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Protein

DNA repair and recombination protein RAD54-like

Gene

Rad54l

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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). Deficient mice also show significantly shorter telomeres than wild-type controls, indicating that the protein activity plays an essential role in telomere length maintenance in mammals. Deficiency also resulted in an increased frequency of end-to-end chromosome fusions involving telomeres compared to the controls, suggesting a putative role in telomere capping. Non-homologous end joining (NHEJ) and homologous recombination (HR) represent the two major pathways of DNA double-strand break (DSB) repair in eukaryotic cells. LIG4 and RAD54L cooperate to support cellular proliferation, repair spontaneous DSBs, and prevent chromosome and single chromatid aberrations.By similarity8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1908ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: MGI
  • chromosome organization Source: MGI
  • determination of adult lifespan Source: MGI
  • DNA strand renaturation Source: MGI
  • double-strand break repair Source: MGI
  • double-strand break repair via homologous recombination Source: MGI
  • response to drug Source: MGI
  • response to ionizing radiation Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
DNA repair and recombination protein RAD54-like (EC:3.6.4.-)
Alternative name(s):
RAD54 homolog
Short name:
mHR54
Short name:
mRAD54
Gene namesi
Name:Rad54l
Synonyms:Rad54
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:894697. Rad54l.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 747747DNA repair and recombination protein RAD54-likePRO_0000074338Add
BLAST

Proteomic databases

EPDiP70270.
MaxQBiP70270.
PaxDbiP70270.
PRIDEiP70270.

PTM databases

iPTMnetiP70270.
PhosphoSiteiP70270.

Expressioni

Tissue specificityi

Hardly detectable in most tissues. Dramatically increased in thymus, spleen and testis.1 Publication

Gene expression databases

BgeeiP70270.
CleanExiMM_RAD54L.
GenevisibleiP70270. MM.

Interactioni

Subunit structurei

Interacts (via N-terminus) with RAD51.By similarity

Protein-protein interaction databases

BioGridi202569. 6 interactions.
IntActiP70270. 6 interactions.
STRINGi10090.ENSMUSP00000099765.

Structurei

3D structure databases

ProteinModelPortaliP70270.
SMRiP70270. Positions 98-744.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini170 – 345176Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini500 – 653154Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 98Required for chromatin remodeling, strand pairing activities and coupling of ATPase activityBy similarity

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi296 – 2994DEGH box

Sequence similaritiesi

Belongs to the SNF2/RAD54 helicase family.Curated
Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0390. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00550000074619.
HOGENOMiHOG000204521.
HOVERGENiHBG058654.
InParanoidiP70270.
KOiK10875.
OMAiVTRPVII.
OrthoDBiEOG7DJSKN.
PhylomeDBiP70270.
TreeFamiTF101224.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P70270-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRRSLAPSQL ARRKPEDRSS DDEDWQPGTV TPKKRKSSSE TQVQECFLSP
60 70 80 90 100
FRKPLTQLLN RPPCLDSSQH EAFIRSILSK PFKVPIPNYQ GPLGSRALGL
110 120 130 140 150
KRAGVRRALH DPLEEGALVL YEPPPLSAHD QLKLDKEKLP VHVVVDPILS
160 170 180 190 200
KVLRPHQREG VKFLWECVTS RRIPGSHGCI MADEMGLGKT LQCITLMWTL
210 220 230 240 250
LRQSPECKPE IEKAVVVSPS SLVKNWYNEV EKWLGGRIQP LAIDGGSKDE
260 270 280 290 300
IDRKLEGFMN QRGARVPSPI LIISYETFRL HVGVLKKGNV GLVICDEGHR
310 320 330 340 350
LKNSENQTYQ ALDSLNTSRR VLISGTPIQN DLLEYFSLVH FVNSGILGTA
360 370 380 390 400
HEFKKHFELP ILKSRDAAAS EADRQRGEER LRELIGIVNR CLIRRTSDIL
410 420 430 440 450
SKYLPVKIEQ VVCCRLTPLQ TELYKRFLRQ AKPEEELREG KMSVSSLSSI
460 470 480 490 500
TSLKKLCNHP ALIYDKCVAE EDGFEGTLGI FPPGYNSKAV EPQLSGKMLV
510 520 530 540 550
LDYILAVTRS RSSDKVVLVS NYTQTLDLFE KLCRVRRYLY VRLDGTMSIK
560 570 580 590 600
KRAKVVERFN SPSSPDFVFM LSSKAGGCGL NLIGANRLVM FDPDWNPAND
610 620 630 640 650
EQAMARVWRD GQKKICYIYR LLSAGTIEEK IFQRQSHKKA LSSCVVDEEQ
660 670 680 690 700
DVERHFSLGE LKELFTLDEA SLSDTHDRLH CRRCVNNRQV WPPPDGSDCT
710 720 730 740
SDLAQWNHST DKRGLQDEVL QAAWDASSTA ITFVFHQRSH EEQRGLH
Length:747
Mass (Da):84,694
Last modified:August 16, 2004 - v2
Checksum:iA08DFFCB95BF8A50
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031A → V in AAH21643 (PubMed:15489334).Curated
Sequence conflicti148 – 1481I → V in CAA66380 (PubMed:8805304).Curated
Sequence conflicti504 – 5041I → V in BAC40627 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97796 mRNA. Translation: CAA66380.1.
AK088876 mRNA. Translation: BAC40627.1.
BC021643 mRNA. Translation: AAH21643.1.
CCDSiCCDS18504.1.
RefSeqiNP_001116430.1. NM_001122958.1.
NP_001116431.1. NM_001122959.1.
NP_033041.3. NM_009015.3.
XP_006502940.1. XM_006502877.2.
XP_006502941.1. XM_006502878.2.
UniGeneiMm.3655.

