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P46063

- RECQ1_HUMAN

UniProt

P46063 - RECQ1_HUMAN

Protein

ATP-dependent DNA helicase Q1

Gene

RECQL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 3 (16 Dec 2008)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi113 – 1208ATPCurated

    GO - Molecular functioni

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

    GO - Biological processi

    1. DNA duplex unwinding Source: GOC
    2. DNA recombination Source: InterPro
    3. DNA repair Source: ProtInc
    4. DNA replication Source: InterPro
    5. DNA strand renaturation Source: UniProtKB

    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 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
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:9948. RECQL.

    Subcellular locationi

    Nucleus 1 Publication

    GO - Cellular componenti

    1. membrane Source: UniProtKB
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi119 – 1191K → A: Abrogates helicase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34315.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 649649ATP-dependent DNA helicase Q1PRO_0000205049Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei514 – 5141N6-acetyllysine1 Publication
    Modified residuei522 – 5221N6-acetyllysine1 Publication
    Modified residuei634 – 6341Phosphoserine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP46063.
    PaxDbiP46063.
    PRIDEiP46063.

    PTM databases

    PhosphoSiteiP46063.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiP46063.
    BgeeiP46063.
    CleanExiHS_RECQL.
    GenevestigatoriP46063.

    Organism-specific databases

    HPAiCAB009743.
    HPA030960.

    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. 11 interactions.
    DIPiDIP-29216N.
    IntActiP46063. 5 interactions.
    MINTiMINT-3016374.
    STRINGi9606.ENSP00000395449.

    Structurei

    Secondary structure

    1
    649
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi65 – 684
    Helixi76 – 8510
    Helixi96 – 1049
    Beta strandi109 – 1124
    Helixi121 – 1288
    Beta strandi130 – 1378
    Helixi141 – 15414
    Beta strandi158 – 1603
    Helixi167 – 17812
    Beta strandi186 – 1894
    Helixi191 – 1955
    Helixi198 – 20912
    Beta strandi213 – 2197
    Helixi221 – 2244
    Helixi226 – 2283
    Helixi233 – 2397
    Helixi240 – 2445
    Beta strandi248 – 2569
    Helixi259 – 26810
    Beta strandi275 – 2784
    Beta strandi286 – 2927
    Helixi297 – 30812
    Turni309 – 3146
    Beta strandi316 – 3205
    Helixi324 – 33613
    Beta strandi341 – 3444
    Helixi350 – 36112
    Beta strandi364 – 3707
    Beta strandi383 – 3908
    Helixi395 – 4028
    Beta strandi412 – 4187
    Helixi420 – 42910
    Turni430 – 4323
    Helixi436 – 44712
    Beta strandi450 – 4523
    Helixi454 – 4629
    Helixi476 – 4794
    Beta strandi484 – 4885
    Helixi490 – 50516
    Helixi512 – 5198
    Helixi525 – 5273
    Helixi539 – 55113
    Beta strandi554 – 5618
    Beta strandi566 – 5727
    Helixi574 – 5807
    Beta strandi587 – 5915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2V1XX-ray2.00A/B49-615[»]
    2WWYX-ray2.90A/B49-616[»]
    ProteinModelPortaliP46063.
    SMRiP46063. Positions 64-593.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP46063.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini100 – 275176Helicase ATP-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini300 – 451152Helicase 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.
    HOGENOMiHOG000044388.
    HOVERGENiHBG057654.
    InParanoidiP46063.
    KOiK10899.
    OMAiQKFRPLQ.
    OrthoDBiEOG7K0ZC0.
    PhylomeDBiP46063.
    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]

    Sequencei

    Sequence statusi: Complete.

    P46063-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVSALTEE LDSITSELHA VEIQIQELTE RQQELIQKKK VLTKKIKQCL    50
    EDSDAGASNE YDSSPAAWNK EDFPWSGKVK DILQNVFKLE KFRPLQLETI 100
    NVTMAGKEVF LVMPTGGGKS LCYQLPALCS DGFTLVICPL ISLMEDQLMV 150
    LKQLGISATM LNASSSKEHV KWVHAEMVNK NSELKLIYVT PEKIAKSKMF 200
    MSRLEKAYEA RRFTRIAVDE VHCCSQWGHD FRPDYKALGI LKRQFPNASL 250
    IGLTATATNH VLTDAQKILC IEKCFTFTAS FNRPNLYYEV RQKPSNTEDF 300
    IEDIVKLING RYKGQSGIIY CFSQKDSEQV TVSLQNLGIH AGAYHANLEP 350
    EDKTTVHRKW SANEIQVVVA TVAFGMGIDK PDVRFVIHHS MSKSMENYYQ 400
    ESGRAGRDDM KADCILYYGF GDIFRISSMV VMENVGQQKL YEMVSYCQNI 450
    SKCRRVLMAQ HFDEVWNSEA CNKMCDNCCK DSAFERKNIT EYCRDLIKIL 500
    KQAEELNEKL TPLKLIDSWM GKGAAKLRVA GVVAPTLPRE DLEKIIAHFL 550
    IQQYLKEDYS FTAYATISYL KIGPKANLLN NEAHAITMQV TKSTQNSFRA 600
    ESSQTCHSEQ GDKKMEEKNS GNFQKKAANM LQQSGSKNTG AKKRKIDDA 649
    Length:649
    Mass (Da):73,457
    Last modified:December 16, 2008 - v3
    Checksum:iF616DC3191F79391
    GO

