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Q3L8U1 (CHD9_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chromodomain-helicase-DNA-binding protein 9

Short name=CHD-9
EC=3.6.4.12
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 names
Name:CHD9
Synonyms:KIAA0308, KISH2, PRIC320
ORF Names:AD-013, x0008
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2897 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.2

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with PPARA. Probably interacts with ESR1 and NR1I3. Ref.2

Subcellular location

Cytoplasm. Nucleus Ref.1.

Tissue specificity

Widely expressed at low levels. In bone marrow, expression is restricted to osteoprogenitor cells adjacent to mature osteoblasts. Ref.1 Ref.2

Post-translational modification

Phosphorylated on serine and tyrosine residues. Ref.1

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 2 chromo domains.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence AAF24170.1 differs from that shown. Reason: Erroneous translation. Wrong choice of frame.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PPARAQ078692EBI-960730,EBI-78615

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3L8U1-1)

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.
Isoform 2 (identifier: Q3L8U1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     2336-2351: Missing.
Isoform 3 (identifier: Q3L8U1-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 28972897Chromodomain-helicase-DNA-binding protein 9
PRO_0000233172

Regions

Domain690 – 76172Chromo 1
Domain773 – 83967Chromo 2
Domain872 – 1046175Helicase ATP-binding
Domain1186 – 1337152Helicase C-terminal
Nucleotide binding885 – 8928ATP Potential
Region2332 – 2481150Binds A/T-rich DNA
Region2429 – 24368A.T hook-like
Motif868 – 8725LXXLL motif 1
Motif997 – 10004DEAH box
Motif1036 – 10405LXXLL motif 2
Motif2031 – 20355LXXLL motif 3
Motif2721 – 27255LXXLL motif 4
Motif2793 – 27986LXXLL motif 5
Compositional bias220 – 31293Ser-rich
Compositional bias562 – 666105Lys-rich
Compositional bias2128 – 219871Ser-rich
Compositional bias2639 – 265012Poly-Ala
Compositional bias2785 – 27884Poly-Ala
Compositional bias2878 – 288811Poly-Ser

Amino acid modifications

Modified residue4991N6-acetyllysine Ref.13
Modified residue5501Phosphoserine Ref.10 Ref.12 Ref.14
Modified residue6111Phosphoserine Ref.10
Modified residue14681Phosphoserine Ref.9 Ref.14
Modified residue14721Phosphoserine Ref.9 Ref.14
Modified residue20261Phosphoserine Ref.10
Modified residue20581Phosphoserine Ref.12
Modified residue20591Phosphoserine Ref.12

Natural variations

Alternative sequence22061R → RA in isoform 3.
VSP_018085
Alternative sequence2336 – 235116Missing in isoform 2 and isoform 3.
VSP_018086
Natural variant23121D → E. Ref.1 Ref.2 Ref.6
Corresponds to variant rs6499548 [ dbSNP | Ensembl ].
VAR_047355

Experimental info

Sequence conflict98 – 1003SQF → PQL in AAT66509. Ref.3
Sequence conflict1191S → P in AAT66509. Ref.3
Sequence conflict2081V → A in AAT66509. Ref.3
Sequence conflict4731L → I in AAT66509. Ref.3
Sequence conflict8361R → C in ABD24032. Ref.2
Sequence conflict8361R → C in BAA20767. Ref.6
Sequence conflict10721A → V in ABD24032. Ref.2
Sequence conflict10721A → V in BAB14112. Ref.8
Sequence conflict11221S → F in AAT66509. Ref.3
Sequence conflict13721S → P in AAT66509. Ref.3
Sequence conflict14421S → G in ABD24032. Ref.2
Sequence conflict14421S → G in BAB14112. Ref.8
Sequence conflict17241A → T in AAT66509. Ref.3
Sequence conflict17541S → L in AAT66509. Ref.3
Sequence conflict18671T → A in AAT66509. Ref.3
Sequence conflict20251A → V in AAT66509. Ref.3
Sequence conflict20691T → A in AAT66509. Ref.3
Sequence conflict20781V → G in AAT66509. Ref.3
Sequence conflict21891S → F in AAT66509. Ref.3
Sequence conflict27591S → N in AAT66509. Ref.3
Sequence conflict27761T → A in AAQ24287. Ref.1
Sequence conflict27761T → A in BAA20767. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 2.
Checksum: 91884A5E2F8ED183

FASTA2,897326,022
        10         20         30         40         50         60 
MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP 

        70         80         90        100        110        120 
THQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF NCSPIHPQNQ PNGLFPDVSD 

