dbPTM

XRCC6_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	XRCC6_HUMAN
UniProt AC	P12956
Protein Name	X-ray repair cross-complementing protein 6
Gene Name	XRCC6
Organism	Homo sapiens (Human).
Sequence Length	609
Subcellular Localization	Nucleus . Chromosome .
Protein Description	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. Required for osteocalcin gene expression. 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. 5'-dRP lyase activity 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. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway..
Protein Sequence	MSGWESYYKTEGDEEAEEEQEENLEASGDYKYSGRDSLIFLVDASKAMFESQSEDELTPFDMSIQCIQSVYISKIISSDRDLLAVVFYGTEKDKNSVNFKNIYVLQELDNPGAKRILELDQFKGQQGQKRFQDMMGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDNPHGNDSAKASRARTKAGDLRDTGIFLDLMHLKKPGGFDISLFYRDIISIAEDEDLRVHFEESSKLEDLLRKVRAKETRKRALSRLKLKLNKDIVISVGIYNLVQKALKPPPIKLYRETNEPVKTKTRTFNTSTGGLLLPSDTKRSQIYGSRQIILEKEETEELKRFDDPGLMLMGFKPLVLLKKHHYLRPSLFVYPEESLVIGSSTLFSALLIKCLEKEVAALCRYTPRRNIPPYFVALVPQEEELDDQKIQVTPPGFQLVFLPFADDKRKMPFTEKIMATPEQVGKMKAIVEKLRFTYRSDSFENPVLQQHFRNLEALALDLMEPEQAVDLTLPKVEAMNKRLGSLVDEFKELVYPPDYNPEGKVTKRKHDNEGSGSKRPKVEYSEEELKTHISKGTLGKFTVPMLKEACRAYGLKSGLKKQELLEALTKHFQD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGWESYYK ------CCCHHCCCC	53.25	22223895
2	Phosphorylation	------MSGWESYYK ------CCCHHCCCC	53.25	25159151
6	Phosphorylation	--MSGWESYYKTEGD --CCCHHCCCCCCCC	27.53	25159151
7	Phosphorylation	-MSGWESYYKTEGDE -CCCHHCCCCCCCCH	9.47	23663014
8	Phosphorylation	MSGWESYYKTEGDEE CCCHHCCCCCCCCHH	22.25	23663014
9	Sumoylation	SGWESYYKTEGDEEA CCHHCCCCCCCCHHH	31.69	-
10	Phosphorylation	GWESYYKTEGDEEAE CHHCCCCCCCCHHHH	29.13	27251275
27	Phosphorylation	QEENLEASGDYKYSG HHHHHHHCCCCCCCC	23.87	30278072
30	Phosphorylation	NLEASGDYKYSGRDS HHHHCCCCCCCCCCE	18.49	28450419
31	Ubiquitination	LEASGDYKYSGRDSL HHHCCCCCCCCCCEE	37.37	-
31	Acetylation	LEASGDYKYSGRDSL HHHCCCCCCCCCCEE	37.37	19608861
31	Sumoylation	LEASGDYKYSGRDSL HHHCCCCCCCCCCEE	37.37	19608861
31	Ubiquitination	LEASGDYKYSGRDSL HHHCCCCCCCCCCEE	37.37	21906983
32	Phosphorylation	EASGDYKYSGRDSLI HHCCCCCCCCCCEEE	15.32	28152594
33	Phosphorylation	ASGDYKYSGRDSLIF HCCCCCCCCCCEEEE	24.17	28152594
37	Phosphorylation	YKYSGRDSLIFLVDA CCCCCCCEEEEEEEH	23.23	28450419
45	Phosphorylation	LIFLVDASKAMFESQ EEEEEEHHHHHHHCC	19.24	21712546
