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P27641 (XRCC5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
X-ray repair cross-complementing protein 5

EC=3.6.4.-
Alternative name(s):
ATP-dependent DNA helicase 2 subunit 2
ATP-dependent DNA helicase II 80 kDa subunit
CTC box-binding factor 85 kDa subunit
Short name=CTC85
Short name=CTCBF
DNA repair protein XRCC5
Ku autoantigen protein p86 homolog
Ku80
Nuclear factor IV
Gene names
Name:Xrcc5
Synonyms:G22p2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length732 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Single-stranded DNA-dependent ATP-dependent helicase. Has a role in chromosome translocation. The DNA helicase II complex binds preferentially to fork-like ends of double-stranded DNA in a cell cycle-dependent manner. It works in the 3'-5' direction. Binding to DNA may be mediated by XRCC6. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair and V(D)J recombination. The XRCC5/6 dimer acts as regulatory subunit of the DNA-dependent protein kinase complex DNA-PK by increasing the affinity of the catalytic subunit PRKDC to DNA by 100-fold. The XRCC5/6 dimer is probably involved in stabilizing broken DNA ends and bringing them together. The assembly of the DNA-PK complex to DNA ends is required for the NHEJ ligation step. In association with NAA15, the XRCC5/6 dimer binds to the osteocalcin promoter and activates osteocalcin expression. expression. The XRCC5/6 dimer probably also acts as a 5'-deoxyribose-5-phosphate lyase (5'-dRP lyase), by catalyzing the beta-elimination of the 5' deoxyribose-5-phosphate at an abasic site near double-strand breaks. XRCC5 probably acts as the catalytic subunit of 5'-dRP activity, and allows to 'clean' the termini of abasic sites, a class of nucleotide damage commonly associated with strand breaks, before such broken ends can be joined. The XRCC5/6 dimer together with APEX1 acts as a negative regulator of transcription By similarity.

Subunit structure

Heterodimer of a 70 kDa and a 80 kDa subunit. The dimer associates in a DNA-dependent manner with PRKDC to form the DNA-dependent protein kinase complex DNA-PK, and with the LIG4-XRCC4 complex. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1 By similarity. Identified in a complex with DEAF1 and XRCC6 By similarity.

Subcellular location

Nucleus. Nucleusnucleolus By similarity. Chromosome.

Developmental stage

Expression increases during promyelocyte differentiation. Ref.5

Induction

Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light. Ref.5

Domain

The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage By similarity.

Post-translational modification

Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity By similarity.

Sumoylated By similarity.

Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites By similarity.

Sequence similarities

Belongs to the ku80 family.

Contains 1 Ku domain.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Transcription
Transcription regulation
   Cellular componentChromosome
Nucleus
   LigandATP-binding
DNA-binding
Nucleotide-binding
   Molecular functionActivator
Helicase
Hydrolase
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

brain development

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Inferred from mutant phenotype PubMed 17554309. Source: MGI

cellular hyperosmotic salinity response

Inferred from electronic annotation. Source: Ensembl

cellular response to X-ray

Inferred from electronic annotation. Source: Ensembl

cellular response to fatty acid

Inferred from electronic annotation. Source: Ensembl

double-strand break repair

Inferred from mutant phenotype PubMed 12531011. Source: MGI

double-strand break repair via nonhomologous end joining

Inferred from sequence or structural similarity. Source: UniProtKB

hematopoietic stem cell differentiation

Inferred from mutant phenotype PubMed 17554309. Source: MGI

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of neurogenesis

Inferred from mutant phenotype PubMed 10716994. Source: MGI

response to drug

Inferred from electronic annotation. Source: Ensembl

telomere maintenance

Inferred from electronic annotation. Source: InterPro

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentKu70:Ku80 complex

Inferred from sequence or structural similarity. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 12604618. Source: MGI

nonhomologous end joining complex

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear chromosome, telomeric region

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay PubMed 12604618. Source: MGI

   Molecular_function5'-deoxyribose-5-phosphate lyase activity

Inferred from electronic annotation. Source: Ensembl

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent DNA helicase activity

Inferred from electronic annotation. Source: InterPro

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

double-stranded telomeric DNA binding

Inferred from electronic annotation. Source: Ensembl

transcription regulatory region DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 732731X-ray repair cross-complementing protein 5
PRO_0000084341

Regions

Domain251 – 460210Ku
Region138 – 16528Leucine-zipper
Motif720 – 7289EEXXXDL motif
Compositional bias478 – 52043Pro-rich

Amino acid modifications

Modified residue2651N6-acetyllysine By similarity
Modified residue3321N6-acetyllysine By similarity
Modified residue5781Phosphoserine; by PRKDC By similarity
Modified residue5801Phosphoserine; by PRKDC By similarity
Modified residue5811Phosphoserine; by PRKDC By similarity
Modified residue6661N6-acetyllysine By similarity
Modified residue7161Phosphothreonine; by PRKDC By similarity

