Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

X-ray repair cross-complementing protein 5

Gene

Xrcc5

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

Functioni

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. 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

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Helicase, Hydrolase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-6798695. Neutrophil degranulation.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Xrcc5
Synonyms:G22p2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:104517. Xrcc5.

Subcellular locationi

  • Nucleus By similarity
  • Nucleusnucleolus By similarity
  • Chromosome By similarity

GO - Cellular componenti

  • cytoplasm Source: MGI
  • Ku70:Ku80 complex Source: UniProtKB
  • membrane Source: MGI
  • nonhomologous end joining complex Source: UniProtKB
  • nuclear chromosome, telomeric region Source: MGI
  • nucleolus Source: UniProtKB-SubCell
  • nucleoplasm Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000843412 – 732X-ray repair cross-complementing protein 5Add BLAST731

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei258PhosphoserineBy similarity1
Modified residuei265N6-acetyllysineBy similarity1
Modified residuei318PhosphoserineBy similarity1
Modified residuei332N6-acetyllysineBy similarity1
Modified residuei535PhosphothreonineBy similarity1
Cross-linki569Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei578Phosphoserine; by PRKDCBy similarity1
Modified residuei580Phosphoserine; by PRKDCBy similarity1
Modified residuei581Phosphoserine; by PRKDCBy similarity1
Modified residuei666N6-acetyllysineBy similarity1
Modified residuei716Phosphothreonine; by PRKDCBy similarity1

Post-translational modificationi

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. Ubiquitinated by RNF138, leading to remove the Ku complex from DNA breaks.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP27641.
MaxQBiP27641.
PaxDbiP27641.
PeptideAtlasiP27641.
PRIDEiP27641.

PTM databases

iPTMnetiP27641.
PhosphoSitePlusiP27641.

Expressioni

Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

Inductioni

Up-regulation during myogenesis is inhibited by cAMP, 3-aminobenzamide and sodium butyrate. Expression in myoblasts is unaffected by X-rays and UV light.1 Publication

Gene expression databases

BgeeiENSMUSG00000026187.
GenevisibleiP27641. MM.

Interactioni

Subunit structurei

Heterodimer composed of XRCC5/Ku80 and XRCC6/Ku70. 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 to form the core of the non-homologous end joining (NHEJ) complex. Additional components of the NHEJ complex include NHEJ1/XLF and C9orf142/PAXX. The dimer also associates with NAA15, and this complex displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, XRCC5 binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/XRCC6 dimer associates in a DNA-dependent manner with APEX1. Identified in a complex with DEAF1 and XRCC6. Interacts with NR4A3; the DNA-dependent protein kinase complex DNA-PK phosphorylates and activates NR4A3 and prevents NR4A3 ubiquitinylation and degradation. Interacts with RNF138. Interacts with MRI isoform 1 (MRI-1) and isoform 4 (MRI-2).By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi204608. 7 interactors.
IntActiP27641. 5 interactors.
STRINGi10090.ENSMUSP00000027379.

Structurei

3D structure databases

ProteinModelPortaliP27641.
SMRiP27641.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini251 – 460KuAdd BLAST210

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni138 – 165Leucine-zipperAdd BLAST28

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi720 – 728EEXXXDL motif9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi478 – 520Pro-richAdd BLAST43

Domaini

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

Sequence similaritiesi

Belongs to the ku80 family.Curated
Contains 1 Ku domain.Curated

Phylogenomic databases

eggNOGiKOG2326. Eukaryota.
ENOG410YKH9. LUCA.
GeneTreeiENSGT00390000015674.
HOVERGENiHBG006237.
InParanoidiP27641.
KOiK10885.
OMAiMASNKEC.
OrthoDBiEOG091G11VD.
PhylomeDBiP27641.
TreeFamiTF101205.

Family and domain databases

Gene3Di1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR006164. 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]
PANTHERiPTHR12604:SF4. PTHR12604:SF4. 1 hit.
PfamiPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF016570. Ku80. 1 hit.
SMARTiSM00559. Ku78. 1 hit.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P27641-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAWSGNKAAV VLCVDVGVAM GNSFPGEESP IEQAKKVMTM FVQRQVFSES
60 70 80 90 100
KDEIALVLYG TDGTDNALAG KDQYQNITVC RHLMLPDFDL LEDIGNKIQP
110 120 130 140 150
SSQQADFLDA LIVCMDLIQR ETIGKKFGKK HIEVFTDLSS PFSQDQLDVI
160 170 180 190 200
ICNLKKSGIS LQFFLPFPID KNGEPGERGD LDSGLDHLKP SFPQKGLTEQ
210 220 230 240 250
QKEGIRMVTR VMLSLEGEDG LDEIYSFSES LRQLCVFKKI ERRSMPWPCQ
260 270 280 290 300
LTIGPNLSIK IVAYKSIVQE KFKKSWVVVD ARTLKKEDIQ KETVYCLNDD
310 320 330 340 350
DETEVSKEDT IQGYRYGSDI IPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ
360 370 380 390 400
VHRRFFMGHQ VLKVFAAKDD EAAAVALSSL VHALDELNMV AIVRYAYDKR
410 420 430 440 450
SNPQVGVAFP YIKDAYECLV YVQLPFMEDL RQYMFSSLKN NKKCTPTEAQ
460 470 480 490 500
LSAIDDLIDS MSLVKKNEEE DIVEDLFPTS KIPNPEFQRL YQCLLHRALH
510 520 530 540 550
LQERLPPIQQ HILNMLDPPT EMKAKCESPL SKVKTLFPLT EVIKKKNQVT
560 570 580 590 600
AQDVFQDNHE EGPAAKKYKT EKEEDHISIS SLAEGNITKV GSVNPVENFR
610 620 630 640 650
FLVRQKIASF EEASLQLISH IEQFLDTNET LYFMKSMDCI KAFREEAIQF
660 670 680 690 700
SEEQRFNSFL EALREKVEIK QLNHFWEIVV QDGVTLITKD EGPGSSITAE
710 720 730
EATKFLAPKD KAKEDTTGPE EAGDVDDLLD MI
Length:732
Mass (Da):83,057
Last modified:February 5, 2008 - v4
Checksum:i391F0FAF7EB04288
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5G → V in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti24F → I in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti57V → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti66 – 69NALA → MPLS in CAA46999 (PubMed:1641347).Curated4
Sequence conflicti120R → H in AAD49720 (Ref. 2) Curated1
Sequence conflicti139S → G in BAE38207 (PubMed:16141072).Curated1
Sequence conflicti139S → R in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti144Q → K in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti157S → C in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti226S → F in AAD49720 (Ref. 2) Curated1
Sequence conflicti409 – 410FP → SL in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti414D → G in BAC38276 (PubMed:16141072).Curated1
Sequence conflicti415A → T in AAD49720 (Ref. 2) Curated1
Sequence conflicti418C → R in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti442K → M in AAD49720 (Ref. 2) Curated1
Sequence conflicti479T → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti515 – 516ML → IW in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti524A → Q in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti530 – 531LS → PL in CAA46999 (PubMed:1641347).Curated2
Sequence conflicti558N → H in AAD49720 (Ref. 2) Curated1
Sequence conflicti692G → A in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti703T → K in CAA46999 (PubMed:1641347).Curated1
Sequence conflicti708P → H in BAE39415 (PubMed:16141072).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35608.1.
PIRiS26303.
RefSeqiNP_033559.2. NM_009533.2.
UniGeneiMm.246952.

Genome annotation databases

EnsembliENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
GeneIDi22596.
KEGGimmu:22596.
UCSCiuc007bkl.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS35608.1.
PIRiS26303.
RefSeqiNP_033559.2. NM_009533.2.
UniGeneiMm.246952.

3D structure databases

ProteinModelPortaliP27641.
SMRiP27641.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204608. 7 interactors.
IntActiP27641. 5 interactors.
STRINGi10090.ENSMUSP00000027379.

PTM databases

iPTMnetiP27641.
PhosphoSitePlusiP27641.

Proteomic databases

EPDiP27641.
MaxQBiP27641.
PaxDbiP27641.
PeptideAtlasiP27641.
PRIDEiP27641.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027379; ENSMUSP00000027379; ENSMUSG00000026187.
GeneIDi22596.
KEGGimmu:22596.
UCSCiuc007bkl.2. mouse.

Organism-specific databases

CTDi7520.
MGIiMGI:104517. Xrcc5.

Phylogenomic databases

eggNOGiKOG2326. Eukaryota.
ENOG410YKH9. LUCA.
GeneTreeiENSGT00390000015674.
HOVERGENiHBG006237.
InParanoidiP27641.
KOiK10885.
OMAiMASNKEC.
OrthoDBiEOG091G11VD.
PhylomeDBiP27641.
TreeFamiTF101205.

Enzyme and pathway databases

ReactomeiR-MMU-5693571. Nonhomologous End-Joining (NHEJ).
R-MMU-6798695. Neutrophil degranulation.

Miscellaneous databases

PROiP27641.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000026187.
GenevisibleiP27641. MM.

Family and domain databases

Gene3Di1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
InterProiIPR006164. 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]
PANTHERiPTHR12604:SF4. PTHR12604:SF4. 1 hit.
PfamiPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]
PIRSFiPIRSF016570. Ku80. 1 hit.
SMARTiSM00559. Ku78. 1 hit.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF101420. SSF101420. 1 hit.
SSF53300. SSF53300. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiXRCC5_MOUSE
AccessioniPrimary (citable) accession number: P27641
Secondary accession number(s): Q3TE46
, Q3TJT0, Q3TN82, Q80UT1, Q8C4N6, Q8K1K7, Q9R169
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 153 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.