CPLM-010427

Genbank Nucleotide ID

DNA-dependent protein kinase catalytic subunit

Protein Synonyms/Alias

DNA-PK catalytic subunit; DNA-PKcs; DNPK1; p460

Homo sapiens (Human)

Position	Peptide	Type	References
71	GLLVFVRKSLNSIEF	ubiquitination	[1]
99	FLEKMGQKIAPYSVE	ubiquitination	[1, 2]
108	APYSVEIKNTCTSVY	ubiquitination	[1, 3, 4]
117	TCTSVYTKDRAAKCK	acetylation	[5]
117	TCTSVYTKDRAAKCK	ubiquitination	[1, 2, 6, 7]
122	YTKDRAAKCKIPALD	ubiquitination	[1]
124	KDRAAKCKIPALDLL	ubiquitination	[1]
148	SRLMDEFKIGELFSK	ubiquitination	[1, 2]
155	KIGELFSKFYGELAL	ubiquitination	[1, 2]
163	FYGELALKKKIPDTV	ubiquitination	[1, 2]
164	YGELALKKKIPDTVL	ubiquitination	[1]
165	GELALKKKIPDTVLE	ubiquitination	[1]
205	RAFLGELKTQMTSAV	ubiquitination	[1, 2, 3, 4]
216	TSAVREPKLPVLAGC	ubiquitination	[1]
225	PVLAGCLKGLSSLLC	ubiquitination	[2]
236	SLLCNFTKSMEEDPQ	ubiquitination	[1, 6, 7]
254	EIFNFVLKAIRPQID	acetylation	[5]
254	EIFNFVLKAIRPQID	ubiquitination	[1, 2, 3, 4, 6]
263	IRPQIDLKRYAVPSA	ubiquitination	[1, 2, 3, 4, 6, 7]
310	HTNVELKKAALSALE	ubiquitination	[1, 2, 3, 4]
329	QVSNMVAKNAEMHKN	ubiquitination	[2]
337	NAEMHKNKLQYFMEQ	ubiquitination	[2]
357	RNVDSNNKELSIAIR	ubiquitination	[1, 2, 3, 4, 8]
374	GLFAGPCKVINAKDV	ubiquitination	[1, 6]
379	PCKVINAKDVDFMYV	ubiquitination	[1, 2]
393	VELIQRCKQMFLTQT	ubiquitination	[1]
471	VFLALAAKGPVLRNC	ubiquitination	[1, 2, 3, 4, 6]
493	GLIRICSKPVVLPKG	ubiquitination	[1, 6, 7]
499	SKPVVLPKGPESESE	ubiquitination	[1]
520	EVRTGKWKVPTYKDY	ubiquitination	[1]
525	KWKVPTYKDYVDLFR	ubiquitination	[1, 2, 3, 4, 6, 8]
574	EFVKSVLKIVEKLDL	ubiquitination	[1, 2]
668	PLISGFYKLLSITVR	ubiquitination	[2]
679	ITVRNAKKIKYFEGV	ubiquitination	[1]
681	VRNAKKIKYFEGVSP	ubiquitination	[1, 2, 3, 4]
689	YFEGVSPKSLKHSPE	ubiquitination	[1, 2, 3, 4, 6, 7]
692	GVSPKSLKHSPEDPE	ubiquitination	[1, 2]
700	HSPEDPEKYSCFALF	ubiquitination	[1]
712	ALFVKFGKEVAVKMK	ubiquitination	[1, 2]
717	FGKEVAVKMKQYKDE	ubiquitination	[1, 2]
790	HVMQPYYKDILPCLD	ubiquitination	[1]
801	PCLDGYLKTSALSDE	ubiquitination	[1, 3, 4, 6]
810	SALSDETKNNWEVSA	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
824	ALSRAAQKGFNKVVL	ubiquitination	[1]
828	AAQKGFNKVVLKHLK	acetylation	[5]
828	AAQKGFNKVVLKHLK	ubiquitination	[1, 7]
832	GFNKVVLKHLKKTKN	acetylation	[5]
832	GFNKVVLKHLKKTKN	ubiquitination	[1, 3, 4]
836	VVLKHLKKTKNLSSN	ubiquitination	[1]
