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P12956

- XRCC6_HUMAN

UniProt

P12956 - XRCC6_HUMAN

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Protein

X-ray repair cross-complementing protein 6

Gene

XRCC6

Organism
Homo sapiens (Human)
Status
Reviewed - 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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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.7 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei31 – 311Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityCurated

GO - Molecular functioni

  1. 5'-deoxyribose-5-phosphate lyase activity Source: UniProtKB
  2. ATP binding Source: UniProtKB-KW
  3. ATP-dependent DNA helicase activity Source: ProtInc
  4. damaged DNA binding Source: InterPro
  5. DNA binding Source: UniProtKB
  6. double-stranded DNA binding Source: ProtInc
  7. poly(A) RNA binding Source: UniProtKB
  8. protein C-terminus binding Source: UniProtKB
  9. telomeric DNA binding Source: InterPro
  10. transcription regulatory region DNA binding Source: BHF-UCL

GO - Biological processi

  1. brain development Source: Ensembl
  2. cellular hyperosmotic salinity response Source: Ensembl
  3. cellular response to X-ray Source: Ensembl
  4. DNA duplex unwinding Source: GOC
  5. DNA ligation Source: ProtInc
  6. DNA repair Source: Reactome
  7. double-strand break repair Source: Reactome
  8. double-strand break repair via nonhomologous end joining Source: UniProtKB
  9. establishment of integrated proviral latency Source: Reactome
  10. innate immune response Source: Reactome
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  12. positive regulation of neurogenesis Source: Ensembl
  13. positive regulation of transcription, DNA-templated Source: UniProtKB
  14. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  15. positive regulation of type I interferon production Source: Reactome
  16. telomere maintenance Source: BHF-UCL
  17. transcription, DNA-templated Source: UniProtKB-KW
  18. V(D)J recombination Source: Ensembl
  19. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator, Helicase, Hydrolase, Lyase

Keywords - Biological processi

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

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1022. Nonhomologous End-joining (NHEJ).
REACT_1201. Processing of DNA ends prior to end rejoining.
REACT_163993. IRF3-mediated induction of type I IFN.
REACT_9058. 2-LTR circle formation.

Names & Taxonomyi

Protein namesi
Recommended name:
X-ray repair cross-complementing protein 6 (EC:3.6.4.-, EC:4.2.99.-)
Alternative name(s):
5'-deoxyribose-5-phosphate lyase Ku70
Short name:
5'-dRP lyase Ku70
70 kDa subunit of Ku antigen
ATP-dependent DNA helicase 2 subunit 1
ATP-dependent DNA helicase II 70 kDa subunit
CTC box-binding factor 75 kDa subunit
Short name:
CTC75
Short name:
CTCBF
DNA repair protein XRCC6
Lupus Ku autoantigen protein p70
Short name:
Ku70
Thyroid-lupus autoantigen
Short name:
TLAA
X-ray repair complementing defective repair in Chinese hamster cells 6
Gene namesi
Name:XRCC6
Synonyms:G22P1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 22

Organism-specific databases

HGNCiHGNC:4055. XRCC6.

Subcellular locationi

Nucleus 1 Publication. Chromosome 1 Publication

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. Ku70:Ku80 complex Source: UniProtKB
  3. membrane Source: UniProtKB
  4. nonhomologous end joining complex Source: UniProtKB
  5. nuclear telomere cap complex Source: BHF-UCL
  6. nucleolus Source: Ensembl
  7. nucleoplasm Source: Reactome
  8. nucleus Source: HPA
  9. transcription factor complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi31 – 311K → A: Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164. 1 Publication
Mutagenesisi160 – 1601K → A: Abolishes adduct formation; when associated with A-31 and A-160. 1 Publication
Mutagenesisi164 – 1641K → A: Abolishes adduct formation; when associated with A-31 and A-164. 1 Publication

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

PharmGKBiPA28467.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 609608X-ray repair cross-complementing protein 6PRO_0000210179Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei6 – 61Phosphoserine; by PRKDC1 Publication
Modified residuei31 – 311N6-acetyllysine1 Publication
Modified residuei51 – 511Phosphoserine; by PRKDC1 Publication
Modified residuei331 – 3311N6-acetyllysine1 Publication
Modified residuei338 – 3381N6-acetyllysine1 Publication
Modified residuei455 – 4551Phosphothreonine2 Publications
Modified residuei461 – 4611N6-acetyllysine1 Publication
Modified residuei477 – 4771Phosphoserine1 Publication
Modified residuei520 – 5201Phosphoserine1 Publication
Modified residuei550 – 5501Phosphoserine1 Publication

Post-translational modificationi

Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-51 does not affect DNA repair.7 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP12956.
PaxDbiP12956.
PRIDEiP12956.

2D gel databases

SWISS-2DPAGEP12956.

PTM databases

PhosphoSiteiP12956.

Miscellaneous databases

PMAP-CutDBP12956.

Expressioni

Developmental stagei

Expression does not increase during promyelocyte differentiation.1 Publication

Inductioni

In osteoblasts, by FGF2.

Gene expression databases

BgeeiP12956.
CleanExiHS_XRCC6.
ExpressionAtlasiP12956. baseline and differential.
GenevestigatoriP12956.

Organism-specific databases

HPAiCAB004254.
HPA047549.

Interactioni

Subunit structurei

Heterodimer of a 70 kDa (XRCC6) and a 80 kDa (XRCC5) 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 binds to the osteocalcin promoter and activates osteocalcin expression. In addition, XRCC6 interacts with the osteoblast-specific transcription factors MSX2, RUNX2 and DLX5. Interacts with ELF3. Interacts with XRCC6BP1. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Interacts with CLU (By similarity). Binds to CDK9 isoform 2. Identified in a complex with DEAF1 and XRCC5. Interacts with DEAF1 (via the SAND domain); the interaction is direct and may be inhibited by DNA-binding.By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARAP1Q96P482EBI-353208,EBI-710003
BAXQ078122EBI-353208,EBI-516580
COILP384323EBI-353208,EBI-945751
HMBOX1Q6NT762EBI-353208,EBI-2549423
HTTP428583EBI-353208,EBI-466029
NDRG1Q925972EBI-353208,EBI-716486
PPIDQ087524EBI-353208,EBI-716596
PRKDCP785275EBI-353208,EBI-352053
SIRT1Q96EB67EBI-353208,EBI-1802965
TCF7L2Q9NQB09EBI-353208,EBI-924724
TP53P046372EBI-353208,EBI-366083
WRNQ141914EBI-353208,EBI-368417
XRCC5P130109EBI-353208,EBI-357997

Protein-protein interaction databases

BioGridi108822. 234 interactions.
DIPiDIP-24188N.
IntActiP12956. 123 interactions.
MINTiMINT-1416738.
STRINGi9606.ENSP00000352257.

Structurei

Secondary structure

1
609
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 439Combined sources
Helixi46 – 494Combined sources
Beta strandi53 – 564Combined sources
Helixi59 – 7618Combined sources
Beta strandi82 – 898Combined sources
Beta strandi102 – 1098Combined sources
Helixi113 – 1208Combined sources
Helixi124 – 13512Combined sources
Helixi143 – 15513Combined sources
Beta strandi161 – 17111Combined sources
Turni175 – 1784Combined sources
Helixi180 – 19617Combined sources
Beta strandi198 – 2058Combined sources
Turni213 – 2164Combined sources
Helixi217 – 2193Combined sources
Helixi239 – 25012Combined sources
Beta strandi256 – 26611Combined sources
Beta strandi268 – 2747Combined sources
Beta strandi286 – 2894Combined sources
Turni290 – 2923Combined sources
Beta strandi295 – 30410Combined sources
Turni305 – 3073Combined sources
Helixi313 – 3153Combined sources
Beta strandi316 – 3227Combined sources
Beta strandi325 – 3295Combined sources
Helixi331 – 3366Combined sources
Beta strandi343 – 35210Combined sources
Helixi353 – 3553Combined sources
Helixi358 – 3603Combined sources
Beta strandi366 – 3705Combined sources
Turni372 – 3743Combined sources
Helixi378 – 39114Combined sources
Beta strandi394 – 4018Combined sources
Beta strandi403 – 4053Combined sources
Beta strandi409 – 4168Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi430 – 4367Combined sources
Helixi440 – 4423Combined sources
Helixi456 – 46813Combined sources
Helixi481 – 49414Combined sources
Helixi511 – 5188Combined sources
Helixi521 – 5299Combined sources
Helixi561 – 5699Combined sources
Helixi573 – 5753Combined sources
Helixi578 – 58710Combined sources
Helixi596 – 60712Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JEQX-ray2.70A1-609[»]
1JEYX-ray2.50A1-609[»]
1JJRNMR-A556-609[»]
3RZXX-ray2.61B537-558[»]
ProteinModelPortaliP12956.
SMRiP12956. Positions 34-609.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12956.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini261 – 468208KuAdd
BLAST
Domaini573 – 60735SAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni550 – 60960Interaction with DEAF1Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 6160Ser-rich (potentially targets for phosphorylation)Add
BLAST
Compositional biasi11 – 2919Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi330 – 34213Asp/Glu-rich (acidic)Add
BLAST

