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Q3L8U1

- CHD9_HUMAN

UniProt

Q3L8U1 - CHD9_HUMAN

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Protein
Chromodomain-helicase-DNA-binding protein 9
Gene
CHD9, KIAA0308, KISH2, PRIC320, AD-013, x0008
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi885 – 8928ATP Reviewed prediction

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
Complete GO annotation...

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. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleoplasm Source: Reactome
Complete GO annotation...

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 9
PRO_0000233172Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei499 – 4991N6-acetyllysine1 Publication
Modified residuei550 – 5501Phosphoserine3 Publications
Modified residuei611 – 6111Phosphoserine1 Publication
Modified residuei1468 – 14681Phosphoserine2 Publications
Modified residuei1472 – 14721Phosphoserine2 Publications
Modified residuei2026 – 20261Phosphoserine1 Publication
Modified residuei2058 – 20581Phosphoserine1 Publication
Modified residuei2059 – 20591Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine and tyrosine residues.1 Publication

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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini690 – 76172Chromo 1
Add
BLAST
Domaini773 – 83967Chromo 2
Add
BLAST
Domaini872 – 1046175Helicase ATP-binding
Add
BLAST
Domaini1186 – 1337152Helicase C-terminal
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2332 – 2481150Binds A/T-rich DNA
Add
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-rich
Add
BLAST
Compositional biasi562 – 666105Lys-rich
Add
BLAST
Compositional biasi2128 – 219871Ser-rich
Add
BLAST
Compositional biasi2639 – 265012Poly-Ala
Add
BLAST
Compositional biasi2785 – 27884Poly-Ala
Compositional biasi2878 – 288811Poly-Ser
Add
BLAST

Sequence similaritiesi

Contains 2 chromo domains.

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.

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.
VSP_018085
Alternative sequencei2336 – 235116Missing in isoform 2 and isoform 3.
VSP_018086Add
BLAST

Sequence conflict

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

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 93 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

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