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Q92698 (RAD54_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA repair and recombination protein RAD54-like

EC=3.6.4.-
Alternative name(s):
RAD54 homolog
Short name=hHR54
Short name=hRAD54
Gene names
Name:RAD54L
Synonyms:RAD54A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length747 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in DNA repair and mitotic recombination. Functions in the recombinational DNA repair (RAD52) pathway. Dissociates RAD51 from nucleoprotein filaments formed on dsDNA. Could be involved in the turnover of RAD51 protein-dsDNA filaments By similarity. May play also an essential role in telomere length maintenance and telomere capping in mammalian cells. Ref.7 Ref.9 Ref.10

Subunit structure

Interacts (via N-terminus) with RAD51. Ref.6

Subcellular location

Nucleus Ref.1.

Induction

Expression increases approximately 3-fold in late G1 phase compared to other phases of the cell cycle. Ref.1

Sequence similarities

Belongs to the SNF2/RAD54 helicase family.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TNKS2Q9H2K23EBI-5333483,EBI-4398527

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 747747DNA repair and recombination protein RAD54-like
PRO_0000074337

Regions

Domain170 – 345176Helicase ATP-binding
Domain500 – 653154Helicase C-terminal
Nucleotide binding183 – 1908ATP Potential
Region2 – 98Required for chromatin remodeling, strand pairing activities and coupling of ATPase activity By similarity
Motif296 – 2994DEGH box

Natural variations

Natural variant211D → G. Ref.2
Corresponds to variant rs28363192 [ dbSNP | Ensembl ].
VAR_055363
Natural variant631P → H in a colon adenocarcinoma sample. Ref.11
VAR_019559
Natural variant741I → M. Ref.2
Corresponds to variant rs28363209 [ dbSNP | Ensembl ].
VAR_055364
Natural variant1511K → E. Ref.11
Corresponds to variant rs2295466 [ dbSNP | Ensembl ].
VAR_019560
Natural variant2021R → C. Ref.2
Corresponds to variant rs28363218 [ dbSNP | Ensembl ].
VAR_055365
Natural variant3251G → R in a breast cancer sample; invasive ductal. Ref.11
VAR_019561
Natural variant3801R → Q. Ref.2
Corresponds to variant rs28363234 [ dbSNP | Ensembl ].
VAR_055366
Natural variant4441V → E in a non-Hodgkin lymphoma sample. Ref.11
VAR_019562
Natural variant5341R → C. Ref.2
Corresponds to variant rs28363240 [ dbSNP | Ensembl ].
VAR_055367
Natural variant5831I → T. Ref.2
Corresponds to variant rs28363243 [ dbSNP | Ensembl ].
VAR_055368

Experimental info

Mutagenesis1891K → R: Unable to rescue the MMS-sensitive phenotype of S cerevisiae rad54delta cells. Ref.1
Sequence conflict7381R → H in CAA66379. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q92698 [UniParc].

Last modified August 16, 2004. Version 2.
Checksum: 718100974CA6687B

FASTA74784,352
        10         20         30         40         50         60 
MRRSLAPSQL AKRKPEGRSC DDEDWQPGLV TPRKRKSSSE TQIQECFLSP FRKPLSQLTN 

        70         80         90        100        110        120 
QPPCLDSSQH EAFIRSILSK PFKVPIPNYQ GPLGSRALGL KRAGVRRALH DPLEKDALVL 

       130        140        150        160        170        180 
YEPPPLSAHD QLKLDKEKLP VHVVVDPILS KVLRPHQREG VKFLWECVTS RRIPGSHGCI 

       190        200        210        220        230        240 
MADEMGLGKT LQCITLMWTL LRQSPECKPE IDKAVVVSPS SLVKNWYNEV GKWLGGRIQP 

       250        260        270        280        290        300 
LAIDGGSKDE IDQKLEGFMN QRGARVSSPI LIISYETFRL HVGVLQKGSV GLVICDEGHR 

       310        320        330        340        350        360 
LKNSENQTYQ ALDSLNTSRR VLISGTPIQN DLLEYFSLVH FVNSGILGTA HEFKKHFELP 

       370        380        390        400        410        420 
ILKGRDAAAS EADRQLGEER LRELTSIVNR CLIRRTSDIL SKYLPVKIEQ VVCCRLTPLQ 

       430        440        450        460        470        480 
TELYKRFLRQ AKPAEELLEG KMSVSSLSSI TSLKKLCNHP ALIYDKCVEE EDGFVGALDL 

       490        500        510        520        530        540 
FPPGYSSKAL EPQLSGKMLV LDYILAVTRS RSSDKVVLVS NYTQTLDLFE KLCRARRYLY 

       550        560        570        580        590        600 
VRLDGTMSIK KRAKVVERFN SPSSPDFVFM LSSKAGGCGL NLIGANRLVM FDPDWNPAND 

       610        620        630        640        650        660 
EQAMARVWRD GQKKTCYIYR LLSAGTIEEK IFQRQSHKKA LSSCVVDEEQ DVERHFSLGE 

       670        680        690        700        710        720 
LKELFILDEA SLSDTHDRLH CRRCVNSRQI RPPPDGSDCT SDLAGWNHCT DKWGLRDEVL 

