CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018030
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein 5 
Protein Synonyms/Alias
 CHD-5; ATP-dependent helicase CHD5 
Gene Name
 CHD5 
Gene Synonyms/Alias
 KIAA0444 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
284RFGGISNKRKKGSSSubiquitination[1]
588RFYRYGIKPEWMMIHubiquitination[1]
933PHMLRRLKADVFKNMubiquitination[1]
1406QLKSDRDKPLPPLLAubiquitination[2]
1430GFNARQRKAFLNAIMubiquitination[1, 2]
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] 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] 
Functional Description
 May play a role in the development of the nervous system and the pathogenesis of neural tumors. 
Sequence Annotation
 DOMAIN 497 554 Chromo 1.
 DOMAIN 592 653 Chromo 2.
 DOMAIN 712 896 Helicase ATP-binding.
 DOMAIN 1028 1193 Helicase C-terminal.
 ZN_FING 343 390 PHD-type 1.
 ZN_FING 416 463 PHD-type 2.
 NP_BIND 725 732 ATP (Potential).
 MOTIF 847 850 DEAH box.  
Keyword
 ATP-binding; Chromatin regulator; Complete proteome; DNA-binding; Helicase; Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1954 AA 
Protein Sequence
MRGPVGTEEE LPRLFAEEME NEDEMSEEED GGLEAFDDFF PVEPVSLPKK KKPKKLKENK 60
CKGKRKKKEG SNDELSENEE DLEEKSESEG SDYSPNKKKK KKLKDKKEKK AKRKKKDEDE 120
DDNDDGCLKE PKSSGQLMAE WGLDDVDYLF SEEDYHTLTN YKAFSQFLRP LIAKKNPKIP 180
MSKMMTVLGA KWREFSANNP FKGSSAAAAA AAVAAAVETV TISPPLAVSP PQVPQPVPIR 240
KAKTKEGKGP GVRKKIKGSK DGKKKGKGKK TAGLKFRFGG ISNKRKKGSS SEEDEREESD 300
FDSASIHSAS VRSECSAALG KKSKRRRKKK RIDDGDGYET DHQDYCEVCQ QGGEIILCDT 360
CPRAYHLVCL DPELEKAPEG KWSCPHCEKE GIQWEPKDDD DEEEEGGCEE EEDDHMEFCR 420
VCKDGGELLC CDACPSSYHL HCLNPPLPEI PNGEWLCPRC TCPPLKGKVQ RILHWRWTEP 480
PAPFMVGLPG PDVEPSLPPP KPLEGIPERE FFVKWAGLSY WHCSWVKELQ LELYHTVMYR 540
NYQRKNDMDE PPPFDYGSGD EDGKSEKRKN KDPLYAKMEE RFYRYGIKPE WMMIHRILNH 600
SFDKKGDVHY LIKWKDLPYD QCTWEIDDID IPYYDNLKQA YWGHRELMLG EDTRLPKRLL 660
KKGKKLRDDK QEKPPDTPIV DPTVKFDKQP WYIDSTGGTL HPYQLEGLNW LRFSWAQGTD 720
TILADEMGLG KTVQTIVFLY SLYKEGHSKG PYLVSAPLST IINWEREFEM WAPDFYVVTY 780
TGDKESRSVI RENEFSFEDN AIRSGKKVFR MKKEVQIKFH VLLTSYELIT IDQAILGSIE 840
WACLVVDEAH RLKNNQSKFF RVLNSYKIDY KLLLTGTPLQ NNLEELFHLL NFLTPERFNN 900
LEGFLEEFAD ISKEDQIKKL HDLLGPHMLR RLKADVFKNM PAKTELIVRV ELSQMQKKYY 960
KFILTRNFEA LNSKGGGNQV SLLNIMMDLK KCCNHPYLFP VAAVEAPVLP NGSYDGSSLV 1020
KSSGKLMLLQ KMLKKLRDEG HRVLIFSQMT KMLDLLEDFL EYEGYKYERI DGGITGGLRQ 1080
EAIDRFNAPG AQQFCFLLST RAGGLGINLA TADTVIIYDS DWNPHNDIQA FSRAHRIGQN 1140
KKVMIYRFVT RASVEERITQ VAKRKMMLTH LVVRPGLGSK SGSMTKQELD DILKFGTEEL 1200
FKDDVEGMMS QGQRPVTPIP DVQSSKGGNL AASAKKKHGS TPPGDNKDVE DSSVIHYDDA 1260
AISKLLDRNQ DATDDTELQN MNEYLSSFKV AQYVVREEDG VEEVEREIIK QEENVDPDYW 1320
EKLLRHHYEQ QQEDLARNLG KGKRIRKQVN YNDASQEDQE WQDELSDNQS EYSIGSEDED 1380
EDFEERPEGQ SGRRQSRRQL KSDRDKPLPP LLARVGGNIE VLGFNARQRK AFLNAIMRWG 1440
MPPQDAFNSH WLVRDLRGKS EKEFRAYVSL FMRHLCEPGA DGAETFADGV PREGLSRQHV 1500
LTRIGVMSLV RKKVQEFEHV NGKYSTPDLI PEGPEGKKSG EVISSDPNTP VPASPAHLLP 1560
APLGLPDKME AQLGYMDEKD PGAQKPRQPL EVQALPAALD RVESEDKHES PASKERAREE 1620
RPEETEKAPP SPEQLPREEV LPEKEKILDK LELSLIHSRG DSSELRPDDT KAEEKEPIET 1680
QQNGDKEEDD EGKKEDKKGK FKFMFNIADG GFTELHTLWQ NEERAAVSSG KIYDIWHRRH 1740
DYWLLAGIVT HGYARWQDIQ NDPRYMILNE PFKSEVHKGN YLEMKNKFLA RRFKLLEQAL 1800
VIEEQLRRAA YLNMTQDPNH PAMALNARLA EVECLAESHQ HLSKESLAGN KPANAVLHKV 1860
LNQLEELLSD MKADVTRLPS MLSRIPPVAA RLQMSERSIL SRLTNRAGDP TIQQGAFGSS 1920
QMYSNNFGPN FRGPGPGGIV NYNQMPLGPY VTDI 1954 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
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
 PS00598; CHROMO_1
 PS50013; CHROMO_2
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS