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ATP-dependent DNA helicase Q5 (EC 3.6.4.12) (DNA helicase, RecQ-like type 5) (RecQ5) (RecQ protein-like 5)

 RECQ5_HUMAN             Reviewed;         991 AA.
O94762; Q6P4G0; Q9H0B1; Q9P1W7; Q9UNC8;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
30-AUG-2002, sequence version 2.
25-OCT-2017, entry version 180.
RecName: Full=ATP-dependent DNA helicase Q5;
EC=3.6.4.12;
AltName: Full=DNA helicase, RecQ-like type 5;
Short=RecQ5;
AltName: Full=RecQ protein-like 5;
Name=RECQL5; Synonyms=RECQ5;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA).
TISSUE=Testis;
PubMed=9878247; DOI=10.1006/geno.1998.5595;
Kitao S., Ohsugi I., Ichikawa K., Goto M., Furuichi Y., Shimamoto A.;
"Cloning of two new human helicase genes of the RecQ family:
biological significance of multiple species in higher eukaryotes.";
Genomics 54:443-452(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA AND GAMMA).
PubMed=10471747; DOI=10.1093/nar/27.18.3762;
Sekelsky J.J., Brodsky M.H., Rubin G.M., Hawley R.S.;
"Drosophila and human RecQ5 exist in different isoforms generated by
alternative splicing.";
Nucleic Acids Res. 27:3762-3769(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA),
SUBCELLULAR LOCATION, AND INTERACTION WITH TOP3A AND TOP3B.
TISSUE=Testis;
PubMed=10710432; DOI=10.1093/nar/28.7.1647;
Shimamoto A., Nishikawa K., Kitao S., Furuichi Y.;
"Human RecQ5-beta, a large isomer of RecQ5 DNA helicase, localizes in
the nucleoplasm and interacts with topoisomerases 3-alpha and 3-
beta.";
Nucleic Acids Res. 28:1647-1655(2000).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS GAMMA AND 4).
TISSUE=Duodenum, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-991.
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=20643585; DOI=10.1016/j.dnarep.2010.06.009;
Blundred R., Myers K., Helleday T., Goldman A.S., Bryant H.E.;
"Human RECQL5 overcomes thymidine-induced replication stress.";
DNA Repair 9:964-975(2010).
[10]
INTERACTION WITH RAD51, MUTAGENESIS OF PHE-666, AND FUNCTION.
PubMed=20348101; DOI=10.1074/jbc.M110.110478;
Schwendener S., Raynard S., Paliwal S., Cheng A., Kanagaraj R.,
Shevelev I., Stark J.M., Sung P., Janscak P.;
"Physical interaction of RECQ5 helicase with RAD51 facilitates its
anti-recombinase activity.";
J. Biol. Chem. 285:15739-15745(2010).
[11]
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, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=20231364; DOI=10.1128/MCB.01583-09;
Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.;
"RecQL5 promotes genome stabilization through two parallel
mechanisms--interacting with RNA polymerase II and acting as a
helicase.";
Mol. Cell. Biol. 30:2460-2472(2010).
[12]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22973052; DOI=10.1091/mbc.E12-02-0110;
Tadokoro T., Ramamoorthy M., Popuri V., May A., Tian J., Sykora P.,
Rybanska I., Wilson D.M. III, Croteau D.L., Bohr V.A.;
"Human RECQL5 participates in the removal of endogenous DNA damage.";
Mol. Biol. Cell 23:4273-4285(2012).
[13]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND INTERACTION
WITH TOP2A.
PubMed=22013166; DOI=10.1093/nar/gkr844;
Ramamoorthy M., Tadokoro T., Rybanska I., Ghosh A.K., Wersto R.,
May A., Kulikowicz T., Sykora P., Croteau D.L., Bohr V.A.;
"RECQL5 cooperates with Topoisomerase II alpha in DNA decatenation and
cell cycle progression.";
Nucleic Acids Res. 40:1621-1635(2012).
[14]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23715498; DOI=10.1093/carcin/bgt183;
Ramamoorthy M., May A., Tadokoro T., Popuri V., Seidman M.M.,
Croteau D.L., Bohr V.A.;
"The RecQ helicase RECQL5 participates in psoralen-induced interstrand
cross-link repair.";
Carcinogenesis 34:2218-2230(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-727; SER-815 AND
THR-839, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491 AND SER-815, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
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, AND MUTAGENESIS OF
ASP-157; TRP-504; TYR-508; ARG-515; LYS-516; HIS-552; LEU-556;
LYS-598; LEU-602 AND LYS-603.
PubMed=23748380; DOI=10.1038/nsmb.2596;
Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.;
"Structural mimicry in transcription regulation of human RNA
polymerase II by the DNA helicase RECQL5.";
Nat. Struct. Mol. Biol. 20:892-899(2013).
-!- FUNCTION: 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.
{ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101,
ECO:0000269|PubMed:20643585, ECO:0000269|PubMed:22013166,
ECO:0000269|PubMed:22973052, ECO:0000269|PubMed:23715498,
ECO:0000269|PubMed:23748380}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
{ECO:0000269|PubMed:22013166}.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10710432,
ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:20348101,
ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:23748380}.
-!- INTERACTION:
P24928:POLR2A; NbExp=8; IntAct=EBI-15710057, EBI-295301;
-!- SUBCELLULAR LOCATION: Isoform Beta: Nucleus, nucleoplasm
{ECO:0000269|PubMed:10710432}. Note=Recruited to sites of DNA
damage, such as single-strand breaks and inter-strand cross-links,
and at stalled replication forks. {ECO:0000269|PubMed:20643585,
ECO:0000269|PubMed:22013166, ECO:0000269|PubMed:22973052,
ECO:0000269|PubMed:23715498}.
-!- SUBCELLULAR LOCATION: Isoform Alpha: Cytoplasm
{ECO:0000269|PubMed:10710432}.
-!- SUBCELLULAR LOCATION: Isoform Gamma: Cytoplasm
{ECO:0000269|PubMed:10710432}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=Beta;
IsoId=O94762-1; Sequence=Displayed;
Name=Alpha; Synonyms=RecQ5b;
IsoId=O94762-2; Sequence=VSP_005568;
Name=Gamma; Synonyms=RecQ5a;
IsoId=O94762-3; Sequence=VSP_005569, VSP_005570;
Name=4;
IsoId=O94762-4; Sequence=VSP_057431;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- SIMILARITY: Belongs to the helicase family. RecQ subfamily.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RECQL5ID286.html";
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EMBL; AB006533; BAA74454.1; -; mRNA.
EMBL; AF135183; AAD43061.1; -; mRNA.
EMBL; AF135183; AAD43062.1; -; mRNA.
EMBL; AB042823; BAA95952.1; -; mRNA.
EMBL; AB042824; BAA95953.1; -; mRNA.
EMBL; AB042825; BAA95954.1; -; mRNA.
EMBL; AC087749; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471099; EAW89292.1; -; Genomic_DNA.
EMBL; BC016911; AAH16911.1; -; mRNA.
EMBL; BC063440; AAH63440.1; -; mRNA.
EMBL; AL136869; CAB66803.3; -; mRNA.
CCDS; CCDS32735.1; -. [O94762-3]
CCDS; CCDS42380.1; -. [O94762-1]
CCDS; CCDS45777.1; -. [O94762-2]
RefSeq; NP_001003715.1; NM_001003715.3. [O94762-3]
RefSeq; NP_001003716.1; NM_001003716.3. [O94762-2]
RefSeq; NP_004250.4; NM_004259.6. [O94762-1]
RefSeq; XP_016880832.1; XM_017025343.1. [O94762-1]
RefSeq; XP_016880833.1; XM_017025344.1. [O94762-3]
UniGene; Hs.632229; -.
PDB; 4BK0; X-ray; 1.90 A; A/B=515-620.
PDB; 5LB3; X-ray; 1.80 A; B/E=11-453.
PDB; 5LB5; X-ray; 2.00 A; A/B/C/D=11-453.
PDB; 5LB8; X-ray; 3.40 A; A/D=11-526.