Sequence similaritiesi

Belongs to the ku70 family.Curated
Contains 1 Ku domain.Curated
Contains 1 SAP domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG305318.
GeneTreeiENSGT00390000001422.
HOGENOMiHOG000006588.
HOVERGENiHBG006236.
InParanoidiP12956.
KOiK10884.
OMAiCRYTPRK.
OrthoDBiEOG7QG43F.
PhylomeDBiP12956.
TreeFamiTF315101.

Family and domain databases

Gene3Di1.10.1600.10. 1 hit.
1.10.720.30. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
4.10.970.10. 1 hit.
InterProiIPR006165. Ku70.
IPR006164. Ku70/Ku80_beta-barrel_dom.
IPR027388. Ku70_bridge/pillars_dom.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR003034. SAP_dom.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view]
PANTHERiPTHR12604:SF2. PTHR12604:SF2. 1 hit.
PfamiPF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
PIRSFiPIRSF003033. Ku70. 1 hit.
SMARTiSM00559. Ku78. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00578. ku70. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12956-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE
60 70 80 90 100
SQSEDELTPF DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK
110 120 130 140 150
NIYVLQELDN PGAKRILELD QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC
160 170 180 190 200
ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS AKASRARTKA GDLRDTGIFL
210 220 230 240 250
DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE DLLRKVRAKE
260 270 280 290 300
TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT
310 320 330 340 350
RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF
360 370 380 390 400
KPLVLLKKHH YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY
410 420 430 440 450
TPRRNIPPYF VALVPQEEEL DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE
460 470 480 490 500
KIMATPEQVG KMKAIVEKLR FTYRSDSFEN PVLQQHFRNL EALALDLMEP
510 520 530 540 550
EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV TKRKHDNEGS
560 570 580 590 600
GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL

EALTKHFQD
Length:609
Mass (Da):69,843
Last modified:January 23, 2007 - v2
Checksum:iBBD3CD434526DFCB
GO
Isoform 2 (identifier: P12956-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     65-105: Missing.

Note: No experimental confirmation available.

Show »
Length:568
Mass (Da):65,149
Checksum:iB6DBBED4C80118C1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201Q → D AA sequence (PubMed:1537839)Curated
Sequence conflicti101 – 1011N → K AA sequence (PubMed:8605992)Curated
Sequence conflicti103 – 1031Y → L AA sequence (PubMed:8605992)Curated
Sequence conflicti116 – 1161I → S AA sequence (PubMed:8605992)Curated
Sequence conflicti125 – 1251Q → S AA sequence (PubMed:8605992)Curated
Sequence conflicti181 – 1811A → T in CAG47015. 1 PublicationCurated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei65 – 10541Missing in isoform 2. 1 PublicationVSP_056030Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04607 mRNA. Translation: AAA61177.1.
J04611 mRNA. Translation: AAA51733.1.
M32865 mRNA. Translation: AAA36155.1.
S38729 mRNA. Translation: AAB22381.1.
AK055786 mRNA. Translation: BAG51575.1.
CR542219 mRNA. Translation: CAG47015.1.
AY870329 Genomic DNA. Translation: AAW34364.1.
Z83840 Genomic DNA. Translation: CAB46206.1.
CH471095 Genomic DNA. Translation: EAW60448.1.
BC008343 mRNA. Translation: AAH08343.1.
BC010034 mRNA. Translation: AAH10034.1.
BC012154 mRNA. Translation: AAH12154.1.
BC018259 mRNA. Translation: AAH18259.1.
BC072449 mRNA. Translation: AAH72449.1.
CCDSiCCDS14021.1. [P12956-1]
PIRiA30299. A30894.
RefSeqiNP_001275905.1. NM_001288976.1. [P12956-1]
NP_001275906.1. NM_001288977.1. [P12956-2]
NP_001460.1. NM_001469.4. [P12956-1]
UniGeneiHs.292493.
Hs.730702.

Genome annotation databases

EnsembliENST00000359308; ENSP00000352257; ENSG00000196419. [P12956-1]
ENST00000360079; ENSP00000353192; ENSG00000196419. [P12956-1]
ENST00000402580; ENSP00000384941; ENSG00000196419. [P12956-2]
ENST00000405878; ENSP00000384257; ENSG00000196419. [P12956-1]
GeneIDi2547.
KEGGihsa:2547.
UCSCiuc003bao.1. human. [P12956-1]

Polymorphism databases

DMDMi125729.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

NIEHS-SNPs
Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04607 mRNA. Translation: AAA61177.1 .
J04611 mRNA. Translation: AAA51733.1 .
M32865 mRNA. Translation: AAA36155.1 .
S38729 mRNA. Translation: AAB22381.1 .
AK055786 mRNA. Translation: BAG51575.1 .
CR542219 mRNA. Translation: CAG47015.1 .
AY870329 Genomic DNA. Translation: AAW34364.1 .
Z83840 Genomic DNA. Translation: CAB46206.1 .
CH471095 Genomic DNA. Translation: EAW60448.1 .
BC008343 mRNA. Translation: AAH08343.1 .
BC010034 mRNA. Translation: AAH10034.1 .
BC012154 mRNA. Translation: AAH12154.1 .
BC018259 mRNA. Translation: AAH18259.1 .
BC072449 mRNA. Translation: AAH72449.1 .
CCDSi CCDS14021.1. [P12956-1 ]
PIRi A30299. A30894.
RefSeqi NP_001275905.1. NM_001288976.1. [P12956-1 ]
NP_001275906.1. NM_001288977.1. [P12956-2 ]
NP_001460.1. NM_001469.4. [P12956-1 ]
UniGenei Hs.292493.
Hs.730702.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JEQ X-ray 2.70 A 1-609 [» ]
1JEY X-ray 2.50 A 1-609 [» ]
1JJR NMR - A 556-609 [» ]
3RZX X-ray 2.61 B 537-558 [» ]
ProteinModelPortali P12956.
SMRi P12956. Positions 34-609.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108822. 234 interactions.
DIPi DIP-24188N.
IntActi P12956. 123 interactions.
MINTi MINT-1416738.
STRINGi 9606.ENSP00000352257.

PTM databases

PhosphoSitei P12956.

Polymorphism databases

DMDMi 125729.

2D gel databases

SWISS-2DPAGE P12956.

Proteomic databases

MaxQBi P12956.
PaxDbi P12956.
PRIDEi P12956.

Protocols and materials databases

DNASUi 2547.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000359308 ; ENSP00000352257 ; ENSG00000196419 . [P12956-1 ]
ENST00000360079 ; ENSP00000353192 ; ENSG00000196419 . [P12956-1 ]
ENST00000402580 ; ENSP00000384941 ; ENSG00000196419 . [P12956-2 ]
ENST00000405878 ; ENSP00000384257 ; ENSG00000196419 . [P12956-1 ]
GeneIDi 2547.
KEGGi hsa:2547.
UCSCi uc003bao.1. human. [P12956-1 ]

Organism-specific databases

CTDi 2547.
GeneCardsi GC22P042017.
HGNCi HGNC:4055. XRCC6.
HPAi CAB004254.
HPA047549.
MIMi 152690. gene.
neXtProti NX_P12956.
PharmGKBi PA28467.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG305318.
GeneTreei ENSGT00390000001422.
HOGENOMi HOG000006588.
HOVERGENi HBG006236.
InParanoidi P12956.
KOi K10884.
OMAi CRYTPRK.
OrthoDBi EOG7QG43F.
PhylomeDBi P12956.
TreeFami TF315101.

Enzyme and pathway databases

Reactomei REACT_1022. Nonhomologous End-joining (NHEJ).
REACT_1201. Processing of DNA ends prior to end rejoining.
REACT_163993. IRF3-mediated induction of type I IFN.
REACT_9058. 2-LTR circle formation.

Miscellaneous databases

ChiTaRSi XRCC6. human.
EvolutionaryTracei P12956.
GeneWikii Ku70.
GenomeRNAii 2547.
NextBioi 10043.
PMAP-CutDB P12956.
PROi P12956.
SOURCEi Search...

Gene expression databases

Bgeei P12956.
CleanExi HS_XRCC6.
ExpressionAtlasi P12956. baseline and differential.
Genevestigatori P12956.

Family and domain databases

Gene3Di 1.10.1600.10. 1 hit.
1.10.720.30. 1 hit.
2.40.290.10. 1 hit.
3.40.50.410. 1 hit.
4.10.970.10. 1 hit.
InterProi IPR006165. Ku70.
IPR006164. Ku70/Ku80_beta-barrel_dom.
IPR027388. Ku70_bridge/pillars_dom.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR003034. SAP_dom.
IPR016194. SPOC_like_C_dom.
IPR002035. VWF_A.
[Graphical view ]
PANTHERi PTHR12604:SF2. PTHR12604:SF2. 1 hit.
Pfami PF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view ]
PIRSFi PIRSF003033. Ku70. 1 hit.
SMARTi SM00559. Ku78. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view ]
SUPFAMi SSF100939. SSF100939. 1 hit.
SSF53300. SSF53300. 1 hit.
TIGRFAMsi TIGR00578. ku70. 1 hit.
PROSITEi PS50800. SAP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a cDNA that encodes a 70-kDa novel human thyroid autoantigen."
    Chan J.Y., Lerman M.I., Prabhakar B.S., Isozaki O., Santisteban P., Kuppers R.C., Oates E.L., Notkins A.L., Kohn L.D.
    J. Biol. Chem. 264:3651-3654(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Molecular cloning of cDNA encoding the p70 (Ku) lupus autoantigen."
    Reeves W.H., Sthoeger Z.M.
    J. Biol. Chem. 264:5047-5052(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, ROLE IN LUPUS ERYTHEMATOSUS.
  3. "Nucleotide sequence and genomic structure analyses of the p70 subunit of the human Ku autoantigen: evidence for a family of genes encoding Ku (p70)-related polypeptides."
    Griffith A.J., Craft J., Evans J., Mimori T., Hardin J.A.
    Mol. Biol. Rep. 16:91-97(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Kidney.
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. NIEHS SNPs program
    Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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 1).
    Tissue: Brain, Kidney, Lung, Placenta and Skin.
  10. "Identification of proteins binding to interferon-inducible transcriptional enhancers in hematopoietic cells."
    Wedrychowski A., Henzel W., Huston L., Paslidis N., Ellerson D., McRae M., Seong D., Howard O.M.Z., Deisseroth A.
    J. Biol. Chem. 267:4533-4540(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 10-30 AND 299-317.
  11. "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: PROTEIN SEQUENCE OF 101-114 AND 116-125, DEVELOPMENTAL STAGE.
    Tissue: Cervix carcinoma.
  12. "The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium."
    Chung U., Igarashi T., Nishishita T., Iwanari H., Iwamatsu A., Suwa A., Mimori T., Hata K., Ebisu S., Ogata E., Fujita T., Okazaki T.
    J. Biol. Chem. 271:8593-8598(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 288-293 AND 300-312, FUNCTION, INTERACTION WITH APEX1.
  13. "Purification of the sequence-specific transcription factor CTCBF, involved in the control of human collagen IV genes: subunits with homology to Ku antigen."
    Genersch E., Eckerskorn C., Lottspeich F., Herzog C., Kuehn K., Poeschl E.
    EMBO J. 14:791-800(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 301-308 AND 556-565.
  14. "Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen."
    Tuteja N., Tuteja R., Ochem A., Taneja P., Huang N.W., Simoncsits A., Susic S., Rahman K., Marusic L., Chen J., Zhang J., Wang S., Pongor S., Falaschi A.
    EMBO J. 13:4991-5001(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 346-352, FUNCTION.
  15. "Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions."
    Jin S., Weaver D.T.
    EMBO J. 16:6874-6885(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-51.
  16. "Productive and nonproductive complexes of Ku and DNA-dependent protein kinase at DNA termini."
    West R.B., Yaneva M., Lieber M.R.
    Mol. Cell. Biol. 18:5908-5920(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PRKDC.
  17. "DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer."
    Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.
    Biochemistry 38:1819-1828(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-6.
  18. "Ku, a DNA repair protein with multiple cellular functions?"
    Featherstone C., Jackson S.P.
    Mutat. Res. 434:3-15(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  19. Cited for: INTERACTION WITH XRCC6BP1.
    Tissue: Liver.
  20. "Defining interactions between DNA-PK and ligase IV/XRCC4."
    Hsu H.-L., Yannone S.M., Chen D.J.
    DNA Repair 1:225-235(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PRKDC.
  21. "Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex."
    Willis D.M., Loewy A.P., Charlton-Kachigian N., Shao J.-S., Ornitz D.M., Towler D.A.
    J. Biol. Chem. 277:37280-37291(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH NAA15; MSX2; RUNX2 AND DLX5.
    Tissue: Heart and Osteoblast.
  22. "Coordinated assembly of Ku and p460 subunits of the DNA-dependent protein kinase on DNA ends is necessary for XRCC4-ligase IV recruitment."
    Calsou P., Delteil C., Frit P., Drouet J., Salles B.
    J. Mol. Biol. 326:93-103(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH G22P2; PRKDC AND XRCC4, PHOSPHORYLATION.
  23. "Positive and negative modulation of the transcriptional activity of the ETS factor ESE-1 through interaction with p300, CREB-binding protein, and Ku 70/86."
    Wang H., Fang R., Cho J.-Y., Libermann T.A., Oettgen P.
    J. Biol. Chem. 279:25241-25250(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ELF3.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-477, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  26. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-520, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  27. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338 AND LYS-461, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "55K isoform of CDK9 associates with Ku70 and is involved in DNA repair."
    Liu H., Herrmann C.H., Chiang K., Sung T.L., Moon S.H., Donehower L.A., Rice A.P.
    Biochem. Biophys. Res. Commun. 397:245-250(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH CDK9.
  29. "Ku is a 5'-dRP/AP lyase that excises nucleotide damage near broken ends."
    Roberts S.A., Strande N., Burkhalter M.D., Strom C., Havener J.M., Hasty P., Ramsden D.A.
    Nature 464:1214-1217(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS A 5'-DRP LYASE, MUTAGENESIS OF LYS-31; LYS-160 AND LYS-164.
  30. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-550, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  31. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  32. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Deformed epidermal autoregulatory factor-1 (DEAF1) interacts with the Ku70 subunit of the DNA-dependent protein kinase complex."
    Jensik P.J., Huggenvik J.I., Collard M.W.
    PLoS ONE 7:E33404-E33404(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, IDENTIFICATION IN A COMPLEX WITH DEAF1 AND XRCC5, INTERACTION WITH DEAF1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  35. "The three-dimensional structure of the C-terminal DNA-binding domain of human Ku70."
    Zhang Z., Zhu L., Lin D., Chen F., Chen D.J., Chen Y.
    J. Biol. Chem. 276:38231-38236(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 557-610.
  36. "Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair."
    Walker J.R., Corpina R.A., Goldberg J.
    Nature 412:607-614(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-609 IN COMPLEX WITH G22P2.

Entry informationi

Entry nameiXRCC6_HUMAN
AccessioniPrimary (citable) accession number: P12956
Secondary accession number(s): B1AHC8
, Q6FG89, Q9UCQ2, Q9UCQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Miscellaneous

Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC5 and XRCC6. Existence of a major autoantigenic epitope or epitopes on the C-terminal 190 amino acids of XRCC6 containing the leucine repeat. The majority of autoantibodies to XRCC6 in most sera from patients with SLE seem to be reactive with this region.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3