P13010 (XRCC5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
X-ray repair cross-complementing protein 5
EC=3.6.4.-

Alternative name(s):
86 kDa subunit of Ku antigen
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
Ku80
Ku86
Lupus Ku autoantigen protein p86
Nuclear factor IV
Thyroid-lupus autoantigen
Short name=TLAA
X-ray repair complementing defective repair in Chinese hamster cells 5 (double-strand-break rejoining)

Gene names

Name:	XRCC5
Synonyms:	G22P2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	732 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. 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. Ref.9 Ref.13 Ref.17 Ref.25
Subunit structure	Heterodimer of a 70 kDa and a 80 kDa 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 displays DNA binding activity towards the osteocalcin FGF response element (OCFRE). In addition, the 80 kDa subunit binds to the osteoblast-specific transcription factors MSX2 and RUNX2. Interacts with ELF3. May interact with APLF. The XRCC5/6 dimer associates in a DNA-dependent manner with APEX1. Ref.13 Ref.17 Ref.18 Ref.21 Ref.22
Subcellular location	Nucleus. Nucleus › nucleolus. Chromosome Ref.27.
Developmental stage	Expression increases during promyelocyte differentiation. Ref.10
Induction	In osteoblasts, by FGF2.
Domain	The EEXXXDDL motif is required for the interaction with catalytic subunit PRKDC and its recruitment to sites of DNA damage. Ref.20
Post-translational modification	Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity. Ref.16 Sumoylated. Ref.19 Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA damage, leading to its degradation and removal from DNA damage sites. Ref.28
Miscellaneous	Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC6 and XRCC5.
Sequence similarities	Belongs to the ku80 family. Contains 1 Ku domain.

Ontologies

Keywords
Biological process	DNA damage DNA recombination DNA repair Transcription Transcription regulation
Cellular component	Chromosome Nucleus
Coding sequence diversity	Polymorphism
Disease	Systemic lupus erythematosus
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Activator Helicase Hydrolase
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Traceable author statement PubMed 8073286. Source: ProtInc cell proliferation Inferred from electronic annotation. Source: Compara double-strand break repair via nonhomologous end joining Inferred from mutant phenotype Ref.25. Source: UniProtKB hematopoietic stem cell differentiation Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of transcription, DNA-dependent Inferred from mutant phenotype Ref.13. Source: UniProtKB positive regulation of neurogenesis Inferred from electronic annotation. Source: Compara telomere maintenance Traceable author statement PubMed 15824061. Source: BHF-UCL transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW viral reproduction Traceable author statement. Source: Reactome
Cellular_component	Ku70:Ku80 complex Inferred from direct assay Ref.25. Source: UniProtKB cytoplasm Inferred from electronic annotation. Source: Compara nonhomologous end joining complex Inferred from direct assay Ref.25. Source: UniProtKB nuclear telomere cap complex Traceable author statement PubMed 15100233. Source: BHF-UCL nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent DNA helicase activity Traceable author statement Ref.9. Source: ProtInc damaged DNA binding Inferred from electronic annotation. Source: InterPro double-stranded DNA binding Traceable author statement Ref.9. Source: ProtInc telomeric DNA binding Inferred from direct assay PubMed 10535943. Source: BHF-UCL transcription regulatory region DNA binding Inferred from direct assay PubMed 18809223. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
HOXB7	P09629	9	EBI-357997,EBI-1248457
PRKDC	P78527	6	EBI-357997,EBI-352053
XRCC6	P12956	8	EBI-357997,EBI-353208

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.9 Ref.10

Chain

2 – 732

731

X-ray repair cross-complementing protein 5

PRO_0000084340

Regions

Domain

251 – 460

210

Ku

Region

138 – 165

28

Leucine-zipper

Motif

720 – 728

9

EEXXXDL motif

Compositional bias

478 – 519

42

Pro-rich

Amino acid modifications

Modified residue

144

1

N6-acetyllysine Ref.24

Modified residue

265

1

N6-acetyllysine Ref.24

Modified residue

332

1

N6-acetyllysine Ref.24

Modified residue

577

1

Phosphoserine; by PRKDC Ref.16

Modified residue

579

1

Phosphoserine; by PRKDC Probable

Modified residue

580

1

Phosphoserine; by PRKDC Ref.16

Modified residue

660

1

N6-acetyllysine Ref.24

Modified residue

665

1

N6-acetyllysine Ref.24

Modified residue

715

1

Phosphothreonine; by PRKDC Probable

Natural variations

Natural variant

463

1

L → F.
Corresponds to variant rs1805380 [ dbSNP | Ensembl ].

