CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001455
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ATP-dependent DNA helicase Q4 
Protein Synonyms/Alias
 DNA helicase, RecQ-like type 4; RecQ4; RTS; RecQ protein-like 4 
Gene Name
 RECQL4 
Gene Synonyms/Alias
 RECQ4 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
332SSQARAGKAEGTAPLubiquitination[1]
376LRSRLLRKQAWKQKWacetylation[2]
380LLRKQAWKQKWRKKGacetylation[2]
382RKQAWKQKWRKKGECacetylation[2]
385AWKQKWRKKGECFGGacetylation[2]
385AWKQKWRKKGECFGGubiquitination[1]
386WKQKWRKKGECFGGGacetylation[2]
386WKQKWRKKGECFGGGubiquitination[1]
568QRESVLQKIRAAQVHubiquitination[1]
695LLTLLQGKRFQNLDSubiquitination[1, 3]
738GSGGRAPKTTAEAYHubiquitination[1]
843STDFLAVKRLVQRVFubiquitination[1, 3, 4]
1048GDLTAEEKDQICDFLubiquitination[1]
1101EERSTRLKDLLGRYFubiquitination[1, 3, 4]
1154LSLRPEEKFSSRAVAubiquitination[3]
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] p300-mediated acetylation of the Rothmund-Thomson-syndrome gene product RECQL4 regulates its subcellular localization.
 Dietschy T, Shevelev I, Pena-Diaz J, Hühn D, Kuenzle S, Mak R, Miah MF, Hess D, Fey M, Hottiger MO, Janscak P, Stagljar I.
 J Cell Sci. 2009 Apr 15;122(Pt 8):1258-67. [PMID: 19299466]
 [3] 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]
 [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] 
Functional Description
 DNA-dependent ATPase. May modulate chromosome segregation. 
Sequence Annotation
 DOMAIN 489 662 Helicase ATP-binding.
 DOMAIN 683 850 Helicase C-terminal.
 NP_BIND 502 509 ATP (Potential).
 MOTIF 605 608 DEAH box.  
Keyword
 3D-structure; ATP-binding; Cataract; Complete proteome; Craniosynostosis; Cytoplasm; Disease mutation; Dwarfism; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1208 AA 
Protein Sequence
MERLRDVRER LQAWERAFRR QRGRRPSQDD VEAAPEETRA LYREYRTLKR TTGQAGGGLR 60
SSESLPAAAE EAPEPRCWGP HLNRAATKSP QPTPGRSRQG SVPDYGQRLK ANLKGTLQAG 120
PALGRRPWPL GRASSKASTP KPPGTGPVPS FAEKVSDEPP QLPEPQPRPG RLQHLQASLS 180
QRLGSLDPGW LQRCHSEVPD FLGAPKACRP DLGSEESQLL IPGESAVLGP GAGSQGPEAS 240
AFQEVSIRVG SPQPSSSGGE KRRWNEEPWE SPAQVQQESS QAGPPSEGAG AVAVEEDPPG 300
EPVQAQPPQP CSSPSNPRYH GLSPSSQARA GKAEGTAPLH IFPRLARHDR GNYVRLNMKQ 360
KHYVRGRALR SRLLRKQAWK QKWRKKGECF GGGGATVTTK ESCFLNEQFD HWAAQCPRPA 420
SEEDTDAVGP EPLVPSPQPV PEVPSLDPTV LPLYSLGPSG QLAETPAEVF QALEQLGHQA 480
FRPGQERAVM RILSGISTLL VLPTGAGKSL CYQLPALLYS RRSPCLTLVV SPLLSLMDDQ 540
VSGLPPCLKA ACIHSGMTRK QRESVLQKIR AAQVHVLMLT PEALVGAGGL PPAAQLPPVA 600
FACIDEAHCL SQWSHNFRPC YLRVCKVLRE RMGVHCFLGL TATATRRTAS DVAQHLAVAE 660
EPDLHGPAPV PTNLHLSVSM DRDTDQALLT LLQGKRFQNL DSIIIYCNRR EDTERIAALL 720
RTCLHAAWVP GSGGRAPKTT AEAYHAGMCS RERRRVQRAF MQGQLRVVVA TVAFGMGLDR 780
PDVRAVLHLG LPPSFESYVQ AVGRAGRDGQ PAHCHLFLQP QGEDLRELRR HVHADSTDFL 840
AVKRLVQRVF PACTCTCTRP PSEQEGAVGG ERPVPKYPPQ EAEQLSHQAA PGPRRVCMGH 900
ERALPIQLTV QALDMPEEAI ETLLCYLELH PHHWLELLAT TYTHCRLNCP GGPAQLQALA 960
HRCPPLAVCL AQQLPEDPGQ GSSSVEFDMV KLVDSMGWEL ASVRRALCQL QWDHEPRTGV 1020
RRGTGVLVEF SELAFHLRSP GDLTAEEKDQ ICDFLYGRVQ ARERQALARL RRTFQAFHSV 1080
AFPSCGPCLE QQDEERSTRL KDLLGRYFEE EEGQEPGGME DAQGPEPGQA RLQDWEDQVR 1140
CDIRQFLSLR PEEKFSSRAV ARIFHGIGSP CYPAQVYGQD RRFWRKYLHL SFHALVGLAT 1200
EELLQVAR 1208 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IDA:UniProtKB.
 GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IMP:UniProtKB.
 GO:0000405; F:bubble DNA binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; IDA:UniProtKB.
 GO:0000733; P:DNA strand renaturation; IDA:UniProtKB.
 GO:0007275; P:multicellular organismal development; TAS:ProtInc. 
Interpro
 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR004589; DNA_helicase_ATP-dep_RecQ.
 IPR021110; DNA_rep_checkpnt_protein.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR001878; Znf_CCHC. 
Pfam
 PF00270; DEAD
 PF11719; Drc1-Sld2
 PF00271; Helicase_C 
SMART
 SM00487; DEXDc
 SM00490; HELICc
 SM00343; ZnF_C2HC 
PROSITE
 PS00690; DEAH_ATP_HELICASE
 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 
PRINTS