P46063 (RECQ1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
ATP-dependent DNA helicase Q1
EC=3.6.4.12

Alternative name(s):
DNA helicase, RecQ-like type 1
Short name=RecQ1
DNA-dependent ATPase Q1
RecQ protein-like 1

Gene names

Name:	RECQL
Synonyms:	RECQ1, RECQL1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	649 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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. Ref.1 Ref.8 Ref.9
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with EXO1 and MLH1. Ref.9
Subcellular location	Nucleus Ref.1.
Tissue specificity	High expression in heart, lung, skeletal muscle and kidney, low expression in brain. Ref.1
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: InterPro DNA repair Traceable author statement Ref.1. Source: ProtInc DNA replication Inferred from electronic annotation. Source: InterPro DNA strand renaturation Inferred from direct assay PubMed 19177149. Source: UniProtKB
Cellular_component	microtubule cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent 3'-5' DNA helicase activity Inferred from electronic annotation. Source: InterPro ATP-dependent DNA helicase activity Traceable author statement Ref.1. Source: ProtInc DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

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

Amino acid modifications

Modified residue

514

1

N6-acetyllysine Ref.10

Modified residue

522

1

N6-acetyllysine Ref.10

Modified residue

634

1

Phosphoserine Ref.11

Natural variations

Natural variant

102

1

V → I.
Corresponds to variant rs1065751 [ dbSNP | Ensembl ].

VAR_034679

Natural variant

372

1

V → I.
Corresponds to variant rs2230003 [ dbSNP | Ensembl ].

VAR_051732

Natural variant

487

1

K → T. Ref.1
Corresponds to variant rs6501 [ dbSNP | Ensembl ].

VAR_016140

Natural variant

495

1

D → H.
Corresponds to variant rs6499 [ dbSNP | Ensembl ].

VAR_016141

Experimental info

Mutagenesis

119

1

K → A: Abrogates helicase activity. Ref.9

Sequence conflict

1

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

E → K in AAP35783. Ref.3

Sequence conflict

617

1

E → K in AAH01052. Ref.7

Secondary structure

1

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649

Helix Strand Turn

Details...

Helix

65 – 68

4

Helix

76 – 85

10

Helix

96 – 104

9

Beta strand

109 – 112

4

Helix

121 – 128

8

Beta strand

130 – 137

8

Helix

141 – 154

14

Beta strand

158 – 160

3

Helix

167 – 178

12

Beta strand

186 – 189

4

Helix

191 – 195

5

Helix

198 – 209

12

Beta strand

213 – 219

7

Helix

221 – 224

4

Helix

226 – 228

3

Helix

233 – 239

7

Helix

240 – 244

5

Beta strand

248 – 256

9

Helix

259 – 268

10

Beta strand

275 – 278

4

Beta strand

286 – 292

7

Helix

297 – 308

12

Turn

309 – 314

6

Beta strand

316 – 320

5

Helix

324 – 336

13

Beta strand

341 – 344

4

Helix

350 – 361

12

Beta strand

364 – 370

7

Beta strand

383 – 390

8

Helix

395 – 402

8

Beta strand

412 – 418

7

Helix

420 – 429

10

Turn

430 – 432

3

Helix

436 – 447

12

Beta strand

450 – 452

3

Helix

454 – 462

9

Helix

476 – 479

4

Beta strand

484 – 488

5

Helix

490 – 505

16

Helix

512 – 519

8

Helix

525 – 527

3

Helix

539 – 551

13

Beta strand

554 – 561

8

Beta strand

566 – 572

7

Helix

574 – 580

7

Beta strand

587 – 591

5

Sequences

	Sequence		Length	Mass (Da)
	P46063 [UniParc]. Last modified December 16, 2008. Version 3. Checksum: F616DC3191F79391	FASTA	649	73,457
	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 GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA

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] [Europe PMC] [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] [Europe PMC] [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]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Placenta.
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[8]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION.
[9]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH EXO1 AND MLH1, MUTAGENESIS OF LYS-119.
[10]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-514 AND LYS-522, MASS SPECTROMETRY.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-634, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L36140 mRNA. Translation: AAA60261.1. Frameshift.
D37984 mRNA. Translation: BAA07200.1.
BT007119 mRNA. Translation: AAP35783.1.
AK291627 mRNA. Translation: BAF84316.1.
AC006559 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96434.1.
BC001052 mRNA. Translation: AAH01052.1.

IPI

IPI00178431.

PIR

A55311. A58836.

RefSeq

NP_002898.2. NM_002907.3.
NP_116559.1. NM_032941.2.

UniGene

Hs.235069.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2V1X	X-ray	2.00	A/B	49-616	[»]
2WWY	X-ray	2.90	A/B	49-616	[»]

ProteinModelPortal

P46063.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29216N.

IntAct

P46063. 2 interactions.

STRING

9606.ENSP00000395449.

PTM databases

PhosphoSite

P46063.

Polymorphism databases

DMDM

218512113.

Proteomic databases

PaxDb

P46063.

PRIDE

P46063.

Protocols and materials databases

DNASU

5965.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000421138; ENSP00000395449; ENSG00000004700.
ENST00000444129; ENSP00000416739; ENSG00000004700.

GeneID

5965.

KEGG

hsa:5965.

UCSC

uc001rex.3. human.

Organism-specific databases

CTD

5965.

GeneCards

GC12M021621.

H-InvDB

HIX0010478.

HGNC

HGNC:9948. RECQL.

HPA

CAB009743.
HPA030960.

MIM

600537. gene.

neXtProt

NX_P46063.

PharmGKB

PA34315.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0514.

HOGENOM

HOG000044388.

HOVERGEN

HBG057654.

InParanoid

P46063.

KO

K10899.

OMA

ESSQTCH.

PhylomeDB

P46063.

Gene expression databases

ArrayExpress

P46063.

Bgee

P46063.

CleanEx

HS_RECQL.

Genevestigator

P46063.

GermOnline

ENSG00000004700. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09382. RQC. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00614. recQ_fam. 1 hit.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1293236.

ChiTaRS

RECQL. human.

EvolutionaryTrace

P46063.

GenomeRNAi

5965.

NextBio

23220.

SOURCE

Search...

Entry information

Entry name

RECQ1_HUMAN

Accession

Primary (citable) accession number: P46063
Secondary accession number(s): A8K6G2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	December 16, 2008
Last modified:	May 1, 2013
This is version 137 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.