UniProt Accession

 B1AHC8_HUMAN; B1AHC8 

Genbank Protein ID

 Z83840; AK055786; CH471095 

Genbank Nucleotide ID

 BAG51575.1; EAW60448.1 

Protein Name

 X-ray repair complementing defective repair in Chinese hamster cells 6 (Ku autoantigen, 70kDa), isoform CRA_b 

Protein Synonyms/Alias

 X-ray repair cross-complementing protein 6; cDNA FLJ31224 fis, clone KIDNE2004305, highly similar to ATP-dependent DNA helicase 2 subunit 1 (EC 3.6.1.-) 

Gene Name

 XRCC6 

Gene Synonyms/Alias

 hCG_2013151 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
31	LEASGDYKYSGRDSL	ubiquitination	[1, 2, 3]
73	ELDNPGAKRILELDQ	ubiquitination	[3]
82	ILELDQFKGQQGQKR	ubiquitination	[1, 2, 4, 5, 6, 7]
88	FKGQQGQKRFQDMMG	ubiquitination	[6]
141	PHGNDSAKASRARTK	acetylation	[8]
141	PHGNDSAKASRARTK	ubiquitination	[1, 2, 3, 5, 6, 7]
148	KASRARTKAGDLRDT	ubiquitination	[6]
165	FLDLMHLKKPGGFDI	ubiquitination	[4]
166	LDLMHLKKPGGFDIS	ubiquitination	[2, 6]
197	VHFEESSKLEDLLRK	ubiquitination	[1, 2, 4, 7]
241	NLVQKALKPPPIKLY	acetylation	[7]
241	NLVQKALKPPPIKLY	ubiquitination	[1, 6]
246	ALKPPPIKLYRETNE	acetylation	[7]
246	ALKPPPIKLYRETNE	ubiquitination	[2, 4, 6, 7]
256	RETNEPVKTKTRTFN	ubiquitination	[1]
276	LLLPSDTKRSQIYGS	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
290	SRQIILEKEETEELK	acetylation	[7, 8, 9]
290	SRQIILEKEETEELK	ubiquitination	[1, 2, 6, 7]
297	KEETEELKRFDDPGL	acetylation	[7, 9]
297	KEETEELKRFDDPGL	ubiquitination	[1, 2, 3, 6, 7]
310	GLMLMGFKPLVLLKK	ubiquitination	[1, 3, 4, 6]
316	FKPLVLLKKHHYLRP	ubiquitination	[1, 2, 3, 4, 6, 7]
317	KPLVLLKKHHYLRPS	ubiquitination	[6, 7]
351	LLIKCLEKEVAALCR	ubiquitination	[6]
402	FLPFADDKRKMPFTE	ubiquitination	[1, 2, 3, 4, 6]
404	PFADDKRKMPFTEKI	ubiquitination	[4, 6, 7]
410	RKMPFTEKIMATPEQ	ubiquitination	[1, 2, 3, 4, 6]
420	ATPEQVGKMKAIVEK	acetylation	[7, 8, 9]
420	ATPEQVGKMKAIVEK	ubiquitination	[1, 2, 3, 6, 7]
427	KMKAIVEKLRFTYRS	acetylation	[9]
427	KMKAIVEKLRFTYRS	ubiquitination	[1, 6, 7]
475	PKVEAMNKRLGSLVD	ubiquitination	[1]
485	GSLVDEFKELVYPPD	ubiquitination	[1, 2, 3, 6]
498	PDYNPEGKVTKRKHD	ubiquitination	[1, 6]
501	NPEGKVTKRKHDNEG	ubiquitination	[6]
512	DNEGSGSKRPKVEYS	ubiquitination	[1]
515	GSGSKRPKVEYSEEE	ubiquitination	[1, 3, 6, 7]
524	EYSEEELKTHISKGT	ubiquitination	[1, 2, 4, 6, 7]
529	ELKTHISKGTLGKFT	acetylation	[7]
529	ELKTHISKGTLGKFT	ubiquitination	[6, 7]
534	ISKGTLGKFTVPMLK	ubiquitination	[1, 3, 4, 6]
541	KFTVPMLKEACRAYG	ubiquitination	[6]
550	ACRAYGLKSGLKKQE	ubiquitination	[5, 6]
554	YGLKSGLKKQELLEA	ubiquitination	[6]
555	GLKSGLKKQELLEAL	ubiquitination	[1]
564	ELLEALTKHFQD***	acetylation	[10]
564	ELLEALTKHFQD***	ubiquitination	[1, 2, 4, 6]

Reference

 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [6] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [7] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [8] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [9] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [10] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224] 

Functional Description

  

Sequence Annotation

  

Keyword

 ATP-binding; Complete proteome; Helicase; Hydrolase; Nucleotide-binding; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 568 AA 

Protein Sequence

Gene Ontology

 GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
 GO:0004003; F:ATP-dependent DNA helicase activity; IEA:InterPro.
 GO:0003684; F:damaged DNA binding; IEA:InterPro.
 GO:0042162; F:telomeric DNA binding; IEA:InterPro.
 GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
 GO:0000723; P:telomere maintenance; IEA:InterPro. 

Interpro

 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. 

Pfam

 PF02735; Ku
 PF03730; Ku_C
 PF03731; Ku_N
 PF02037; SAP 

SMART

 SM00559; Ku78
 SM00513; SAP 

PROSITE

 PS50800; SAP 

PRINTS