51	Phosphorylation	ASKAMFESQSEDELT HHHHHHHCCCCCCCC	27.95	26074081
53	Phosphorylation	KAMFESQSEDELTPF HHHHHCCCCCCCCCC	57.18	26074081
58	Phosphorylation	SQSEDELTPFDMSIQ CCCCCCCCCCHHHHH	21.62	27251275
63	Phosphorylation	ELTPFDMSIQCIQSV CCCCCHHHHHHHHHH	16.02	27251275
73	Ubiquitination	CIQSVYISKIISSDR HHHHHHHHHHHCCCC	10.50	-
82	Ubiquitination	IISSDRDLLAVVFYG HHCCCCCEEEEEEEC	3.26	21890473
88	Ubiquitination	DLLAVVFYGTEKDKN CEEEEEEECCCCCCC	16.13	-
92	2-Hydroxyisobutyrylation	VVFYGTEKDKNSVNF EEEECCCCCCCCCCC	74.06	-
92	Acetylation	VVFYGTEKDKNSVNF EEEECCCCCCCCCCC	74.06	23954790
92	Methylation	VVFYGTEKDKNSVNF EEEECCCCCCCCCCC	74.06	-
92	Ubiquitination	VVFYGTEKDKNSVNF EEEECCCCCCCCCCC	74.06	21906983
94	Acetylation	FYGTEKDKNSVNFKN EECCCCCCCCCCCEE	63.29	25953088
94	Ubiquitination	FYGTEKDKNSVNFKN EECCCCCCCCCCCEE	63.29	21906983
100	2-Hydroxyisobutyrylation	DKNSVNFKNIYVLQE CCCCCCCEEEEEEEE	36.91	-
100	Acetylation	DKNSVNFKNIYVLQE CCCCCCCEEEEEEEE	36.91	25953088
100	Succinylation	DKNSVNFKNIYVLQE CCCCCCCEEEEEEEE	36.91	23954790
100	Ubiquitination	DKNSVNFKNIYVLQE CCCCCCCEEEEEEEE	36.91	21890473
103	Phosphorylation	SVNFKNIYVLQELDN CCCCEEEEEEEECCC	12.42	28152594
114	2-Hydroxyisobutyrylation	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	-
114	Acetylation	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	25953088
114	Methylation	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	-
114	Succinylation	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	23954790
114	Ubiquitination	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	21890473
114	Ubiquitination	ELDNPGAKRILELDQ ECCCCCHHHHHHHHH	45.98	22053931
123	Sumoylation	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	-
123	2-Hydroxyisobutyrylation	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	-
123	Acetylation	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	26051181
123	Methylation	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	30782933
123	Sumoylation	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	-
123	Ubiquitination	ILELDQFKGQQGQKR HHHHHHHCCHHHHHH	50.61	21906983
129	Ubiquitination	FKGQQGQKRFQDMMG HCCHHHHHHHHHHCC	63.10	-
141	Acetylation	MMGHGSDYSLSEVLW HCCCCCCCCHHHHHH	17.14	-
141	Ubiquitination	MMGHGSDYSLSEVLW HCCCCCCCCHHHHHH	17.14	-
148	Ubiquitination	YSLSEVLWVCANLFS CCHHHHHHHHHHHCC	6.58	-
155	Phosphorylation	WVCANLFSDVQFKMS HHHHHHCCCCCHHCC	39.78	22037767