VAR_014724

Natural variant

508

1

I → V.
Corresponds to variant rs2287558 [ dbSNP | Ensembl ].

VAR_053784

Experimental info

Mutagenesis

720 – 721

2

EE → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. Ref.20

Mutagenesis

726 – 727

2

DD → AA: Abolishes interaction with PRKDC and its recruitment to sites of DNA damage. Ref.20

Sequence conflict

14 – 16

3

MDV → YSY AA sequence Ref.10

Sequence conflict

117

1

V → A in BAF83429. Ref.3

Sequence conflict

134

1

I → V in BAD96323. Ref.4

Sequence conflict

178

1

R → S in BAD96323. Ref.4

Sequence conflict

315

1

R → L in CAA40736. Ref.11

Sequence conflict

461

1

M → R AA sequence Ref.10

Sequence conflict

479

1

T → G AA sequence Ref.10

Sequence conflict

540

1

I → T in BAF83429. Ref.3

Secondary structure

1

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732

Helix Strand Turn

Details...

Beta strand

8 – 15

8

Helix

18 – 21

4

Helix

30 – 47

18

Beta strand

53 – 60

8

Turn

70 – 72

3

Beta strand

77 – 84

8

Helix

88 – 95

8

Helix

107 – 121

15

Beta strand

122 – 125

4

Beta strand

128 – 135

8

Helix

144 – 146

3

Helix

147 – 156

10

Beta strand

159 – 167

9

Turn

194 – 196

3

Helix

199 – 216

18

Helix

218 – 223

6

Beta strand

224 – 226

3

Helix

227 – 230

4

Turn

235 – 237

3

Helix

238 – 240

3

Beta strand

247 – 253

7

Turn

254 – 256

3

Beta strand

257 – 267

11

Beta strand

277 – 280

4

Turn

281 – 283

3

Beta strand

289 – 301

13

Helix

307 – 309

3

Beta strand

310 – 316

7

Beta strand

319 – 322

4

Helix

325 – 331

7

Beta strand

338 – 347

10

Helix

348 – 350

3

Helix

353 – 355

3

Beta strand

357 – 366

10

Helix

371 – 386

16

Beta strand

389 – 401

13

Beta strand

404 – 412

9

Beta strand

417 – 423

7

Helix

427 – 429

3

Beta strand

438 – 440

3

Beta strand

442 – 444

3

Helix

448 – 460

13

Beta strand

464 – 467

4

Turn

468 – 471

4

Beta strand

474 – 476

3

Helix

479 – 481

3

Helix

485 – 499

15

Beta strand

501 – 503

3

Helix

510 – 516

7

Helix

520 – 536

17

Beta strand

581 – 586

6

Beta strand

588 – 592

5

Helix

594 – 601

8

Beta strand

603 – 605

3

Turn

608 – 610

3

Helix

611 – 626

16

Helix

629 – 649

21

Helix

652 – 667

16

Helix

673 – 680

8

Beta strand

691 – 693

3

Helix

698 – 701

4

Turn

702 – 704

3

Sequences

	Sequence		Length	Mass (Da)
	P13010 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2363CA84834E74A3	FASTA	732	82,705
	10 20 30 40 50 60 MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG 70 80 90 100 110 120 TDGTDNPLSG GDQYQNITVH RHLMLPDFDL LEDIESKIQP GSQQADFLDA LIVSMDVIQH 130 140 150 160 170 180 ETIGKKFEKR HIEIFTDLSS RFSKSQLDII IHSLKKCDIS LQFFLPFSLG KEDGSGDRGD 190 200 210 220 230 240 GPFRLGGHGP SFPLKGITEQ QKEGLEIVKM VMISLEGEDG LDEIYSFSES LRKLCVFKKI 250 260 270 280 290 300 ERHSIHWPCR LTIGSNLSIR IAAYKSILQE RVKKTWTVVD AKTLKKEDIQ KETVYCLNDD 310 320 330 340 350 360 DETEVLKEDI IQGFRYGSDI VPFSKVDEEQ MKYKSEGKCF SVLGFCKSSQ VQRRFFMGNQ 370 380 390 400 410 420 VLKVFAARDD EAAAVALSSL IHALDDLDMV AIVRYAYDKR ANPQVGVAFP HIKHNYECLV 430 440 450 460 470 480 YVQLPFMEDL RQYMFSSLKN SKKYAPTEAQ LNAVDALIDS MSLAKKDEKT DTLEDLFPTT 490 500 510 520 530 540 KIPNPRFQRL FQCLLHRALH PREPLPPIQQ HIWNMLNPPA EVTTKSQIPL SKIKTLFPLI 550 560 570 580 590 600 EAKKKDQVTA QEIFQDNHED GPTAKKLKTE QGGAHFSVSS LAEGSVTSVG SVNPAENFRV 610 620 630 640 650 660 LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS EEQRFNNFLK 670 680 690 700 710 720 ALQEKVEIKQ LNHFWEIVVQ DGITLITKEE ASGSSVTAEE AKKFLAPKDK PSGDTAAVFE 730 EGGDVDDLLD MI

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA-derived amino acid sequence of the 86-kDa subunit of the Ku antigen." Yaneva M., Wen J., Ayala A., Cook R. J. Biol. Chem. 264:13407-13411(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 4-22.
[2]	"Isolation and characterization of cDNA encoding the 80-kDa subunit protein of the human autoantigen Ku (p70/p80) recognized by autoantibodies from patients with scleroderma-polymyositis overlap syndrome." Mimori T., Ohosone Y., Hama N., Suwa A., Akizuki M., Homma M., Griffith A.J., Hardin J.A. Proc. Natl. Acad. Sci. U.S.A. 87:1777-1781(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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]. Tissue: Neuroblastoma.
[4]	Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S. Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Coronary artery.
[5]	NIEHS SNPs program Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Thyroid and Uterus.
[8]	"Purification and characterization of proximal sequence element-binding protein 1, a transcription activating protein related to Ku and TREF that binds the proximal sequence element of the human U1 promoter." Knuth M.W., Gunderson S.I., Thompson N.E., Strasheim L.A., Burgess R.R. J. Biol. Chem. 265:17911-17920(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-22.
[9]	"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 2-20, FUNCTION, INVOLVEMENT IN LUPUS ERYTHEMATOSUS.
[10]	"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 2-16; 98-113; 443-461 AND 473-479, DEVELOPMENTAL STAGE. Tissue: Cervix carcinoma.
[11]	"The autoantigen Ku is indistinguishable from NF IV, a protein forming multimeric protein-DNA complexes." Stuiver M.H., Coenjaerts F.E.J., van der Vlied P.C. J. Exp. Med. 172:1049-1054(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 105-732, PARTIAL PROTEIN SEQUENCE.
[12]	"DNA-dependent ATPase from HeLa cells is related to human Ku autoantigen." Cao Q.P., Pitt S., Leszyk J., Baril E.F. Biochemistry 33:8548-8557(1994) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 186-193; 317-326; 545-559 AND 656-661.
[13]	"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 526-531; 535-542 AND 704-708, FUNCTION, INTERACTION WITH APEX1.
[14]	"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 526-565 AND 709-732.
[15]	"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 534-542.
[16]	"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-577; SER-579; SER-580 AND THR-715.
[17]	"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 AND RUNX2. Tissue: Heart and Osteoblast.
[18]	"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.
[19]	"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates." Gocke C.B., Yu H., Kang J. J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[20]	"Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage." Falck J., Coates J., Jackson S.P. Nature 434:605-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: DOMAIN, MUTAGENESIS OF 720-GLU-GLU-721 AND 726-ASP-ASP-727.
[21]	"A novel human AP endonuclease with conserved zinc-finger-like motifs involved in DNA strand break responses." Kanno S., Kuzuoka H., Sasao S., Hong Z., Lan L., Nakajima S., Yasui A. EMBO J. 26:2094-2103(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APLF.
[22]	"APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks." Iles N., Rulten S., El-Khamisy S.F., Caldecott K.W. Mol. Cell. Biol. 27:3793-3803(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APLF.
[23]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[24]	"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-144; LYS-265; LYS-332; LYS-660 AND LYS-665, MASS SPECTROMETRY.
[25]	"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.
[26]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[27]	"Systematic analysis of protein pools, isoforms, and modifications affecting turnover and subcellular localization." Ahmad Y., Boisvert F.M., Lundberg E., Uhlen M., Lamond A.I. Mol. Cell. Proteomics 11:M111.013680.01-M111.013680.15(2012) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[28]	"The E3 ligase RNF8 regulates KU80 removal and NHEJ repair." Feng L., Chen J. Nat. Struct. Mol. Biol. 19:201-206(2012) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY RNF8.
[29]	"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 7-565 IN COMPLEX WITH XRCC6.
+	Additional computationally mapped references.

Web resources

NIEHS SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

J04977 mRNA. Translation: AAA59475.1.
M30938 mRNA. Translation: AAA36154.1.
AK290740 mRNA. Translation: BAF83429.1.
AK222603 mRNA. Translation: BAD96323.1.
DQ787434 Genomic DNA. Translation: ABG46942.1.
CH471063 Genomic DNA. Translation: EAW70562.1.
BC019027 mRNA. Translation: AAH19027.1.
BC095442 mRNA. Translation: AAH95442.1.
X57500 mRNA. Translation: CAA40736.1.

IPI

IPI00220834.

PIR

A32626. A35051.
D42397.
S62889.

RefSeq

NP_066964.1. NM_021141.3.

UniGene

Hs.388739.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEQ	X-ray	2.70	B	1-565	[»]
1JEY	X-ray	2.50	B	1-565	[»]
1Q2Z	NMR	-	A	592-708	[»]
1RW2	NMR	-	A	566-709	[»]
3RZ9	X-ray	2.29	B	559-571	[»]

ProteinModelPortal

P13010.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31379N.

IntAct

P13010. 38 interactions.

MINT

MINT-131739.

STRING

9606.ENSP00000329528.

PTM databases

PhosphoSite

P13010.

Polymorphism databases

DMDM

125731.

2D gel databases

SWISS-2DPAGE

P13010.

Proteomic databases

PaxDb

P13010.

PRIDE

P13010.

Protocols and materials databases

DNASU

7520.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000392132; ENSP00000375977; ENSG00000079246.
ENST00000392133; ENSP00000375978; ENSG00000079246.

GeneID

7520.

KEGG

hsa:7520.

UCSC

uc002vfy.3. human.

Organism-specific databases

CTD

7520.

GeneCards

GC02P216972.

HGNC

HGNC:12833. XRCC5.

HPA

CAB004468.
HPA025813.

MIM

194364. gene.

neXtProt

NX_P13010.

PharmGKB

PA37425.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG299744.

HOVERGEN

HBG006237.

InParanoid

P13010.

KO

K10885.

OMA

HRALHPQ.

OrthoDB

EOG4NZTSV.

PhylomeDB

P13010.

Enzyme and pathway databases

Pathway_Interaction_DB

bard1pathway. BARD1 signaling events.
ar_pathway. Coregulation of Androgen receptor activity.
telomerasepathway. Regulation of Telomerase.

Reactome

REACT_116125. Disease.
REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

P13010.

Bgee

P13010.

CleanEx

HS_XRCC5.

Genevestigator

P13010.

GermOnline

ENSG00000079246. Homo sapiens.

Family and domain databases

Gene3D

1.10.1600.10. 1 hit.
1.25.40.240. 1 hit.
2.40.290.10. 1 hit.

InterPro

IPR006164. 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]

PANTHER

PTHR12604:SF3. PTHR12604:SF3. 1 hit.

Pfam

PF02735. Ku. 1 hit.
PF03730. Ku_C. 1 hit.
PF03731. Ku_N. 1 hit.
PF08785. Ku_PK_bind. 1 hit.
[Graphical view]

PIRSF

PIRSF016570. Ku80. 1 hit.

SMART

SM00559. Ku78. 1 hit.
SM00327. VWA. 1 hit.
[Graphical view]

SUPFAM

SSF101420. Ku_PK_bind. 1 hit.
SSF100939. SPOC-like. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

XRCC5. human.

EvolutionaryTrace

P13010.

GenomeRNAi

7520.

NextBio

29431.

PMAP-CutDB

P13010.

SOURCE

Search...

Entry information

Entry name

XRCC5_HUMAN

Accession

Primary (citable) accession number: P13010
Secondary accession number(s): A8K3X5 , Q0Z7V0, Q4VBQ5, Q53HH7, Q7M4N0, Q9UCQ0, Q9UCQ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 155 of the entry and version 3 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.