ATP-dependent DNA helicase Q1 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    ATP-dependent DNA helicase Q1
    EC=3.6.1.-
Alternative name(s):
    DNA-dependent ATPase Q1

Gene names

Name:	RECQL
Synonyms:	RECQL1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	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.
Subunit structure	Interacts with EXO1 and MLH1.
Subcellular location	Nucleus.
Tissue specificity	High expression in heart, lung, skeletal muscle and kidney, low expression in brain.
Sequence similarities	Belongs to the helicase family. RecQ subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence AAA60261.1 differs from that shown. Reason: Frameshift at positions 615 and 649.

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Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Ref.1 Traceable author statement. Source: ProtInc
Cellular component	nucleus Ref.1 Traceable author statement. Source: ProtInc
Molecular function	ATP binding Inferred from electronic annotation. Source: InterPro ATP-dependent DNA helicase activity Ref.1 Traceable author statement. Source: ProtInc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Ref.6 Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 649

649

ATP-dependent DNA helicase Q1

PRO_0000205049

Regions

Domain

100 – 275

176

Helicase ATP-binding

Domain

300 – 451

152

Helicase C-terminal

Nucleotide binding

113 – 120

8

ATP Probable

Motif

219 – 222

4

DEVH box

Natural variations

Natural variant

102

1

V → I: dbSNP rs1065751.

VAR_034679

Natural variant

487

1

K → T: dbSNP rs6501.

VAR_016140

Natural variant

495

1

D → H: dbSNP rs6499 and dbSNP rs4987215.

VAR_016141

Experimental info

Mutagenesis

119

1

K → A: Abrogates helicase activity

Sequence conflict

1

M → S in BAA07200. Ref.2

Sequence conflict

175

1

A → D in AAA60261. Ref.1

Sequence conflict

453

1

C → S in AAA60261. Ref.1

Sequence conflict

566

1

T → A in AAA60261. Ref.1

Sequence conflict

617

1

K → E in BAA07200. Ref.2

Secondary structure

1

.

649

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P46063-1 [UniParc].

Last modified March 28, 2003. Version 2.
Checksum: FEB4561191F79391
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FASTA

649

73,456

        10         20         30         40         50         60 
MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL EDSDAGASNE 

        70         80         90        100        110        120 
YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI NVTMAGKEVF LVMPTGGGKS 

       130        140        150        160        170        180 
LCYQLPALCS DGFTLVICPL ISLMEDQLMV LKQLGISATM LNASSSKEHV KWVHAEMVNK 

       190        200        210        220        230        240 
NSELKLIYVT PEKIAKSKMF MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI 

       250        260        270        280        290        300 
LKRQFPNASL IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF 

       310        320        330        340        350        360 
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP EDKTTVHRKW 

       370        380        390        400        410        420 
SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ ESGRAGRDDM KADCILYYGF 

       430        440        450        460        470        480 
GDIFRISSMV VMENVGQQKL YEMVSYCQNI SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK 

       490        500        510        520        530        540 
DSAFERKNIT EYCRDLIKIL KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE 

       550        560        570        580        590        600 
DLEKIIAHFL IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA 

       610        620        630        640 
ESSQTCHSEQ GDKKMEKKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and characterization of RECQL, a potential human homologue of the Escherichia coli DNA helicase RecQ." Puranam K.L., Blackshear P.J. J. Biol. Chem. 269:29838-29845(1994) [PubMed: 7961977] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 34-38; 186-193; 293-304; 396-404; 431-439 AND 594-599, FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT THR-487. Tissue: Cervix carcinoma.
[2]	"Molecular cloning of cDNA encoding human DNA helicase Q1 which has homology to Escherichia coli Rec Q helicase and localization of the gene at chromosome 12p12." Seki M., Miyazawa H., Tada S., Yanagisawa J., Yamaoka T., Hoshino S., Ozawa K., Eki T., Nogami M., Okumura K., Taguchi H., Hanaoka F., Enomoto T. Nucleic Acids Res. 22:4566-4573(1994) [PubMed: 7527136] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[5]	"Purification of two DNA-dependent adenosinetriphosphatases having DNA helicase activity from HeLa cells and comparison of the properties of the two enzymes." Seki M., Yanagisawa J., Kohda T., Sonoyama T., Ui M., Enomoto T. J. Biochem. 115:523-531(1994) [PubMed: 8056767] [Abstract] Cited for: FUNCTION.
[6]	"RECQ1 helicase interacts with human mismatch repair factors that regulate genetic recombination." Doherty K.M., Sharma S., Uzdilla L.A., Wilson T.M., Cui S., Vindigni A., Brosh R.M. Jr. J. Biol. Chem. 280:28085-28094(2005) [PubMed: 15886194] [Abstract] Cited for: FUNCTION, INTERACTION WITH EXO1 AND MLH1, MUTAGENESIS OF LYS-119.
+	Additional computationally mapped references.

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Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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Cross-references

Sequence databases

L36140 mRNA. Translation: AAA60261.1. Frameshift.
D37984 mRNA. Translation: BAA07200.1.
BT007119 mRNA. Translation: AAP35783.1.
BC001052 mRNA. Translation: AAH01052.1.

PIR

A55311. A58836.

RefSeq

NP_002898.2.
NP_116559.1.

UniGene

Hs.235069