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O94762

- RECQ5_HUMAN

UniProt

O94762 - RECQ5_HUMAN

Protein

ATP-dependent DNA helicase Q5

Gene

RECQL5

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (30 Aug 2002)
      Previous versions | rss
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    Functioni

    Isoform beta is a DNA helicase that plays an important role in DNA replication, transcription and repair. Inhibits elongation of stalled transcripts at DNA damage sites by binding to the RNA polymerase II subunit POLR2A and blocking the TCEA1 binding site. Required for mitotic chromosome separation after cross-over events and cell cycle progress. Required for efficient DNA repair, including repair of inter-strand cross-links. Stimulates DNA decatenation mediated by TOP2A. Prevents sister chromatid exchange and homologous recombination.7 Publications

    Catalytic activityi

    ATP + H2O = ADP + phosphate.1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi52 – 598ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent helicase activity Source: InterPro
    3. DNA helicase activity Source: UniProtKB
    4. nucleic acid binding Source: InterPro
    5. RNA polymerase II core binding Source: UniProtKB

    GO - Biological processi

    1. chromosome separation Source: UniProtKB
    2. DNA duplex unwinding Source: GOC
    3. DNA metabolic process Source: UniProtKB
    4. DNA recombination Source: InterPro
    5. DNA repair Source: UniProtKB
    6. DNA replication Source: UniProtKB
    7. mitotic nuclear division Source: UniProtKB
    8. negative regulation of transcription elongation from RNA polymerase II promoter Source: UniProtKB

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, Cell division, DNA damage, DNA repair, DNA replication

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent DNA helicase Q5 (EC:3.6.4.12)
    Alternative name(s):
    DNA helicase, RecQ-like type 5
    Short name:
    RecQ5
    RecQ protein-like 5
    Gene namesi
    Name:RECQL5
    Synonyms:RECQ5
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9950. RECQL5.

    Subcellular locationi

    Isoform Beta : Nucleusnucleoplasm
    Note: Recruited to sites of DNA damage, such as single-strand breaks and inter-strand cross-links, and at stalled replication forks.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. DNA-directed RNA polymerase II, holoenzyme Source: UniProtKB
    3. nuclear membrane Source: HPA
    4. nucleolus Source: HPA
    5. nucleoplasm Source: UniProtKB
    6. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi157 – 1571D → A: Abolishes helicase activity.
    Mutagenesisi504 – 5041W → A: Abolishes interaction with POLR2A.
    Mutagenesisi508 – 5081Y → A: Abolishes interaction with POLR2A.
    Mutagenesisi515 – 5151R → E: Abolishes interaction with POLR2A.
    Mutagenesisi516 – 5161K → E: Abolishes interaction with POLR2A.
    Mutagenesisi550 – 5501R → A: Impairs protein folding and abolishes interaction with POLR2A. 1 Publication
    Mutagenesisi552 – 5521H → A: Abolishes interaction with POLR2A.
    Mutagenesisi556 – 5561L → E: Abolishes interaction with POLR2A.
    Mutagenesisi584 – 5841E → A or D: Abolishes interaction with POLR2A. 1 Publication
    Mutagenesisi597 – 5971Y → A: Reduces interaction with POLR2A. 1 Publication
    Mutagenesisi598 – 5981K → E: Abolishes interaction with POLR2A.
    Mutagenesisi602 – 6021L → D or E: Abolishes interaction with POLR2A. 1 Publication
    Mutagenesisi603 – 6031K → E: Abolishes interaction with POLR2A.
    Mutagenesisi666 – 6661F → A: Abolishes interaction with RAD51. 1 Publication

    Organism-specific databases

    PharmGKBiPA34317.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 991991ATP-dependent DNA helicase Q5PRO_0000205055Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei815 – 8151Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiO94762.
    PaxDbiO94762.
    PRIDEiO94762.

    PTM databases

    PhosphoSiteiO94762.

    Expressioni

    Tissue specificityi

    Ubiquitous.

    Gene expression databases

    ArrayExpressiO94762.
    BgeeiO94762.
    CleanExiHS_RECQL5.
    GenevestigatoriO94762.

    Organism-specific databases

    HPAiHPA029970.
    HPA029971.

    Interactioni

    Subunit structurei

    Monomer. Interacts with TOP2A, TOP3A and TOP3B. Isoform beta interacts with RNA polymerase II subunit POLR2A. Identified in a complex with the RNA polymerase II core bound to DNA. Isoform beta interacts with RAD51.5 Publications

    Protein-protein interaction databases

    BioGridi114797. 34 interactions.
    DIPiDIP-32964N.
    IntActiO94762. 14 interactions.
    MINTiMINT-1378331.
    STRINGi9606.ENSP00000317636.

    Structurei

    Secondary structure

    1
    991
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni535 – 5384
    Helixi547 – 58943
    Helixi594 – 61320

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4BK0X-ray1.90A/B515-620[»]
    ProteinModelPortaliO94762.
    SMRiO94762. Positions 15-443, 524-620.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini39 – 213175Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini241 – 403163Helicase C-terminalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni490 – 620131Interaction with POLR2AAdd
    BLAST
    Regioni652 – 72574Interaction with RAD51Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi157 – 1604DEAH 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.
    HOGENOMiHOG000206773.
    HOVERGENiHBG057065.
    InParanoidiO94762.
    KOiK10902.
    OMAiWSKTCIG.
    OrthoDBiEOG7SJD3T.
    PhylomeDBiO94762.
    TreeFamiTF317614.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.40.50.300. 2 hits.
    InterProiIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR010716. RecQ_helicase-like_5.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view]
    PfamiPF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF06959. RecQ5. 1 hit.
    [Graphical view]
    ProDomiPD120154. RecQ_helicase-like_5. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    TIGRFAMsiTIGR00614. recQ_fam. 1 hit.
    PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform Beta (identifier: O94762-1) [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

    MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV    50
    CMPTGAGKSL CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL 100
    NSKLSAQERK ELLADLEREK PQTKILYITP EMAASSSFQP TLNSLVSRHL 150
    LSYLVVDEAH CVSQWGHDFR PDYLRLGALR SRLGHAPCVA LTATATPQVQ 200
    EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG NLKDFCLKAL 250
    GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL 300
    VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA 350
    GRDGKPSWCR LYYSRNDRDQ VSFLIRKEVA KLQEKRGNKA SDKATIMAFD 400
    ALVTFCEELG CRHAAIAKYF GDALPACAKG CDHCQNPTAV RRRLEALERS 450
    SSWSKTCIGP SQGNGFDPEL YEGGRKGYGD FSRYDEGSGG SGDEGRDEAH 500
    KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR RIPRLTVKAR 550
    EHCLRLLEEA LSSNRQSTRT ADEADLRAKA VELEHETFRN AKVANLYKAS 600
    VLKKVADIHR ASKDGQPYDM GGSAKSCSAQ AEPPEPNEYD IPPASHVYSL 650
    KPKRVGAGFP KGSCPFQTAT ELMETTRIRE QAPQPERGGE HEPPSRPCGL 700
    LDEDGSEPLP GPRGEVPGGS AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ 750
    QLLATAAHKD SQSIARFFCR RVESPALLAS APEAEGACPS CEGVQGPPMA 800
    PEKYTGEEDG AGGHSPAPPQ TEECLRERPS TCPPRDQGTP EVQPTPAKDT 850
    WKGKRPRSQQ ENPESQPQKR PRPSAKPSVV AEVKGSVSAS EQGTLNPTAQ 900
    DPFQLSAPGV SLKEAANVVV KCLTPFYKEG KFASKELFKG FARHLSHLLT 950
    QKTSPGRSVK EEAQNLIRHF FHGRARCESE ADWHGLCGPQ R 991
    Length:991
    Mass (Da):108,858
    Last modified:August 30, 2002 - v2
    Checksum:i983668133DED865A
    GO
    Isoform Alpha (identifier: O94762-2) [UniParc]FASTAAdd to Basket

    Also known as: RecQ5b

    The sequence of this isoform differs from the canonical sequence as follows:
         411-991: Missing.

    Show »
    Length:410
    Mass (Da):45,679
    Checksum:i4B3035ED9892A112
    GO
    Isoform Gamma (identifier: O94762-3) [UniParc]FASTAAdd to Basket

    Also known as: RecQ5a

    The sequence of this isoform differs from the canonical sequence as follows:
         411-435: CRHAAIAKYFGDALPACAKGCDHCQ → RWGRGHGKSLRAAWCSQVVSRHAEL
         436-991: Missing.

