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PRKDC

Protein FULL name:

DNA-dependent protein kinase catalytic subunit, DNPK1, p460.,


Protein SHORT name:

DNA-PK catalytic subunit DNA-PKcs


PRKDC (Homo sapiens) is product of expression of PRKDC gene.


PRKDC is involved in:

NHEJ in Homo sapiens




FUNCTION: Serine/threonine-protein kinase that acts as a molecular sensor for DNA damage. Involved in DNA nonhomologous end joining (NHEJ) required for double-strand break (DSB) repair and V(D)J recombination. Must be bound to DNA to express its catalytic properties. Promotes processing of hairpin DNA structures in V(D)J recombination by activation of the hairpin endonuclease artemis (DCLRE1C). The assembly of the DNA-PK complex at DNA ends is also required for the NHEJ ligation step. Required to protect and align broken ends of DNA. May also act as a scaffold protein to aid the localization of DNA repair proteins to the site of damage. Found at the ends of chromosomes, suggesting a further role in the maintenance of telomeric stability and the prevention of chromosomal end fusion. Also involved in modulation of transcription. Recognizes the substrate consensus sequence [ST]-Q. Phosphorylates 'Ser-139' of histone variant H2AX/H2AFX, thereby regulating DNA damage response mechanism. Phosphorylates DCLRE1C, c-Abl/ABL1, histone H1, HSPCA, c-jun/JUN, p53/TP53, PARP1, POU2F1, DHX9, SRF, XRCC1, XRCC1, XRCC4, XRCC5, XRCC6, WRN, MYC and RFA2. Can phosphorylate C1D not only in the presence of linear DNA but also in the presence of supercoiled DNA. Ability to phosphorylate TP53/p53 in the presence of supercoiled DNA is dependent on C1D.

CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein.

ENZYME REGULATION: Inhibited by wortmannin. Activity of the enzyme seems to be attenuated by autophosphorylation.

SUBUNIT: DNA-PK is a heterotrimer of PRKDC and the Ku p70-p86 (XRCC6-XRCC5) dimer. Formation of this complex may be promoted by interaction with ILF3. Associates with the DNA-bound Ku heterodimer, but it can also bind to and be activated by free DNA. Interacts with DNA-PKcs-interacting protein (KIP) with the region upstream the kinase domain. PRKDC alone also interacts with and phosphorylates DCLRE1C, thereby activating the latent endonuclease activity of this protein. Interacts with C1D. Interacts with TTI1 and TELO2.

INTERACTION: O43918:AIRE; NbExp=1; IntAct=EBI-352053, EBI-1753081; P42575:CASP2; NbExp=2; IntAct=EBI-352053, EBI-520342; P09629:HOXB7; NbExp=1; IntAct=EBI-352053, EBI-1248457; Q9HB75:LRDD; NbExp=5; IntAct=EBI-352053, EBI-520427;

SUBCELLULAR LOCATION: Nucleus.

PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. Autophosphorylated on Thr-2609, Thr-2638 and Thr-2647. Thr-2609 is a DNA damage-inducible phosphorylation site (inducible with ionizing radiation, IR). Autophosphorylation induces a conformational change that leads to remodeling of the DNA-PK complex, requisite for efficient end processing and DNA repair.

SIMILARITY: Belongs to the PI3/PI4-kinase family.

SIMILARITY: Contains 1 FAT domain.

SIMILARITY: Contains 1 FATC domain.

SIMILARITY: Contains 2 HEAT repeats.

SIMILARITY: Contains 1 PI3K/PI4K domain.

SIMILARITY: Contains 3 TPR repeats.

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 38258929
9188646
13654237
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P78527 P78527
PFAM: PF02259
PF02260
PF08163
PF00454
PF02259
PF02260
PF08163
PF00454
InterPro: IPR016024
IPR003152
IPR011009
IPR012582
IPR000403
IPR018936
IPR003151
IPR014009
IPR016024
IPR003152
IPR011009
IPR012582
IPR000403
IPR018936
IPR003151
IPR014009
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MAGSGAGVRCSLLRLQETLSAADRCGAALAGHQLIRGLGQECVLSSSPAV
LALQTSLVFSRDFGLLVFVRKSLNSIEFRECREEILKFLCIFLEKMGQKI
APYSVEIKNTCTSVYTKDRAAKCKIPALDLLIKLLQTFRSSRLMDEFKIG
ELFSKFYGELALKKKIPDTVLEKVYELLGLLGEVHPSEMINNAENLFRAF
LGELKTQMTSAVREPKLPVLAGCLKGLSSLLCNFTKSMEEDPQTSREIFN
FVLKAIRPQIDLKRYAVPSAGLRLFALHASQFSTCLLDNYVSLFEVLLKW
CAHTNVELKKAALSALESFLKQVSNMVAKNAEMHKNKLQYFMEQFYGIIR
NVDSNNKELSIAIRGYGLFAGPCKVINAKDVDFMYVELIQRCKQMFLTQT
DTGDDRVYQMPSFLQSVASVLLYLDTVPEVYTPVLEHLVVMQIDSFPQYS
PKMQLVCCRAIVKVFLALAAKGPVLRNCISTVVHQGLIRICSKPVVLPKG
PESESEDHRASGEVRTGKWKVPTYKDYVDLFRHLLSSDQMMDSILADEAF
FSVNSSSESLNHLLYDEFVKSVLKIVEKLDLTLEIQTVGEQENGDEAPGV
WMIPTSDPAANLHPAKPKDFSAFINLVEFCREILPEKQAEFFEPWVYSFS
YELILQSTRLPLISGFYKLLSITVRNAKKIKYFEGVSPKSLKHSPEDPEK
YSCFALFVKFGKEVAVKMKQYKDELLASCLTFLLSLPHNIIELDVRAYVP
ALQMAFKLGLSYTPLAEVGLNALEEWSIYIDRHVMQPYYKDILPCLDGYL
KTSALSDETKNNWEVSALSRAAQKGFNKVVLKHLKKTKNLSSNEAISLEE
IRIRVVQMLGSLGGQINKNLLTVTSSDEMMKSYVAWDREKRLSFAVPFRE
MKPVIFLDVFLPRVTELALTASDRQTKVAACELLHSMVMFMLGKATQMPE
GGQGAPPMYQLYKRTFPVLLRLACDVDQVTRQLYEPLVMQLIHWFTNNKK
FESQDTVALLEAILDGIVDPVDSTLRDFCGRCIREFLKWSIKQITPQQQE
KSPVNTKSLFKRLYSLALHPNAFKRLGASLAFNNIYREFREEESLVEQFV
FEALVIYMESLALAHADEKSLGTIQQCCDAIDHLCRIIEKKHVSLNKAKK
RRLPRGFPPSASLCLLDLVKWLLAHCGRPQTECRHKSIELFYKFVPLLPG
NRSPNLWLKDVLKEEGVSFLINTFEGGGCGQPSGILAQPTLLYLRGPFSL
QATLCWLDLLLAALECYNTFIGERTVGALQVLGTEAQSSLLKAVAFFLES
IAMHDIIAAEKCFGTGAAGNRTSPQEGERYNYSKCTVVVRIMEFTTTLLN
TSPEGWKLLKKDLCNTHLMRVLVQTLCEPASIGFNIGDVQVMAHLPDVCV
NLMKALKMSPYKDILETHLREKITAQSIEELCAVNLYGPDAQVDRSRLAA
VVSACKQLHRAGLLHNILPSQSTDLHHSVGTELLSLVYKGIAPGDERQCL
PSLDLSCKQLASGLLELAFAFGGLCERLVSLLLNPAVLSTASLGSSQGSV
IHFSHGEYFYSLFSETINTELLKNLDLAVLELMQSSVDNTKMVSAVLNGM
LDQSFRERANQKHQGLKLATTILQHWKKCDSWWAKDSPLETKMAVLALLA
KILQIDSSVSFNTSHGSFPEVFTTYISLLADTKLDLHLKGQAVTLLPFFT
SLTGGSLEELRRVLEQLIVAHFPMQSREFPPGTPRFNNYVDCMKKFLDAL
ELSQSPMLLELMTEVLCREQQHVMEELFQSSFRRIARRGSCVTQVGLLES
VYEMFRKDDPRLSFTRQSFVDRSLLTLLWHCSLDALREFFSTIVVDAIDV
LKSRFTKLNESTFDTQITKKMGYYKILDVMYSRLPKDDVHAKESKINQVF
HGSCITEGNELTKTLIKLCYDAFTENMAGENQLLERRRLYHCAAYNCAIS
VICCVFNELKFYQGFLFSEKPEKNLLIFENLIDLKRRYNFPVEVEVPMER
KKKYIEIRKEAREAANGDSDGPSYMSSLSYLADSTLSEEMSQFDFSTGVQ
SYSYSSQDPRPATGRFRRREQRDPTVHDDVLELEMDELNRHECMAPLTAL
VKHMHRSLGPPQGEEDSVPRDLPSWMKFLHGKLGNPIVPLNIRLFLAKLV
INTEEVFRPYAKHWLSPLLQLAASENNGGEGIHYMVVEIVATILSWTGLA
TPTGVPKDEVLANRLLNFLMKHVFHPKRAVFRHNLEIIKTLVECWKDCLS
IPYRLIFEKFSGKDPNSKDNSVGIQLLGIVMANDLPPYDPQCGIQSSEYF
QALVNNMSFVRYKEVYAAAAEVLGLILRYVMERKNILEESLCELVAKQLK
QHQNTMEDKFIVCLNKVTKSFPPLADRFMNAVFFLLPKFHGVLKTLCLEV
VLCRVEGMTELYFQLKSKDFVQVMRHRDDERQKVCLDIIYKMMPKLKPVE
LRELLNPVVEFVSHPSTTCREQMYNILMWIHDNYRDPESETDNDSQEIFK
LAKDVLIQGLIDENPGLQLIIRNFWSHETRLPSNTLDRLLALNSLYSPKI
EVHFLSLATNFLLEMTSMSPDYPNPMFEHPLSECEFQEYTIDSDWRFRST
VLTPMFVETQASQGTLQTRTQEGSLSARWPVAGQIRATQQQHDFTLTQTA
DGRSSFDWLTGSSTDPLVDHTSPSSDSLLFAHKRSERLQRAPLKSVGPDF
GKKRLGLPGDEVDNKVKGAAGRTDLLRLRRRFMRDQEKLSLMYARKGVAE
QKREKEIKSELKMKQDAQVVLYRSYRHGDLPDIQIKHSSLITPLQAVAQR
DPIIAKQLFSSLFSGILKEMDKFKTLSEKNNITQKLLQDFNRFLNTTFSF
FPPFVSCIQDISCQHAALLSLDPAAVSAGCLASLQQPVGIRLLEEALLRL
LPAELPAKRVRGKARLPPDVLRWVELAKLYRSIGEYDVLRGIFTSEIGTK
QITQSALLAEARSDYSEAAKQYDEALNKQDWVDGEPTEAEKDFWELASLD
CYNHLAEWKSLEYCSTASIDSENPPDLNKIWSEPFYQETYLPYMIRSKLK
LLLQGEADQSLLTFIDKAMHGELQKAILELHYSQELSLLYLLQDDVDRAK
YYIQNGIQSFMQNYSSIDVLLHQSRLTKLQSVQALTEIQEFISFISKQGN
LSSQVPLKRLLNTWTNRYPDAKMDPMNIWDDIITNRCFFLSKIEEKLTPL
PEDNSMNVDQDGDPSDRMEVQEQEEDISSLIRSCKFSMKMKMIDSARKQN
NFSLAMKLLKELHKESKTRDDWLVSWVQSYCRLSHCRSRSQGCSEQVLTV
LKTVSLLDENNVSSYLSKNILAFRDQNILLGTTYRIIANALSSEPACLAE
IEEDKARRILELSGSSSEDSEKVIAGLYQRAFQHLSEAVQAAEEEAQPPS
WSCGPAAGVIDAYMTLADFCDQQLRKEEENASVIDSAELQAYPALVVEKM
LKALKLNSNEARLKFPRLLQIIERYPEETLSLMTKEISSVPCWQFISWIS
HMVALLDKDQAVAVQHSVEEITDNYPQAIVYPFIISSESYSFKDTSTGHK
NKEFVARIKSKLDQGGVIQDFINALDQLSNPELLFKDWSNDVRAELAKTP
VNKKNIEKMYERMYAALGDPKAPGLGAFRRKFIQTFGKEFDKHFGKGGSK
LLRMKLSDFNDITNMLLLKMNKDSKPPGNLKECSPWMSDFKVEFLRNELE
IPGQYDGRGKPLPEYHVRIAGFDERVTVMASLRRPKRIIIRGHDEREHPF
LVKGGEDLRQDQRVEQLFQVMNGILAQDSACSQRALQLRTYSVVPMTSRL
GLIEWLENTVTLKDLLLNTMSQEEKAAYLSDPRAPPCEYKDWLTKMSGKH
DVGAYMLMYKGANRTETVTSFRKRESKVPADLLKRAFVRMSTSPEAFLAL
RSHFASSHALICISHWILGIGDRHLNNFMVAMETGGVIGIDFGHAFGSAT
QFLPVPELMPFRLTRQFINLMLPMKETGLMYSIMVHALRAFRSDPGLLTN
TMDVFVKEPSFDWKNFEQKMLKKGGSWIQEINVAEKNWYPRQKICYAKRK
LAGANPAVITCDELLLGHEKAPAFRDYVAVARGSKDHNIRAQEPESGLSE
ETQVKCLMDQATDPNILGRTWEGWEPWM

PRKDC (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
The human double-stranded DNA-activated protein kinase phosphorylates the 90-kDa heat-shock protein, hsp90 alpha at two NH2-terminal threonine residues. Lees-Miller SP, Anderson CW J Biol Chem Oct. 15, 1989
A DNA-activated protein kinase from HeLa cell nuclei. Carter T, Vancurova I, Sun I, Lou W, DeLeon S Mol Cell Biol Dec. 1, 1990
DNA-activated protein kinase in Raji Burkitt's lymphoma cells. Phosphorylation of c-Myc oncoprotein. Iijima S, Teraoka H, Date T, Tsukada K Eur J Biochem June 1, 1992
c-Jun is phosphorylated by the DNA-dependent protein kinase in vitro; definition of the minimal kinase recognition motif. Bannister AJ, Gottlieb TM, Kouzarides T, Jackson SP Nucleic Acids Res March 11, 1993
The carboxyl-terminal transactivation domain of human serum response factor contains DNA-activated protein kinase phosphorylation sites. Liu SH, Ma JT, Yueh AY, Lees-Miller SP, Anderson CW, Ng SY J Biol Chem Oct. 5, 1993
Gene for the catalytic subunit of the human DNA-activated protein kinase maps to the site of the XRCC7 gene on chromosome 8. Sipley JD, Menninger JC, Hartley KO, Ward DC, Jackson SP, Anderson CW Proc Natl Acad Sci U S A Aug. 1, 1995
DNA-dependent protein kinase catalytic subunit: a relative of phosphatidylinositol 3-kinase and the ataxia telangiectasia gene product. Hartley KO, Gell D, Smith GC, Zhang H, Divecha N, Connelly MA, Admon A, Lees-Miller SP, Anderson CW, Jackson SP Cell Sept. 8, 1995
Human DNA-activated protein kinase (DNA-PK) is homologous to phosphatidylinositol kinases. Poltoratsky VP, Shi X, York JD, Lieber MR, Carter TH J Immunol Nov. 15, 1995
CPP32/Yama/apopain cleaves the catalytic component of DNA-dependent protein kinase in the holoenzyme. Teraoka H, Yumoto Y, Watanabe F, Tsukada K, Suwa A, Enari M, Nagata S FEBS Lett Sept. 9, 1996
Alternate splice-site utilization in the gene for the catalytic subunit of the DNA-activated protein kinase, DNA-PKcs. Connelly MA, Zhang H, Kieleczawa J, Anderson CW Gene Oct. 10, 1996
MCM4 and PRKDC, human genes encoding proteins MCM4 and DNA-PKcs, are close neighbours located on chromosome 8q12-->q13. Ladenburger EM, Fackelmayer FO, Hameister H, Knippers R Cytogenet Cell Genet Jan. 1, 1997
Mapping of amino acid residues in the p34 subunit of human single-stranded DNA-binding protein phosphorylated by DNA-dependent protein kinase and Cdc2 kinase in vitro. Niu H, Erdjument-Bromage H, Pan ZQ, Lee SH, Tempst P, Hurwitz J J Biol Chem May 9, 1997
Interaction between DNA-dependent protein kinase and a novel protein, KIP. Wu X, Lieber MR Mutat Res Oct. 1, 1997
DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Shieh SY, Ikeda M, Taya Y, Prives C Cell Oct. 31, 1997
Double-strand break repair by Ku70 requires heterodimerization with Ku80 and DNA binding functions. Jin S, Weaver DT EMBO J Nov. 17, 1997
DNA-dependent protein kinase: DNA binding and activation in the absence of Ku. Hammarsten O, Chu G Proc Natl Acad Sci U S A Feb. 20, 1998
DNA-dependent protein kinase interacts with antigen receptor response element binding proteins NF90 and NF45. Ting NS, Kao PN, Chan DW, Lintott LG, Lees-Miller SP J Biol Chem Feb. 23, 1998
DNA end-independent activation of DNA-PK mediated via association with the DNA-binding protein C1D. Yavuzer U, Smith GC, Bliss T, Werner D, Jackson SP Genes Dev July 15, 1998
Inhibition of phosphoinositide 3-kinase related kinases by the radiosensitizing agent wortmannin. Sarkaria JN, Tibbetts RS, Busby EC, Kennedy AP, Hill DE, Abraham RT Cancer Res Oct. 1, 1998
DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer. Chan DW, Ye R, Veillette CJ, Lees-Miller SP Biochemistry Jan. 9, 1999
Suppression of the poly(ADP-ribose) polymerase activity by DNA-dependent protein kinase in vitro. Ariumi Y, Masutani M, Copeland TD, Mimori T, Sugimura T, Shimotohno K, Ueda K, Hatanaka M, Noda M Oncogene Aug. 12, 1999
Frameshift mutation in PRKDC, the gene for DNA-PKcs, in the DNA repair-defective, human, glioma-derived cell line M059J. Anderson CW, Dunn JJ, Freimuth PI, Galloway AM, Allalunis-Turner MJ Radiat Res July 1, 2001
Hairpin opening and overhang processing by an Artemis/DNA-dependent protein kinase complex in nonhomologous end joining and V(D)J recombination. Ma Y, Pannicke U, Schwarz K, Lieber MR Cell March 22, 2002
Defining interactions between DNA-PK and ligase IV/XRCC4. Hsu HL, Yannone SM, Chen DJ DNA Repair (Amst) March 28, 2002
Werner protein is a target of DNA-dependent protein kinase in vivo and in vitro, and its catalytic activities are regulated by phosphorylation. Karmakar P, Piotrowski J, Brosh RM Jr, Sommers JA, Miller SP, Cheng WH, Snowden CM, Ramsden DA, Bohr VA J Biol Chem May 24, 2002
Autophosphorylation of the DNA-dependent protein kinase catalytic subunit is required for rejoining of DNA double-strand breaks. Chan DW, Chen BP, Prithivirajsingh S, Kurimasa A, Story MD, Qin J, Chen DJ Genes Dev Sept. 15, 2002
Identification of in vitro and in vivo phosphorylation sites in the catalytic subunit of the DNA-dependent protein kinase. Douglas P, Sapkota GP, Morrice N, Yu Y, Goodarzi AA, Merkle D, Meek K, Alessi DR, Lees-Miller SP Biochem J Nov. 15, 2002
Threonines 2638/2647 in DNA-PK are essential for cellular resistance to ionizing radiation. Soubeyrand S, Pope L, Pakuts B, Hache RJ Cancer Res March 15, 2003
Down-regulation of histone H2B by DNA-dependent protein kinase in response to DNA damage through modulation of octamer transcription factor 1. Schild-Poulter C, Shih A, Yarymowich NC, Hache RJ Cancer Res Nov. 1, 2003
DNA-PK is activated by nucleosomes and phosphorylates H2AX within the nucleosomes in an acetylation-dependent manner. Park EJ, Chan DW, Park JH, Oettinger MA, Kwon J Nucleic Acids Res Dec. 1, 2003
DNA-dependent protein kinase (DNA-PK) phosphorylates nuclear DNA helicase II/RNA helicase A and hnRNP proteins in an RNA-dependent manner. Zhang S, Schlott B, Gorlach M, Grosse F Nucleic Acids Res Jan. 1, 2004
The metallo-beta-lactamase/beta-CASP domain of Artemis constitutes the catalytic core for V(D)J recombination. Poinsignon C, Moshous D, Callebaut I, de Chasseval R, Villey I, de Villartay JP J Exp Med Jan. 2, 2004
Functional and biochemical dissection of the structure-specific nuclease ARTEMIS. Pannicke U, Ma Y, Hopfner KP, Niewolik D, Lieber MR, Schwarz K EMBO J May 5, 2004
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
Artemis is a phosphorylation target of ATM and ATR and is involved in the G2/M DNA damage checkpoint response. Zhang X, Succi J, Feng Z, Prithivirajsingh S, Story MD, Legerski RJ Mol Cell Biol Oct. 1, 2004
A biochemically defined system for mammalian nonhomologous DNA end joining. Ma Y, Lu H, Tippin B, Goodman MF, Shimazaki N, Koiwai O, Hsieh CL, Schwarz K, Lieber MR Mol Cell Dec. 3, 2004
The life and death of DNA-PK. Collis SJ, DeWeese TL, Jeggo PA, Parker AR Oncogene Jan. 3, 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
Artemis deficiency confers a DNA double-strand break repair defect and Artemis phosphorylation status is altered by DNA damage and cell cycle progression. Wang J, Pluth JM, Cooper PK, Cowan MJ, Chen DJ, Yannone SM DNA Repair (Amst) May 2, 2005
The Artemis:DNA-PKcs endonuclease cleaves DNA loops, flaps, and gaps. Ma Y, Schwarz K, Lieber MR DNA Repair (Amst) July 12, 2005
DNA-PK is responsible for enhanced phosphorylation of histone H2AX under hypertonic conditions. Reitsema T, Klokov D, Banath JP, Olive PL DNA Repair (Amst) Sept. 28, 2005
XRCC1 is phosphorylated by DNA-dependent protein kinase in response to DNA damage. Levy N, Martz A, Bresson A, Spenlehauer C, de Murcia G, Menissier-de Murcia J Nucleic Acids Res Jan. 1, 2006
Phosphoproteome analysis of the human mitotic spindle. Nousiainen M, Sillje HH, Sauer G, Nigg EA, Korner R Proc Natl Acad Sci U S A April 4, 2006
Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M Cell Nov. 3, 2006
Patterns of somatic mutation in human cancer genomes. Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR Nature March 8, 2007
ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ Science May 25, 2007
Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ Cell Dec. 14, 2007
A quantitative atlas of mitotic phosphorylation. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP Proc Natl Acad Sci U S A Aug. 5, 2008
Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M Mol Cell Aug. 8, 2008
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
Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S Anal Chem June 1, 2009
Large-scale proteomics analysis of the human kinome. Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H Mol Cell Proteomics July 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
Tti1 and Tel2 are critical factors in mammalian target of rapamycin complex assembly. Kaizuka T, Hara T, Oshiro N, Kikkawa U, Yonezawa K, Takehana K, Iemura S, Natsume T, Mizushima N J Biol Chem June 25, 2010


Last modification of this entry: Oct. 6, 2010.

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