165	Ubiquitination	QFKMSHKRIMLFTNE CHHCCCCEEEEEECC	17.71	21890473
166	Ubiquitination	FKMSHKRIMLFTNED HHCCCCEEEEEECCC	3.16	-
167	Sulfoxidation	KMSHKRIMLFTNEDN HCCCCEEEEEECCCC	2.67	28183972
170	Phosphorylation	HKRIMLFTNEDNPHG CCEEEEEECCCCCCC	33.46	20068231
180	Phosphorylation	DNPHGNDSAKASRAR CCCCCCHHHHHHHHH	35.35	29255136
182	Acetylation	PHGNDSAKASRARTK CCCCHHHHHHHHHHH	51.34	23236377
182	Ubiquitination	PHGNDSAKASRARTK CCCCHHHHHHHHHHH	51.34	21906983
189	2-Hydroxyisobutyrylation	KASRARTKAGDLRDT HHHHHHHHHCCHHHC	44.83	-
189	Ubiquitination	KASRARTKAGDLRDT HHHHHHHHHCCHHHC	44.83	-
194	Methylation	RTKAGDLRDTGIFLD HHHHCCHHHCCEEEE	44.15	115481459
197	Ubiquitination	AGDLRDTGIFLDLMH HCCHHHCCEEEEEEC	16.97	21890473
203	Sulfoxidation	TGIFLDLMHLKKPGG CCEEEEEECCCCCCC	3.29	21406390
206	2-Hydroxyisobutyrylation	FLDLMHLKKPGGFDI EEEEECCCCCCCCCE	42.09	-
206	Acetylation	FLDLMHLKKPGGFDI EEEEECCCCCCCCCE	42.09	27178108
206	Ubiquitination	FLDLMHLKKPGGFDI EEEEECCCCCCCCCE	42.09	21890473
207	Methylation	LDLMHLKKPGGFDIS EEEECCCCCCCCCEE	56.08	-
207	Ubiquitination	LDLMHLKKPGGFDIS EEEECCCCCCCCCEE	56.08	-
222	Phosphorylation	LFYRDIISIAEDEDL EEEEHHHHHHCCCCC	18.97	30266825
230	Methylation	IAEDEDLRVHFEESS HHCCCCCCHHHHCCH	31.99	115481467
236	Phosphorylation	LRVHFEESSKLEDLL CCHHHHCCHHHHHHH	26.10	30266825
237	Phosphorylation	RVHFEESSKLEDLLR CHHHHCCHHHHHHHH	44.53	30266825
238	2-Hydroxyisobutyrylation	VHFEESSKLEDLLRK HHHHCCHHHHHHHHH	66.24	-
238	Acetylation	VHFEESSKLEDLLRK HHHHCCHHHHHHHHH	66.24	21339330
238	Ubiquitination	VHFEESSKLEDLLRK HHHHCCHHHHHHHHH	66.24	21906983
241	Acetylation	EESSKLEDLLRKVRA HCCHHHHHHHHHHHC	62.53	-
241	Ubiquitination	EESSKLEDLLRKVRA HCCHHHHHHHHHHHC	62.53	-
244	Methylation	SKLEDLLRKVRAKET HHHHHHHHHHHCHHH	42.60	115481483
246	Acetylation	LEDLLRKVRAKETRK HHHHHHHHHCHHHHH	6.10	-
246	Ubiquitination	LEDLLRKVRAKETRK HHHHHHHHHCHHHHH	6.10	21890473
256	Ubiquitination	KETRKRALSRLKLKL HHHHHHHHHHHHHHC	3.39	-
265	Ubiquitination	RLKLKLNKDIVISVG HHHHHCCCCEEEEEE	60.30	-
270	Phosphorylation	LNKDIVISVGIYNLV CCCCEEEEEEHHHHH	11.91	28387310
274	Phosphorylation	IVISVGIYNLVQKAL EEEEEEHHHHHHHHH	9.12	28387310
276	Ubiquitination	ISVGIYNLVQKALKP EEEEHHHHHHHHHCC	2.13	21890473
282	Acetylation	NLVQKALKPPPIKLY HHHHHHHCCCCCEEE	61.41	23749302
282	Ubiquitination	NLVQKALKPPPIKLY HHHHHHHCCCCCEEE	61.41	21906983
287	Acetylation	ALKPPPIKLYRETNE HHCCCCCEEEECCCC	45.28	23749302
287	Malonylation	ALKPPPIKLYRETNE HHCCCCCEEEECCCC	45.28	26320211
287	Sumoylation	ALKPPPIKLYRETNE HHCCCCCEEEECCCC	45.28	28112733
287	Ubiquitination	ALKPPPIKLYRETNE HHCCCCCEEEECCCC	45.28	21890473
290	Acetylation	PPPIKLYRETNEPVK CCCCEEEECCCCCCC	55.49	-
290	Ubiquitination	PPPIKLYRETNEPVK CCCCEEEECCCCCCC	55.49	-
290	Acetylation	PPPIKLYRETNEPVK CCCCEEEECCCCCCC	55.49	19608861
290	Ubiquitination	PPPIKLYRETNEPVK CCCCEEEECCCCCCC	55.49	19608861
292	Phosphorylation	PIKLYRETNEPVKTK CCEEEECCCCCCCCC	35.56	22817900
297	Acetylation	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	-
297	Ubiquitination	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	-
297	Sumoylation	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	-
297	Acetylation	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	19608861
297	Sumoylation	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	-
297	Ubiquitination	RETNEPVKTKTRTFN ECCCCCCCCCEEEEE	55.83	19608861
299	Ubiquitination	TNEPVKTKTRTFNTS CCCCCCCCEEEEECC	30.23	-
300	Phosphorylation	NEPVKTKTRTFNTST CCCCCCCEEEEECCC	39.92	22199227
301	Methylation	EPVKTKTRTFNTSTG CCCCCCEEEEECCCC	38.59	115481499
302	Phosphorylation	PVKTKTRTFNTSTGG CCCCCEEEEECCCCC	26.86	21712546
305	Phosphorylation	TKTRTFNTSTGGLLL CCEEEEECCCCCEEC	24.39	25159151
306	O-linked_Glycosylation	KTRTFNTSTGGLLLP CEEEEECCCCCEECC	26.59	30444036
306	Phosphorylation	KTRTFNTSTGGLLLP CEEEEECCCCCEECC	26.59	25159151
307	Phosphorylation	TRTFNTSTGGLLLPS EEEEECCCCCEECCC	32.98	25159151
310	Ubiquitination	FNTSTGGLLLPSDTK EECCCCCEECCCCCC	4.73	21890473
314	Phosphorylation	TGGLLLPSDTKRSQI CCCEECCCCCCCHHH	58.86	21815630
316	Ubiquitination	GLLLPSDTKRSQIYG CEECCCCCCCHHHCC	32.47	21890473
316	Phosphorylation	GLLLPSDTKRSQIYG CEECCCCCCCHHHCC	32.47	28857561
317	Ubiquitination	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	-
317	Sumoylation	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	-
317	2-Hydroxyisobutyrylation	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	-
317	Acetylation	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	15023334
317	Sumoylation	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	28112733
317	Ubiquitination	LLLPSDTKRSQIYGS EECCCCCCCHHHCCC	55.85	21906983
318	Methylation	LLPSDTKRSQIYGSR ECCCCCCCHHHCCCE	35.57	115481491
319	Phosphorylation	LPSDTKRSQIYGSRQ CCCCCCCHHHCCCEE	23.61	21406692
322	Phosphorylation	DTKRSQIYGSRQIIL CCCCHHHCCCEEEEE	11.04	28152594
324	Phosphorylation	KRSQIYGSRQIILEK CCHHHCCCEEEEECH	12.21	28152594
331	Sumoylation	SRQIILEKEETEELK CEEEEECHHHHHHHH	58.36	-
331	2-Hydroxyisobutyrylation	SRQIILEKEETEELK CEEEEECHHHHHHHH	58.36	-
331	Acetylation	SRQIILEKEETEELK CEEEEECHHHHHHHH	58.36	19608861
331	Sumoylation	SRQIILEKEETEELK CEEEEECHHHHHHHH	58.36	19608861
331	Ubiquitination	SRQIILEKEETEELK CEEEEECHHHHHHHH	58.36	21906983
334	Phosphorylation	IILEKEETEELKRFD EEECHHHHHHHHCCC	35.53	23312004
338	Acetylation	KEETEELKRFDDPGL HHHHHHHHCCCCCCC	55.06	19608861
338	Sumoylation	KEETEELKRFDDPGL HHHHHHHHCCCCCCC	55.06	19608861
338	Ubiquitination	KEETEELKRFDDPGL HHHHHHHHCCCCCCC	55.06	21906983
346	Sulfoxidation	RFDDPGLMLMGFKPL CCCCCCCEECCCCCE	2.76	28183972
348	Sulfoxidation	DDPGLMLMGFKPLVL CCCCCEECCCCCEEE	3.55	28183972
351	Ubiquitination	GLMLMGFKPLVLLKK CCEECCCCCEEEHHC	31.54	-
351	Ubiquitination	GLMLMGFKPLVLLKK CCEECCCCCEEEHHC	31.54	21906983
357	2-Hydroxyisobutyrylation	FKPLVLLKKHHYLRP CCCEEEHHCCCCCCC	45.99	-
357	Acetylation	FKPLVLLKKHHYLRP CCCEEEHHCCCCCCC	45.99	26051181
357	Ubiquitination	FKPLVLLKKHHYLRP CCCEEEHHCCCCCCC	45.99	21906983
358	Ubiquitination	KPLVLLKKHHYLRPS CCEEEHHCCCCCCCC	35.27	-
392	Acetylation	LLIKCLEKEVAALCR HHHHHHHHHHHHHHH	44.53	25953088
392	Ubiquitination	LLIKCLEKEVAALCR HHHHHHHHHHHHHHH	44.53	-
402	Ubiquitination	AALCRYTPRRNIPPY HHHHHCCCCCCCCCC	25.05	21890473
404	Ubiquitination	LCRYTPRRNIPPYFV HHHCCCCCCCCCCEE	46.78	21890473
410	Ubiquitination	RRNIPPYFVALVPQE CCCCCCCEEEECCCH	2.98	21890473
420	Acetylation	LVPQEEELDDQKIQV ECCCHHHCCCCCEEE	11.28	-
420	Ubiquitination	LVPQEEELDDQKIQV ECCCHHHCCCCCEEE	11.28	-
420	Acetylation	LVPQEEELDDQKIQV ECCCHHHCCCCCEEE	11.28	19608861
420	Ubiquitination	LVPQEEELDDQKIQV ECCCHHHCCCCCEEE	11.28	19608861
424	Sumoylation	EEELDDQKIQVTPPG HHHCCCCCEEECCCC	41.94	-
427	Acetylation	LDDQKIQVTPPGFQL CCCCCEEECCCCCEE	11.19	-
427	Ubiquitination	LDDQKIQVTPPGFQL CCCCCEEECCCCCEE	11.19	-
427	Acetylation	LDDQKIQVTPPGFQL CCCCCEEECCCCCEE	11.19	19608861
427	Ubiquitination	LDDQKIQVTPPGFQL CCCCCEEECCCCCEE	11.19	19608861
428	Phosphorylation	DDQKIQVTPPGFQLV CCCCEEECCCCCEEE	13.85	28122231
443	Sumoylation	FLPFADDKRKMPFTE EEECCCCCCCCCCHH	55.24	-
443	Sumoylation	FLPFADDKRKMPFTE EEECCCCCCCCCCHH	55.24	-
443	Ubiquitination	FLPFADDKRKMPFTE EEECCCCCCCCCCHH	55.24	21906983
445	Ubiquitination	PFADDKRKMPFTEKI ECCCCCCCCCCHHHH	57.58	21906983
