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O94762 (RECQ5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RECQL5
Synonyms:RECQ5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length991 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Isoform betais 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Catalytic activity

ATP + H2O = ADP + phosphate. Ref.11

Subunit structure

Monomer. Interacts with TOP2A, TOP3A and TOP3B. Isoform betainteracts with RNA polymerase II subunit POLR2A. Identified in a complex with the RNA polymerase II core bound to DNA. Isoform betainteracts with RAD51. Ref.3 Ref.8 Ref.9 Ref.11 Ref.13

Subcellular location

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. Ref.3 Ref.7 Ref.10 Ref.11 Ref.12

Isoform Alpha: Cytoplasm Ref.3 Ref.7 Ref.10 Ref.11 Ref.12.

Isoform Gamma: Cytoplasm Ref.3 Ref.7 Ref.10 Ref.11 Ref.12.

Tissue specificity

Ubiquitous.

Sequence similarities

Belongs to the helicase family. RecQ subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA repair
DNA replication
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA duplex unwinding

Inferred from direct assay Ref.11. Source: GOC

DNA metabolic process

Non-traceable author statement Ref.3. Source: UniProtKB

DNA recombination

Inferred from electronic annotation. Source: InterPro

DNA repair

Inferred from mutant phenotype Ref.10. Source: UniProtKB

DNA replication

Inferred from mutant phenotype Ref.11. Source: UniProtKB

chromosome separation

Inferred from mutant phenotype Ref.11. Source: UniProtKB

mitotic nuclear division

Inferred from mutant phenotype Ref.11. Source: UniProtKB

negative regulation of transcription elongation from RNA polymerase II promoter

Inferred from direct assay Ref.13. Source: UniProtKB

   Cellular_componentDNA-directed RNA polymerase II, holoenzyme

Inferred from direct assay PubMed 22231121. Source: UniProtKB

cytoplasm

Non-traceable author statement Ref.3. Source: UniProtKB

nuclear membrane

Inferred from direct assay. Source: HPA

nucleolus

Inferred from direct assay. Source: HPA

nucleoplasm

Non-traceable author statement Ref.3. Source: UniProtKB

nucleus

Inferred from direct assay Ref.11. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

DNA helicase activity

Inferred from direct assay Ref.11. Source: UniProtKB

RNA polymerase II core binding

Inferred from direct assay Ref.13. Source: UniProtKB

nucleic acid binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform Beta (identifier: O94762-1)

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.
Isoform Alpha (identifier: O94762-2)

Also known as: RecQ5b;

The sequence of this isoform differs from the canonical sequence as follows:
     411-991: Missing.
Isoform Gamma (identifier: O94762-3)

Also known as: RecQ5a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 991991ATP-dependent DNA helicase Q5
PRO_0000205055

Regions

Domain39 – 213175Helicase ATP-binding
Domain241 – 403163Helicase C-terminal
Nucleotide binding52 – 598ATP Potential
Region490 – 620131Interaction with POLR2A
Region652 – 72574Interaction with RAD51
Motif157 – 1604DEAH box

Amino acid modifications

Modified residue8151Phosphoserine Ref.6

Natural variations

Alternative sequence411 – 991581Missing in isoform Alpha.
VSP_005568
Alternative sequence411 – 43525CRHAA…CDHCQ → RWGRGHGKSLRAAWCSQVVS RHAEL in isoform Gamma.
VSP_005569
Alternative sequence436 – 991556Missing in isoform Gamma.
VSP_005570
Natural variant4801D → G.
Corresponds to variant rs820196 [ dbSNP | Ensembl ].
VAR_024272
Natural variant6281S → N.
Corresponds to variant rs35566780 [ dbSNP | Ensembl ].
VAR_051733

Experimental info

Mutagenesis1571D → A: Abolishes helicase activity.
Mutagenesis5041W → A: Abolishes interaction with POLR2A.
Mutagenesis5081Y → A: Abolishes interaction with POLR2A.
Mutagenesis5151R → E: Abolishes interaction with POLR2A.
Mutagenesis5161K → E: Abolishes interaction with POLR2A.
Mutagenesis5501R → A: Impairs protein folding and abolishes interaction with POLR2A. Ref.9
Mutagenesis5521H → A: Abolishes interaction with POLR2A.
Mutagenesis5561L → E: Abolishes interaction with POLR2A.
Mutagenesis5841E → A or D: Abolishes interaction with POLR2A. Ref.9
Mutagenesis5971Y → A: Reduces interaction with POLR2A. Ref.9
Mutagenesis5981K → E: Abolishes interaction with POLR2A.
Mutagenesis6021L → D or E: Abolishes interaction with POLR2A. Ref.9
Mutagenesis6031K → E: Abolishes interaction with POLR2A.
Mutagenesis6661F → A: Abolishes interaction with RAD51. Ref.8

Secondary structure

....... 991
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Beta [UniParc].