    Sequence cautioni

    The sequence AAA60261.1 differs from that shown. Reason: Frameshift at positions 615 and 649.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1 – 11M → S in BAA07200. (PubMed:7527136)Curated
    Sequence conflicti175 – 1751A → D in AAA60261. (PubMed:7961977)Curated
    Sequence conflicti453 – 4531C → S in AAA60261. (PubMed:7961977)Curated
    Sequence conflicti566 – 5661T → A in AAA60261. (PubMed:7961977)Curated
    Sequence conflicti617 – 6171E → K in AAP35783. 1 PublicationCurated
    Sequence conflicti617 – 6171E → K in AAH01052. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti102 – 1021V → I.
    Corresponds to variant rs1065751 [ dbSNP | Ensembl ].
    VAR_034679
    Natural varianti372 – 3721V → I.
    Corresponds to variant rs2230003 [ dbSNP | Ensembl ].
    VAR_051732
    Natural varianti487 – 4871K → T.1 Publication
    Corresponds to variant rs6501 [ dbSNP | Ensembl ].
    VAR_016140
    Natural varianti495 – 4951D → H.
    Corresponds to variant rs6499 [ dbSNP | Ensembl ].
    VAR_016141

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_005253461.2.
    XP_005253519.1. XM_005253462.2.
    XP_005253520.1. XM_005253463.1.
    XP_005253521.1. XM_005253464.1.
    XP_006719196.1. XM_006719133.1.
    UniGeneiHs.235069.

    Genome annotation databases

    EnsembliENST00000421138; ENSP00000395449; ENSG00000004700.
    ENST00000444129; ENSP00000416739; ENSG00000004700.
    GeneIDi5965.
    KEGGihsa:5965.
    UCSCiuc001rex.3. human.

    Polymorphism databases

    DMDMi218512113.

    Keywords - Coding sequence diversityi

    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
    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 .
    CCDSi CCDS31756.1.
    PIRi A58836. A55311.
    RefSeqi NP_002898.2. NM_002907.3.
    NP_116559.1. NM_032941.2.
    XP_005253518.1. XM_005253461.2.
    XP_005253519.1. XM_005253462.2.
    XP_005253520.1. XM_005253463.1.
    XP_005253521.1. XM_005253464.1.
    XP_006719196.1. XM_006719133.1.
    UniGenei Hs.235069.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2V1X X-ray 2.00 A/B 49-615 [» ]
    2WWY X-ray 2.90 A/B 49-616 [» ]
    ProteinModelPortali P46063.
    SMRi P46063. Positions 64-593.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111897. 11 interactions.
    DIPi DIP-29216N.
    IntActi P46063. 5 interactions.
    MINTi MINT-3016374.
    STRINGi 9606.ENSP00000395449.

    Chemistry

    ChEMBLi CHEMBL1293236.

    PTM databases

    PhosphoSitei P46063.

    Polymorphism databases

    DMDMi 218512113.

    Proteomic databases

    MaxQBi P46063.
    PaxDbi P46063.
    PRIDEi P46063.

    Protocols and materials databases

    DNASUi 5965.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000421138 ; ENSP00000395449 ; ENSG00000004700 .
    ENST00000444129 ; ENSP00000416739 ; ENSG00000004700 .
    GeneIDi 5965.
    KEGGi hsa:5965.
    UCSCi uc001rex.3. human.

    Organism-specific databases

    CTDi 5965.
    GeneCardsi GC12M021621.
    H-InvDB HIX0010478.
    HGNCi HGNC:9948. RECQL.
    HPAi CAB009743.
    HPA030960.
    MIMi 600537. gene.
    neXtProti NX_P46063.
    PharmGKBi PA34315.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0514.
    HOGENOMi HOG000044388.
    HOVERGENi HBG057654.
    InParanoidi P46063.
    KOi K10899.
    OMAi QKFRPLQ.
    OrthoDBi EOG7K0ZC0.
    PhylomeDBi P46063.
    TreeFami TF323555.

    Miscellaneous databases

    ChiTaRSi RECQL. human.
    EvolutionaryTracei P46063.
    GeneWikii RECQL.
    GenomeRNAii 5965.
    NextBioi 23220.
    PROi P46063.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P46063.
    Bgeei P46063.
    CleanExi HS_RECQL.
    Genevestigatori P46063.

    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 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    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: October 1, 2014
    This is version 150 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

    External Data

    Dasty 3