UniProt Accession

 RECQ1_HUMAN; P46063; A8K6G2 

Genbank Protein ID

 L36140; D37984; BT007119; AK291627; AC006559; CH471094; BC001052 

Genbank Nucleotide ID

 AAA60261.1; BAA07200.1; AAP35783.1; BAF84316.1; EAW96434.1; AAH01052.1 

Protein Name

 ATP-dependent DNA helicase Q1 

Protein Synonyms/Alias

 DNA helicase, RecQ-like type 1; RecQ1; DNA-dependent ATPase Q1; RecQ protein-like 1 

Gene Name

 RECQL 

Gene Synonyms/Alias

 RECQ1; RECQL1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
38	RQQELIQKKKVLTKK	ubiquitination	[1, 2, 3, 4, 5, 6]
39	QQELIQKKKVLTKKI	ubiquitination	[5]
47	KVLTKKIKQCLEDSD	ubiquitination	[1, 4, 5, 6]
91	QNVFKLEKFRPLQLE	ubiquitination	[1, 4, 6]
180	VHAEMVNKNSELKLI	ubiquitination	[4]
193	LIYVTPEKIAKSKMF	acetylation	[7]
198	PEKIAKSKMFMSRLE	ubiquitination	[5]
206	MFMSRLEKAYEARRF	acetylation	[7]
452	SYCQNISKCRRVLMA	ubiquitination	[4]
480	KMCDNCCKDSAFERK	ubiquitination	[8]
487	KDSAFERKNITEYCR	methylation	[9]
487	KDSAFERKNITEYCR	ubiquitination	[5]
501	RDLIKILKQAEELNE	ubiquitination	[5]
509	QAEELNEKLTPLKLI	acetylation	[10]
514	NEKLTPLKLIDSWMG	acetylation	[7, 11]
522	LIDSWMGKGAAKLRV	acetylation	[7, 11]
522	LIDSWMGKGAAKLRV	ubiquitination	[5]

Reference

 [1] 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]
 [2] 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]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [4] 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]
 [5] 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]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [7] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [8] 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]
 [9] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510]
 [10] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [11] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773] 

Functional Description

 DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Exhibits a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction. 

Sequence Annotation

 DOMAIN 100 275 Helicase ATP-binding.
 DOMAIN 300 451 Helicase C-terminal.
 NP_BIND 113 120 ATP (Probable).
 MOTIF 219 222 DEVH box.
 MOD_RES 514 514 N6-acetyllysine.
 MOD_RES 522 522 N6-acetyllysine.
 MOD_RES 634 634 Phosphoserine.  

Keyword

 3D-structure; Acetylation; ATP-binding; Complete proteome; Direct protein sequencing; DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 649 AA 

Protein Sequence

Gene Ontology

 GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IEA:InterPro.
 GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0006310; P:DNA recombination; IEA:InterPro.
 GO:0006281; P:DNA repair; TAS:ProtInc.
 GO:0006260; P:DNA replication; IEA:InterPro.
 GO:0000733; P:DNA strand renaturation; IDA:UniProtKB. 

Interpro

 IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
 IPR004589; DNA_helicase_ATP-dep_RecQ.
 IPR014001; Helicase_ATP-bd.
 IPR001650; Helicase_C.
 IPR027417; P-loop_NTPase.
 IPR018982; RQC_domain.
 IPR011991; WHTH_DNA-bd_dom. 

Pfam

 PF00270; DEAD
 PF00271; Helicase_C
 PF09382; RQC 

SMART

 SM00487; DEXDc
 SM00490; HELICc 

PROSITE

 PS51192; HELICASE_ATP_BIND_1
 PS51194; HELICASE_CTER 

PRINTS