Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Z129

- RECQ1_MOUSE

UniProt

Q9Z129 - RECQ1_MOUSE

Protein

ATP-dependent DNA helicase Q1

Gene

Recql

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

    1. annealing helicase activity Source: Ensembl
    2. ATP binding Source: UniProtKB-KW
    3. ATP-dependent 3'-5' DNA helicase activity Source: InterPro
    4. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. DNA recombination Source: InterPro
    2. DNA repair Source: InterPro
    3. DNA replication Source: InterPro

    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: Chromosome 6

    Organism-specific databases

    MGIiMGI:103021. Recql.

    Subcellular locationi

    Nucleus By similarity

    GO - Cellular componenti

    1. microtubule cytoskeleton Source: Ensembl
    2. nucleus Source: UniProtKB-SubCell

    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

    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

    ArrayExpressiQ9Z129.
    BgeeiQ9Z129.
    CleanExiMM_RECQL.
    GenevestigatoriQ9Z129.

    Interactioni

    Subunit structurei

    Interacts with EXO1 and MLH1.By similarity

    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.
    InParanoidiQ3TPI5.
    KOiK10899.
    OMAiQKFRPLQ.
    OrthoDBiEOG7K0ZC0.
    TreeFamiTF323555.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR011545. 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.
    [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. Align

    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

    MASVSALTEE LESVASELHA IDIQIQELTE RRQELLQRKS VLTGKIKQYL    50
    EDSSAEASSD LDTSPAAWNK EDFPWFGKVK DVLQNVFKLQ KFRPLQLETI 100
    NVTMARKDIF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV 150
    LKQLGISATM LNASSSKEHV KWVHAEMVNK NSQLKLIYVT PEKIAKSKMF 200
    MSRLEKAYEA GRLTGAAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL 250
    MGLTATATNH VLKDVQKILC VGKCLTFTAS FNRPNLFYEV RQKPSSAEDF 300
    TEDIVKLING RYKGQSGIIY CFSQKDSEQI TISLQKLGIH AGTYHANMEP 350
    EDKTKVHTQW SANELQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ 400
    ESGRAGRDDS RADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNV 450
    SKCRRVLIAQ HFDEVWNADA CNKMCDNCCK DVSFEKKNVT QHCRDLIKIL 500
    KQAEGLNEKL TPLKLIDAWM GKGAAKLRVA GVVAPALPRE DLERIVAHAL 550
    LQQYLKEDYS FTAYATISYL KVGPRACLLS NEAHAVTMQV KKSAQSSVRG 600
    ALSEARQVEQ VDSKGEEQSS GNSQKSKSRL QPSGSKNAGA KKRKLDDA 648
    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:
    EMBL
    GenBank
    DDBJ
    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]
    XP_006506989.1. XM_006506926.1. [Q9Z129-1]
    XP_006506990.1. XM_006506927.1. [Q9Z129-1]
    UniGeneiMm.27407.

    Genome annotation databases

    EnsembliENSMUST00000032370; ENSMUSP00000032370; ENSMUSG00000030243. [Q9Z129-2]
    ENSMUST00000111803; ENSMUSP00000107434; ENSMUSG00000030243. [Q9Z129-1]
    GeneIDi19691.
    KEGGimmu:19691.
    UCSCiuc009epf.2. mouse. [Q9Z129-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS39695.1. [Q9Z129-1 ]
    CCDS57465.1. [Q9Z129-2 ]
    RefSeqi NP_001191836.1. NM_001204907.1. [Q9Z129-2 ]
    NP_075529.2. NM_023042.3. [Q9Z129-1 ]
    XP_006506989.1. XM_006506926.1. [Q9Z129-1 ]
    XP_006506990.1. XM_006506927.1. [Q9Z129-1 ]
    UniGenei Mm.27407.

    3D structure databases

    ProteinModelPortali Q9Z129.
    SMRi Q9Z129. Positions 64-593.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9Z129.

    Proteomic databases

    PaxDbi Q9Z129.
    PRIDEi Q9Z129.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032370 ; ENSMUSP00000032370 ; ENSMUSG00000030243 . [Q9Z129-2 ]
    ENSMUST00000111803 ; ENSMUSP00000107434 ; ENSMUSG00000030243 . [Q9Z129-1 ]
    GeneIDi 19691.
    KEGGi mmu:19691.
    UCSCi uc009epf.2. mouse. [Q9Z129-1 ]

    Organism-specific databases

    CTDi 5965.
    MGIi MGI:103021. Recql.

    Phylogenomic databases

    eggNOGi COG0514.
    GeneTreei ENSGT00550000074520.
    HOGENOMi HOG000044388.
    HOVERGENi HBG057654.
    InParanoidi Q3TPI5.
    KOi K10899.
    OMAi QKFRPLQ.
    OrthoDBi EOG7K0ZC0.
    TreeFami TF323555.

    Miscellaneous databases

    NextBioi 297024.
    PROi Q9Z129.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Z129.
    Bgeei Q9Z129.
    CleanExi MM_RECQL.
    Genevestigatori Q9Z129.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProi 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.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF09382. RQC. 1 hit.
    [Graphical view ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 3 hits.
    TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
    PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 128 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