PDB; 5LBA; X-ray; 2.50 A; A/B/C/D=11-453.
PDBsum; 4BK0; -.
PDBsum; 5LB3; -.
PDBsum; 5LB5; -.
PDBsum; 5LB8; -.
PDBsum; 5LBA; -.
ProteinModelPortal; O94762; -.
SMR; O94762; -.
BioGrid; 114797; 58.
DIP; DIP-32964N; -.
IntAct; O94762; 30.
MINT; MINT-1378331; -.
STRING; 9606.ENSP00000317636; -.
iPTMnet; O94762; -.
PhosphoSitePlus; O94762; -.
BioMuta; RECQL5; -.
EPD; O94762; -.
MaxQB; O94762; -.
PaxDb; O94762; -.
PeptideAtlas; O94762; -.
PRIDE; O94762; -.
Ensembl; ENST00000317905; ENSP00000317636; ENSG00000108469. [O94762-1]
Ensembl; ENST00000340830; ENSP00000341983; ENSG00000108469. [O94762-3]
Ensembl; ENST00000420326; ENSP00000414933; ENSG00000108469. [O94762-2]
Ensembl; ENST00000423245; ENSP00000394820; ENSG00000108469. [O94762-4]
Ensembl; ENST00000584999; ENSP00000462248; ENSG00000108469. [O94762-3]
GeneID; 9400; -.
KEGG; hsa:9400; -.
UCSC; uc002joz.5; human. [O94762-1]
UCSC; uc060jzt.1; human.
CTD; 9400; -.
DisGeNET; 9400; -.
EuPathDB; HostDB:ENSG00000108469.14; -.
GeneCards; RECQL5; -.
HGNC; HGNC:9950; RECQL5.
HPA; HPA029970; -.
HPA; HPA029971; -.
MIM; 603781; gene.
neXtProt; NX_O94762; -.
OpenTargets; ENSG00000108469; -.
PharmGKB; PA34317; -.
eggNOG; KOG0352; Eukaryota.
eggNOG; COG0514; LUCA.
GeneTree; ENSGT00550000074520; -.
HOGENOM; HOG000206773; -.
HOVERGEN; HBG057065; -.
InParanoid; O94762; -.
KO; K10902; -.
OMA; KTCIGPS; -.
OrthoDB; EOG091G03BU; -.
PhylomeDB; O94762; -.
TreeFam; TF317614; -.
ChiTaRS; RECQL5; human.
GeneWiki; RECQL5; -.
GenomeRNAi; 9400; -.
PRO; PR:O94762; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000108469; -.
CleanEx; HS_RECQL5; -.
ExpressionAtlas; O94762; baseline and differential.
Genevisible; O94762; HS.
GO; GO:0005694; C:chromosome; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0016591; C:DNA-directed RNA polymerase II, holoenzyme; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; NAS:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043140; F:ATP-dependent 3'-5' DNA helicase activity; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
GO; GO:0009378; F:four-way junction helicase activity; IBA:GO_Central.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000993; F:RNA polymerase II core binding; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0072757; P:cellular response to camptothecin; IEA:Ensembl.
GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
GO; GO:0051304; P:chromosome separation; IMP:UniProtKB.
GO; GO:0006259; P:DNA metabolic process; NAS:UniProtKB.
GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
GO; GO:0006260; P:DNA replication; IMP:UniProtKB.
GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:2000042; P:negative regulation of double-strand break repair via homologous recombination; IEA:Ensembl.
GO; GO:0034244; P:negative regulation of transcription elongation from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:1990414; P:replication-born double-strand break repair via sister chromatid exchange; IEA:Ensembl.
CDD; cd00079; HELICc; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
InterPro; IPR002464; DNA/RNA_helicase_DEAH_CS.
InterPro; IPR004589; DNA_helicase_ATP-dep_RecQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR010716; RECQ5.
InterPro; IPR032284; RecQ_Zn-bd.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF00270; DEAD; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF06959; RecQ5; 1.
Pfam; PF16124; RecQ_Zn_bind; 1.
