CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012947
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein 9 
Protein Synonyms/Alias
 CHD-9; ATP-dependent helicase CHD9; Chromatin-related mesenchymal modulator; 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 Name
 CHD9 
Gene Synonyms/Alias
 KIAA0308; KISH2; PRIC320; AD-013; x0008 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
197QNSLSQSKNFMNVSGubiquitination[1]
490RQPPSSKKSDGSGTYacetylation[2]
499DGSGTYTKLQNTQVRacetylation[2]
1008RLKNKNCKLLEGLKLubiquitination[1]
1323MFDRASLKLGLDKAVubiquitination[1]
1598TSSFDIQKAEWLRKYubiquitination[3]
1694VFKHGYEKYNTIRADubiquitination[1]
1716RVGKPDEKAVAAEQRubiquitination[3]
2038LPRLLDAKGIILEEMubiquitination[1, 3]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 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). 
Sequence Annotation
 DOMAIN 690 761 Chromo 1.
 DOMAIN 773 839 Chromo 2.
 DOMAIN 872 1046 Helicase ATP-binding.
 DOMAIN 1186 1337 Helicase C-terminal.
 NP_BIND 885 892 ATP (Potential).
 REGION 2332 2481 Binds A/T-rich DNA.
 REGION 2429 2436 A.T hook-like.
 MOTIF 868 872 LXXLL motif 1.
 MOTIF 997 1000 DEAH box.
 MOTIF 1036 1040 LXXLL motif 2.
 MOTIF 2031 2035 LXXLL motif 3.
 MOTIF 2721 2725 LXXLL motif 4.
 MOTIF 2793 2798 LXXLL motif 5.
 MOD_RES 499 499 N6-acetyllysine.
 MOD_RES 550 550 Phosphoserine.
 MOD_RES 611 611 Phosphoserine.
 MOD_RES 645 645 Phosphotyrosine (By similarity).
 MOD_RES 1468 1468 Phosphoserine.
 MOD_RES 1472 1472 Phosphoserine.
 MOD_RES 2026 2026 Phosphoserine.
 MOD_RES 2058 2058 Phosphoserine.
 MOD_RES 2059 2059 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; ATP-binding; Chromatin regulator; Complete proteome; Cytoplasm; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2897 AA 
Protein Sequence
MTDPMMDFFD DANLFGETLE GLSDDAFVQP GPVSLVDELN LGAEFEPLHI DSLNHVQGTP 60
THQKMTDFEQ LNQFDSIKFH HVNQSFGSPA EHVLSPHSQF NCSPIHPQNQ PNGLFPDVSD 120
GSPMWGHQTA TTISNQNGSP FHQQGHSHSM HQNKSFVAHH DFALFQANEQ QTQCTSLRSQ 180
QNRNNLNPGQ NSLSQSKNFM NVSGPHRVNV NHPPQMTNAS NSQQSISMQQ FSQTSNPSAH 240
FHKCSSHQEG NFNGPSPNMT SCSVSNSQQF SSHYSFSSNH ISPNSLLQSS AVLASNHTNQ 300
TLSDFTGSNS FSPHRGIKQE STQHILNPNT SLNSNNFQIL HSSHPQGNYS NSKLSPVHMN 360
FPDPVDSGTQ MGHFNDHVET NGFSSLEENL LHQVESQTEP FTGLDPEDLL QEGLLPHFDE 420
STFGQDNSSH ILDHDLDRQF TSHLVTRPSD MAQTQLQSQA RSWHSSFSNH QHLHDRNHLC 480
LQRQPPSSKK SDGSGTYTKL QNTQVRVMSE KKQRKKVESE SKQEKANRII SEAIAKAKER 540
GERNIPRVMS PENFPTASVE GKEEKKGRRM KSKPKDKDSK KTKTCSKLKE KTKIGKLIIT 600
LGKKQKRKNE SSDEISDAEQ MPQHTLKDQD SQKRRSNRQI KRKKYAEDIE GKQSEEEVKG 660
SMKIKKNSAP LPGEQPLQLF VENPSEEDAA IVDKILSSRT VKKEISPGVM IDTEEFFVKY 720
KNYSYLHCEW ATEEQLLKDK RIQQKIKRFK LRQAQRAHFF ADMEEEPFNP DYVEVDRVLE 780
VSFCEDKDTG EPVIYYLVKW CSLPYEDSTW ELKEDVDLAK IEEFEQLQAS RPDTRRLDRP 840
PSNIWKKIDQ SRDYKNGNQL REYQLEGLNW LLFNWYNRRN CILADEMGLG KTIQSITFLY 900
EILLTGIRGP FLIIAPLSTI ANWEREFRTW TDINVVVYHG SLISRQMIQQ YEMYFRDSQG 960
RIIRGAYRFQ AIITTFEMIL GGCGELNAIE WRCVIIDEAH RLKNKNCKLL EGLKLMNLEH 1020
KVLLTGTPLQ NTVEELFSLL HFLEPLRFPS ESTFMQEFGD LKTEEQVQKL QAILKPMMLR 1080
RLKEDVEKKL APKEETIIEV ELTNIQKKYY RAILEKNFSF LSKGAGQTNV PNLVNTMMEL 1140
RKCCNHPYLI KGAEEKILGE FRDTYNPAAS DFHLQAMIQS AGKLVLIDKL LPKMKAGGHK 1200
VLIFSQMVRC LDILEDYLIH KRYLYERIDG RVRGNLRQAA IDRFSKPDSD RFVFLLCTRA 1260
GGLGINLTAA DTCIIFDSDW NPQNDLQAQA RCHRIGQNKA VKVYRLVTRN SYEREMFDRA 1320
SLKLGLDKAV LQSMSGRESN VGGIQQLSKK EIEDLLRRGA YGAIMEEEDE GSKFCEEDID 1380
QILLRRTKTI TIESEGRGST FAKASFVASG NRTDISLDDP NFWQKWAKKA EIDIEAISGR 1440
NSLVIDTPRI RKQTRPFSAT KDELAELSEA ESEGDEKPKL RRPCDRSNGY GRTECFRVEK 1500
NLLVYGWGRW REILSHGRFK RQLNEHDVEI ICRALLAYCL VHYRGDEKIK GFIWDLITPT 1560
EDGQTRELQN HLGLSAPVPR GRKGKKVKTQ TSSFDIQKAE WLRKYNPEQL LQDEGYKKHI 1620
KHHCNKVLLR VRMLYYLKQE VIGNECQKVF DGVDASDIDV WVPEPDHSEV PAEWWDFDAD 1680
KSLLIGVFKH GYEKYNTIRA DPALCFLERV GKPDEKAVAA EQRANDYMDG DVEDPEYKPA 1740
PAIFKDDIED DVSSPGDLVI ADGDGQLMEG DKVYWPTQSA LTTRLRRLIT AYQRTNKNRQ 1800
IQQIQPTFSV PTSVMQPIYE EATLNPKMAA KIERQQRWTR REEADFYRVV STFGVVFDPD 1860
RGQFDWTKFR AMARLHKKTD DSLEKYLYAF MSMCRRVCRL PSKEELVDPN IFIQPITEER 1920
ASRTLYRIEL LRKVREQALR HPQLFERLKL CHPNPDLPVW WECGPHDRDL LIGAAKHGVS 1980
RTDYHILRDP ELSFMAAQRN YSQSKMAHSR TSTPLLQQYQ VALSASPLTS LPRLLDAKGI 2040
ILEEMKVKSE NLKEEPQSSE EESMSSVETR TLIKSEPVSP KNGVLPQATG DQKSGGKCET 2100
DRRMVAARTE PLTPNPASKK PRVHKRGSES SSDSDSDSER SSCSSRSSSS SSSSSCSHSR 2160
SGSSSSSSSS CSSASSSSSS STSSSSSSSS SSSEESDSDE EEAQKRESTT HMKAYDEESV 2220
ASLSTTQDET QDSFQMNNGT PESAYILQGG YMLAASYWPK DRVMINRLDS ICQTVLKGKW 2280
PSARRSYDAN TVASFYTTKL LDSPGAATEY SDPSVPTPPG AGVKEEHDQS TQMSKVKKHV 2340
REKEFTVKIK DEGGLKLTFQ KQGLAQKRPF DGEDGALGQQ QYLTRLRELQ SASETSLVNF 2400
PKSIPVSGTS IQPTLGANGV ILDNQPIVKK RRGRRKNVEG VDIFFFNRNK PPNHVSLGLT 2460
SSQISTGINP ALSYTQPQGI PDTESPVPVI NLKDGTRLAG DDAPKRKDLE KWLKEHPGYV 2520
EDLGAFIPRM QLHEGRPKQK RHRCRNPNKL DVNSLTGEER VQLINRRNAR KVGGAFAPPL 2580
KDLCRFLKEN SEYGVAPEWG DVVKQSGFLP ESMYERILTG PVVREEVSRR GRRPKSGIAK 2640
ATAAAAAASA TSVSGNPLLA NGLLPGVDLT TLQALQQNLQ NLQSLQVTAG LMGMPTGLPS 2700
GGEAKNMAAM FPMLLSGMAG LPNLLGMGGL LTKPTESGTE DKKGSDSKES EGKTERTESQ 2760
SSENGGENSV SSSPSTSSTA ALNTAAAANP LALNPLLLSN ILYPGMLLTP GLNLHIPTLS 2820
QSNTFDVQNK NSDLGSSKSV EVKEEDSRIK DQEDKGGTEP SPLNENSTDE GSEKADASSG 2880
SDSTSSSSED SDSSNED 2897 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0044255; P:cellular lipid metabolic process; TAS:Reactome.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0044281; P:small molecule metabolic process; TAS:Reactome.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 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. 
Pfam
 PF07533; BRK
 PF00385; Chromo
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00592; BRK
 SM00298; CHROMO
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS