CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-024559
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Putative ATP-dependent RNA helicase DDX11-like protein 8 
Protein Synonyms/Alias
 DEAD/H box protein 11-like 8 
Gene Name
 DDX11L8 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
38YRVLEAGKIGIFESPubiquitination[1, 2, 3, 4]
154LQHRVQLKYAAKRLRubiquitination[3, 4]
250QFVHEVKKSPFGKDVubiquitination[3]
255VKKSPFGKDVRLVSLubiquitination[3]
313PKRRRQEKQAACPFYubiquitination[3]
337DEALAEVKDMEQLLAubiquitination[1, 2, 3, 4]
347EQLLALGKEARACPYubiquitination[1, 2, 3, 4, 5]
462AVLGGNIKQNPNTQSubiquitination[1]
496IDNINLFKVQRYCEKubiquitination[2]
503KVQRYCEKSMISRKLubiquitination[3, 4]
509EKSMISRKLFGFTERubiquitination[3, 4, 6]
528FSSREQPKLAGFQQFubiquitination[1, 4, 6, 7]
613VHFAQVVKECRAVVIubiquitination[3, 4]
723QVHAHWEKGGLLGRLubiquitination[3]
734LGRLAARKKIFQEPKubiquitination[3]
741KKIFQEPKSAHQVEQubiquitination[3]
812RSAELQEKMAYLDQTubiquitination[1, 2, 3, 4, 5, 6, 8]
831PGQAPPGKALVENLCubiquitination[3, 4, 6]
840LVENLCMKAVNQSIGubiquitination[2, 3, 4, 8]
854GRAIRHQKDFASIVLubiquitination[3]
874ARPPVLAKLPAWIRAubiquitination[2, 3]
898PAIAAVQKFHREKSAubiquitination[3]
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] 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]
 [3] 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]
 [4] 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]
 [5] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [6] 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]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572] 
Functional Description
 Putative DNA helicase (By similarity). 
Sequence Annotation
 DOMAIN 9 447 Helicase ATP-binding.
 NP_BIND 44 51 ATP (By similarity).
 MOTIF 395 398 DEAH.  
Keyword
 ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome; RNA-binding. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 907 AA 
Protein Sequence
MANETQKVGA IHFPFPFTPY SIQEDFMAEL YRVLEAGKIG IFESPTGTGK SLSLICGALS 60
WLRDFEQKKR EEEARLLETG TGPLHDEKDE SLCLSSSCEG AAGTPRPAGE PAWVTQFVQK 120
KEERDLVDRL KVEQARRKQR EERLQQLQHR VQLKYAAKRL RQEEEETENL LRLSREMLET 180
GPEAERLEQL ESGEEELVLA EYESDEEKKV ASGHRVDEDE DDLEEEHITK IYHCSRTHSQ 240
LAQFVHEVKK SPFGKDVRLV SLGSRQNLCV NEDVRSLGSV QLINDRCVDM QRSRHEKKKG 300
AEEEKPKRRR QEKQAACPFY NHEQMGLLRD EALAEVKDME QLLALGKEAR ACPYYRSRLA 360
IPAAKLVVLP YQMLLHAATR QAAGIRLQDQ VVIIDEAHNL IDTITGMHSV EVSGSQLCQA 420
HSQLLQYMER YGKRLKAKNL MYLKQILYLL EKFVAVLGGN IKQNPNTQSL SQTGTELKTI 480
NDFLFQSQID NINLFKVQRY CEKSMISRKL FGFTERYGAV FSSREQPKLA GFQQFLQSLQ 540
PRTTEALAAP ADESQASVPQ PASPLMHIEG FLAALTTANQ DGRVILSRQG SLSESTLKFL 600
LLNPAVHFAQ VVKECRAVVI AGGTMQPVSD FRQQLLACAG VEAERVVEFS CGHVIPPDNI 660
PLVICSGISN QPLEFTFQKR DLPQMMDEVG RILCNLCGVV SGGVVCFFSS YEYLRQVHAH 720
WEKGGLLGRL AARKKIFQEP KSAHQVEQVL LAYSRCIQAC GQERGQVTEA LLLSVVGGKM 780
SEGINFSDNL GRCVVMVGMP FPNIRSAELQ EKMAYLDQTL PRAPGQAPPG KALVENLCMK 840
AVNQSIGRAI RHQKDFASIV LLDQRYARPP VLAKLPAWIR ASVEVKATFG PAIAAVQKFH 900
REKSASS 907 
Gene Ontology
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003723; F:RNA binding; IEA:UniProtKB-KW. 
Interpro
 IPR006555; ATP-dep_Helicase_C.
 IPR027076; DDX11/CHL1.
 IPR010614; DEAD_2.
 IPR013020; DNA_helicase_DNA-repair_Rad3.
 IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
 IPR006554; Helicase-like_DEXD_c2.
 IPR027417; P-loop_NTPase. 
Pfam
 PF06733; DEAD_2
 PF13307; Helicase_C_2 
SMART
 SM00488; DEXDc2
 SM00491; HELICc2 
PROSITE
 PS51193; HELICASE_ATP_BIND_2 
PRINTS