCurated
    Sequence conflicti2078 – 20781V → G in AAT66509. 1 PublicationCurated
    Sequence conflicti2189 – 21891S → F in AAT66509. 1 PublicationCurated
    Sequence conflicti2759 – 27591S → N in AAT66509. 1 PublicationCurated
    Sequence conflicti2776 – 27761T → A in AAQ24287. (PubMed:16095617)Curated
    Sequence conflicti2776 – 27761T → A in BAA20767. (PubMed:9205841)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti2312 – 23121D → E.3 Publications
    Corresponds to variant rs6499548 [ dbSNP | Ensembl ].
    VAR_047355

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei2206 – 22061R → RA in isoform 3. 1 PublicationVSP_018085
    Alternative sequencei2336 – 235116Missing in isoform 2 and isoform 3. 3 PublicationsVSP_018086Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY243500 mRNA. Translation: AAQ24287.1.
    DQ333316 mRNA. Translation: ABD24032.1.
    AY647157 mRNA. Translation: AAT66509.1.
    AC007906 Genomic DNA. No translation available.
    AC079416 Genomic DNA. No translation available.
    BC140815 mRNA. Translation: AAI40816.1.
    AB002306 mRNA. Translation: BAA20767.3.
    AF150735 mRNA. Translation: AAF24170.1. Sequence problems.
    AK022582 mRNA. Translation: BAB14112.1. Different initiation.
    CCDSiCCDS45485.1. [Q3L8U1-2]
    RefSeqiNP_079410.4. NM_025134.4. [Q3L8U1-2]
    XP_005256227.1. XM_005256170.1. [Q3L8U1-1]
    XP_005256228.1. XM_005256171.1. [Q3L8U1-3]
    XP_005256229.1. XM_005256172.1. [Q3L8U1-2]
    UniGeneiHs.59159.
    Hs.622347.

    Genome annotation databases

    EnsembliENST00000398510; ENSP00000381522; ENSG00000177200. [Q3L8U1-1]
    ENST00000447540; ENSP00000396345; ENSG00000177200. [Q3L8U1-3]
    ENST00000564845; ENSP00000455307; ENSG00000177200. [Q3L8U1-2]
    ENST00000566029; ENSP00000457466; ENSG00000177200. [Q3L8U1-2]
    GeneIDi80205.
    KEGGihsa:80205.
    UCSCiuc002egy.3. human. [Q3L8U1-2]
    uc002ehb.3. human. [Q3L8U1-1]
    uc002ehc.3. human. [Q3L8U1-3]

    Polymorphism databases

    DMDMi215273951.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY243500 mRNA. Translation: AAQ24287.1 .
    DQ333316 mRNA. Translation: ABD24032.1 .
    AY647157 mRNA. Translation: AAT66509.1 .
    AC007906 Genomic DNA. No translation available.
    AC079416 Genomic DNA. No translation available.
    BC140815 mRNA. Translation: AAI40816.1 .
    AB002306 mRNA. Translation: BAA20767.3 .
    AF150735 mRNA. Translation: AAF24170.1 . Sequence problems.
    AK022582 mRNA. Translation: BAB14112.1 . Different initiation.
    CCDSi CCDS45485.1. [Q3L8U1-2 ]
    RefSeqi NP_079410.4. NM_025134.4. [Q3L8U1-2 ]
    XP_005256227.1. XM_005256170.1. [Q3L8U1-1 ]
    XP_005256228.1. XM_005256171.1. [Q3L8U1-3 ]
    XP_005256229.1. XM_005256172.1. [Q3L8U1-2 ]
    UniGenei Hs.59159.
    Hs.622347.

    3D structure databases

    ProteinModelPortali Q3L8U1.
    SMRi Q3L8U1. Positions 715-1403, 2482-2529, 2545-2626.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123174. 7 interactions.
    IntActi Q3L8U1. 5 interactions.
    STRINGi 9606.ENSP00000381522.

    PTM databases

    PhosphoSitei Q3L8U1.

    Polymorphism databases

    DMDMi 215273951.

