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Ku80 (XRCC5)

Protein FULL name:

X-ray repair cross-complementing protein 5, X-ray repair complementing defective repair in Chinese hamster cells 5, ATP-dependent DNA helicase 2 subunit 2, ATP-dependent DNA helicase II 80 kDa subunit, Lupus Ku autoantigen protein p86, 86 kDa subunit of Ku antigen, Ku86, Ku80, Thyroid-lupus autoantigen, CTC box-binding factor 85 kDa subunit, Nuclear factor IV, DNA repair protein XRCC5


Protein SHORT name:

TLAA, CTCBF, CTC85, G22P2, Ku80, Ku86


Ku80 (XRCC5) (Homo sapiens) is product of expression of XRCC5 gene.


Ku80 (XRCC5) is involved in:

NHEJ in Homo sapiens
     


Keywords:



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.

SUBUNIT: 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.

INTERACTION: P09629:HOXB7; NbExp=1; IntAct=EBI-357997, EBI-1248457; P12956:XRCC6; NbExp=1; IntAct=EBI-357997, EBI-353208;

SUBCELLULAR LOCATION: Nucleus.

DEVELOPMENTAL STAGE: Expression increases during promyelocyte differentiation.

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.

PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity.

PTM: Sumoylated.

MISCELLANEOUS: Individuals with systemic lupus erythematosus (SLE) and related disorders produce extremely large amounts of autoantibodies to XRCC6 and XRCC5.

SIMILARITY: Belongs to the ku80 family.

SIMILARITY: Contains 1 Ku domain.

WEB RESOURCE: Name=NIEHS SNPs; [LINK]


NCBI GenPept GI number(s): 125731
10863945
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P13010 P13010
PFAM: PF02735
PF03730
PF03731
PF08785
PF02735
PF03730
PF03731
PF08785
InterPro: IPR006164
IPR005160
IPR005161
IPR014893
IPR016194
IPR002035
IPR006164
IPR005160
IPR005161
IPR014893
IPR016194
IPR002035
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MVRSGNKAAVVLCMDVGFTMSNSIPGIESPFEQAKKVITMFVQRQVFAEN
KDEIALVLFGTDGTDNPLSGGDQYQNITVHRHLMLPDFDLLEDIESKIQP
GSQQADFLDALIVSMDVIQHETIGKKFEKRHIEIFTDLSSRFSKSQLDII
IHSLKKCDISLQFFLPFSLGKEDGSGDRGDGPFRLGGHGPSFPLKGITEQ
QKEGLEIVKMVMISLEGEDGLDEIYSFSESLRKLCVFKKIERHSIHWPCR
LTIGSNLSIRIAAYKSILQERVKKTWTVVDAKTLKKEDIQKETVYCLNDD
DETEVLKEDIIQGFRYGSDIVPFSKVDEEQMKYKSEGKCFSVLGFCKSSQ
VQRRFFMGNQVLKVFAARDDEAAAVALSSLIHALDDLDMVAIVRYAYDKR
ANPQVGVAFPHIKHNYECLVYVQLPFMEDLRQYMFSSLKNSKKYAPTEAQ
LNAVDALIDSMSLAKKDEKTDTLEDLFPTTKIPNPRFQRLFQCLLHRALH
PREPLPPIQQHIWNMLNPPAEVTTKSQIPLSKIKTLFPLIEAKKKDQVTA
QEIFQDNHEDGPTAKKLKTEQGGAHFSVSSLAEGSVTSVGSVNPAENFRV
LVKQKKASFEEASNQLINHIEQFLDTNETPYFMKSIDCIRAFREEAIKFS
EEQRFNNFLKALQEKVEIKQLNHFWEIVVQDGITLITKEEASGSSVTAEE
AKKFLAPKDKPSGDTAAVFEEGGDVDDLLDMI

Ku80 (XRCC5) (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
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 Aug. 15, 1989
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 AJ, Hardin JA Proc Natl Acad Sci U S A March 1, 1990
The autoantigen Ku is indistinguishable from NF IV, a protein forming multimeric protein-DNA complexes. Stuiver MH, Coenjaerts FE, van der Vliet PC J Exp Med Oct. 1, 1990
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 MW, Gunderson SI, Thompson NE, Strasheim LA, Burgess RR J Biol Chem Oct. 15, 1990
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 OM, Deisseroth A J Biol Chem March 5, 1992
DNA-dependent ATPase from HeLa cells is related to human Ku autoantigen. Cao QP, Pitt S, Leszyk J, Baril EF Biochemistry July 19, 1994
Human DNA helicase II: a novel DNA unwinding enzyme identified as the Ku autoantigen. Tuteja N, Tuteja R, Ochem A, Taneja P, Huang NW, Simoncsits A, Susic S, Rahman K, Marusic L, Chen J, et al. EMBO J Oct. 17, 1994
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, Kuhn K, Poschl E EMBO J Jan. 15, 1995
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 MJ, Jost JP FEBS Lett March 18, 1996
DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer. Chan DW, Ye R, Veillette CJ, Lees-Miller SP Biochemistry Jan. 9, 1999
Structure of the Ku heterodimer bound to DNA and its implications for double-strand break repair. Walker JR, Corpina RA, Goldberg J Nature Aug. 9, 2001
Regulation of osteocalcin gene expression by a novel Ku antigen transcription factor complex. Willis DM, Loewy AP, Charlton-Kachigian N, Shao JS, Ornitz DM, Towler DA J Biol Chem Oct. 4, 2002
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 TO, 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 Feb. 1, 2004
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 JY, Libermann TA, Oettgen P J Biol Chem June 11, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates. Gocke CB, Yu H, Kang J J Biol Chem Jan. 11, 2005
Conserved modes of recruitment of ATM, ATR and DNA-PKcs to sites of DNA damage. Falck J, Coates J, Jackson SP Nature March 31, 2005
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 April 18, 2007
APLF (C2orf13) is a novel human protein involved in the cellular response to chromosomal DNA strand breaks. Iles N, Rulten S, El-Khamisy SF, Caldecott KW Mol Cell Biol May 1, 2007
Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK Sci Signal Jan. 1, 2009
Lysine acetylation targets protein complexes and co-regulates major cellular functions. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M Science Aug. 14, 2009
Ku is a 5'-dRP/AP lyase that excises nucleotide damage near broken ends. Roberts SA, Strande N, Burkhalter MD, Strom C, Havener JM, Hasty P, Ramsden DA Nature April 22, 2010


Last modification of this entry: Oct. 12, 2010.

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