ProDom; PD120154; RecQ_helicase-like_5; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00614; recQ_fam; 1.
PROSITE; PS00690; DEAH_ATP_HELICASE; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell cycle;
Cell division; Complete proteome; Cytoplasm; DNA damage; DNA repair;
DNA replication; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome.
CHAIN 1 991 ATP-dependent DNA helicase Q5.
/FTId=PRO_0000205055.
DOMAIN 39 213 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 241 403 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
NP_BIND 52 59 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 490 620 Interaction with POLR2A.
REGION 652 725 Interaction with RAD51.
MOTIF 157 160 DEAH box.
MOD_RES 488 488 Phosphoserine.
{ECO:0000250|UniProtKB:D4ACP5}.
MOD_RES 491 491 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 727 727 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 815 815 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 839 839 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 43 69 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_057431.
VAR_SEQ 411 991 Missing (in isoform Alpha).
{ECO:0000303|PubMed:10471747,
ECO:0000303|PubMed:10710432,
ECO:0000303|PubMed:9878247}.
/FTId=VSP_005568.
VAR_SEQ 411 435 CRHAAIAKYFGDALPACAKGCDHCQ -> RWGRGHGKSLRA
AWCSQVVSRHAEL (in isoform Gamma).
{ECO:0000303|PubMed:10471747,
ECO:0000303|PubMed:10710432,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005569.
VAR_SEQ 436 991 Missing (in isoform Gamma).
{ECO:0000303|PubMed:10471747,
ECO:0000303|PubMed:10710432,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_005570.
VARIANT 480 480 D -> G (in dbSNP:rs820196).
/FTId=VAR_024272.
VARIANT 628 628 S -> N (in dbSNP:rs35566780).
/FTId=VAR_051733.
MUTAGEN 157 157 D->A: Abolishes helicase activity.
MUTAGEN 504 504 W->A: Abolishes interaction with POLR2A.
MUTAGEN 508 508 Y->A: Abolishes interaction with POLR2A.
MUTAGEN 515 515 R->E: Abolishes interaction with POLR2A.
MUTAGEN 516 516 K->E: Abolishes interaction with POLR2A.
MUTAGEN 550 550 R->A: Impairs protein folding and
abolishes interaction with POLR2A.
{ECO:0000269|PubMed:20231364}.
MUTAGEN 552 552 H->A: Abolishes interaction with POLR2A.
MUTAGEN 556 556 L->E: Abolishes interaction with POLR2A.
MUTAGEN 584 584 E->A,D: Abolishes interaction with
POLR2A. {ECO:0000269|PubMed:20231364}.
MUTAGEN 597 597 Y->A: Reduces interaction with POLR2A.
{ECO:0000269|PubMed:20231364}.
MUTAGEN 598 598 K->E: Abolishes interaction with POLR2A.
MUTAGEN 602 602 L->D,E: Abolishes interaction with
POLR2A. {ECO:0000269|PubMed:20231364}.
MUTAGEN 603 603 K->E: Abolishes interaction with POLR2A.
MUTAGEN 666 666 F->A: Abolishes interaction with RAD51.
{ECO:0000269|PubMed:20348101}.
HELIX 12 22 {ECO:0000244|PDB:5LB3}.
HELIX 32 43 {ECO:0000244|PDB:5LB3}.
STRAND 48 51 {ECO:0000244|PDB:5LB3}.
HELIX 60 68 {ECO:0000244|PDB:5LB3}.
STRAND 69 71 {ECO:0000244|PDB:5LB3}.
STRAND 73 76 {ECO:0000244|PDB:5LB3}.
HELIX 80 92 {ECO:0000244|PDB:5LB3}.
STRAND 97 104 {ECO:0000244|PDB:5LB3}.
HELIX 106 116 {ECO:0000244|PDB:5LB3}.
STRAND 118 120 {ECO:0000244|PDB:5LB3}.
STRAND 125 128 {ECO:0000244|PDB:5LB3}.
HELIX 130 133 {ECO:0000244|PDB:5LB3}.
TURN 136 138 {ECO:0000244|PDB:5LB3}.