    Proteomic databases

    MaxQBi Q3L8U1.
    PaxDbi Q3L8U1.
    PRIDEi Q3L8U1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000398510 ; ENSP00000381522 ; ENSG00000177200 . [Q3L8U1-1 ]
    ENST00000447540 ; ENSP00000396345 ; ENSG00000177200 . [Q3L8U1-3 ]
    ENST00000564845 ; ENSP00000455307 ; ENSG00000177200 . [Q3L8U1-2 ]
    ENST00000566029 ; ENSP00000457466 ; ENSG00000177200 . [Q3L8U1-2 ]
    GeneIDi 80205.
    KEGGi hsa:80205.
    UCSCi uc002egy.3. human. [Q3L8U1-2 ]
    uc002ehb.3. human. [Q3L8U1-1 ]
    uc002ehc.3. human. [Q3L8U1-3 ]

    Organism-specific databases

    CTDi 80205.
    GeneCardsi GC16P053041.
    HGNCi HGNC:25701. CHD9.
    HPAi HPA042053.
    HPA049420.
    neXtProti NX_Q3L8U1.
    PharmGKBi PA128394727.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0553.
    HOVERGENi HBG081150.
    InParanoidi Q3L8U1.
    KOi K14438.
    OMAi QEDKGGT.
    OrthoDBi EOG7NSB1C.
    PhylomeDBi Q3L8U1.
    TreeFami TF313572.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_116145. PPARA activates gene expression.
    REACT_118659. RORA activates circadian gene expression.
    REACT_118713. YAP1- and WWTR1 (TAZ)-stimulated gene expression.
    REACT_118789. REV-ERBA represses gene expression.
    REACT_147904. Activation of gene expression by SREBF (SREBP).
    REACT_19241. Regulation of lipid metabolism by Peroxisome proliferator-activated receptor alpha (PPARalpha).
    REACT_200608. Transcriptional activation of mitochondrial biogenesis.
    REACT_24941. Circadian Clock.
    REACT_27161. Transcriptional regulation of white adipocyte differentiation.

    Miscellaneous databases

    GeneWikii CHD9.
    GenomeRNAii 80205.
    NextBioi 70576.
    PROi Q3L8U1.

    Gene expression databases

    ArrayExpressi Q3L8U1.
    Bgeei Q3L8U1.
    CleanExi HS_CHD9.
    Genevestigatori Q3L8U1.

    Family and domain databases

    Gene3Di 3.40.50.300. 2 hits.
    InterProi IPR006576. BRK_domain.
    IPR023780. Chromo_domain.
    IPR000953. Chromo_domain/shadow.
    IPR016197. Chromodomain-like.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR000330. SNF2_N.
    [Graphical view ]
    Pfami PF07533. BRK. 2 hits.
    PF00385. Chromo. 2 hits.
    PF00271. Helicase_C. 1 hit.
    PF00176. SNF2_N. 1 hit.
    [Graphical view ]
    SMARTi SM00592. BRK. 2 hits.
    SM00298. CHROMO. 2 hits.
    SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 2 hits.
    SSF54160. SSF54160. 2 hits.
    PROSITEi PS50013. CHROMO_2. 2 hits.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization and functional analysis of CReMM, a novel chromodomain helicase DNA-binding protein."
      Shur I., Benayahu D.
      J. Mol. Biol. 352:646-655(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION, VARIANT GLU-2312.
      Tissue: Bone marrow stroma.
    2. "PRIC320, a transcription coactivator, isolated from peroxisome proliferator-binding protein complex."
      Surapureddi S., Viswakarma N., Yu S., Guo D., Rao M.S., Reddy J.K.
      Biochem. Biophys. Res. Commun. 343:535-543(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, VARIANT GLU-2312, INTERACTION WITH PPARA; ESR1 AND NR1I3.
    3. "Cloning of the mammalian orthologs of Drosophila melanogaster gene KISMET."
      Colin C., Dahia P.L.M., Stiles C.D., Sogayar M.C.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Pharynx carcinoma.
    4. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [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 1).
    6. "Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 124-2897 (ISOFORM 3), VARIANT GLU-2312.
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 485-639.
      Tissue: Adrenal gland.
    8. "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] OF 886-1616.
    9. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1468 AND SER-1472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-611 AND SER-2026, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-550; SER-2058 AND SER-2059, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    13. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-499, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "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-550; SER-1468 AND SER-1472, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiCHD9_HUMAN
    AccessioniPrimary (citable) accession number: Q3L8U1
    Secondary accession number(s): B2RTU2
    , B9ZVQ0, O15025, Q1WF12, Q6DTK9, Q9H9V7, Q9UHM2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 2, 2006
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 94 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 16
      Human chromosome 16: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3