       730        740 
QAAWDAASTA ITFVFHQRSH EEQRGLR 

« Hide

References

« Hide 'large scale' references
[1]"Human and mouse homologs of the Saccharomyces cerevisiae RAD54 DNA repair gene: evidence for functional conservation."
Kanaar R., Troelstra C., Swagemakers S.M.A., Essers J., Smit B., Franssen J.-H., Pastink A., Bezzubova O.Y., Buerstedde J.-M., Clever B., Heyer W.-D., Hoeijmakers J.H.J.
Curr. Biol. 6:828-838(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, CELL CYCLE REGULATION, MUTAGENESIS OF LYS-189.
Tissue: Testis.
[2]NIEHS SNPs program
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-21; MET-74; CYS-202; GLN-380; CYS-534 AND THR-583.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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].
[5]"Characterization of the human homologue of RAD54: a gene located on chromosome 1p32 at a region of high loss of heterozygosity in breast tumors."
Rasio D., Murakumo Y., Robbins D., Roth T., Silver A., Negrini M., Schmidt C., Burczak J., Fishel R., Croce C.M.
Cancer Res. 57:2378-2383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[6]"Interaction of human recombination proteins Rad51 and Rad54."
Golub E.I., Kovalenko O.V., Gupta R.C., Ward D.C., Radding C.M.
Nucleic Acids Res. 25:4106-4110(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RAD51.
[7]"The human RAD54 recombinational DNA repair protein is a double-stranded DNA-dependent ATPase."
Swagemakers S.M.A., Essers J., de Wit J., Hoeijmakers J.H.J., Kanaar R.
J. Biol. Chem. 273:28292-28297(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Analysis of the RAD54 gene on chromosome 1p as a potential tumor-suppressor gene in parathyroid adenomas."
Carling T., Imanishi Y., Gaz R.D., Arnold A.
Int. J. Cancer 83:80-82(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF INVOLVEMENT IN PARATHYROID ADENOMAS.
[9]"The architecture of the human Rad54-DNA complex provides evidence for protein translocation along DNA."
Ristic D., Wyman C., Paulusma C., Kanaar R.
Proc. Natl. Acad. Sci. U.S.A. 98:8454-8460(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Homologous DNA pairing by human recombination factors Rad51 and Rad54."
Sigurdsson S., Van Komen S., Petukhova G., Sung P.
J. Biol. Chem. 277:42790-42794(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"Mutations in the RAD54 recombination gene in primary cancers."
Matsuda M., Miyagawa K., Takahashi M., Fukuda T., Kataoka T., Asahara T., Inui H., Watatani M., Yasutomi M., Kamada N., Dohi K., Kamiya K.
Oncogene 18:3427-3430(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-63; GLU-151; ARG-325 AND GLU-444.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X97795 mRNA. Translation: CAA66379.1.
AY623117 Genomic DNA. Translation: AAT38113.1.
AL121602 Genomic DNA. Translation: CAI22117.1.
BC121059 mRNA. Translation: AAI21060.1.
BC121060 mRNA. Translation: AAI21061.1.
CCDSCCDS532.1.
RefSeqNP_001136020.1. NM_001142548.1.
NP_003570.2. NM_003579.3.
UniGeneHs.642042.

3D structure databases

ProteinModelPortalQ92698.
SMRQ92698. Positions 98-744.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114018. 3 interactions.
DIPDIP-48628N.
IntActQ92698. 1 interaction.
STRING9606.ENSP00000361043.

Chemistry

ChEMBLCHEMBL2146297.

PTM databases

PhosphoSiteQ92698.

Polymorphism databases

DMDM51316508.

Proteomic databases

MaxQBQ92698.
PaxDbQ92698.
PRIDEQ92698.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000371975; ENSP00000361043; ENSG00000085999.
ENST00000442598; ENSP00000396113; ENSG00000085999.
GeneID8438.
KEGGhsa:8438.
UCSCuc001cpl.2. human.

Organism-specific databases

CTD8438.
GeneCardsGC01P046713.
HGNCHGNC:9826. RAD54L.
HPAHPA028954.
HPA051537.
MIM603615. gene.
neXtProtNX_Q92698.
PharmGKBPA34181.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0553.
HOGENOMHOG000204521.
HOVERGENHBG058654.
InParanoidQ92698.
KOK10875.
OMAVTRPVII.
OrthoDBEOG7DJSKN.
PhylomeDBQ92698.
TreeFamTF101224.

Gene expression databases

BgeeQ92698.
CleanExHS_RAD54L.
GenevestigatorQ92698.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR013967. Rad54_N.
IPR000330. SNF2_N.
[Graphical view]
PfamPF00271. Helicase_C. 1 hit.
PF08658. Rad54_N. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSRAD54L. human.
GeneWikiDNA_repair_and_recombination_protein_RAD54-like.
GenomeRNAi8438.
NextBio31570.
PROQ92698.
SOURCESearch...

Entry information

Entry nameRAD54_HUMAN
AccessionPrimary (citable) accession number: Q92698
Secondary accession number(s): Q5TE31, Q6IUY3
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: July 9, 2014
This is version 118 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

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 1

Human chromosome 1: entries, gene names and cross-references to MIM