CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038653
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Chromodomain-helicase-DNA-binding protein 4 
Protein Synonyms/Alias
  
Gene Name
 Chd4 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
383CLDPDMEKAPEGKWSacetylation[1]
484ALKGKVQKILIWKWGacetylation[1]
614ILNHSVDKKGHVHYLacetylation[2]
676LKKVKLRKLERPPETacetylation[2]
1031ALIRASGKLLLLQKMacetylation[1]
1037GKLLLLQKMLKNLKEacetylation[1]
1037GKLLLLQKMLKNLKEubiquitination[3]
1072FLEHEGYKYERIDGGubiquitination[3]
1376RKGLRNDKDKPLPPLacetylation[2]
1552KIEENSLKEEESTEGubiquitination[3]
1845AVLHKVLKQLEELLSacetylation[1]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [3] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Nucleus; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1902 AA 
Protein Sequence
MASGLGSPSP CSAGSEEEDM DALLNNSLPP PHPENEEDPD EDLSEAETPK LKKKKKPKKP 60
RDPKIPKSKR QKKELGDSSG EGPEFVEEEE EVALRSDSEG SDYTPGKKKK KKLGPKKEKK 120
SKSKRKEEEE EEDEDDDSKE PKSSAQLLED WGMEDIDHVF SEEDYRTLTN YKAFSQFVRP 180
LIAAKNPKIA VSKMMMVLGA KWREFSTNNP FKGSSGASVA AAAAAAVAVV ESMVTATEVA 240
PPPPPVEVPI RKAKTKEGKG PNARRKPKGS PRVPDAKKPK PKKVAPLKIK LGGFGSKRKR 300
SSSEDDDLDV ESDFDDASIN SYSVSDGSTS RSSRSRKKLR TAKKKKKDHQ DYCEVCQQGG 360
EIILCDTCPR AYHMVCLDPD MEKAPEGKWS CPHCEKEGIQ WEAKEDNSEG EEILEEVGGD 420
PEEEDDHHME FCRVCKDGGE LLCCDTCPSS YHIHCLNPPL PEIPNGEWLC PRCTCPALKG 480
KVQKILIWKW GQPPSPTPVP RPPDADPNTP SPKPLEGRPE RQFFVKWQGM SYWHCSWVSE 540
LQLELHCQVM FRNYQRKNDM DEPPSGDFGG DEEKSRKRKN KDPKFAEMEE RFYRYGIKPE 600
WMMIHRILNH SVDKKGHVHY LIKWRDLPYD QASWESEDVE IQDYDLFKQS YWNHRELMRG 660
EEGRPGKKLK KVKLRKLERP PETPTVDPTV KYERQPEYLD ATGGTLHPYQ MEGLNWLRFS 720
WAQGTDTILA DEMGLGKTVQ TAVFLYSLYK EGHSKGPFLV SAPLSTIINW EREFEMWAPD 780
MYVVTYVGDK DSRAIIRENE FSFEDNAIRG GKKASRMKKE ASVKFHVLLT SYELITIDMA 840
ILGSIDWACL IVDEAHRLKN NQSKFFRVLN GYSLQHKLLL TGTPLQNNLE ELFHLLNFLT 900
PERFHNLEGF LEEFADIAKE DQIKKLHDML GPHMLRRLKA DVFKNMPSKT ELIVRVELSP 960
MQKKYYKYIL TRNFEALNAR GGGNQVSLLN VVMDLKKCCN HPYLFPVAAM EAPKMPNGMY 1020
DGSALIRASG KLLLLQKMLK NLKEGGHRVL IFSQMTKMLD LLEDFLEHEG YKYERIDGGI 1080
TGNMRQEAID RFNAPGAQQF CFLLSTRAGG LGINLATADT VIIYDSDWNP HNDIQAFSRA 1140
HRIGQNKKVM IYRFVTRASV EERITQVAKK KMMLTHLVVR PGLGSKTGSM SKQELDDILK 1200
FGTEELFKDE ATDGGGDNKE GEDSSVIHYD DKAIERLLDR NQDETEDTEL QGMNEYLSSF 1260
KVAQYVVREE EMGEEEEVER EIIKQEESVD PDYWEKLLRH HYEQQQEDLA RNLGKGKRIR 1320
KQVNYNDGSQ EDRDWQDDQS DNQSDYSVAS EEGDEDFDER SEAPRRPSRK GLRNDKDKPL 1380
PPLLARVGGN IEVLGFNARQ RKAFLNAIMR YGMPPQDAFT TQWLVRDLRG KSEKEFKAYV 1440
SLFMRHLCEP GADGAETFAD GVPREGLSRQ HVLTRIGVMS LIRKKVQEFE HVNGRWSMPE 1500
LAEVEENKKM SQPGSPSPKT PTPSTPGDTQ PNTPAPVPPA EDGIKIEENS LKEEESTEGE 1560
KEVKSTAPEA TVECAQPPAP APATAPATAT APEDDKAPAE PPEGEEKVEK AEVKERTEEP 1620
METEAKGTTE VEKVEEKSAV DLTPIVVEDK EEKKEEEEKK DVMLQNGETP KDLSDEKQKK 1680
NSKQRFMFNI ADGGFTELHS LWQNEERAAT VTKKTYEIWH RRHDYWLLAG IINHGYARWQ 1740
DIQNDPRYAI LNEPFKGEMN RGNFLEIKNK FLARRFKLLE QALVIEEQLR RAAYLNMSED 1800
PSHPSMALNT RFAEVECLAE SHQHLSKESM AGNKPANAVL HKVLKQLEEL LSDMKADVTR 1860
LPATIARIPP VAVRLQMSER NILSRLANRA PEPPPQQVAQ QQ 1902 
Gene Ontology
 GO:0016581; C:NuRD complex; IDA:MGI.
 GO:0005524; F:ATP binding; IEA:InterPro.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR012957; CHD_C2.
 IPR012958; CHD_N.
 IPR023780; Chromo_domain.
 IPR000953; Chromo_domain/shadow.
 IPR016197; Chromodomain-like.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR009462; DUF1086.
 IPR009463; DUF1087.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF08074; CHDCT2
 PF08073; CHDNT
 PF00385; Chromo
 PF06461; DUF1086
 PF06465; DUF1087
 PF00271; Helicase_C
 PF00628; PHD
 PF00176; SNF2_N 
SMART
 SM00298; CHROMO
 SM00487; DEXDc
 SM00490; HELICc
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS50013; CHROMO_2
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS