P12956 (XRCC6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	XRCC6
Synonyms:	G22P1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein 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. 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. Ref.2 Ref.10 Ref.12 Ref.14 Ref.19 Ref.27 Ref.28
Subunit structure	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. Ref.10 Ref.14 Ref.17 Ref.18 Ref.19 Ref.21 Ref.27
Subcellular location	Nucleus. Chromosome.
Developmental stage	Expression does not increase during promyelocyte differentiation. Ref.9
Induction	In osteoblasts, by FGF2.
Post-translational modification	Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-51 does not affect DNA repair.
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.
Sequence similarities	Belongs to the ku70 family. Contains 1 Ku domain. Contains 1 SAP domain.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Disease	Systemic lupus erythematosus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase Lyase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	DNA ligation Traceable author statement. Source: ProtInc double-strand break repair via nonhomologous end joining Inferred from mutant phenotype Ref.28. Source: UniProtKB initiation of viral infection Traceable author statement. Source: Reactome negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.10. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from mutant phenotype. Source: BHF-UCL provirus integration Traceable author statement. Source: Reactome telomere maintenance Traceable author statement. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	DNA-dependent protein kinase-DNA ligase 4 complex Inferred from electronic annotation. Source: InterPro Ku70:Ku80 complex Inferred from direct assay Ref.28. Source: UniProtKB membrane fraction Traceable author statement. Source: ProtInc nuclear telomere cap complex Traceable author statement. Source: BHF-UCL transcription factor complex Inferred from direct assay Ref.19. Source: UniProtKB
Molecular function	5'-deoxyribose-5-phosphate lyase activity Inferred from mutant phenotype Ref.28. Source: UniProtKB ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement. Source: ProtInc double-stranded DNA binding Traceable author statement. Source: ProtInc protein C-terminus binding Inferred from physical interaction. Source: UniProtKB transcription regulatory region DNA binding Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ARAP1	Q96P48	2	EBI-353208,EBI-710003
HTT	P42858	3	EBI-353208,EBI-466029
NDRG1	Q92597	2	EBI-353208,EBI-716486
TCF7L2	Q9NQB0	9	EBI-353208,EBI-924724
TP53	P04637	2	EBI-353208,EBI-366083
WRN	Q14191	7	EBI-353208,EBI-368417
XRCC5	P13010	8	EBI-353208,EBI-357997

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 609

608

X-ray repair cross-complementing protein 6

PRO_0000210179

Regions

Domain

261 – 468

208

Ku

Domain

573 – 607

35

SAP

Compositional bias

2 – 61

60

Ser-rich (potentially targets for phosphorylation)

Compositional bias

11 – 29

19

Asp/Glu-rich (acidic)

Compositional bias

330 – 342

13

Asp/Glu-rich (acidic)

Sites

Active site

31

1

Schiff-base intermediate with DNA; for 5'-deoxyribose-5-phosphate lyase activity Probable

Amino acid modifications

Modified residue

2

1

N-acetylserine Potential

Modified residue

6

1

Phosphoserine; by PRKDC Ref.15

Modified residue

27

1

Phosphoserine Ref.22

Modified residue

31

1

N6-acetyllysine Ref.26

Modified residue

51

1

Phosphoserine; by PRKDC Ref.13

Modified residue

222

1

Phosphoserine Ref.23

Modified residue

331

1

N6-acetyllysine Ref.26

Modified residue

338

1

N6-acetyllysine Ref.26

Modified residue

455

1

Phosphothreonine Ref.24 Ref.25

Modified residue

461

1

N6-acetyllysine Ref.26

Modified residue

468

1

N6-acetyllysine Ref.26

Modified residue

520

1

Phosphoserine Ref.25

Experimental info

Mutagenesis

31

1

K → A: Diminishes the ability to form a Schiff base. Abolishes adduct formation; when associated with A-160 and A-164. Ref.28

Mutagenesis

160

1

K → A: Abolishes adduct formation; when associated with A-31 and A-160. Ref.28

Mutagenesis

164

1

K → A: Abolishes adduct formation; when associated with A-31 and A-164. Ref.28

Sequence conflict

20

1

Q → D AA sequence Ref.8

Sequence conflict

101

1

N → K AA sequence Ref.9

Sequence conflict

103

1

Y → L AA sequence Ref.9

Sequence conflict

116

1

I → S AA sequence Ref.9

Sequence conflict

125

1

Q → S AA sequence Ref.9

Sequence conflict

181

1

A → T in CAG47015. Ref.4

Secondary structure

1

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609

Helix Strand Turn

Details...

Beta strand

36 – 43

8

Helix

47 – 49

3

Beta strand

53 – 56

4

Helix

59 – 76

18

Beta strand

82 – 89

8

Beta strand

100 – 109

10

Helix

113 – 120

8

Helix

124 – 134

11

Helix

143 – 155

13

Beta strand

162 – 171

10

Helix

182 – 196

15

Beta strand

198 – 205

8

Helix

213 – 215

3

Helix

217 – 219

3

Helix

239 – 250

12

Beta strand

256 – 266

11

Beta strand

268 – 274

7

Turn

290 – 292

3

Beta strand

295 – 304

10

Turn

305 – 307

3

Helix

313 – 315

3

Beta strand

316 – 321

6

Beta strand

326 – 329

4

Helix

331 – 336

6

Beta strand

343 – 352

10

Helix

353 – 355

3

Beta strand

366 – 370

5

Turn

372 – 374

3

Helix

378 – 392

15

Beta strand

394 – 401

8

Beta strand

403 – 405

3

Beta strand

409 – 416

8

Beta strand

426 – 428

3

Beta strand

430 – 436

7

Helix

440 – 442

3

Helix

456 – 468

13

Helix

481 – 494

14

Helix

511 – 518

8

Helix

521 – 529

9

Helix

561 – 569

9

Helix

573 – 575

3

Helix

578 – 587

10

Helix

596 – 607

12

Sequences

	Sequence		Length	Mass (Da)
	P12956 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: BBD3CD434526DFCB	FASTA	609	69,843
	10 20 30 40 50 60 MSGWESYYKT EGDEEAEEEQ EENLEASGDY KYSGRDSLIF LVDASKAMFE SQSEDELTPF 70 80 90 100 110 120 DMSIQCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK NIYVLQELDN PGAKRILELD 130 140 150 160 170 180 QFKGQQGQKR FQDMMGHGSD YSLSEVLWVC ANLFSDVQFK MSHKRIMLFT NEDNPHGNDS 190 200 210 220 230 240 AKASRARTKA GDLRDTGIFL DLMHLKKPGG FDISLFYRDI ISIAEDEDLR VHFEESSKLE 250 260 270 280 290 300 DLLRKVRAKE TRKRALSRLK LKLNKDIVIS VGIYNLVQKA LKPPPIKLYR ETNEPVKTKT 310 320 330 340 350 360 RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF KPLVLLKKHH 370 380 390 400 410 420 YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY TPRRNIPPYF VALVPQEEEL 430 440 450 460 470 480 DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE KIMATPEQVG KMKAIVEKLR FTYRSDSFEN 490 500 510 520 530 540 PVLQQHFRNL EALALDLMEP EQAVDLTLPK VEAMNKRLGS LVDEFKELVY PPDYNPEGKV 550 560 570 580 590 600 TKRKHDNEGS GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL KSGLKKQELL EALTKHFQD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 2917966] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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: 2466842] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 1608402] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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].
[5]	NIEHS SNPs program Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	"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: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Kidney, Lung, Placenta and Skin.
[8]	"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: 1537839] [Abstract] Cited for: PROTEIN SEQUENCE OF 10-30 AND 299-317.
[9]	"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: 8605992] [Abstract] Cited for: PROTEIN SEQUENCE OF 101-114 AND 116-125, DEVELOPMENTAL STAGE. Tissue: Cervix carcinoma.
[10]	"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: 8621488] [Abstract] Cited for: PROTEIN SEQUENCE OF 288-293 AND 300-312, FUNCTION, INTERACTION WITH APEX1.
[11]	"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: 7882982] [Abstract] Cited for: PROTEIN SEQUENCE OF 301-308 AND 556-565.
[12]	"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: 7957065] [Abstract] Cited for: PROTEIN SEQUENCE OF 346-352, FUNCTION.
[13]	"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: 9362500] [Abstract] Cited for: PHOSPHORYLATION AT SER-51.
[14]	"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: 9742108] [Abstract] Cited for: FUNCTION, INTERACTION WITH PRKDC.
[15]	"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: 10026262] [Abstract] Cited for: PHOSPHORYLATION AT SER-6.
[16]	"Ku, a DNA repair protein with multiple cellular functions?" Featherstone C., Jackson S.P. Mutat. Res. 434:3-15(1999) [PubMed: 10377944] [Abstract] Cited for: REVIEW.
[17]	"Isolation of Ku70-binding proteins (KUBs)." Yang C.-R., Yeh S.-Y., Leskov K., Odegaard E., Hsu H.L., Chang C., Kinsella T.J., Chen D.J., Boothman D.A. Nucleic Acids Res. 27:2165-2174(1999) [PubMed: 10219089] [Abstract] Cited for: INTERACTION WITH XRCC6BP1. Tissue: Liver.
[18]	"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: 12509254] [Abstract] Cited for: INTERACTION WITH PRKDC.
[19]	"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: 12145306] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH NAA15; MSX2; RUNX2 AND DLX5. Tissue: Heart and Osteoblast.
[20]	"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: 12547193] [Abstract] Cited for: IDENTIFICATION IN A COMPLEX WITH G22P2; PRKDC AND XRCC4, PHOSPHORYLATION.
[21]	"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: 15075319] [Abstract] Cited for: INTERACTION WITH ELF3.
[22]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[23]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, MASS SPECTROMETRY. Tissue: Hepatoma.
[24]	"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: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[25]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-520, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[26]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338; LYS-461 AND LYS-468, MASS SPECTROMETRY.
[27]	"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: 20493174] [Abstract] Cited for: FUNCTION IN DNA REPAIR, INTERACTION WITH CDK9.
[28]	"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: 20383123] [Abstract] Cited for: FUNCTION AS A 5'-DRP LYASE, MUTAGENESIS OF LYS-31; LYS-160 AND LYS-164.
[29]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[30]	"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: 11457852] [Abstract] Cited for: STRUCTURE BY NMR OF 557-610.
[31]	"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: 11493912] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 36-609 IN COMPLEX WITH G22P2.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04607 mRNA. Translation: AAA61177.1.
J04611 mRNA. Translation: AAA51733.1.
M32865 mRNA. Translation: AAA36155.1.
S38729 mRNA. Translation: AAB22381.1.
CR542219 mRNA. Translation: CAG47015.1.
AY870329 Genomic DNA. Translation: AAW34364.1.
Z83840 Genomic DNA. Translation: CAB46206.1.
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.

IPI

IPI00644712.

PIR

A30894. A30299.

RefSeq

NP_001460.1. NM_001469.3.

UniGene

Hs.292493.

3D structure databases

PDBe
RCSB PDB
PDBj

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	536-609	[»]
3RZX	X-ray	2.61	B	537-558	[»]

ProteinModelPortal

P12956.

SMR

P12956. Positions 34-609.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-24188N.

IntAct

P12956. 75 interactions.

MINT

MINT-1416738.

STRING

P12956.

PTM databases

PhosphoSite

P12956.

Polymorphism databases

DMDM

125729.

2D gel databases

SWISS-2DPAGE

P12956.

Proteomic databases

PRIDE

P12956.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000359308; ENSP00000352257; ENSG00000196419.
ENST00000360079; ENSP00000353192; ENSG00000196419.
ENST00000405878; ENSP00000384257; ENSG00000196419.

GeneID

2547.

KEGG

hsa:2547.

UCSC

uc003bao.1. human.

Organism-specific databases

CTD

2547.

GeneCards

GC22P042017.

H-InvDB

HIX0016526.
HIX0147981.

HGNC

HGNC:4055. XRCC6.

HPA

CAB004254.

MIM

152690. gene.

neXtProt

NX_P12956.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12401.

HOGENOM

HBG600453.

HOVERGEN

HBG006236.

InParanoid

P12956.

OMA

VCRYTPR.

OrthoDB

EOG451DQB.

PhylomeDB

P12956.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.
ar_pathway. Coregulation of Androgen receptor activity.
telomerasepathway. Regulation of Telomerase.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Reactome

REACT_216. DNA Repair.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P12956.

Bgee

P12956.

CleanEx

HS_XRCC6.

Genevestigator

P12956.

GermOnline

ENSG00000196419. Homo sapiens.

Family and domain databases

InterPro

IPR006164. DNA_helicase_ATP-dep_Ku.
IPR006165. DNA_helicase_ATP-dep_Ku70.
IPR005160. Ku_C.
IPR005161. Ku_N.
IPR003034. SAP_DNA-bd.
IPR016194. SPOC-like.
[Graphical view]

Gene3D

G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.
G3DSA:2.40.290.10. G3DSA:2.40.290.10. 1 hit.
G3DSA:1.10.1600.10. Ku_C. 1 hit.

KO

K10884.

Pfam

PF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]

PIRSF

PIRSF003033. Ku70. 1 hit.

SMART

SM00559. Ku78. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]

SUPFAM

SSF100939. SPOC-like. 1 hit.

TIGRFAMs

TIGR00578. Ku70. 1 hit.

PROSITE

PS50800. SAP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

10043.

PMAP-CutDB

P12956.

SOURCE

Search...

Entry information

Entry name

XRCC6_HUMAN

Accession

Primary (citable) accession number: P12956
Secondary accession number(s): Q6FG89, Q9UCQ2, Q9UCQ3

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 153 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.