Experimental info

Sequence conflict51G → V in CAA46999. Ref.1
Sequence conflict241F → I in CAA46999. Ref.1
Sequence conflict571V → A in CAA46999. Ref.1
Sequence conflict66 – 694NALA → MPLS in CAA46999. Ref.1
Sequence conflict1201R → H in AAD49720. Ref.2
Sequence conflict1391S → G in BAE38207. Ref.3
Sequence conflict1391S → R in CAA46999. Ref.1
Sequence conflict1441Q → K in CAA46999. Ref.1
Sequence conflict1571S → C in CAA46999. Ref.1
Sequence conflict2261S → F in AAD49720. Ref.2
Sequence conflict409 – 4102FP → SL in CAA46999. Ref.1
Sequence conflict4141D → G in BAC38276. Ref.3
Sequence conflict4151A → T in AAD49720. Ref.2
Sequence conflict4181C → R in CAA46999. Ref.1
Sequence conflict4421K → M in AAD49720. Ref.2
Sequence conflict4791T → A in CAA46999. Ref.1
Sequence conflict515 – 5162ML → IW in CAA46999. Ref.1
Sequence conflict5241A → Q in CAA46999. Ref.1
Sequence conflict530 – 5312LS → PL in CAA46999. Ref.1
Sequence conflict5581N → H in AAD49720. Ref.2
Sequence conflict6921G → A in CAA46999. Ref.1
Sequence conflict7031T → K in CAA46999. Ref.1
Sequence conflict7081P → H in BAE39415. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P27641 [UniParc].

Last modified February 5, 2008. Version 4.
Checksum: 391F0FAF7EB04288

FASTA73283,057
        10         20         30         40         50         60 
MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES KDEIALVLYG 

        70         80         90        100        110        120 
TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP SSQQADFLDA LIVCMDLIQR 

       130        140        150        160        170        180 
ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI ICNLKKSGIS LQFFLPFPID KNGEPGERGD 

       190        200        210        220        230        240 
LDSGLDHLKP SFPQKGLTEQ QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI 

       250        260        270        280        290        300 
ERRSMPWPCQ LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD 

       310        320        330        340        350        360 
DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ VHRRFFMGHQ 

       370        380        390        400        410        420 
VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR SNPQVGVAFP YIKDAYECLV 

       430        440        450        460        470        480 
YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS 

       490        500        510        520        530        540 
KIPNPEFQRL YQCLLHRALH LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT 

       550        560        570        580        590        600 
EVIKKKNQVT AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR 

       610        620        630        640        650        660 
FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF SEEQRFNSFL 

       670        680        690        700        710        720 
EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE EATKFLAPKD KAKEDTTGPE 

       730 
EAGDVDDLLD MI 

« Hide

References

« Hide 'large scale' references
[1]"The nucleotide sequence of a mouse cDNA encoding the 80 kDa subunit of the Ku (p70/p80) autoantigen."
Falzon M., Kuff E.L.
Nucleic Acids Res. 20:3784-3784(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: BALB/c.
[2]"Ku gene mutation of radiosensitive mouse mammary carcinoma cell line SX-9."
Jiang G.C., Yuan L.Z., Wei K.
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Mammary carcinoma.
[3]"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. expand/collapse author list , 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: C57BL/6J and NOD.
Tissue: Embryonic head, Embryonic heart, Embryonic liver, Kidney and Thymus.
[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].
Strain: 129/Sv X 129SvCp and FVB/N.
Tissue: Embryonic stem cell and Mammary tumor.
[5]"Non-histone protein 1 (NHP1) is a member of the Ku protein family which is upregulated in differentiating mouse myoblasts and human promyelocytes."
Oderwald H., Hughes M.J., Jost J.-P.
FEBS Lett. 382:313-318(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE, INDUCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X66323 mRNA. Translation: CAA46999.1.
AF166486 mRNA. Translation: AAD49720.1.
AK081633 mRNA. Translation: BAC38276.1.
AK165470 mRNA. Translation: BAE38207.1.
AK167312 mRNA. Translation: BAE39415.1.
AK168913 mRNA. Translation: BAE40726.1.
AK169838 mRNA. Translation: BAE41402.1.
BC029218 mRNA. Translation: AAH29218.1.
BC051660 mRNA. Translation: AAH51660.1.
PIRS26303.
RefSeqNP_033559.2. NM_009533.2.
UniGeneMm.246952.

3D structure databases

ProteinModelPortalP27641.
SMRP27641. Positions 6-545, 591-710.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204608. 6 interactions.
IntActP27641. 4 interactions.

PTM databases

PhosphoSiteP27641.

Proteomic databases

PaxDbP27641.
PRIDEP27641.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
GeneID22596.
KEGGmmu:22596.
UCSCuc007bkl.2. mouse.

Organism-specific databases

CTD7520.
MGIMGI:104517. Xrcc5.

Phylogenomic databases

eggNOGNOG299744.
GeneTreeENSGT00390000015674.
HOVERGENHBG006237.
InParanoidP27641.
KOK10885.
OMAGYMLGGT.
OrthoDBEOG7DVD9X.
PhylomeDBP27641.
TreeFamTF101205.

Gene expression databases

ArrayExpressP27641.
BgeeP27641.
GenevestigatorP27641.

Family and domain databases

Gene3D1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProIPR006164. Ku70/Ku80_beta-barrel_dom.
IPR024193. Ku80.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR014893. Ku_PK_bind.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERPTHR12604:SF3. PTHR12604:SF3. 1 hit.
PfamPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]
PIRSFPIRSF016570. Ku80. 1 hit.
SMARTSM00559. Ku78. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMSSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.
ProtoNetSearch...

Other

NextBio302945.
PROP27641.
SOURCESearch...

Entry information

Entry nameXRCC5_MOUSE
AccessionPrimary (citable) accession number: P27641
Secondary accession number(s): Q3TE46 expand/collapse secondary AC list , Q3TJT0, Q3TN82, Q80UT1, Q8C4N6, Q8K1K7, Q9R169
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 128 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot