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Protein

ATP-dependent DNA helicase Q5

Gene

RECQL5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

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 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9950. RECQL5.

Subcellular locationi

Isoform Beta :
  1. Nucleusnucleoplasm

  2. 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
Complete GO annotation...

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.

Polymorphism and mutation databases

BioMutaiRECQL5.

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 residuei491 – 4911Phosphoserine1 Publication
Modified residuei815 – 8151Phosphoserine2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO94762.
PaxDbiO94762.
PRIDEiO94762.

PTM databases

PhosphoSiteiO94762.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO94762.
CleanExiHS_RECQL5.
ExpressionAtlasiO94762. baseline and differential.
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. 37 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 – 5384Combined sources
Helixi547 – 58943Combined sources
Helixi594 – 61320Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000206773.
HOVERGENiHBG057065.
InParanoidiO94762.
KOiK10902.
OMAiTCIGPSQ.
OrthoDBiEOG7SJD3T.
PhylomeDBiO94762.
TreeFamiTF317614.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV
60 70 80 90 100
CMPTGAGKSL CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL
110 120 130 140 150
NSKLSAQERK ELLADLEREK PQTKILYITP EMAASSSFQP TLNSLVSRHL
160 170 180 190 200
LSYLVVDEAH CVSQWGHDFR PDYLRLGALR SRLGHAPCVA LTATATPQVQ
210 220 230 240 250
EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG NLKDFCLKAL
260 270 280 290 300
GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL
310 320 330 340 350
VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA
360 370 380 390 400
GRDGKPSWCR LYYSRNDRDQ VSFLIRKEVA KLQEKRGNKA SDKATIMAFD
410 420 430 440 450
ALVTFCEELG CRHAAIAKYF GDALPACAKG CDHCQNPTAV RRRLEALERS
460 470 480 490 500
SSWSKTCIGP SQGNGFDPEL YEGGRKGYGD FSRYDEGSGG SGDEGRDEAH
510 520 530 540 550
KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR RIPRLTVKAR
560 570 580 590 600
EHCLRLLEEA LSSNRQSTRT ADEADLRAKA VELEHETFRN AKVANLYKAS
610 620 630 640 650
VLKKVADIHR ASKDGQPYDM GGSAKSCSAQ AEPPEPNEYD IPPASHVYSL
660 670 680 690 700
KPKRVGAGFP KGSCPFQTAT ELMETTRIRE QAPQPERGGE HEPPSRPCGL
710 720 730 740 750
LDEDGSEPLP GPRGEVPGGS AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ
760 770 780 790 800
QLLATAAHKD SQSIARFFCR RVESPALLAS APEAEGACPS CEGVQGPPMA
810 820 830 840 850
PEKYTGEEDG AGGHSPAPPQ TEECLRERPS TCPPRDQGTP EVQPTPAKDT
860 870 880 890 900
WKGKRPRSQQ ENPESQPQKR PRPSAKPSVV AEVKGSVSAS EQGTLNPTAQ
910 920 930 940 950
DPFQLSAPGV SLKEAANVVV KCLTPFYKEG KFASKELFKG FARHLSHLLT
960 970 980 990
QKTSPGRSVK EEAQNLIRHF FHGRARCESE ADWHGLCGPQ R
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
Isoform 4 (identifier: O94762-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     43-69: Missing.

Note: No experimental confirmation available.

Show »
Length:964
Mass (Da):106,051
Checksum:i333A7E6A073D1AF0
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 sequencei43 – 6927Missing in isoform 4. 1 PublicationVSP_057431Add
BLAST
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:
EMBLi
GenBanki
DDBJi
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.
AC087749 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89292.1.
BC016911 mRNA. Translation: AAH16911.1.
BC063440 mRNA. Translation: AAH63440.1.
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]
ENST00000423245; ENSP00000394820; ENSG00000108469. [O94762-4]
ENST00000584999; ENSP00000462248; ENSG00000108469. [O94762-3]
GeneIDi9400.
KEGGihsa:9400.
UCSCiuc002joz.4. human. [O94762-3]
uc002jpb.2. human. [O94762-2]
uc010dgk.3. human.
uc010dgl.3. human. [O94762-1]

Polymorphism and mutation databases

BioMutaiRECQL5.

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:
EMBLi
GenBanki
DDBJi
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.
AC087749 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89292.1.
BC016911 mRNA. Translation: AAH16911.1.
BC063440 mRNA. Translation: AAH63440.1.
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi114797. 37 interactions.
DIPiDIP-32964N.
IntActiO94762. 14 interactions.
MINTiMINT-1378331.
STRINGi9606.ENSP00000317636.

PTM databases

PhosphoSiteiO94762.

Polymorphism and mutation databases

BioMutaiRECQL5.

Proteomic databases

MaxQBiO94762.
PaxDbiO94762.
PRIDEiO94762.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000317905; ENSP00000317636; ENSG00000108469. [O94762-1]
ENST00000340830; ENSP00000341983; ENSG00000108469. [O94762-3]
ENST00000420326; ENSP00000414933; ENSG00000108469. [O94762-2]
ENST00000423245; ENSP00000394820; ENSG00000108469. [O94762-4]
ENST00000584999; ENSP00000462248; ENSG00000108469. [O94762-3]
GeneIDi9400.
KEGGihsa:9400.
UCSCiuc002joz.4. human. [O94762-3]
uc002jpb.2. human. [O94762-2]
uc010dgk.3. human.
uc010dgl.3. human. [O94762-1]

Organism-specific databases

CTDi9400.
GeneCardsiGC17M073622.
HGNCiHGNC:9950. RECQL5.
HPAiHPA029970.
HPA029971.
MIMi603781. gene.
neXtProtiNX_O94762.
PharmGKBiPA34317.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0514.
GeneTreeiENSGT00550000074520.
HOGENOMiHOG000206773.
HOVERGENiHBG057065.
InParanoidiO94762.
KOiK10902.
OMAiTCIGPSQ.
OrthoDBiEOG7SJD3T.
PhylomeDBiO94762.
TreeFamiTF317614.

Miscellaneous databases

ChiTaRSiRECQL5. human.
GeneWikiiRECQL5.
GenomeRNAii9400.
NextBioi35211.
PROiO94762.
SOURCEiSearch...

Gene expression databases

BgeeiO94762.
CleanExiHS_RECQL5.
ExpressionAtlasiO94762. baseline and differential.
GenevestigatoriO94762.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    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.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS GAMMA AND 4).
    Tissue: Duodenum and Uterus.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-991.
    Tissue: Testis.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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.
  10. "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.
  11. "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.
  12. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  13. "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.
  14. "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.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "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): Q6P4G0
, Q9H0B1, Q9P1W7, Q9UNC8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 30, 2002
Last modified: April 29, 2015
This is version 154 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

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.