CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016277
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Chromodomain-helicase-DNA-binding protein 1-like 
Protein Synonyms/Alias
 Amplified in liver cancer protein 1 
Gene Name
 CHD1L 
Gene Synonyms/Alias
 ALC1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
130CVTYAGDKEERACLQubiquitination[1, 2]
141ACLQQDLKQESRFHVubiquitination[3]
291ALQKKYYKAILMKDLubiquitination[1]
296YYKAILMKDLDAFENubiquitination[1]
308FENETAKKVKLQNILubiquitination[1]
590EPSKEDRKSFEQLVNubiquitination[1]
600EQLVNLQKTLLEKASubiquitination[1]
605LQKTLLEKASQEGRSubiquitination[1, 4]
630GLVEGSTKRKRVLSPubiquitination[1]
793DDKESRNKGQDLLALubiquitination[1, 5]
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] 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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] 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]
 [5] 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] 
Functional Description
 DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding. 
Sequence Annotation
 DOMAIN 58 223 Helicase ATP-binding.
 DOMAIN 351 513 Helicase C-terminal.
 DOMAIN 704 897 Macro.
 NP_BIND 71 78 ATP (By similarity).
 MOTIF 174 177 DEAH box.
 MOD_RES 636 636 Phosphoserine.
 MOD_RES 891 891 Phosphoserine.  
Keyword
 Alternative splicing; ATP-binding; Coiled coil; Complete proteome; DNA damage; DNA repair; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 897 AA 
Protein Sequence
MERAGATSRG GQAPGFLLRL HTEGRAEAAR VQEQDLRQWG LTGIHLRSYQ LEGVNWLAQR 60
FHCQNGCILG DEMGLGKTCQ TIALFIYLAG RLNDEGPFLI LCPLSVLSNW KEEMQRFAPG 120
LSCVTYAGDK EERACLQQDL KQESRFHVLL TTYEICLKDA SFLKSFPWSV LVVDEAHRLK 180
NQSSLLHKTL SEFSVVFSLL LTGTPIQNSL QELYSLLSFV EPDLFSKEEV GDFIQRYQDI 240
EKESESASEL HKLLQPFLLR RVKAEVATEL PKKTEVVIYH GMSALQKKYY KAILMKDLDA 300
FENETAKKVK LQNILSQLRK CVDHPYLFDG VEPEPFEVGD HLTEASGKLH LLDKLLAFLY 360
SGGHRVLLFS QMTQMLDILQ DYMDYRGYSY ERVDGSVRGE ERHLAIKNFG QQPIFVFLLS 420
TRAGGVGMNL TAADTVIFVD SDFNPQNDLQ AAARAHRIGQ NKSVKVIRLI GRDTVEEIVY 480
RKAASKLQLT NMIIEGGHFT LGAQKPAADA DLQLSEILKF GLDKLLASEG STMDEIDLES 540
ILGETKDGQW VSDALPAAEG GSRDQEEGKN HMYLFEGKDY SKEPSKEDRK SFEQLVNLQK 600
TLLEKASQEG RSLRNKGSVL IPGLVEGSTK RKRVLSPEEL EDRQKKRQEA AAKRRRLIEE 660
KKRQKEEAEH KKKMAWWESN NYQSFCLPSE ESEPEDLENG EESSAELDYQ DPDATSLKYV 720
SGDVTHPQAG AEDALIVHCV DDSGHWGRGG LFTALEKRSA EPRKIYELAG KMKDLSLGGV 780
LLFPVDDKES RNKGQDLLAL IVAQHRDRSN VLSGIKMAAL EEGLKKIFLA AKKKKASVHL 840
PRIGHATKGF NWYGTERLIR KHLAARGIPT YIYYFPRSKS AVLHAQSSSS SSRQLVP 897 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004003; F:ATP-dependent DNA helicase activity; TAS:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IDA:UniProtKB.
 GO:0006338; P:chromatin remodeling; IDA:UniProtKB.
 GO:0006281; P:DNA repair; TAS:UniProtKB. 
Interpro
 IPR002589; A1pp.
 IPR002464; DNA/RNA_helicase_DEAH_CS.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR000330; SNF2_N. 
Pfam
 PF00271; Helicase_C
 PF00176; SNF2_N 
SMART
 SM00487; DEXDc
 SM00490; HELICc 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER
 PS51154; MACRO 
PRINTS