    Show »
    Length:435
    Mass (Da):48,509
    Checksum:i00EC15408C5D09AA
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti480 – 4801D → G.
    Corresponds to variant rs820196 [ dbSNP | Ensembl ].
    VAR_024272
    Natural varianti628 – 6281S → N.
    Corresponds to variant rs35566780 [ dbSNP | Ensembl ].
    VAR_051733

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei411 – 991581Missing in isoform Alpha. 3 PublicationsVSP_005568Add
    BLAST
    Alternative sequencei411 – 43525CRHAA…CDHCQ → RWGRGHGKSLRAAWCSQVVS RHAEL in isoform Gamma. 3 PublicationsVSP_005569Add
    BLAST
    Alternative sequencei436 – 991556Missing in isoform Gamma. 3 PublicationsVSP_005570Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006533 mRNA. Translation: BAA74454.1.
    AF135183 mRNA. Translation: AAD43061.1.
    AF135183 mRNA. Translation: AAD43062.1.
    AB042823 mRNA. Translation: BAA95952.1.
    AB042824 mRNA. Translation: BAA95953.1.
    AB042825 mRNA. Translation: BAA95954.1.
    BC016911 mRNA. Translation: AAH16911.1.
    AL136869 mRNA. Translation: CAB66803.3.
    CCDSiCCDS32735.1. [O94762-3]
    CCDS42380.1. [O94762-1]
    CCDS45777.1. [O94762-2]
    RefSeqiNP_001003715.1. NM_001003715.3. [O94762-3]
    NP_001003716.1. NM_001003716.3. [O94762-2]
    NP_004250.4. NM_004259.6. [O94762-1]
    UniGeneiHs.632229.

    Genome annotation databases

    EnsembliENST00000317905; ENSP00000317636; ENSG00000108469. [O94762-1]
    ENST00000340830; ENSP00000341983; ENSG00000108469. [O94762-3]
    ENST00000420326; ENSP00000414933; ENSG00000108469. [O94762-2]
    ENST00000584999; ENSP00000462248; ENSG00000108469. [O94762-3]
    GeneIDi9400.
    KEGGihsa:9400.
    UCSCiuc002joz.4. human. [O94762-3]
    uc002jpb.2. human. [O94762-2]
    uc010dgl.3. human. [O94762-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB006533 mRNA. Translation: BAA74454.1 .
    AF135183 mRNA. Translation: AAD43061.1 .
    AF135183 mRNA. Translation: AAD43062.1 .
    AB042823 mRNA. Translation: BAA95952.1 .
    AB042824 mRNA. Translation: BAA95953.1 .
    AB042825 mRNA. Translation: BAA95954.1 .
    BC016911 mRNA. Translation: AAH16911.1 .
    AL136869 mRNA. Translation: CAB66803.3 .
    CCDSi CCDS32735.1. [O94762-3 ]
    CCDS42380.1. [O94762-1 ]
    CCDS45777.1. [O94762-2 ]
    RefSeqi NP_001003715.1. NM_001003715.3. [O94762-3 ]
    NP_001003716.1. NM_001003716.3. [O94762-2 ]
    NP_004250.4. NM_004259.6. [O94762-1 ]
    UniGenei Hs.632229.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4BK0 X-ray 1.90 A/B 515-620 [» ]
    ProteinModelPortali O94762.
    SMRi O94762. Positions 15-443, 524-620.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114797. 34 interactions.
    DIPi DIP-32964N.
    IntActi O94762. 14 interactions.
    MINTi MINT-1378331.
    STRINGi 9606.ENSP00000317636.

    PTM databases

    PhosphoSitei O94762.

    Proteomic databases

    MaxQBi O94762.
    PaxDbi O94762.
    PRIDEi O94762.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000317905 ; ENSP00000317636 ; ENSG00000108469 . [O94762-1 ]
    ENST00000340830 ; ENSP00000341983 ; ENSG00000108469 . [O94762-3 ]
    ENST00000420326 ; ENSP00000414933 ; ENSG00000108469 . [O94762-2 ]
    ENST00000584999 ; ENSP00000462248 ; ENSG00000108469 . [O94762-3 ]
    GeneIDi 9400.
    KEGGi hsa:9400.
    UCSCi uc002joz.4. human. [O94762-3 ]
    uc002jpb.2. human. [O94762-2 ]
    uc010dgl.3. human. [O94762-1 ]

    Organism-specific databases

    CTDi 9400.
    GeneCardsi GC17M073622.
    HGNCi HGNC:9950. RECQL5.
    HPAi HPA029970.
    HPA029971.
    MIMi 603781. gene.
    neXtProti NX_O94762.
    PharmGKBi PA34317.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0514.
    HOGENOMi HOG000206773.
    HOVERGENi HBG057065.
    InParanoidi O94762.
    KOi K10902.
    OMAi WSKTCIG.
    OrthoDBi EOG7SJD3T.
    PhylomeDBi O94762.
    TreeFami TF317614.

    Miscellaneous databases

    ChiTaRSi RECQL5. human.
    GeneWikii RECQL5.
    GenomeRNAii 9400.
    NextBioi 35211.
    PROi O94762.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94762.
    Bgeei O94762.
    CleanExi HS_RECQL5.
    Genevestigatori O94762.

    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.
    IPR002464. DNA/RNA_helicase_DEAH_CS.
    IPR004589. DNA_helicase_ATP-dep_RecQ.
    IPR014001. Helicase_ATP-bd.
    IPR001650. Helicase_C.
    IPR027417. P-loop_NTPase.
    IPR010716. RecQ_helicase-like_5.
    IPR011991. WHTH_DNA-bd_dom.
    [Graphical view ]
    Pfami PF00270. DEAD. 1 hit.
    PF00271. Helicase_C. 1 hit.
    PF06959. RecQ5. 1 hit.
    [Graphical view ]
    ProDomi PD120154. RecQ_helicase-like_5. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00487. DEXDc. 1 hit.
    SM00490. HELICc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    TIGRFAMsi TIGR00614. recQ_fam. 1 hit.
    PROSITEi PS00690. DEAH_ATP_HELICASE. 1 hit.
    PS51192. HELICASE_ATP_BIND_1. 1 hit.
    PS51194. HELICASE_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of two new human helicase genes of the RecQ family: biological significance of multiple species in higher eukaryotes."
      Kitao S., Ohsugi I., Ichikawa K., Goto M., Furuichi Y., Shimamoto A.
      Genomics 54:443-452(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
      Tissue: Testis.
    2. "Drosophila and human RecQ5 exist in different isoforms generated by alternative splicing."
      Sekelsky J.J., Brodsky M.H., Rubin G.M., Hawley R.S.
      Nucleic Acids Res. 27:3762-3769(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND GAMMA).
    3. "Human RecQ5-beta, a large isomer of RecQ5 DNA helicase, localizes in the nucleoplasm and interacts with topoisomerases 3-alpha and 3-beta."
      Shimamoto A., Nishikawa K., Kitao S., Furuichi Y.
      Nucleic Acids Res. 28:1647-1655(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA), SUBCELLULAR LOCATION, INTERACTION WITH TOP3A AND TOP3B.
      Tissue: Testis.
    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM GAMMA).
      Tissue: Duodenum.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-991.
      Tissue: Testis.
    6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "Human RECQL5 overcomes thymidine-induced replication stress."
      Blundred R., Myers K., Helleday T., Goldman A.S., Bryant H.E.
      DNA Repair 9:964-975(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    8. "Physical interaction of RECQ5 helicase with RAD51 facilitates its anti-recombinase activity."
      Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R., Shevelev I., Stark J.M., Sung P., Janscak P.
      J. Biol. Chem. 285:15739-15745(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RAD51, MUTAGENESIS OF PHE-666, FUNCTION.
    9. "RecQL5 promotes genome stabilization through two parallel mechanisms--interacting with RNA polymerase II and acting as a helicase."
      Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.
      Mol. Cell. Biol. 30:2460-2472(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH RNA POLYMERASE II, INTERACTION WITH POLR2A AND RAD51, MUTAGENESIS OF ARG-550; GLU-584; TYR-597 AND LEU-602, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and cell cycle progression."
      Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R., May A., Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.
      Nucleic Acids Res. 40:1621-1635(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH TOP2A.
    12. "The RecQ helicase RECQL5 participates in psoralen-induced interstrand cross-link repair."
      Ramamoorthy M., May A., Tadokoro T., Popuri V., Seidman M.M., Croteau D.L., Bohr V.A.
      Carcinogenesis 34:2218-2230(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. "Structural mimicry in transcription regulation of human RNA polymerase II by the DNA helicase RECQL5."
      Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.
      Nat. Struct. Mol. Biol. 20:892-899(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 515-620, STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH RNA POLYMERASE II AND DNA, INTERACTION WITH POLR2A, SUBUNIT, FUNCTION, MUTAGENSIS OF ASP-157; TRP-504; TYR-508; ARG-515; LYS-515; HIS-552; LEU-556; LYS-598; LEU-602 AND LYS-603.

    Entry informationi

    Entry nameiRECQ5_HUMAN
    AccessioniPrimary (citable) accession number: O94762
    Secondary accession number(s): Q9H0B1, Q9P1W7, Q9UNC8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: August 30, 2002
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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

    External Data

    Dasty 3