CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022547
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein 7 
Protein Synonyms/Alias
 CHD-7; ATP-dependent helicase CHD7 
Gene Name
 CHD7 
Gene Synonyms/Alias
 KIAA1416 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
565PSEPFLEKPVPDMTQacetylation[1]
617DPSKGFGKDDFPGGVacetylation[2]
934AKIEEFEKLMSREPEubiquitination[3, 4, 5]
2230VGADTGSKSISEKGSacetylation[2]
2266AGAVSRGKNFDEESNubiquitination[6]
2446EKVVDLSKASREATSubiquitination[7]
2657VNKRNGKKMGGAMAPubiquitination[6]
2667GAMAPPMKDLPRWLEubiquitination[6]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [6] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [7] 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] 
Functional Description
 Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production. 
Sequence Annotation
 DOMAIN 800 867 Chromo 1.
 DOMAIN 882 947 Chromo 2.
 DOMAIN 980 1154 Helicase ATP-binding.
 DOMAIN 1294 1464 Helicase C-terminal.
 NP_BIND 993 1000 ATP (Potential).
 MOTIF 1105 1108 DEAH box.
 MOD_RES 637 637 Phosphoserine.
 MOD_RES 725 725 Phosphoserine.
 MOD_RES 1577 1577 Phosphoserine.
 MOD_RES 1581 1581 Phosphoserine.
 MOD_RES 1874 1874 Phosphoserine.
 MOD_RES 2231 2231 Phosphoserine.
 MOD_RES 2233 2233 Phosphoserine.
 MOD_RES 2237 2237 Phosphoserine.
 MOD_RES 2251 2251 Phosphoserine.
 MOD_RES 2272 2272 Phosphoserine.
 MOD_RES 2275 2275 Phosphoserine.
 MOD_RES 2356 2356 Phosphoserine.
 MOD_RES 2395 2395 Phosphoserine.
 MOD_RES 2472 2472 Phosphothreonine.
 MOD_RES 2533 2533 Phosphoserine.
 MOD_RES 2535 2535 Phosphoserine.
 MOD_RES 2551 2551 Phosphothreonine.
 MOD_RES 2559 2559 Phosphoserine.
 MOD_RES 2619 2619 Phosphoserine.
 MOD_RES 2956 2956 Phosphoserine.
 MOD_RES 2961 2961 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Chromatin regulator; Coiled coil; Complete proteome; Disease mutation; DNA-binding; Helicase; Hydrolase; Hypogonadotropic hypogonadism; Kallmann syndrome; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; rRNA processing; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2997 AA 
Protein Sequence
MADPGMMSLF GEDGNIFSEG LEGLGECGYP ENPVNPMGQQ MPIDQGFASL QPSLHHPSTN 60
QNQTKLTHFD HYNQYEQQKM HLMDQPNRMM SNTPGNGLAS PHSQYHTPPV PQVPHGGSGG 120
GQMGVYPGMQ NERHGQSFVD SSSMWGPRAV QVPDQIRAPY QQQQPQPQPP QPAPSGPPAQ 180
GHPQHMQQMG SYMARGDFSM QQHGQPQQRM SQFSQGQEGL NQGNPFIATS GPGHLSHVPQ 240
QSPSMAPSLR HSVQQFHHHP STALHGESVA HSPRFSPNPP QQGAVRPQTL NFSSRSQTVP 300
SPTINNSGQY SRYPYSNLNQ GLVNNTGMNQ NLGLTNNTPM NQSVPRYPNA VGFPSNSGQG 360
LMHQQPIHPS GSLNQMNTQT MHPSQPQGTY ASPPPMSPMK AMSNPAGTPP PQVRPGSAGI 420
PMEVGSYPNM PHPQPSHQPP GAMGIGQRNM GPRNMQQSRP FIGMSSAPRE LTGHMRPNGC 480
PGVGLGDPQA IQERLIPGQQ HPGQQPSFQQ LPTCPPLQPH PGLHHQSSPP HPHHQPWAQL 540
HPSPQNTPQK VPVHQHSPSE PFLEKPVPDM TQVSGPNAQL VKSDDYLPSI EQQPQQKKKK 600
KKNNHIVAED PSKGFGKDDF PGGVDNQELN RNSLDGSQEE KKKKKRSKAK KDPKEPKEPK 660
EKKEPKEPKT PKAPKIPKEP KEKKAKTATP KPKSSKKSSN KKPDSEASAL KKKVNKGKTE 720
GSENSDLDKT PPPSPPPEED EDPGVQKRRS SRQVKRKRYT EDLEFKISDE EADDADAAGR 780
DSPSNTSQSE QQESVDAEGP VVEKIMSSRS VKKQKESGEE VEIEEFYVKY KNFSYLHCQW 840
ASIEDLEKDK RIQQKIKRFK AKQGQNKFLS EIEDELFNPD YVEVDRIMDF ARSTDDRGEP 900
VTHYLVKWCS LPYEDSTWER RQDIDQAKIE EFEKLMSREP ETERVERPPA DDWKKSESSR 960
EYKNNNKLRE YQLEGVNWLL FNWYNMRNCI LADEMGLGKT IQSITFLYEI YLKGIHGPFL 1020
VIAPLSTIPN WEREFRTWTE LNVVVYHGSQ ASRRTIQLYE MYFKDPQGRV IKGSYKFHAI 1080
ITTFEMILTD CPELRNIPWR CVVIDEAHRL KNRNCKLLEG LKMMDLEHKV LLTGTPLQNT 1140
VEELFSLLHF LEPSRFPSET TFMQEFGDLK TEEQVQKLQA ILKPMMLRRL KEDVEKNLAP 1200
KEETIIEVEL TNIQKKYYRA ILEKNFTFLS KGGGQANVPN LLNTMMELRK CCNHPYLING 1260
AEEKILEEFK ETHNAESPDF QLQAMIQAAG KLVLIDKLLP KLKAGGHRVL IFSQMVRCLD 1320
ILEDYLIQRR YPYERIDGRV RGNLRQAAID RFSKPDSDRF VFLLCTRAGG LGINLTAADT 1380
CIIFDSDWNP QNDLQAQARC HRIGQSKSVK IYRLITRNSY EREMFDKASL KLGLDKAVLQ 1440
SMSGRENATN GVQQLSKKEI EDLLRKGAYG ALMDEEDEGS KFCEEDIDQI LLRRTHTITI 1500
ESEGKGSTFA KASFVASGNR TDISLDDPNF WQKWAKKAEL DIDALNGRNN LVIDTPRVRK 1560
QTRLYSAVKE DELMEFSDLE SDSEEKPCAK PRRPQDKSQG YARSECFRVE KNLLVYGWGR 1620
WTDILSHGRY KRQLTEQDVE TICRTILVYC LNHYKGDENI KSFIWDLITP TADGQTRALV 1680
NHSGLSAPVP RGRKGKKVKA QSTQPVVQDA DWLASCNPDA LFQEDSYKKH LKHHCNKVLL 1740
RVRMLYYLRQ EVIGDQADKI LEGADSSEAD VWIPEPFHAE VPADWWDKEA DKSLLIGVFK 1800
HGYEKYNSMR ADPALCFLER VGMPDAKAIA AEQRGTDMLA DGGDGGEFDR EDEDPEYKPT 1860
RTPFKDEIDE FANSPSEDKE ESMEIHATGK HSESNAELGQ LYWPNTSTLT TRLRRLITAY 1920
QRSYKRQQMR QEALMKTDRR RRRPREEVRA LEAEREAIIS EKRQKWTRRE EADFYRVVST 1980
FGVIFDPVKQ QFDWNQFRAF ARLDKKSDES LEKYFSCFVA MCRRVCRMPV KPDDEPPDLS 2040
SIIEPITEER ASRTLYRIEL LRKIREQVLH HPQLGERLKL CQPSLDLPEW WECGRHDRDL 2100
LVGAAKHGVS RTDYHILNDP ELSFLDAHKN FAQNRGAGNT SSLNPLAVGF VQTPPVISSA 2160
HIQDERVLEQ AEGKVEEPEN PAAKEKCEGK EEEEETDGSG KESKQECEAE ASSVKNELKG 2220
VEVGADTGSK SISEKGSEED EEEKLEDDDK SEESSQPEAG AVSRGKNFDE ESNASMSTAR 2280
DETRDGFYME DGDPSVAQLL HERTFAFSFW PKDRVMINRL DNICEAVLKG KWPVNRRQMF 2340
DFQGLIPGYT PTTVDSPLQK RSFAELSMVG QASISGSEDI TTSPQLSKED ALNLSVPRQR 2400
RRRRRKIEIE AERAAKRRNL MEMVAQLRES QVVSENGQEK VVDLSKASRE ATSSTSNFSS 2460
LSSKFILPNV STPVSDAFKT QMELLQAGLS RTPTRHLLNG SLVDGEPPMK RRRGRRKNVE 2520
GLDLLFMSHK RTSLSAEDAE VTKAFEEDIE TPPTRNIPSP GQLDPDTRIP VINLEDGTRL 2580
VGEDAPKNKD LVEWLKLHPT YTVDMPSYVP KNADVLFSSF QKPKQKRHRC RNPNKLDINT 2640
LTGEERVPVV NKRNGKKMGG AMAPPMKDLP RWLEENPEFA VAPDWTDIVK QSGFVPESMF 2700
DRLLTGPVVR GEGASRRGRR PKSEIARAAA AAAAVASTSG INPLLVNSLF AGMDLTSLQN 2760
LQNLQSLQLA GLMGFPPGLA TAATAGGDAK NPAAVLPLML PGMAGLPNVF GLGGLLNNPL 2820
SAATGNTTTA SSQGEPEDST SKGEEKGNEN EDENKDSEKS TDAVSAADSA NGSVGAATAP 2880
AGLPSNPLAF NPFLLSTMAP GLFYPSMFLP PGLGGLTLPG FPALAGLQNA VGSSEEKAAD 2940
KAEGGPFKDG ETLEGSDAEE SLDKTAESSL LEDEIAQGEE LDSLDGGDEI ENNENDE 2997 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0003682; F:chromatin binding; TAS:BHF-UCL.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
 GO:0007512; P:adult heart development; IEA:Compara.
 GO:0007628; P:adult walking behavior; IEA:Compara.
 GO:0048844; P:artery morphogenesis; IEA:Compara.
 GO:0008015; P:blood circulation; IEA:Compara.
 GO:0007417; P:central nervous system development; IMP:BHF-UCL.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0050890; P:cognition; IMP:BHF-UCL.
 GO:0021545; P:cranial nerve development; IMP:BHF-UCL.
 GO:0035116; P:embryonic hindlimb morphogenesis; IEA:Compara.
 GO:0060324; P:face development; IMP:BHF-UCL.
 GO:0030540; P:female genitalia development; IEA:Compara.
 GO:0048806; P:genitalia development; IMP:BHF-UCL.
 GO:0003007; P:heart morphogenesis; IMP:BHF-UCL.
 GO:0001701; P:in utero embryonic development; IMP:BHF-UCL.
 GO:0042472; P:inner ear morphogenesis; IMP:BHF-UCL.
 GO:0060173; P:limb development; IMP:BHF-UCL.
 GO:0043584; P:nose development; IMP:BHF-UCL.
 GO:0060021; P:palate development; IMP:BHF-UCL.
 GO:0040018; P:positive regulation of multicellular organism growth; IEA:Compara.
 GO:0060123; P:regulation of growth hormone secretion; IMP:BHF-UCL.
 GO:0006355; P:regulation of transcription, DNA-dependent; NAS:BHF-UCL.
 GO:0060041; P:retina development in camera-type eye; IMP:BHF-UCL.
 GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
 GO:0048752; P:semicircular canal morphogenesis; IEA:Compara.
 GO:0007605; P:sensory perception of sound; IEA:Compara.
 GO:0001501; P:skeletal system development; IMP:BHF-UCL.
 GO:0030217; P:T cell differentiation; IMP:BHF-UCL.
 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.
 IPR001005; SANT/Myb.
 IPR000330; SNF2_N. 
Pfam
 PF07533; BRK
 PF00385; Chromo
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00592; BRK
 SM00298; CHROMO
 SM00487; DEXDc
 SM00490; HELICc
 SM00717; SANT 
PROSITE
 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS