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Protein

ATP-dependent DNA helicase Q1

Gene

Recql

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Isoform alpha is a DNA helicase that may play a role in the repair of DNA that is damaged by ultraviolet light or other mutagens. Isoform beta may have important roles in the meiotic process. Both isoforms exhibit a magnesium-dependent ATP-dependent DNA-helicase activity that unwinds single- and double-stranded DNA in a 3'-5' direction.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi113 – 1208ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent DNA helicase Q1 (EC:3.6.4.12)
Alternative name(s):
DNA-dependent ATPase Q1
RecQ protein-like 1
Gene namesi
Name:Recql
Synonyms:Recql1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:103021. Recql.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 648648ATP-dependent DNA helicase Q1PRO_0000205050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei514 – 5141N6-acetyllysineBy similarity
Modified residuei522 – 5221N6-acetyllysineBy similarity
Modified residuei633 – 6331PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Z129.
PaxDbiQ9Z129.
PRIDEiQ9Z129.

PTM databases

PhosphoSiteiQ9Z129.

Expressioni

Tissue specificityi

Isoform alpha is expressed in all tissues examined. Isoform beta is only expressed in spermatocytes, expression increases at pachytene (17 days old) and decreases after completion of meiosis II (7 weeks old).1 Publication

Gene expression databases

BgeeiQ9Z129.
CleanExiMM_RECQL.
ExpressionAtlasiQ9Z129. baseline and differential.
GenevisibleiQ9Z129. MM.

Interactioni

Subunit structurei

Interacts with EXO1 and MLH1.By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107434.

Structurei

3D structure databases

ProteinModelPortaliQ9Z129.
SMRiQ9Z129. Positions 64-593.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini100 – 275176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini299 – 451153Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi219 – 2224DEVH box

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

eggNOGiCOG0514.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000044388.
HOVERGENiHBG057654.
InParanoidiQ9Z129.
OMAiQKFRPLQ.
OrthoDBiEOG7K0ZC0.
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.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09382. RQC. 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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Alpha (identifier: Q9Z129-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASVSALTEE LESVASELHA IDIQIQELTE RRQELLQRKS VLTGKIKQYL
60 70 80 90 100
EDSSAEASSD LDTSPAAWNK EDFPWFGKVK DVLQNVFKLQ KFRPLQLETI
110 120 130 140 150
NVTMARKDIF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV
160 170 180 190 200
LKQLGISATM LNASSSKEHV KWVHAEMVNK NSQLKLIYVT PEKIAKSKMF
210 220 230 240 250
MSRLEKAYEA GRLTGAAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL
260 270 280 290 300
MGLTATATNH VLKDVQKILC VGKCLTFTAS FNRPNLFYEV RQKPSSAEDF
310 320 330 340 350
TEDIVKLING RYKGQSGIIY CFSQKDSEQI TISLQKLGIH AGTYHANMEP
360 370 380 390 400
EDKTKVHTQW SANELQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ
410 420 430 440 450
ESGRAGRDDS RADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNV
460 470 480 490 500
SKCRRVLIAQ HFDEVWNADA CNKMCDNCCK DVSFEKKNVT QHCRDLIKIL
510 520 530 540 550
KQAEGLNEKL TPLKLIDAWM GKGAAKLRVA GVVAPALPRE DLERIVAHAL
560 570 580 590 600
LQQYLKEDYS FTAYATISYL KVGPRACLLS NEAHAVTMQV KKSAQSSVRG
610 620 630 640
ALSEARQVEQ VDSKGEEQSS GNSQKSKSRL QPSGSKNAGA KKRKLDDA
Length:648
Mass (Da):72,484
Last modified:July 27, 2011 - v2
Checksum:iDF84B5E9097BF3F3
GO
Isoform Beta (identifier: Q9Z129-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     622-648: NSQKSKSRLQPSGSKNAGAKKRKLDDA → SHAADTAANV

Show »
Length:631
Mass (Da):70,540
Checksum:i633BAB8A1CA86761
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161A → V in BAA75085 (PubMed:9838113).Curated
Sequence conflicti216 – 2161A → V in BAA75086 (PubMed:9838113).Curated
Sequence conflicti518 – 5181A → T in BAA75085 (PubMed:9838113).Curated
Sequence conflicti518 – 5181A → T in BAA75086 (PubMed:9838113).Curated
Sequence conflicti525 – 5251A → P in BAA75085 (PubMed:9838113).Curated
Sequence conflicti525 – 5251A → P in BAA75086 (PubMed:9838113).Curated
Sequence conflicti602 – 6021L → P in BAA75085 (PubMed:9838113).Curated
Sequence conflicti602 – 6021L → P in BAA75086 (PubMed:9838113).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei622 – 64827NSQKS…KLDDA → SHAADTAANV in isoform Beta. CuratedVSP_005567Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017104 mRNA. Translation: BAA75085.1.
AB017105 mRNA. Translation: BAA75086.1.
AK137589 mRNA. Translation: BAE23422.1.
AK164344 mRNA. Translation: BAE37751.1.
CH466572 Genomic DNA. Translation: EDL10638.1.
CCDSiCCDS39695.1. [Q9Z129-1]
CCDS57465.1. [Q9Z129-2]
RefSeqiNP_001191836.1. NM_001204907.1. [Q9Z129-2]
NP_075529.2. NM_023042.3. [Q9Z129-1]
UniGeneiMm.27407.

Genome annotation databases

EnsembliENSMUST00000111803; ENSMUSP00000107434; ENSMUSG00000030243. [Q9Z129-1]
GeneIDi19691.
UCSCiuc009epf.2. mouse. [Q9Z129-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017104 mRNA. Translation: BAA75085.1.
AB017105 mRNA. Translation: BAA75086.1.
AK137589 mRNA. Translation: BAE23422.1.
AK164344 mRNA. Translation: BAE37751.1.
CH466572 Genomic DNA. Translation: EDL10638.1.
CCDSiCCDS39695.1. [Q9Z129-1]
CCDS57465.1. [Q9Z129-2]
RefSeqiNP_001191836.1. NM_001204907.1. [Q9Z129-2]
NP_075529.2. NM_023042.3. [Q9Z129-1]
UniGeneiMm.27407.

3D structure databases

ProteinModelPortaliQ9Z129.
SMRiQ9Z129. Positions 64-593.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000107434.

PTM databases

PhosphoSiteiQ9Z129.

Proteomic databases

MaxQBiQ9Z129.
PaxDbiQ9Z129.
PRIDEiQ9Z129.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000111803; ENSMUSP00000107434; ENSMUSG00000030243. [Q9Z129-1]
GeneIDi19691.
UCSCiuc009epf.2. mouse. [Q9Z129-1]

Organism-specific databases

CTDi5965.
MGIiMGI:103021. Recql.

Phylogenomic databases

eggNOGiCOG0514.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000044388.
HOVERGENiHBG057654.
InParanoidiQ9Z129.
OMAiQKFRPLQ.
OrthoDBiEOG7K0ZC0.
TreeFamiTF323555.

Miscellaneous databases

NextBioi297024.
PROiQ9Z129.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z129.
CleanExiMM_RECQL.
ExpressionAtlasiQ9Z129. baseline and differential.
GenevisibleiQ9Z129. MM.

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.
IPR018982. RQC_domain.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF09382. RQC. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of two isoforms of mouse DNA helicase Q1/RecQL cDNA; alpha form is expressed ubiquitously and beta form specifically in the testis."
    Wang W.-S., Seki M., Yamaoka T., Seki T., Tada S., Katada T., Fujimoto H., Enomoto T.
    Biochim. Biophys. Acta 1443:198-202(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ALTERNATIVE SPLICING, TISSUE SPECIFICITY.
    Tissue: Spermatocyte and Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA).
    Strain: C57BL/6J.
    Tissue: Bone and Spinal ganglion.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 186-196 AND 502-509, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6.
    Tissue: Brain.

Entry informationi

Entry nameiRECQ1_MOUSE
AccessioniPrimary (citable) accession number: Q9Z129
Secondary accession number(s): Q3TPI5, Q9Z128
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 27, 2011
Last modified: July 22, 2015
This is version 136 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.