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Protein

Chromodomain-helicase-DNA-binding protein 9

Gene

CHD9

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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).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

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_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_268444. Orphan transporters.
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 Componenti: Chromosome 16

Organism-specific databases

HGNCiHGNC:25701. CHD9.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: Reactome
  3. nucleus Source: HPA
  4. plasma membrane Source: HPA
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 9PRO_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

BgeeiQ3L8U1.
CleanExiHS_CHD9.
ExpressionAtlasiQ3L8U1. baseline and differential.
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. 8 interactions.
IntActiQ3L8U1. 5 interactions.
STRINGi9606.ENSP00000381522.

Structurei

3D structure databases

ProteinModelPortaliQ3L8U1.
SMRiQ3L8U1. Positions 769-828, 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.
GeneTreeiENSGT00760000119067.
HOVERGENiHBG081150.
InParanoidiQ3L8U1.
KOiK14438.
OMAiQEDKGGT.
OrthoDBiEOG7NSB1C.
PhylomeDBiQ3L8U1.
TreeFamiTF313572.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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. AlignAdd to basket

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

        10         20         30         40         50
MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI
60 70 80 90 100
DSLNHVQGTP THQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF
110 120 130 140 150
NCSPIHPQNQ PNGLFPDVSD GSPMWGHQTA TTISNQNGSP FHQQGHSHSM
160 170 180 190 200
HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ QNRNNLNPGQ NSLSQSKNFM
210 220 230 240 250
NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH FHKCSSHQEG
260 270 280 290 300
NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLASNHTNQ
310 320 330 340 350
TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS
360 370 380 390 400
NSKLSPVHMN FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP
410 420 430 440 450
FTGLDPEDLL QEGLLPHFDE STFGQDNSSH ILDHDLDRQF TSHLVTRPSD
460 470 480 490 500
MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC LQRQPPSSKK SDGSGTYTKL
510 520 530 540 550
QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER GERNIPRVMS
560 570 580 590 600
PENFPTASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT
610 620 630 640 650
LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDIE
660 670 680 690 700
GKQSEEEVKG SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRT
710 720 730 740 750
VKKEISPGVM IDTEEFFVKY KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK
760 770 780 790 800
LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE VSFCEDKDTG EPVIYYLVKW
810 820 830 840 850
CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP PSNIWKKIDQ
860 870 880 890 900
SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY
910 920 930 940 950
EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ
960 970 980 990 1000
YEMYFRDSQG RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH
1010 1020 1030 1040 1050
RLKNKNCKLL EGLKLMNLEH KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS
1060 1070 1080 1090 1100
ESTFMQEFGD LKTEEQVQKL QAILKPMMLR RLKEDVEKKL APKEETIIEV
1110 1120 1130 1140 1150
ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL RKCCNHPYLI
1160 1170 1180 1190 1200
KGAEEKILGE FRDTYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK
1210 1220 1230 1240 1250
VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD
1260 1270 1280 1290 1300
RFVFLLCTRA GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA
1310 1320 1330 1340 1350
VKVYRLVTRN SYEREMFDRA SLKLGLDKAV LQSMSGRESN VGGIQQLSKK
1360 1370 1380 1390 1400
EIEDLLRRGA YGAIMEEEDE GSKFCEEDID QILLRRTKTI TIESEGRGST
1410 1420 1430 1440 1450
FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR NSLVIDTPRI
1460 1470 1480 1490 1500
RKQTRPFSAT KDELAELSEA ESEGDEKPKL RRPCDRSNGY GRTECFRVEK
1510 1520 1530 1540 1550
NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK
1560 1570 1580 1590 1600
GFIWDLITPT EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE
1610 1620 1630 1640 1650
WLRKYNPEQL LQDEGYKKHI KHHCNKVLLR VRMLYYLKQE VIGNECQKVF
1660 1670 1680 1690 1700
DGVDASDIDV WVPEPDHSEV PAEWWDFDAD KSLLIGVFKH GYEKYNTIRA
1710 1720 1730 1740 1750
DPALCFLERV GKPDEKAVAA EQRANDYMDG DVEDPEYKPA PAIFKDDIED
1760 1770 1780 1790 1800
DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ
1810 1820 1830 1840 1850
IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV
1860 1870 1880 1890 1900
STFGVVFDPD RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL
1910 1920 1930 1940 1950
PSKEELVDPN IFIQPITEER ASRTLYRIEL LRKVREQALR HPQLFERLKL
1960 1970 1980 1990 2000
CHPNPDLPVW WECGPHDRDL LIGAAKHGVS RTDYHILRDP ELSFMAAQRN
2010 2020 2030 2040 2050
YSQSKMAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI ILEEMKVKSE
2060 2070 2080 2090 2100
NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKCET
2110 2120 2130 2140 2150
DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS
2160 2170 2180 2190 2200
SSSSSCSHSR SGSSSSSSSS CSSASSSSSS STSSSSSSSS SSSEESDSDE
2210 2220 2230 2240 2250
EEAQKRESTT HMKAYDEESV ASLSTTQDET QDSFQMNNGT PESAYILQGG
2260 2270 2280 2290 2300
YMLAASYWPK DRVMINRLDS ICQTVLKGKW PSARRSYDAN TVASFYTTKL
2310 2320 2330 2340 2350
LDSPGAATEY SDPSVPTPPG AGVKEEHDQS TQMSKVKKHV REKEFTVKIK
2360 2370 2380 2390 2400
DEGGLKLTFQ KQGLAQKRPF DGEDGALGQQ QYLTRLRELQ SASETSLVNF
2410 2420 2430 2440 2450
PKSIPVSGTS IQPTLGANGV ILDNQPIVKK RRGRRKNVEG VDIFFFNRNK
2460 2470 2480 2490 2500
PPNHVSLGLT SSQISTGINP ALSYTQPQGI PDTESPVPVI NLKDGTRLAG
2510 2520 2530 2540 2550
DDAPKRKDLE KWLKEHPGYV EDLGAFIPRM QLHEGRPKQK RHRCRNPNKL
2560 2570 2580 2590 2600
DVNSLTGEER VQLINRRNAR KVGGAFAPPL KDLCRFLKEN SEYGVAPEWG
2610 2620 2630 2640 2650
DVVKQSGFLP ESMYERILTG PVVREEVSRR GRRPKSGIAK ATAAAAAASA
2660 2670 2680 2690 2700
TSVSGNPLLA NGLLPGVDLT TLQALQQNLQ NLQSLQVTAG LMGMPTGLPS
2710 2720 2730 2740 2750
GGEAKNMAAM FPMLLSGMAG LPNLLGMGGL LTKPTESGTE DKKGSDSKES
2760 2770 2780 2790 2800
EGKTERTESQ SSENGGENSV SSSPSTSSTA ALNTAAAANP LALNPLLLSN
2810 2820 2830 2840 2850
ILYPGMLLTP GLNLHIPTLS QSNTFDVQNK NSDLGSSKSV EVKEEDSRIK
2860 2870 2880 2890
DQEDKGGTEP SPLNENSTDE GSEKADASSG SDSTSSSSED SDSSNED
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. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti98 – 1003SQF → PQL in AAT66509 (Ref. 3) Curated
Sequence conflicti119 – 1191S → P in AAT66509 (Ref. 3) Curated
Sequence conflicti208 – 2081V → A in AAT66509 (Ref. 3) Curated
Sequence conflicti473 – 4731L → I in AAT66509 (Ref. 3) Curated
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 (Ref. 3) Curated
Sequence conflicti1372 – 13721S → P in AAT66509 (Ref. 3) Curated
Sequence conflicti1442 – 14421S → G in ABD24032 (PubMed:16554032).Curated
Sequence conflicti1442 – 14421S → G in BAB14112 (PubMed:14702039).Curated
Sequence conflicti1724 – 17241A → T in AAT66509 (Ref. 3) Curated
Sequence conflicti1754 – 17541S → L in AAT66509 (Ref. 3) Curated
Sequence conflicti1867 – 18671T → A in AAT66509 (Ref. 3) Curated
Sequence conflicti2025 – 20251A → V in AAT66509 (Ref. 3) Curated
Sequence conflicti2069 – 20691T → A in AAT66509 (Ref. 3) Curated
Sequence conflicti2078 – 20781V → G in AAT66509 (Ref. 3) Curated
Sequence conflicti2189 – 21891S → F in AAT66509 (Ref. 3) Curated
Sequence conflicti2759 – 27591S → N in AAT66509 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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. [Q3L8U1-1]
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

ProteinModelPortaliQ3L8U1.
SMRiQ3L8U1. Positions 769-828, 2545-2626.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123174. 8 interactions.
IntActiQ3L8U1. 5 interactions.
STRINGi9606.ENSP00000381522.

PTM databases

PhosphoSiteiQ3L8U1.

Polymorphism databases

DMDMi215273951.

Proteomic databases

MaxQBiQ3L8U1.
PaxDbiQ3L8U1.
PRIDEiQ3L8U1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000398510; ENSP00000381522; ENSG00000177200. [Q3L8U1-1]
ENST00000447540; ENSP00000396345; ENSG00000177200. [Q3L8U1-1]
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]

Organism-specific databases

CTDi80205.
GeneCardsiGC16P053041.
HGNCiHGNC:25701. CHD9.
HPAiHPA042053.
HPA049420.
neXtProtiNX_Q3L8U1.
PharmGKBiPA128394727.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0553.
GeneTreeiENSGT00760000119067.
HOVERGENiHBG081150.
InParanoidiQ3L8U1.
KOiK14438.
OMAiQEDKGGT.
OrthoDBiEOG7NSB1C.
PhylomeDBiQ3L8U1.
TreeFamiTF313572.

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_24941. Circadian Clock.
REACT_264212. Transcriptional activation of mitochondrial biogenesis.
REACT_268444. Orphan transporters.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.

Miscellaneous databases

GeneWikiiCHD9.
GenomeRNAii80205.
NextBioi70576.
PROiQ3L8U1.

Gene expression databases

BgeeiQ3L8U1.
CleanExiHS_CHD9.
ExpressionAtlasiQ3L8U1. baseline and differential.
GenevestigatoriQ3L8U1.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR006576. BRK_domain.
IPR000953. Chromo/shadow_dom.
IPR023780. Chromo_domain.
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]
ProtoNetiSearch...

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(2004) [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(2005) [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 (MAY-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(2003) [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(2003) [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(1996) [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(2003) [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(2005) [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(2008) [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(2008) [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(2008) [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(2009) [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: April 1, 2015
This is version 100 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.