       130        140        150        160        170        180 
GSPMWGHQTA TTISNQNGSP FHQQGHSHSM HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ 

       190        200        210        220        230        240 
QNRNNLNPGQ NSLSQSKNFM NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH 

       250        260        270        280        290        300 
FHKCSSHQEG NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLASNHTNQ 

       310        320        330        340        350        360 
TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS NSKLSPVHMN 

       370        380        390        400        410        420 
FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP FTGLDPEDLL QEGLLPHFDE 

       430        440        450        460        470        480 
STFGQDNSSH ILDHDLDRQF TSHLVTRPSD MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC 

       490        500        510        520        530        540 
LQRQPPSSKK SDGSGTYTKL QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER 

       550        560        570        580        590        600 
GERNIPRVMS PENFPTASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT 

       610        620        630        640        650        660 
LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDIE GKQSEEEVKG 

       670        680        690        700        710        720 
SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRT VKKEISPGVM IDTEEFFVKY 

       730        740        750        760        770        780 
KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE 

       790        800        810        820        830        840 
VSFCEDKDTG EPVIYYLVKW CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP 

       850        860        870        880        890        900 
PSNIWKKIDQ SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY 

       910        920        930        940        950        960 
EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ YEMYFRDSQG 

       970        980        990       1000       1010       1020 
RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH RLKNKNCKLL EGLKLMNLEH 

      1030       1040       1050       1060       1070       1080 
KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS ESTFMQEFGD LKTEEQVQKL QAILKPMMLR 

      1090       1100       1110       1120       1130       1140 
RLKEDVEKKL APKEETIIEV ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL 

      1150       1160       1170       1180       1190       1200 
RKCCNHPYLI KGAEEKILGE FRDTYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK 

      1210       1220       1230       1240       1250       1260 
VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD RFVFLLCTRA 

      1270       1280       1290       1300       1310       1320 
GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA VKVYRLVTRN SYEREMFDRA 

      1330       1340       1350       1360       1370       1380 
SLKLGLDKAV LQSMSGRESN VGGIQQLSKK EIEDLLRRGA YGAIMEEEDE GSKFCEEDID 

      1390       1400       1410       1420       1430       1440 
QILLRRTKTI TIESEGRGST FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR 

      1450       1460       1470       1480       1490       1500 
NSLVIDTPRI RKQTRPFSAT KDELAELSEA ESEGDEKPKL RRPCDRSNGY GRTECFRVEK 

      1510       1520       1530       1540       1550       1560 
NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK GFIWDLITPT 

      1570       1580       1590       1600       1610       1620 
EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE WLRKYNPEQL LQDEGYKKHI 

      1630       1640       1650       1660       1670       1680 
KHHCNKVLLR VRMLYYLKQE VIGNECQKVF DGVDASDIDV WVPEPDHSEV PAEWWDFDAD 

      1690       1700       1710       1720       1730       1740 
KSLLIGVFKH GYEKYNTIRA DPALCFLERV GKPDEKAVAA EQRANDYMDG DVEDPEYKPA 

      1750       1760       1770       1780       1790       1800 
PAIFKDDIED DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ 

      1810       1820       1830       1840       1850       1860 
IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV STFGVVFDPD 

      1870       1880       1890       1900       1910       1920 
RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL PSKEELVDPN IFIQPITEER 

      1930       1940       1950       1960       1970       1980 
ASRTLYRIEL LRKVREQALR HPQLFERLKL CHPNPDLPVW WECGPHDRDL LIGAAKHGVS 

      1990       2000       2010       2020       2030       2040 
RTDYHILRDP ELSFMAAQRN YSQSKMAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI 

      2050       2060       2070       2080       2090       2100 
ILEEMKVKSE NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKCET 

      2110       2120       2130       2140       2150       2160 
DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS SSSSSCSHSR 

      2170       2180       2190       2200       2210       2220 
SGSSSSSSSS CSSASSSSSS STSSSSSSSS SSSEESDSDE EEAQKRESTT HMKAYDEESV 

      2230       2240       2250       2260       2270       2280 
ASLSTTQDET QDSFQMNNGT PESAYILQGG YMLAASYWPK DRVMINRLDS ICQTVLKGKW 

      2290       2300       2310       2320       2330       2340 
PSARRSYDAN TVASFYTTKL LDSPGAATEY SDPSVPTPPG AGVKEEHDQS TQMSKVKKHV 

      2350       2360       2370       2380       2390       2400 
REKEFTVKIK DEGGLKLTFQ KQGLAQKRPF DGEDGALGQQ QYLTRLRELQ SASETSLVNF 