HELIX 139 147 {ECO:0000244|PDB:5LB3}.
STRAND 153 158 {ECO:0000244|PDB:5LB3}.
HELIX 159 162 {ECO:0000244|PDB:5LB3}.
TURN 164 167 {ECO:0000244|PDB:5LBA}.
HELIX 171 175 {ECO:0000244|PDB:5LB3}.
HELIX 176 181 {ECO:0000244|PDB:5LB3}.
STRAND 184 186 {ECO:0000244|PDB:5LB3}.
STRAND 188 193 {ECO:0000244|PDB:5LB3}.
HELIX 197 206 {ECO:0000244|PDB:5LB3}.
STRAND 214 217 {ECO:0000244|PDB:5LB3}.
STRAND 225 231 {ECO:0000244|PDB:5LB3}.
HELIX 232 234 {ECO:0000244|PDB:5LB3}.
HELIX 238 249 {ECO:0000244|PDB:5LB3}.
HELIX 252 254 {ECO:0000244|PDB:5LB3}.
STRAND 260 265 {ECO:0000244|PDB:5LB3}.
HELIX 269 282 {ECO:0000244|PDB:5LB3}.
STRAND 286 289 {ECO:0000244|PDB:5LB3}.
STRAND 291 293 {ECO:0000244|PDB:5LBA}.
HELIX 295 306 {ECO:0000244|PDB:5LB3}.
STRAND 309 316 {ECO:0000244|PDB:5LB3}.
STRAND 328 335 {ECO:0000244|PDB:5LB3}.
HELIX 340 347 {ECO:0000244|PDB:5LB3}.
STRAND 357 363 {ECO:0000244|PDB:5LB3}.
HELIX 365 386 {ECO:0000244|PDB:5LB3}.
HELIX 392 407 {ECO:0000244|PDB:5LB3}.
HELIX 412 420 {ECO:0000244|PDB:5LB3}.
STRAND 428 431 {ECO:0000244|PDB:5LB8}.
HELIX 432 435 {ECO:0000244|PDB:5LB3}.
HELIX 437 450 {ECO:0000244|PDB:5LB3}.
TURN 535 538 {ECO:0000244|PDB:4BK0}.
HELIX 547 589 {ECO:0000244|PDB:4BK0}.
HELIX 594 613 {ECO:0000244|PDB:4BK0}.
SEQUENCE 991 AA; 108858 MW; 983668133DED865A CRC64;
MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV CMPTGAGKSL
CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL NSKLSAQERK ELLADLEREK
PQTKILYITP EMAASSSFQP TLNSLVSRHL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR
SRLGHAPCVA LTATATPQVQ EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG
NLKDFCLKAL GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL
VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA GRDGKPSWCR
LYYSRNDRDQ VSFLIRKEVA KLQEKRGNKA SDKATIMAFD ALVTFCEELG CRHAAIAKYF
GDALPACAKG CDHCQNPTAV RRRLEALERS SSWSKTCIGP SQGNGFDPEL YEGGRKGYGD
FSRYDEGSGG SGDEGRDEAH KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR
RIPRLTVKAR EHCLRLLEEA LSSNRQSTRT ADEADLRAKA VELEHETFRN AKVANLYKAS
VLKKVADIHR ASKDGQPYDM GGSAKSCSAQ AEPPEPNEYD IPPASHVYSL KPKRVGAGFP
KGSCPFQTAT ELMETTRIRE QAPQPERGGE HEPPSRPCGL LDEDGSEPLP GPRGEVPGGS
AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ QLLATAAHKD SQSIARFFCR RVESPALLAS
APEAEGACPS CEGVQGPPMA PEKYTGEEDG AGGHSPAPPQ TEECLRERPS TCPPRDQGTP
EVQPTPAKDT WKGKRPRSQQ ENPESQPQKR PRPSAKPSVV AEVKGSVSAS EQGTLNPTAQ
DPFQLSAPGV SLKEAANVVV KCLTPFYKEG KFASKELFKG FARHLSHLLT QKTSPGRSVK
EEAQNLIRHF FHGRARCESE ADWHGLCGPQ R


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