Genome annotation databases

EnsembliENSMUST00000102704; ENSMUSP00000099765; ENSMUSG00000028702.
ENSMUST00000102705; ENSMUSP00000099766; ENSMUSG00000028702.
GeneIDi19366.
KEGGimmu:19366.
UCSCiuc008ugb.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X97796 mRNA. Translation: CAA66380.1.
AK088876 mRNA. Translation: BAC40627.1.
BC021643 mRNA. Translation: AAH21643.1.
CCDSiCCDS18504.1.
RefSeqiNP_001116430.1. NM_001122958.1.
NP_001116431.1. NM_001122959.1.
NP_033041.3. NM_009015.3.
XP_006502940.1. XM_006502877.2.
XP_006502941.1. XM_006502878.2.
UniGeneiMm.3655.

3D structure databases

ProteinModelPortaliP70270.
SMRiP70270. Positions 98-744.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202569. 6 interactions.
IntActiP70270. 6 interactions.
STRINGi10090.ENSMUSP00000099765.

PTM databases

iPTMnetiP70270.
PhosphoSiteiP70270.

Proteomic databases

EPDiP70270.
MaxQBiP70270.
PaxDbiP70270.
PRIDEiP70270.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000102704; ENSMUSP00000099765; ENSMUSG00000028702.
ENSMUST00000102705; ENSMUSP00000099766; ENSMUSG00000028702.
GeneIDi19366.
KEGGimmu:19366.
UCSCiuc008ugb.2. mouse.

Organism-specific databases

CTDi8438.
MGIiMGI:894697. Rad54l.

Phylogenomic databases

eggNOGiKOG0390. Eukaryota.
COG0553. LUCA.
GeneTreeiENSGT00550000074619.
HOGENOMiHOG000204521.
HOVERGENiHBG058654.
InParanoidiP70270.
KOiK10875.
OMAiVTRPVII.
OrthoDBiEOG7DJSKN.
PhylomeDBiP70270.
TreeFamiTF101224.

Miscellaneous databases

PROiP70270.
SOURCEiSearch...

Gene expression databases

BgeeiP70270.
CleanExiMM_RAD54L.
GenevisibleiP70270. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000330. SNF2_N.
[Graphical view]
PfamiPF00271. Helicase_C. 1 hit.
PF00176. SNF2_N. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], TISSUE SPECIFICITY.
    Tissue: Testis.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: NOD.
    Tissue: Thymus.
  3. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  4. "Disruption of mouse RAD54 reduces ionizing radiation resistance and homologous recombination."
    Essers J., Hendriks R.W., Swagemakers S.M.A., Troelstra C., de Wit J., Bootsma D., Hoeijmakers J.H.J., Kanaar R.
    Cell 89:195-204(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "Mouse Rad54 affects DNA conformation and DNA-damage-induced Rad51 foci formation."
    Tan T.L.R., Essers J., Citterio E., Swagemakers S.M.A., de Wit J., Benson F.E., Hoeijmakers J.H.J., Kanaar R.
    Curr. Biol. 9:325-328(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Mouse RAD54 affects DNA double-strand break repair and sister chromatid exchange."
    Dronkert M.L.G., Beverloo H.B., Johnson R.D., Hoeijmakers J.H.J., Jasin M., Kanaar R.
    Mol. Cell. Biol. 20:3147-3156(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Gene conversion-like sequence transfers between transgenic antibody V genes are independent of RAD54."
    D'Avirro N., Truong D., Luong M., Kanaar R., Selsing E.
    J. Immunol. 169:3069-3075(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Analysis of mouse Rad54 expression and its implications for homologous recombination."
    Essers J., Hendriks R.W., Wesoly J., Beerens C.E.M.T., Smit B., Hoeijmakers J.H.J., Wyman C., Dronkert M.L.G., Kanaar R.
    DNA Repair 1:779-793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: LEVEL OF PROTEIN EXPRESSION, FUNCTION.
  9. "Somatic hypermutation does not require Rad54 and Rad54B-mediated homologous recombination."
    Bross L., Wesoly J., Buerstedde J.-M., Kanaar R., Jacobs H.
    Eur. J. Immunol. 33:352-357(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: FUNCTION.
  11. "Rad54 and DNA ligase IV cooperate to maintain mammalian chromatid stability."
    Mills K.D., Ferguson D.O., Essers J., Eckersdorff M., Kanaar R., Alt F.W.
    Genes Dev. 18:1283-1292(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRAD54_MOUSE
AccessioniPrimary (citable) accession number: P70270
Secondary accession number(s): Q8BSR5, Q8C2C4, Q8K3D4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2004
Last sequence update: August 16, 2004
Last modified: June 8, 2016
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

The nucleus of a mouse embryonic stem (ES) cell contains on average 2.4 x 105 molecules.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.