Last modified August 30, 2002. Version 2.
Checksum: 983668133DED865A

FASTA991108,858
        10         20         30         40         50         60 
MSSHHTTFPF DPERRVRSTL KKVFGFDSFK TPLQESATMA VVKGNKDVFV CMPTGAGKSL 

        70         80         90        100        110        120 
CYQLPALLAK GITIVVSPLI ALIQDQVDHL LTLKVRVSSL NSKLSAQERK ELLADLEREK 

       130        140        150        160        170        180 
PQTKILYITP EMAASSSFQP TLNSLVSRHL LSYLVVDEAH CVSQWGHDFR PDYLRLGALR 

       190        200        210        220        230        240 
SRLGHAPCVA LTATATPQVQ EDVFAALHLK KPVAIFKTPC FRANLFYDVQ FKELISDPYG 

       250        260        270        280        290        300 
NLKDFCLKAL GQEADKGLSG CGIVYCRTRE ACEQLAIELS CRGVNAKAYH AGLKASERTL 

       310        320        330        340        350        360 
VQNDWMEEKV PVIVATISFG MGVDKANVRF VAHWNIAKSM AGYYQESGRA GRDGKPSWCR 

       370        380        390        400        410        420 
LYYSRNDRDQ VSFLIRKEVA KLQEKRGNKA SDKATIMAFD ALVTFCEELG CRHAAIAKYF 

       430        440        450        460        470        480 
GDALPACAKG CDHCQNPTAV RRRLEALERS SSWSKTCIGP SQGNGFDPEL YEGGRKGYGD 

       490        500        510        520        530        540 
FSRYDEGSGG SGDEGRDEAH KREWNLFYQK QMQLRKGKDP KIEEFVPPDE NCPLKEASSR 

       550        560        570        580        590        600 
RIPRLTVKAR EHCLRLLEEA LSSNRQSTRT ADEADLRAKA VELEHETFRN AKVANLYKAS 

       610        620        630        640        650        660 
VLKKVADIHR ASKDGQPYDM GGSAKSCSAQ AEPPEPNEYD IPPASHVYSL KPKRVGAGFP 

       670        680        690        700        710        720 
KGSCPFQTAT ELMETTRIRE QAPQPERGGE HEPPSRPCGL LDEDGSEPLP GPRGEVPGGS 

       730        740        750        760        770        780 
AHYGGPSPEK KAKSSSGGSS LAKGRASKKQ QLLATAAHKD SQSIARFFCR RVESPALLAS 

       790        800        810        820        830        840 
APEAEGACPS CEGVQGPPMA PEKYTGEEDG AGGHSPAPPQ TEECLRERPS TCPPRDQGTP 

       850        860        870        880        890        900 
EVQPTPAKDT WKGKRPRSQQ ENPESQPQKR PRPSAKPSVV AEVKGSVSAS EQGTLNPTAQ 

       910        920        930        940        950        960 
DPFQLSAPGV SLKEAANVVV KCLTPFYKEG KFASKELFKG FARHLSHLLT QKTSPGRSVK 

       970        980        990 
EEAQNLIRHF FHGRARCESE ADWHGLCGPQ R 

« Hide

Isoform Alpha (RecQ5b) [UniParc].

Checksum: 4B3035ED9892A112
Show »

FASTA41045,679
Isoform Gamma (RecQ5a) [UniParc].

Checksum: 00EC15408C5D09AA
Show »

FASTA43548,509

References

« Hide 'large scale' references
[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]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
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. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 831-991.
Tissue: Testis.
[6]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Human RECQL5 participates in the removal of endogenous DNA damage."
Tadokoro T., Ramamoorthy M., Popuri V., May A., Tian J., Sykora P., Rybanska I., Wilson D.M. III, Croteau D.L., Bohr V.A.
Mol. Biol. Cell 23:4273-4285(2012) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32735.1. [O94762-3]
CCDS42380.1. [O94762-1]
CCDS45777.1. [O94762-2]
RefSeqNP_001003715.1. NM_001003715.3. [O94762-3]
NP_001003716.1. NM_001003716.3. [O94762-2]
NP_004250.4. NM_004259.6. [O94762-1]
UniGeneHs.632229.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BK0X-ray1.90A/B515-620[»]
ProteinModelPortalO94762.
SMRO94762. Positions 15-443, 524-620.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114797. 34 interactions.
DIPDIP-32964N.
IntActO94762. 14 interactions.
MINTMINT-1378331.
STRING9606.ENSP00000317636.

PTM databases

PhosphoSiteO94762.

Proteomic databases

MaxQBO94762.
PaxDbO94762.
PRIDEO94762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317905; ENSP00000317636; ENSG00000108469. [O94762-1]
ENST00000340830; ENSP00000341983; ENSG00000108469. [O94762-3]
ENST00000420326; ENSP00000414933; ENSG00000108469. [O94762-2]
ENST00000584999; ENSP00000462248; ENSG00000108469. [O94762-3]
GeneID9400.
KEGGhsa:9400.
UCSCuc002joz.4. human. [O94762-3]
uc002jpb.2. human. [O94762-2]
uc010dgl.3. human. [O94762-1]

Organism-specific databases

CTD9400.
GeneCardsGC17M073622.
HGNCHGNC:9950. RECQL5.
HPAHPA029970.
HPA029971.
MIM603781. gene.
neXtProtNX_O94762.
PharmGKBPA34317.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0514.
HOGENOMHOG000206773.
HOVERGENHBG057065.
InParanoidO94762.
KOK10902.
OMAWSKTCIG.
OrthoDBEOG7SJD3T.
PhylomeDBO94762.
TreeFamTF317614.

Gene expression databases

ArrayExpressO94762.
BgeeO94762.
CleanExHS_RECQL5.
GenevestigatorO94762.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.40.50.300. 2 hits.
InterProIPR011545. 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]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF06959. RecQ5. 1 hit.
[Graphical view]
ProDomPD120154. RecQ_helicase-like_5. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00614. recQ_fam. 1 hit.
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRECQL5. human.
GeneWikiRECQL5.
GenomeRNAi9400.
NextBio35211.
PROO94762.
SOURCESearch...

Entry information

Entry nameRECQ5_HUMAN
AccessionPrimary (citable) accession number: O94762
Secondary accession number(s): Q9H0B1, Q9P1W7, Q9UNC8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 30, 2002
Last modified: July 9, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM