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P23475

- XRCC6_MOUSE

UniProt

P23475 - XRCC6_MOUSE

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Protein

X-ray repair cross-complementing protein 6

Gene

Xrcc6

Organism
Mus musculus (Mouse)
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.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei29 – 291Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activityBy similarity

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: InterPro
  4. damaged DNA binding Source: InterPro
  5. double-stranded telomeric DNA binding Source: Ensembl
  6. poly(A) RNA binding Source: Ensembl
  7. transcription regulatory region DNA binding Source: Ensembl

GO - Biological processi

  1. brain development Source: Ensembl
  2. cellular hyperosmotic salinity response Source: Ensembl
  3. cellular response to DNA damage stimulus Source: MGI
  4. cellular response to X-ray Source: Ensembl
  5. double-strand break repair Source: MGI
  6. double-strand break repair via nonhomologous end joining Source: UniProtKB
  7. negative regulation of transcription, DNA-templated Source: UniProtKB
  8. positive regulation of neurogenesis Source: MGI
  9. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  10. response to ionizing radiation Source: MGI
  11. telomere maintenance Source: InterPro
  12. transcription, DNA-templated Source: UniProtKB-KW
  13. V(D)J recombination Source: MGI
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_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

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/AP lyase Ku70
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
Ku autoantigen protein p70 homolog
Short name:
Ku70
Gene namesi
Name:Xrcc6
Synonyms:G22p1, Ku70
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:95606. Xrcc6.

Subcellular locationi

GO - Cellular componenti

  1. chromosome Source: UniProtKB-KW
  2. cytoplasm Source: MGI
  3. Ku70:Ku80 complex Source: UniProtKB
  4. nonhomologous end joining complex Source: UniProtKB
  5. nucleolus Source: Ensembl
  6. nucleus Source: MGI
  7. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 608607X-ray repair cross-complementing protein 6PRO_0000210180Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei6 – 61Phosphoserine; by PRKDCBy similarity
Modified residuei29 – 291N6-acetyllysineBy similarity
Modified residuei49 – 491Phosphoserine; by PRKDCBy similarity
Modified residuei329 – 3291N6-acetyllysineBy similarity
Modified residuei336 – 3361N6-acetyllysineBy similarity
Modified residuei459 – 4591N6-acetyllysineBy similarity
Modified residuei475 – 4751PhosphoserineBy similarity
Modified residuei518 – 5181PhosphoserineBy similarity
Modified residuei548 – 5481PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-49 does not affect DNA repair (By similarity).By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP23475.
PaxDbiP23475.
PRIDEiP23475.

PTM databases

PhosphoSiteiP23475.

Expressioni

Developmental stagei

Expression increases during promyelocyte differentiation.1 Publication

Gene expression databases

BgeeiP23475.
ExpressionAtlasiP23475. baseline and differential.
GenevestigatoriP23475.

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. Binds to CDK9 (By similarity). 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 similarity). Interacts with CLU.By similarity1 Publication

Protein-protein interaction databases

BioGridi199785. 4 interactions.
IntActiP23475. 4 interactions.
MINTiMINT-2568472.

Structurei

3D structure databases

ProteinModelPortaliP23475.
SMRiP23475. Positions 32-606.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini259 – 466208KuAdd
BLAST
Domaini571 – 60535SAPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni548 – 60760Interaction with DEAF1By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi11 – 2717Asp/Glu-rich (acidic)Add
BLAST
Compositional biasi328 – 34013Asp/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.
HOVERGENiHBG006236.
InParanoidiP23475.
KOiK10884.
OrthoDBiEOG7QG43F.
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.
SM00327. VWA. 1 hit.
[Graphical view]
SUPFAMiSSF100939. SSF100939. 1 hit.
SSF53300. SSF53300. 1 hit.
TIGRFAMsiTIGR00578. ku70. 1 hit.
PROSITEiPS50800. SAP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P23475-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEWESYYKT EGEEEEEEEE SPDTGGEYKY SGRDSLIFLV DASRAMFESQ
60 70 80 90 100
GEDELTPFDM SIQCIQSVYT SKIISSDRDL LAVVFYGTEK DKNSVNFKNI
110 120 130 140 150
YVLQDLDNPG AKRVLELDQF KGQQGKKHFR DTVGHGSDYS LSEVLWVCAN
160 170 180 190 200
LFSDVQLKMS HKRIMLFTNE DDPHGRDSAK ASRARTKASD LRDTGIFLDL
210 220 230 240 250
MHLKKPGGFD VSVFYRDIIT TAEDEDLGVH FEESSKLEDL LRKVRAKETK
260 270 280 290 300
KRVLSRLKFK LGEDVVLMVG IYNLVQKANK PFPVRLYRET NEPVKTKTRT
310 320 330 340 350
FNVNTGSLLL PSDTKRSLTY GTRQIVLEKE ETEELKRFDE PGLILMGFKP
360 370 380 390 400
TVMLKKQHYL RPSLFVYPEE SLVSGSSTLF SALLTKCVEK KVIAVCRYTP
410 420 430 440 450
RKNVSPYFVA LVPQEEELDD QNIQVTPGGF QLVFLPYADD KRKVPFTEKV
460 470 480 490 500
TANQEQIDKM KAIVQKLRFT YRSDSFENPV LQQHFRNLEA LALDMMESEQ
510 520 530 540 550
VVDLTLPKVE AIKKRLGSLA DEFKELVYPP GYNPEGKVAK RKQDDEGSTS
560 570 580 590 600
KKPKVELSEE ELKAHFRKGT LGKLTVPTLK DICKAHGLKS GPKKQELLDA

LIRHLEKN
Length:608
Mass (Da):69,484
Last modified:February 5, 2008 - v5
Checksum:i1C27DBF1DB7A1154
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti225 – 2251E → G in BAE27139. (PubMed:16141072)Curated
Sequence conflicti225 – 2251E → G in BAE27137. (PubMed:16141072)Curated
Sequence conflicti225 – 2251E → G in BAE27135. (PubMed:16141072)Curated
Sequence conflicti391 – 3911K → E in BAE25441. (PubMed:11471062)Curated
Sequence conflicti391 – 3911K → E in AAL90775. (PubMed:11471062)Curated
Sequence conflicti391 – 3911K → E in AAL90774. (PubMed:11471062)Curated
Sequence conflicti400 – 4001P → H in AAA39396. (PubMed:1701785)Curated
Sequence conflicti466 – 4672KL → NV in AAC52675. (PubMed:8661113)Curated
Sequence conflicti466 – 4672KL → NV in AAA39396. (PubMed:1701785)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50378
, U50367, U50368, U50369, U50370, U50371, U50372, U50373, U50374, U50375, U50376, U50377 Genomic DNA. Translation: AAC52675.1.
U34878 Genomic DNA. Translation: AAC53575.1.
AB010282 mRNA. Translation: BAA28874.1.
AF483500 mRNA. Translation: AAL90774.1.
AF483501 mRNA. Translation: AAL90775.1.
AK143570 mRNA. Translation: BAE25441.1.
AK146392 mRNA. Translation: BAE27135.1.
AK146394 mRNA. Translation: BAE27137.1.
AK146396 mRNA. Translation: BAE27139.1.
BC031422 mRNA. Translation: AAH31422.1.
Z14157 mRNA. Translation: CAA78526.1.
M38700 mRNA. Translation: AAA39396.1.
CCDSiCCDS37153.1.
PIRiA43534.
S25149.
RefSeqiNP_034377.2. NM_010247.2.
XP_006520503.1. XM_006520440.1.
XP_006520504.1. XM_006520441.1.
XP_006520505.1. XM_006520442.1.
XP_006520506.1. XM_006520443.1.
UniGeneiMm.288809.

Genome annotation databases

EnsembliENSMUST00000069530; ENSMUSP00000068559; ENSMUSG00000022471.
ENSMUST00000100399; ENSMUSP00000097968; ENSMUSG00000022471.
GeneIDi14375.
KEGGimmu:14375.
UCSCiuc007wxy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U50378
, U50367 , U50368 , U50369 , U50370 , U50371 , U50372 , U50373 , U50374 , U50375 , U50376 , U50377 Genomic DNA. Translation: AAC52675.1 .
U34878 Genomic DNA. Translation: AAC53575.1 .
AB010282 mRNA. Translation: BAA28874.1 .
AF483500 mRNA. Translation: AAL90774.1 .
AF483501 mRNA. Translation: AAL90775.1 .
AK143570 mRNA. Translation: BAE25441.1 .
AK146392 mRNA. Translation: BAE27135.1 .
AK146394 mRNA. Translation: BAE27137.1 .
AK146396 mRNA. Translation: BAE27139.1 .
BC031422 mRNA. Translation: AAH31422.1 .
Z14157 mRNA. Translation: CAA78526.1 .
M38700 mRNA. Translation: AAA39396.1 .
CCDSi CCDS37153.1.
PIRi A43534.
S25149.
RefSeqi NP_034377.2. NM_010247.2.
XP_006520503.1. XM_006520440.1.
XP_006520504.1. XM_006520441.1.
XP_006520505.1. XM_006520442.1.
XP_006520506.1. XM_006520443.1.
UniGenei Mm.288809.

3D structure databases

ProteinModelPortali P23475.
SMRi P23475. Positions 32-606.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199785. 4 interactions.
IntActi P23475. 4 interactions.
MINTi MINT-2568472.

PTM databases

PhosphoSitei P23475.

Proteomic databases

MaxQBi P23475.
PaxDbi P23475.
PRIDEi P23475.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000069530 ; ENSMUSP00000068559 ; ENSMUSG00000022471 .
ENSMUST00000100399 ; ENSMUSP00000097968 ; ENSMUSG00000022471 .
GeneIDi 14375.
KEGGi mmu:14375.
UCSCi uc007wxy.1. mouse.

Organism-specific databases

CTDi 2547.
MGIi MGI:95606. Xrcc6.

Phylogenomic databases

eggNOGi NOG305318.
GeneTreei ENSGT00390000001422.
HOVERGENi HBG006236.
InParanoidi P23475.
KOi K10884.
OrthoDBi EOG7QG43F.
TreeFami TF315101.

Enzyme and pathway databases

Reactomei REACT_196447. IRF3-mediated induction of type I IFN.
REACT_224809. Processing of DNA ends prior to end rejoining.
REACT_254501. Nonhomologous End-joining (NHEJ).

Miscellaneous databases

NextBioi 285869.
PROi P23475.
SOURCEi Search...

Gene expression databases

Bgeei P23475.
ExpressionAtlasi P23475. baseline and differential.
Genevestigatori P23475.

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.
SM00327. VWA. 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. "Genomic structure and chromosomal assignment of the mouse Ku70 gene."
    Takiguchi Y., Kurimasa A., Chen F., Pardington P.E., Kuriyama T., Okinaka R.T., Moyzis R., Chen D.J.
    Genomics 35:129-135(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129.
  2. "Murine cell line SX9 bearing a mutation in the DNA-PKcs gene exhibits aberrant V(D)J recombination not only in the coding joint but also in the signal joint."
    Fukumura R., Araki R., Fujimori A., Mori M., Saito T., Watanabe F., Sarashi M., Itsukaichi H., Eguch-Kasai K., Sato K., Tatsumi K., Abe M.
    J. Biol. Chem. 273:13058-13064(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Mammary carcinoma.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: ILS and ISS.
  4. "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: C57BL/6J and DBA/2.
    Tissue: Spleen.
  5. "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].
    Tissue: Mammary tumor.
  6. "Nucleotide sequence of the 5' region of the murine p70 Ku autoantigen cDNA."
    Baughman G.A., Nemeth J.E., Bourgeois S.
    Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-46.
    Strain: BALB/c.
    Tissue: Thymus.
  7. "Antigenic determinants of the Ku (p70/p80) autoantigen are poorly conserved between species."
    Porges A.J., Ng T., Reeves W.H.
    J. Immunol. 145:4222-4228(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 18-608.
  8. "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.
  9. "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: FUNCTION.
    Tissue: Osteoblast.
  10. "Synthesis and functional analyses of nuclear clusterin, a cell death protein."
    Leskov K.S., Klokov D.Y., Li J., Kinsella T.J., Boothman D.A.
    J. Biol. Chem. 278:11590-11600(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLU.

Entry informationi

Entry nameiXRCC6_MOUSE
AccessioniPrimary (citable) accession number: P23475
Secondary accession number(s): O88212
, Q3UJL8, Q62027, Q62382, Q62453, Q6GTV8, Q8QZX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: February 5, 2008
Last modified: November 26, 2014
This is version 141 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

In osteoblasts from XRCC6 knockout mice, osteocalcin gene expression is nearly abolished.

Keywords - Technical termi

Complete proteome, Multifunctional enzyme, 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

External Data

Dasty 3