      2410       2420       2430       2440       2450       2460 
PKSIPVSGTS IQPTLGANGV ILDNQPIVKK RRGRRKNVEG VDIFFFNRNK PPNHVSLGLT 

      2470       2480       2490       2500       2510       2520 
SSQISTGINP ALSYTQPQGI PDTESPVPVI NLKDGTRLAG DDAPKRKDLE KWLKEHPGYV 

      2530       2540       2550       2560       2570       2580 
EDLGAFIPRM QLHEGRPKQK RHRCRNPNKL DVNSLTGEER VQLINRRNAR KVGGAFAPPL 

      2590       2600       2610       2620       2630       2640 
KDLCRFLKEN SEYGVAPEWG DVVKQSGFLP ESMYERILTG PVVREEVSRR GRRPKSGIAK 

      2650       2660       2670       2680       2690       2700 
ATAAAAAASA TSVSGNPLLA NGLLPGVDLT TLQALQQNLQ NLQSLQVTAG LMGMPTGLPS 

      2710       2720       2730       2740       2750       2760 
GGEAKNMAAM FPMLLSGMAG LPNLLGMGGL LTKPTESGTE DKKGSDSKES EGKTERTESQ 

      2770       2780       2790       2800       2810       2820 
SSENGGENSV SSSPSTSSTA ALNTAAAANP LALNPLLLSN ILYPGMLLTP GLNLHIPTLS 

      2830       2840       2850       2860       2870       2880 
QSNTFDVQNK NSDLGSSKSV EVKEEDSRIK DQEDKGGTEP SPLNENSTDE GSEKADASSG 

      2890 
SDSTSSSSED SDSSNED 

« Hide

Isoform 2 [UniParc].

Checksum: 5D325328A88F5E4E
Show »

FASTA2,881324,055
Isoform 3 [UniParc].

Checksum: E5E272E36C779BB6
Show »

FASTA2,882324,127

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS45485.1. [Q3L8U1-2]
RefSeqNP_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]
UniGeneHs.59159.
Hs.622347.

3D structure databases

ProteinModelPortalQ3L8U1.
SMRQ3L8U1. Positions 715-1403, 2482-2529, 2545-2626.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid123174. 7 interactions.
IntActQ3L8U1. 5 interactions.
STRING9606.ENSP00000381522.

PTM databases

PhosphoSiteQ3L8U1.

Polymorphism databases

DMDM215273951.

Proteomic databases

MaxQBQ3L8U1.
PaxDbQ3L8U1.
PRIDEQ3L8U1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000398510; ENSP00000381522; ENSG00000177200. [Q3L8U1-1]
ENST00000447540; ENSP00000396345; ENSG00000177200. [Q3L8U1-3]
ENST00000564845; ENSP00000455307; ENSG00000177200. [Q3L8U1-2]
ENST00000566029; ENSP00000457466; ENSG00000177200. [Q3L8U1-2]
GeneID80205.
KEGGhsa:80205.
UCSCuc002egy.3. human. [Q3L8U1-2]
uc002ehb.3. human. [Q3L8U1-1]
uc002ehc.3. human. [Q3L8U1-3]

Organism-specific databases

CTD80205.
GeneCardsGC16P053041.
HGNCHGNC:25701. CHD9.
HPAHPA042053.
HPA049420.
neXtProtNX_Q3L8U1.
PharmGKBPA128394727.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOVERGENHBG081150.
InParanoidQ3L8U1.
KOK14438.
OMAQEDKGGT.
OrthoDBEOG7NSB1C.
PhylomeDBQ3L8U1.
TreeFamTF313572.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ3L8U1.
BgeeQ3L8U1.
CleanExHS_CHD9.
GenevestigatorQ3L8U1.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR006576. 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]
PfamPF07533. BRK. 2 hits.
PF00385. Chromo. 2 hits.
PF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00592. BRK. 2 hits.
SM00298. CHROMO. 2 hits.
SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
SSF54160. SSF54160. 2 hits.
PROSITEPS50013. CHROMO_2. 2 hits.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCHD9.
GenomeRNAi80205.
NextBio70576.
PROQ3L8U1.

Entry information

Entry nameCHD9_HUMAN
AccessionPrimary (citable) accession number: Q3L8U1
Secondary accession number(s): B2RTU2 expand/collapse secondary AC list , B9ZVQ0, O15025, Q1WF12, Q6DTK9, Q9H9V7, Q9UHM2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2006
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM