CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021667
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein 8 
Protein Synonyms/Alias
 CHD-8; ATP-dependent helicase CHD8; Helicase with SNF2 domain 1 
Gene Name
 CHD8 
Gene Synonyms/Alias
 HELSNF1; KIAA1564 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
270GATGPPLKPAVTLTSubiquitination[1]
313VLGSLPGKIVLQGNQubiquitination[2]
328LAALTQAKNAQGQPAubiquitination[2, 3]
399QRLSVPVKVVLQPQAubiquitination[2]
798PQASAWKKLELSHEYubiquitination[2]
1058VELTNIQKKYYRAILubiquitination[2]
1093NTMMELRKCCNHPYLubiquitination[2]
1140GKLVLIDKLLPKLKAubiquitination[2]
1270YEREMFDKASLKLGLubiquitination[2]
1274MFDKASLKLGLDKAVubiquitination[2]
1301GIQQFSKKEIEDLLRacetylation[4]
1301GIQQFSKKEIEDLLRubiquitination[2]
1376DDPNFWQKWAKKADLubiquitination[2]
1391DMDLLNSKNNLVIDTubiquitination[2]
1644VFKHGYEKYNTMRADubiquitination[2]
1666KAGRPDDKAIAAEHRubiquitination[2]
1766SYKREQMKIEAAERGubiquitination[2]
2241TAAAQFTKLRRGMDEubiquitination[2]
2320TRIPVINKVDGTLLVubiquitination[5]
2416PIAPESSKKRARRMRubiquitination[2]
2417IAPESSKKRARRMRPubiquitination[2]
Reference
 [1] 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]
 [2] 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]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] 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
 DNA helicase that acts as a chromatin remodeling factor and regulates transcription. Acts as a transcription repressor by remodeling chromatin structure and recruiting histone H1 to target genes. Suppresses p53/TP53-mediated apoptosis by recruiting histone H1 and preventing p53/TP53 transactivation activity. Acts as a negative regulator of Wnt signaling pathway by regulating beta-catenin (CTNNB1) activity. Negatively regulates CTNNB1- targeted gene expression by being recruited specifically to the promoter regions of several CTNNB1 responsive genes. Involved in both enhancer blocking and epigenetic remodeling at chromatin boundary via its interaction with CTCF. Acts as a suppressor of STAT3 activity by suppressing the LIF-induced STAT3 transcriptional activity. Also acts as a transcription activator via its interaction with ZNF143 by participating in efficient U6 RNA polymerase III transcription. 
Sequence Annotation
 DOMAIN 642 709 Chromo 1.
 DOMAIN 724 790 Chromo 2.
 DOMAIN 823 997 Helicase ATP-binding.
 DOMAIN 1137 1288 Helicase C-terminal.
 NP_BIND 836 843 ATP (Potential).
 MOTIF 948 951 DEAH box.
 MOD_RES 553 553 Phosphoserine.
 MOD_RES 562 562 Phosphoserine.
 MOD_RES 1420 1420 Phosphoserine.
 MOD_RES 1424 1424 Phosphoserine.
 MOD_RES 1976 1976 Phosphoserine.
 MOD_RES 1993 1993 Phosphothreonine.
 MOD_RES 2008 2008 Phosphoserine.
 MOD_RES 2046 2046 Phosphoserine.
 MOD_RES 2051 2051 Phosphothreonine.
 MOD_RES 2069 2069 Phosphoserine.
 MOD_RES 2071 2071 Phosphoserine.
 MOD_RES 2182 2182 Phosphoserine.
 MOD_RES 2200 2200 Phosphoserine.
 MOD_RES 2211 2211 Phosphoserine.
 MOD_RES 2519 2519 Phosphoserine.
 CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Activator; Alternative splicing; ATP-binding; Chromatin regulator; Complete proteome; Disease mutation; DNA-binding; Helicase; Hydrolase; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Wnt signaling pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2581 AA 
Protein Sequence
MADPIMDLFD DPNLFGLDSL TDDSFNQVTQ DPIEEALGLP SSLDSLDQMN QDGGGGDVGN 60
SSASELVPPP EETAPTELSK ESTAPAPESI TLHDYTTQPA SQEQPAQPVL QTSTPTSGLL 120
QVSKSQEILS QGNPFMGVSA TAVSSSSAGG QPPQSAPKIV ILKAPPSSSV TGAHVAQIQA 180
QGITSTAQPL VAGTANGGKV TFTKVLTGTP LRPGVSIVSG NTVLAAKVPG NQAAVQRIVQ 240
PSRPVKQLVL QPVKGSAPAG NPGATGPPLK PAVTLTSTPT QGESKRITLV LQQPQSGGPQ 300
GHRHVVLGSL PGKIVLQGNQ LAALTQAKNA QGQPAKVVTI QLQVQQPQQK IQIVPQPPSS 360
QPQPQQPPST QPVTLSSVQQ AQIMGPGQSP GQRLSVPVKV VLQPQAGSSQ GASSGLSVVK 420
VLSASEVAAL SSPASSAPHS GGKTGMEENR RLEHQKKQEK ANRIVAEAIA RARARGEQNI 480
PRVLNEDELP SVRPEEEGEK KRRKKSAGER LKEEKPKKSK TSGASKTKGK SKLNTITPVV 540
GKKRKRNTSS DNSDVEVMPA QSPREDEESS IQKRRSNRQV KRKKYTEDLD IKITDDEEEE 600
EVDVTGPIKP EPILPEPVQE PDGETLPSMQ FFVENPSEED AAIVDKVLSM RIVKKELPSG 660
QYTEAEEFFV KYKNYSYLHC EWATISQLEK DKRIHQKLKR FKTKMAQMRH FFHEDEEPFN 720
PDYVEVDRIL DESHSIDKDN GEPVIYYLVK WCSLPYEDST WELKEDVDEG KIREFKRIQS 780
RHPELKRVNR PQASAWKKLE LSHEYKNRNQ LREYQLEGVN WLLFNWYNRQ NCILADEMGL 840
GKTIQSIAFL QEVYNVGIHG PFLVIAPLST ITNWEREFNT WTEMNTIVYH GSLASRQMIQ 900
QYEMYCKDSR GRLIPGAYKF DALITTFEMI LSDCPELREI EWRCVIIDEA HRLKNRNCKL 960
LDSLKHMDLE HKVLLTGTPL QNTVEELFSL LHFLEPSQFP SESEFLKDFG DLKTEEQVQK 1020
LQAILKPMML RRLKEDVEKN LAPKQETIIE VELTNIQKKY YRAILEKNFS FLSKGAGHTN 1080
MPNLLNTMME LRKCCNHPYL INGAEEKILT EFREACHIIP HDFHLQAMVR SAGKLVLIDK 1140
LLPKLKAGGH KVLIFSQMVR CLDILEDYLI QRRYLYERID GRVRGNLRQA AIDRFSKPDS 1200
DRFVFLLCTR AGGLGINLTA ADTCIIFDSD WNPQNDLQAQ ARCHRIGQSK AVKVYRLITR 1260
NSYEREMFDK ASLKLGLDKA VLQSMSGRDG NITGIQQFSK KEIEDLLRKG AYAAIMEEDD 1320
EGSKFCEEDI DQILLRRTTT ITIESEGKGS TFAKASFVAS ENRTDISLDD PNFWQKWAKK 1380
ADLDMDLLNS KNNLVIDTPR VRKQTRHFST LKDDDLVEFS DLESEDDERP RSRRHDRHHA 1440
YGRTDCFRVE KHLLVYGWGR WRDILSHGRF KRRMTERDVE TICRAILVYC LLHYRGDENI 1500
KGFIWDLISP AENGKTKELQ NHSGLSIPVP RGRKGKKVKS QSTFDIHKAD WIRKYNPDTL 1560
FQDESYKKHL KHQCNKVLLR VRMLYYLRQE VIGDQAEKVL GGAIASEIDI WFPVVDQLEV 1620
PTTWWDSEAD KSLLIGVFKH GYEKYNTMRA DPALCFLEKA GRPDDKAIAA EHRVLDNFSD 1680
IVEGVDFDKD CEDPEYKPLQ GPPKDQDDEG DPLMMMDEEI SVIDGDEAQV TQQPGHLFWP 1740
PGSALTARLR RLVTAYQRSY KREQMKIEAA ERGDRRRRRC EAAFKLKEIA RREKQQRWTR 1800
REQTDFYRVV STFGVEYDPD TMQFHWDRFR TFARLDKKTD ESLTKYFHGF VAMCRQVCRL 1860
PPAAGDEPPD PNLFIEPITE ERASRTLYRI ELLRRLREQV LCHPLLEDRL ALCQPPGPEL 1920
PKWWEPVRHD GELLRGAARH GVSQTDCNIM QDPDFSFLAA RMNYMQNHQA GAPAPSLSRC 1980
STPLLHQQYT SRTASPLPLR PDAPVEKSPE ETATQVPSLE SLTLKLEHEV VARSRPTPQD 2040
YEMRVSPSDT TPLVSRSVPP VKLEDEDDSD SELDLSKLSP SSSSSSSSSS SSSSTDESED 2100
EKEEKLTDQS RSKLYDEESL LSLTMSQDGF PNEDGEQMTP ELLLLQERQR ASEWPKDRVL 2160
INRIDLVCQA VLSGKWPSSR RSQEMVTGGI LGPGNHLLDS PSLTPGEYGD SPVPTPRSSS 2220
AASMAEEEAS AVSTAAAQFT KLRRGMDEKE FTVQIKDEEG LKLTFQKHKL MANGVMGDGH 2280
PLFHKKKGNR KKLVELEVEC MEEPNHLDVD LETRIPVINK VDGTLLVGED APRRAELEMW 2340
LQGHPEFAVD PRFLAYMEDR RKQKWQRCKK NNKAELNCLG MEPVQTANSR NGKKGHHTET 2400
VFNRVLPGPI APESSKKRAR RMRPDLSKMM ALMQGGSTGS LSLHNTFQHS SSGLQSVSSL 2460
GHSSATSASL PFMPFVMGGA PSSPHVDSST MLHHHHHHPH PHHHHHHHPG LRAPGYPSSP 2520
VTTASGTTLR LPPLQPEEDD DEDEEDDDDL SQGYDSSERD FSLIDDPMMP ANSDSSEDAD 2580
D 2581 
Gene Ontology
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0008013; F:beta-catenin binding; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IMP:UniProtKB.
 GO:0003678; F:DNA helicase activity; IMP:UniProtKB.
 GO:0008094; F:DNA-dependent ATPase activity; IDA:UniProtKB.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0002039; F:p53 binding; ISS:UniProtKB.
 GO:0043044; P:ATP-dependent chromatin remodeling; IMP:UniProtKB.
 GO:0060070; P:canonical Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0001701; P:in utero embryonic development; IEA:Compara.
 GO:0043066; P:negative regulation of apoptotic process; IEA:Compara.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IMP:UniProtKB.
 GO:0030178; P:negative regulation of Wnt receptor signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
 GO:0045945; P:positive regulation of transcription from RNA polymerase III promoter; IMP:UniProtKB.
 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
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS