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Protein

ATP-dependent DNA helicase Q1

Gene

RECQL

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi113 – 120ATPCurated8

GO - Molecular functioni

  • annealing helicase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 3'-5' DNA helicase activity Source: GO_Central
  • ATP-dependent DNA helicase activity Source: ProtInc
  • DNA binding Source: GO_Central
  • DNA helicase activity Source: UniProtKB
  • four-way junction helicase activity Source: GO_Central

GO - Biological processi

  • DNA repair Source: ProtInc
  • DNA strand renaturation Source: UniProtKB
  • double-strand break repair via homologous recombination Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004700-MONOMER.
BRENDAi3.6.4.12. 2681.

Names & Taxonomyi

Protein namesi
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 namesi
Name:RECQL
Synonyms:RECQ1, RECQL1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9948. RECQL.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • chromosome Source: GO_Central
  • cytoplasm Source: GO_Central
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi119K → A: Abrogates helicase activity. 1 Publication1

Organism-specific databases

DisGeNETi5965.
OpenTargetsiENSG00000004700.
PharmGKBiPA34315.

Chemistry databases

ChEMBLiCHEMBL1293236.

Polymorphism and mutation databases

BioMutaiRECQL.
DMDMi218512113.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002050491 – 649ATP-dependent DNA helicase Q1Add BLAST649

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei514N6-acetyllysineCombined sources1
Modified residuei522N6-acetyllysineCombined sources1
Modified residuei597PhosphoserineCombined sources1
Modified residuei602PhosphoserineBy similarity1
Modified residuei634PhosphoserineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP46063.
MaxQBiP46063.
PaxDbiP46063.
PeptideAtlasiP46063.
PRIDEiP46063.
TopDownProteomicsiP46063.

PTM databases

iPTMnetiP46063.
PhosphoSitePlusiP46063.
SwissPalmiP46063.

Expressioni

Tissue specificityi

High expression in heart, lung, skeletal muscle and kidney, low expression in brain.1 Publication

Gene expression databases

BgeeiENSG00000004700.
CleanExiHS_RECQL.
ExpressionAtlasiP46063. baseline and differential.
GenevisibleiP46063. HS.

Organism-specific databases

HPAiCAB009743.
HPA030960.
HPA064259.

Interactioni

Subunit structurei

Interacts with EXO1 and MLH1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KPNA2P522922EBI-2823728,EBI-349938
KPNA4O006292EBI-2823728,EBI-396343

Protein-protein interaction databases

BioGridi111897. 31 interactors.
DIPiDIP-29216N.
IntActiP46063. 17 interactors.
MINTiMINT-3016374.
STRINGi9606.ENSP00000395449.

Chemistry databases

BindingDBiP46063.

Structurei

Secondary structure

1649
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi65 – 68Combined sources4
Helixi76 – 85Combined sources10
Helixi96 – 104Combined sources9
Beta strandi109 – 112Combined sources4
Helixi121 – 128Combined sources8
Beta strandi130 – 137Combined sources8
Helixi141 – 154Combined sources14
Beta strandi158 – 160Combined sources3
Helixi167 – 178Combined sources12
Beta strandi186 – 189Combined sources4
Helixi191 – 195Combined sources5
Helixi198 – 209Combined sources12
Beta strandi213 – 219Combined sources7
Helixi221 – 224Combined sources4
Helixi226 – 228Combined sources3
Helixi233 – 239Combined sources7
Helixi240 – 244Combined sources5
Beta strandi248 – 256Combined sources9
Helixi259 – 268Combined sources10
Beta strandi275 – 278Combined sources4
Beta strandi286 – 292Combined sources7
Helixi297 – 308Combined sources12
Turni309 – 314Combined sources6
Beta strandi316 – 320Combined sources5
Helixi324 – 336Combined sources13
Beta strandi341 – 344Combined sources4
Helixi350 – 361Combined sources12
Beta strandi364 – 370Combined sources7
Beta strandi383 – 390Combined sources8
Helixi395 – 402Combined sources8
Beta strandi412 – 418Combined sources7
Helixi420 – 429Combined sources10
Turni430 – 432Combined sources3
Helixi436 – 447Combined sources12
Beta strandi450 – 452Combined sources3
Helixi454 – 462Combined sources9
Helixi476 – 479Combined sources4
Beta strandi484 – 488Combined sources5
Helixi490 – 505Combined sources16
Helixi512 – 519Combined sources8
Helixi525 – 527Combined sources3
Helixi539 – 551Combined sources13
Beta strandi554 – 561Combined sources8
Beta strandi566 – 572Combined sources7
Helixi574 – 580Combined sources7
Beta strandi587 – 591Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V1XX-ray2.00A/B49-616[»]
2WWYX-ray2.90A/B49-616[»]
4U7DX-ray3.40A/B/C/D49-616[»]
ProteinModelPortaliP46063.
SMRiP46063.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46063.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini100 – 275Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST176
Domaini300 – 451Helicase C-terminalPROSITE-ProRule annotationAdd BLAST152

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi219 – 222DEVH box4

Sequence similaritiesi

Belongs to the helicase family. RecQ subfamily.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000044388.
HOVERGENiHBG057654.
InParanoidiP46063.
KOiK10899.
OMAiESSQTCH.
OrthoDBiEOG091G05Q8.
PhylomeDBiP46063.
TreeFamiTF323555.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46063-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL
60 70 80 90 100
EDSDAGASNE YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI
110 120 130 140 150
NVTMAGKEVF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV
160 170 180 190 200
LKQLGISATM LNASSSKEHV KWVHAEMVNK NSELKLIYVT PEKIAKSKMF
210 220 230 240 250
MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL
260 270 280 290 300
IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF
310 320 330 340 350
IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP
360 370 380 390 400
EDKTTVHRKW SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ
410 420 430 440 450
ESGRAGRDDM KADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNI
460 470 480 490 500
SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK DSAFERKNIT EYCRDLIKIL
510 520 530 540 550
KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE DLEKIIAHFL
560 570 580 590 600
IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA
610 620 630 640
ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA
Length:649
Mass (Da):73,457
Last modified:December 16, 2008 - v3
Checksum:iF616DC3191F79391
GO

Sequence cautioni

The sequence AAA60261 differs from that shown. Reason: Frameshift at positions 615 and 649.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1M → S in BAA07200 (PubMed:7527136).Curated1
Sequence conflicti175A → D in AAA60261 (PubMed:7961977).Curated1
Sequence conflicti453C → S in AAA60261 (PubMed:7961977).Curated1
Sequence conflicti566T → A in AAA60261 (PubMed:7961977).Curated1
Sequence conflicti617E → K in AAP35783 (Ref. 3) Curated1
Sequence conflicti617E → K in AAH01052 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_034679102V → I.Corresponds to variant rs1065751dbSNPEnsembl.1
Natural variantiVAR_051732372V → I.Corresponds to variant rs2230003dbSNPEnsembl.1
Natural variantiVAR_016140487K → T.1 PublicationCorresponds to variant rs6501dbSNPEnsembl.1
Natural variantiVAR_016141495D → H.Corresponds to variant rs6499dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31756.1.
PIRiA58836. A55311.
RefSeqiNP_002898.2. NM_002907.3.
NP_116559.1. NM_032941.2.
XP_005253518.1. XM_005253461.3.
XP_005253519.1. XM_005253462.4.
XP_005253520.1. XM_005253463.3.
XP_005253521.1. XM_005253464.3.
UniGeneiHs.235069.

Genome annotation databases

EnsembliENST00000421138; ENSP00000395449; ENSG00000004700.
ENST00000444129; ENSP00000416739; ENSG00000004700.
GeneIDi5965.
KEGGihsa:5965.
UCSCiuc001rex.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS31756.1.
PIRiA58836. A55311.
RefSeqiNP_002898.2. NM_002907.3.
NP_116559.1. NM_032941.2.
XP_005253518.1. XM_005253461.3.
XP_005253519.1. XM_005253462.4.
XP_005253520.1. XM_005253463.3.
XP_005253521.1. XM_005253464.3.
UniGeneiHs.235069.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2V1XX-ray2.00A/B49-616[»]
2WWYX-ray2.90A/B49-616[»]
4U7DX-ray3.40A/B/C/D49-616[»]
ProteinModelPortaliP46063.
SMRiP46063.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111897. 31 interactors.
DIPiDIP-29216N.
IntActiP46063. 17 interactors.
MINTiMINT-3016374.
STRINGi9606.ENSP00000395449.

Chemistry databases

BindingDBiP46063.
ChEMBLiCHEMBL1293236.

PTM databases

iPTMnetiP46063.
PhosphoSitePlusiP46063.
SwissPalmiP46063.

Polymorphism and mutation databases

BioMutaiRECQL.
DMDMi218512113.

Proteomic databases

EPDiP46063.
MaxQBiP46063.
PaxDbiP46063.
PeptideAtlasiP46063.
PRIDEiP46063.
TopDownProteomicsiP46063.

Protocols and materials databases

DNASUi5965.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000421138; ENSP00000395449; ENSG00000004700.
ENST00000444129; ENSP00000416739; ENSG00000004700.
GeneIDi5965.
KEGGihsa:5965.
UCSCiuc001rex.4. human.

Organism-specific databases

CTDi5965.
DisGeNETi5965.
GeneCardsiRECQL.
H-InvDBHIX0010478.
HGNCiHGNC:9948. RECQL.
HPAiCAB009743.
HPA030960.
HPA064259.
MIMi600537. gene.
neXtProtiNX_P46063.
OpenTargetsiENSG00000004700.
PharmGKBiPA34315.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0351. Eukaryota.
COG0514. LUCA.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000044388.
HOVERGENiHBG057654.
InParanoidiP46063.
KOiK10899.
OMAiESSQTCH.
OrthoDBiEOG091G05Q8.
PhylomeDBiP46063.
TreeFamiTF323555.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000004700-MONOMER.
BRENDAi3.6.4.12. 2681.

Miscellaneous databases

ChiTaRSiRECQL. human.
EvolutionaryTraceiP46063.
GeneWikiiRECQL.
GenomeRNAii5965.
PROiP46063.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000004700.
CleanExiHS_RECQL.
ExpressionAtlasiP46063. baseline and differential.
GenevisibleiP46063. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR004589. DNA_helicase_ATP-dep_RecQ.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR032284. RecQ_Zn-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF16124. RecQ_Zn_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 3 hits.
TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRECQ1_HUMAN
AccessioniPrimary (citable) accession number: P46063
Secondary accession number(s): A8K6G2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: December 16, 2008
Last modified: November 2, 2016
This is version 174 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.