838	LKHLKKTKNLSSNEA	ubiquitination	[1, 2, 3, 4, 7, 8]
868	SLGGQINKNLLTVTS	ubiquitination	[1, 2, 7]
881	TSSDEMMKSYVAWDR	ubiquitination	[1, 2]
890	YVAWDREKRLSFAVP	ubiquitination	[1]
902	AVPFREMKPVIFLDV	ubiquitination	[1, 2]
927	TASDRQTKVAACELL	ubiquitination	[2]
963	PPMYQLYKRTFPVLL	ubiquitination	[1, 2, 3, 4, 6, 7]
1038	RCIREFLKWSIKQIT	ubiquitination	[1, 3, 4]
1042	EFLKWSIKQITPQQQ	ubiquitination	[1, 2, 3, 4, 6, 7]
1051	ITPQQQEKSPVNTKS	ubiquitination	[1, 2, 7]
1057	EKSPVNTKSLFKRLY	acetylation	[5]
1057	EKSPVNTKSLFKRLY	ubiquitination	[1, 2, 6, 7]
1074	ALHPNAFKRLGASLA	ubiquitination	[1, 2, 3, 4, 8]
1147	KKHVSLNKAKKRRLP	ubiquitination	[7]
1150	VSLNKAKKRRLPRGF	methylation	[9]
1186	PQTECRHKSIELFYK	ubiquitination	[1, 2]
1193	KSIELFYKFVPLLPG	ubiquitination	[1, 2, 6]
1209	RSPNLWLKDVLKEEG	acetylation	[5]
1209	RSPNLWLKDVLKEEG	ubiquitination	[1, 2, 3, 4, 8]
1311	HDIIAAEKCFGTGAA	ubiquitination	[2]
1334	GERYNYSKCTVVVRI	ubiquitination	[1, 2, 6, 7]
1357	NTSPEGWKLLKKDLC	ubiquitination	[1, 2]
1360	PEGWKLLKKDLCNTH	ubiquitination	[1]
1361	EGWKLLKKDLCNTHL	ubiquitination	[1]
1407	VNLMKALKMSPYKDI	ubiquitination	[1, 2]
1412	ALKMSPYKDILETHL	ubiquitination	[1, 2, 3, 4]
1422	LETHLREKITAQSIE	ubiquitination	[1, 6, 7]
1456	AAVVSACKQLHRAGL	ubiquitination	[1, 2, 6, 7, 8]
1489	ELLSLVYKGIAPGDE	ubiquitination	[1, 2]
1612	FRERANQKHQGLKLA	ubiquitination	[2]
1617	NQKHQGLKLATTILQ	ubiquitination	[1]
1627	TTILQHWKKCDSWWA	ubiquitination	[1, 2, 3, 4]
1628	TILQHWKKCDSWWAK	ubiquitination	[1]
1635	KCDSWWAKDSPLETK	ubiquitination	[1]
1642	KDSPLETKMAVLALL	ubiquitination	[1, 2]
1744	NNYVDCMKKFLDALE	ubiquitination	[1, 7]
1807	SVYEMFRKDDPRLSF	ubiquitination	[1]
1857	VLKSRFTKLNESTFD	ubiquitination	[1, 2, 3, 4, 7]
1869	TFDTQITKKMGYYKI	ubiquitination	[1, 2, 3, 4, 7]
1870	FDTQITKKMGYYKIL	ubiquitination	[1]
1875	TKKMGYYKILDVMYS	ubiquitination	[1, 2, 3, 4]
1886	VMYSRLPKDDVHAKE	ubiquitination	[1]
1892	PKDDVHAKESKINQV	ubiquitination	[1, 2]
1895	DVHAKESKINQVFHG	ubiquitination	[1, 7]
1913	TEGNELTKTLIKLCY	ubiquitination	[1, 3, 4, 7]
1970	QGFLFSEKPEKNLLI	acetylation	[5]
1970	QGFLFSEKPEKNLLI	ubiquitination	[1, 2, 3, 4, 7]
1973	LFSEKPEKNLLIFEN	ubiquitination	[3, 4]
1985	FENLIDLKRRYNFPV	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
2002	EVPMERKKKYIEIRK	ubiquitination	[1]
2003	VPMERKKKYIEIRKE	ubiquitination	[1]
2102	APLTALVKHMHRSLG	ubiquitination	[1]
2127	RDLPSWMKFLHGKLG	ubiquitination	[1, 2, 3, 4]
2132	WMKFLHGKLGNPIVP	ubiquitination	[1, 2, 3, 4]
2227	MKHVFHPKRAVFRHN	ubiquitination	[2]
2239	RHNLEIIKTLVECWK	ubiquitination	[1]
2246	KTLVECWKDCLSIPY	ubiquitination	[1, 6]
2259	PYRLIFEKFSGKDPN	acetylation	[5]
2259	PYRLIFEKFSGKDPN	ubiquitination	[1, 2, 3, 4]
2263	IFEKFSGKDPNSKDN	ubiquitination	[1, 2]
2313	NMSFVRYKEVYAAAA	ubiquitination	[1]
2334	LRYVMERKNILEESL	ubiquitination	[1, 7]
2347	SLCELVAKQLKQHQN	ubiquitination	[1, 2]
2350	ELVAKQLKQHQNTME	ubiquitination	[1, 2]
2359	HQNTMEDKFIVCLNK	ubiquitination	[1]
2366	KFIVCLNKVTKSFPP	ubiquitination	[1, 8]
2369	VCLNKVTKSFPPLAD	ubiquitination	[2, 3, 4, 8]
2418	LYFQLKSKDFVQVMR	ubiquitination	[1, 2]
2433	HRDDERQKVCLDIIY	ubiquitination	[1]
2441	VCLDIIYKMMPKLKP	ubiquitination	[1, 7]
2445	IIYKMMPKLKPVELR	ubiquitination	[1, 3, 4]
2447	YKMMPKLKPVELREL	ubiquitination	[1, 2, 3, 4]
2500	NDSQEIFKLAKDVLI	ubiquitination	[2]
2503	QEIFKLAKDVLIQGL	ubiquitination	[1, 2, 6]
2683	DSLLFAHKRSERLQR	ubiquitination	[1, 2, 3, 4, 7]
2694	RLQRAPLKSVGPDFG	ubiquitination	[1, 2, 3, 4, 7]
2702	SVGPDFGKKRLGLPG	acetylation	[5]
2702	SVGPDFGKKRLGLPG	ubiquitination	[1, 2]
2703	VGPDFGKKRLGLPGD	ubiquitination	[1]
2715	PGDEVDNKVKGAAGR	ubiquitination	[1, 2, 7]
2717	DEVDNKVKGAAGRTD	ubiquitination	[1, 7]
2738	RFMRDQEKLSLMYAR	ubiquitination	[1, 3, 4, 7, 8]
2746	LSLMYARKGVAEQKR	methylation	[9]
2755	VAEQKREKEIKSELK	ubiquitination	[1]
2758	QKREKEIKSELKMKQ	ubiquitination	[1]
2764	IKSELKMKQDAQVVL	ubiquitination	[1, 2, 7]
2786	DLPDIQIKHSSLITP	ubiquitination	[1, 2, 3, 4]
2806	QRDPIIAKQLFSSLF	ubiquitination	[2, 3, 4]
2818	SLFSGILKEMDKFKT	ubiquitination	[1]
2829	KFKTLSEKNNITQKL	ubiquitination	[1, 2]
2835	EKNNITQKLLQDFNR	ubiquitination	[1, 2, 3, 4, 8]
2908	LPAELPAKRVRGKAR	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
2928	LRWVELAKLYRSIGE	ubiquitination	[1, 2, 3, 4, 6, 7, 8]
2950	FTSEIGTKQITQSAL	ubiquitination	[1, 2, 3, 4, 6, 7, 10]
2970	SDYSEAAKQYDEALN	ubiquitination	[1, 2]
2978	QYDEALNKQDWVDGE	ubiquitination	[2]
3050	YMIRSKLKLLLQGEA	ubiquitination	[2]
3067	SLLTFIDKAMHGELQ	ubiquitination	[1, 2]
3158	LSSQVPLKRLLNTWT	ubiquitination	[1, 2, 7]
3172	TNRYPDAKMDPMNIW	ubiquitination	[1, 2]
3192	NRCFFLSKIEEKLTP	ubiquitination	[1, 2, 3, 4, 6, 7]
3196	FLSKIEEKLTPLPED	ubiquitination	[1, 2]
3235	SSLIRSCKFSMKMKM	ubiquitination	[1, 8]
3239	RSCKFSMKMKMIDSA	ubiquitination	[1]
3241	CKFSMKMKMIDSARK	acetylation	[5]
3241	CKFSMKMKMIDSARK	ubiquitination	[1]
3248	KMIDSARKQNNFSLA	methylation	[9]
3248	KMIDSARKQNNFSLA	ubiquitination	[1, 2, 7]
3257	NNFSLAMKLLKELHK	ubiquitination	[1, 3, 4, 8]
3260	SLAMKLLKELHKESK	acetylation	[5]
3260	SLAMKLLKELHKESK	ubiquitination	[1]
3264	KLLKELHKESKTRDD	ubiquitination	[1, 2]
3302	EQVLTVLKTVSLLDE	ubiquitination	[1]
3318	NVSSYLSKNILAFRD	ubiquitination	[1, 2, 3, 4, 6, 7]
3355	LAEIEEDKARRILEL	ubiquitination	[1, 7]
3372	SSSEDSEKVIAGLYQ	ubiquitination	[1, 2, 6]
3426	FCDQQLRKEEENASV	ubiquitination	[1, 2]
3449	YPALVVEKMLKALKL	ubiquitination	[1, 2]
3452	LVVEKMLKALKLNSN	ubiquitination	[1]
3455	EKMLKALKLNSNEAR	ubiquitination	[1, 2, 7]
3550	KDTSTGHKNKEFVAR	ubiquitination	[1]
3552	TSTGHKNKEFVARIK	ubiquitination	[1, 2, 3, 4, 8]
3598	DVRAELAKTPVNKKN	ubiquitination	[1]
3608	VNKKNIEKMYERMYA	acetylation	[5]
3608	VNKKNIEKMYERMYA	ubiquitination	[1]
3621	YAALGDPKAPGLGAF	acetylation	[5]
3621	YAALGDPKAPGLGAF	ubiquitination	[1, 2, 3, 4]
3631	GLGAFRRKFIQTFGK	ubiquitination	[1, 7]
3638	KFIQTFGKEFDKHFG	acetylation	[5]
3638	KFIQTFGKEFDKHFG	ubiquitination	[1, 3, 4]
3642	TFGKEFDKHFGKGGS	acetylation	[5]
3642	TFGKEFDKHFGKGGS	ubiquitination	[1]
3646	EFDKHFGKGGSKLLR	ubiquitination	[1]
3650	HFGKGGSKLLRMKLS	ubiquitination	[1]
3655	GSKLLRMKLSDFNDI	ubiquitination	[1, 7]
3669	ITNMLLLKMNKDSKP	ubiquitination	[1, 2, 3, 4]
3672	MLLLKMNKDSKPPGN	ubiquitination	[1]
3691	SPWMSDFKVEFLRNE	ubiquitination	[1]
3710	GQYDGRGKPLPEYHV	ubiquitination	[1, 2, 3, 4, 7]
3753	REHPFLVKGGEDLRQ	ubiquitination	[1, 2, 3, 4, 7]
3825	NTMSQEEKAAYLSDP	ubiquitination	[1, 2, 3, 4, 11, 12]
3840	RAPPCEYKDWLTKMS	ubiquitination	[1, 3, 4]
3845	EYKDWLTKMSGKHDV	ubiquitination	[1, 2, 3, 4, 7, 8]
3849	WLTKMSGKHDVGAYM	ubiquitination	[1, 7]
3860	GAYMLMYKGANRTET	ubiquitination	[1, 2, 3, 4, 6, 8]
3877	SFRKRESKVPADLLK	ubiquitination	[1]
3884	KVPADLLKRAFVRMS	ubiquitination	[1, 2, 7]
4007	NTMDVFVKEPSFDWK	ubiquitination	[1, 2]
4014	KEPSFDWKNFEQKML	ubiquitination	[1]
4019	DWKNFEQKMLKKGGS	ubiquitination	[1, 2]
4023	FEQKMLKKGGSWIQE	ubiquitination	[1, 2, 7]
4036	QEINVAEKNWYPRQK	ubiquitination	[1, 2, 3, 4, 7]
4043	KNWYPRQKICYAKRK	ubiquitination	[1]
4048	RQKICYAKRKLAGAN	ubiquitination	[1]
4050	KICYAKRKLAGANPA	ubiquitination	[1, 7]
4070	ELLLGHEKAPAFRDY	ubiquitination	[1, 7]
4105	LSEETQVKCLMDQAT	ubiquitination	[1, 7]

[1] 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]
[2] 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]
[3] 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]
[4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
Chen Z, Zhou Y, Song J, Zhang Z.
Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
[5] 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. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
[6] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
[7] 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]
[8] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
[9] Mass spectrometry-based identification and characterisation of lysine and arginine methylation in the human proteome.
Bremang M, Cuomo A, Agresta AM, Stugiewicz M, Spadotto V, Bonaldi T.
Mol Biosyst. 2013 Jul 30;9(9):2231-47. [PMID: 23748837]
[10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[11] 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]
[12] 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]

Functional Description

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 p53/TP53 in the presence of supercoiled DNA is dependent on C1D.

REPEAT 288 323 HEAT 1.
REPEAT 1004 1040 HEAT 2.
REPEAT 1723 1756 TPR 1.
DOMAIN 2883 3539 FAT.
REPEAT 2920 2948 TPR 2.
REPEAT 2949 2982 TPR 3.
DOMAIN 3747 4015 PI3K/PI4K.
DOMAIN 4096 4128 FATC.
REGION 1503 1538 Interaction with C1D.
REGION 1503 1538 Leucine-zipper.
REGION 2436 3212 KIP-binding.
MOD_RES 117 117 N6-acetyllysine.
MOD_RES 828 828 N6-acetyllysine.
MOD_RES 893 893 Phosphoserine.
MOD_RES 1209 1209 N6-acetyllysine.
MOD_RES 1970 1970 N6-acetyllysine.
MOD_RES 2259 2259 N6-acetyllysine.
MOD_RES 2609 2609 Phosphothreonine; by autocatalysis.
MOD_RES 2612 2612 Phosphoserine; by autocatalysis.
MOD_RES 2638 2638 Phosphothreonine; by autocatalysis.
MOD_RES 2647 2647 Phosphothreonine; by autocatalysis.
MOD_RES 3205 3205 Phosphoserine.
MOD_RES 3241 3241 N6-acetyllysine.
MOD_RES 3260 3260 N6-acetyllysine.
MOD_RES 3621 3621 N6-acetyllysine.
MOD_RES 3638 3638 N6-acetyllysine.
MOD_RES 3642 3642 N6-acetyllysine.
MOD_RES 4026 4026 Phosphoserine.

Acetylation; Alternative splicing; ATP-binding; Complete proteome; DNA damage; DNA recombination; DNA repair; DNA-binding; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; S-nitrosylation; Serine/threonine-protein kinase; TPR repeat; Transferase.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005958; C:DNA-dependent protein kinase-DNA ligase 4 complex; IDA:MGI.
GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO:0004677; F:DNA-dependent protein kinase activity; IDA:MGI.
GO:0006915; P:apoptotic process; IEA:Compara.
GO:0002326; P:B cell lineage commitment; IEA:Compara.
GO:0007420; P:brain development; IEA:Compara.
GO:0032869; P:cellular response to insulin stimulus; IMP:BHF-UCL.
GO:0006303; P:double-strand break repair via nonhomologous end joining; TAS:Reactome.
GO:0035234; P:germ cell programmed cell death; IEA:Compara.
GO:0007507; P:heart development; IEA:Compara.
GO:0033152; P:immunoglobulin V(D)J recombination; IEA:Compara.
GO:0018105; P:peptidyl-serine phosphorylation; IDA:BHF-UCL.
GO:0043065; P:positive regulation of apoptotic process; IEA:Compara.
GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
GO:0002328; P:pro-B cell differentiation; IEA:Compara.
GO:0031648; P:protein destabilization; IEA:Compara.
GO:0010332; P:response to gamma radiation; IEA:Compara.
GO:0001756; P:somitogenesis; IEA:Compara.
GO:0033077; P:T cell differentiation in thymus; IEA:Compara.
GO:0002360; P:T cell lineage commitment; IEA:Compara.
GO:0033153; P:T cell receptor V(D)J recombination; IEA:Compara.
GO:0000723; P:telomere maintenance; IEA:Compara.

IPR011989; ARM-like.
IPR016024; ARM-type_fold.
IPR003152; FATC.
IPR011009; Kinase-like_dom.
IPR012582; NUC194.
IPR000403; PI3/4_kinase_cat_dom.
IPR018936; PI3/4_kinase_CS.
IPR003151; PIK-rel_kinase_FAT.
IPR014009; PIK_FAT.

PF02259; FAT
PF02260; FATC
PF08163; NUC194
PF00454; PI3_PI4_kinase

PS51189; FAT
PS51190; FATC
PS50077; HEAT_REPEAT
PS00915; PI3_4_KINASE_1
PS00916; PI3_4_KINASE_2
PS50290; PI3_4_KINASE_3
PS50005; TPR
PS50293; TPR_REGION