451	2-Hydroxyisobutyrylation	RKMPFTEKIMATPEQ CCCCCHHHHCCCHHH	34.42	-
451	Acetylation	RKMPFTEKIMATPEQ CCCCCHHHHCCCHHH	34.42	27452117
451	Ubiquitination	RKMPFTEKIMATPEQ CCCCCHHHHCCCHHH	34.42	21906983
453	Sulfoxidation	MPFTEKIMATPEQVG CCCHHHHCCCHHHHH	5.14	21406390
455	Phosphorylation	FTEKIMATPEQVGKM CHHHHCCCHHHHHHH	15.24	19664994
461	2-Hydroxyisobutyrylation	ATPEQVGKMKAIVEK CCHHHHHHHHHHHHH	38.07	-
461	Acetylation	ATPEQVGKMKAIVEK CCHHHHHHHHHHHHH	38.07	19608861
461	Ubiquitination	ATPEQVGKMKAIVEK CCHHHHHHHHHHHHH	38.07	21906983
463	2-Hydroxyisobutyrylation	PEQVGKMKAIVEKLR HHHHHHHHHHHHHHC	38.15	-
463	Acetylation	PEQVGKMKAIVEKLR HHHHHHHHHHHHHHC	38.15	26210075
463	Ubiquitination	PEQVGKMKAIVEKLR HHHHHHHHHHHHHHC	38.15	-
468	2-Hydroxyisobutyrylation	KMKAIVEKLRFTYRS HHHHHHHHHCCEECC	33.78	-
468	Acetylation	KMKAIVEKLRFTYRS HHHHHHHHHCCEECC	33.78	23954790
468	Malonylation	KMKAIVEKLRFTYRS HHHHHHHHHCCEECC	33.78	26320211
468	Ubiquitination	KMKAIVEKLRFTYRS HHHHHHHHHCCEECC	33.78	21906983
472	Phosphorylation	IVEKLRFTYRSDSFE HHHHHCCEECCCCCC	16.16	30624053
473	Phosphorylation	VEKLRFTYRSDSFEN HHHHCCEECCCCCCC	12.86	23186163
474	Methylation	EKLRFTYRSDSFENP HHHCCEECCCCCCCH	30.81	115481475
475	Ubiquitination	KLRFTYRSDSFENPV HHCCEECCCCCCCHH	27.48	-
475	Phosphorylation	KLRFTYRSDSFENPV HHCCEECCCCCCCHH	27.48	23401153
477	Phosphorylation	RFTYRSDSFENPVLQ CCEECCCCCCCHHHH	35.39	25159151
485	Ubiquitination	FENPVLQQHFRNLEA CCCHHHHHHHHCHHH	33.26	-
498	Ubiquitination	EALALDLMEPEQAVD HHHHHHHCCHHHHHC	8.90	-
498	Sulfoxidation	EALALDLMEPEQAVD HHHHHHHCCHHHHHC	8.90	21406390
501	Ubiquitination	ALDLMEPEQAVDLTL HHHHCCHHHHHCCCH	37.55	-
507	Phosphorylation	PEQAVDLTLPKVEAM HHHHHCCCHHHHHHH	36.23	23879269
510	Sumoylation	AVDLTLPKVEAMNKR HHCCCHHHHHHHHHH	56.68	-
512	Ubiquitination	DLTLPKVEAMNKRLG CCCHHHHHHHHHHHH	48.61	-
515	Ubiquitination	LPKVEAMNKRLGSLV HHHHHHHHHHHHHHH	33.09	-
516	2-Hydroxyisobutyrylation	PKVEAMNKRLGSLVD HHHHHHHHHHHHHHH	35.60	-
516	Acetylation	PKVEAMNKRLGSLVD HHHHHHHHHHHHHHH	35.60	25953088
516	Ubiquitination	PKVEAMNKRLGSLVD HHHHHHHHHHHHHHH	35.60	21906983
520	Phosphorylation	AMNKRLGSLVDEFKE HHHHHHHHHHHHHHH	29.79	19664994
524	Ubiquitination	RLGSLVDEFKELVYP HHHHHHHHHHHHCCC	51.65	21890473
526	Sumoylation	GSLVDEFKELVYPPD HHHHHHHHHHCCCCC	48.36	-
526	Ubiquitination	GSLVDEFKELVYPPD HHHHHHHHHHCCCCC	48.36	21906983
529	Acetylation	VDEFKELVYPPDYNP HHHHHHHCCCCCCCC	7.66	-
529	Ubiquitination	VDEFKELVYPPDYNP HHHHHHHCCCCCCCC	7.66	-
530	Phosphorylation	DEFKELVYPPDYNPE HHHHHHCCCCCCCCC	22.98	28152594
534	Ubiquitination	ELVYPPDYNPEGKVT HHCCCCCCCCCCCCC	38.09	21890473
534	Phosphorylation	ELVYPPDYNPEGKVT HHCCCCCCCCCCCCC	38.09	28152594
539	Acetylation	PDYNPEGKVTKRKHD CCCCCCCCCCCCCCC	45.10	15023334
539	Sumoylation	PDYNPEGKVTKRKHD CCCCCCCCCCCCCCC	45.10	-
539	Ubiquitination	PDYNPEGKVTKRKHD CCCCCCCCCCCCCCC	45.10	21906983
541	Ubiquitination	YNPEGKVTKRKHDNE CCCCCCCCCCCCCCC	28.72	-
541	Phosphorylation	YNPEGKVTKRKHDNE CCCCCCCCCCCCCCC	28.72	26434776
542	Acetylation	NPEGKVTKRKHDNEG CCCCCCCCCCCCCCC	63.54	15023334
542	Ubiquitination	NPEGKVTKRKHDNEG CCCCCCCCCCCCCCC	63.54	-
544	Acetylation	EGKVTKRKHDNEGSG CCCCCCCCCCCCCCC	57.79	15023334
550	Ubiquitination	RKHDNEGSGSKRPKV CCCCCCCCCCCCCCC	33.44	-
550	Phosphorylation	RKHDNEGSGSKRPKV CCCCCCCCCCCCCCC	33.44	20068231
552	Phosphorylation	HDNEGSGSKRPKVEY CCCCCCCCCCCCCCC	27.47	20068231
553	Acetylation	DNEGSGSKRPKVEYS CCCCCCCCCCCCCCC	76.01	15023334
553	Ubiquitination	DNEGSGSKRPKVEYS CCCCCCCCCCCCCCC	76.01	21906983
554	Ubiquitination	NEGSGSKRPKVEYSE CCCCCCCCCCCCCCH	37.66	-
555	Ubiquitination	EGSGSKRPKVEYSEE CCCCCCCCCCCCCHH	49.10	-
556	Sumoylation	GSGSKRPKVEYSEEE CCCCCCCCCCCCHHH	52.29	-
556	Acetylation	GSGSKRPKVEYSEEE CCCCCCCCCCCCHHH	52.29	15023334
556	Sumoylation	GSGSKRPKVEYSEEE CCCCCCCCCCCCHHH	52.29	28112733
556	Ubiquitination	GSGSKRPKVEYSEEE CCCCCCCCCCCCHHH	52.29	21906983
559	Phosphorylation	SKRPKVEYSEEELKT CCCCCCCCCHHHHHH	25.11	23403867
560	Phosphorylation	KRPKVEYSEEELKTH CCCCCCCCHHHHHHH	25.65	23401153
564	Acetylation	VEYSEEELKTHISKG CCCCHHHHHHHHCCC	9.80	-
564	Ubiquitination	VEYSEEELKTHISKG CCCCHHHHHHHHCCC	9.80	21890473
565	2-Hydroxyisobutyrylation	EYSEEELKTHISKGT CCCHHHHHHHHCCCC	41.14	-
565	Acetylation	EYSEEELKTHISKGT CCCHHHHHHHHCCCC	41.14	26822725
565	Ubiquitination	EYSEEELKTHISKGT CCCHHHHHHHHCCCC	41.14	21906983
570	2-Hydroxyisobutyrylation	ELKTHISKGTLGKFT HHHHHHCCCCCCCCH	56.14	-
570	Acetylation	ELKTHISKGTLGKFT HHHHHHCCCCCCCCH	56.14	23749302
570	Ubiquitination	ELKTHISKGTLGKFT HHHHHHCCCCCCCCH	56.14	-
575	Acetylation	ISKGTLGKFTVPMLK HCCCCCCCCHHHHHH	40.76	25953088
575	Ubiquitination	ISKGTLGKFTVPMLK HCCCCCCCCHHHHHH	40.76	21906983
577	Phosphorylation	KGTLGKFTVPMLKEA CCCCCCCHHHHHHHH	27.47	20068231
582	Acetylation	KFTVPMLKEACRAYG CCHHHHHHHHHHHCC	36.69	25953088
582	Ubiquitination	KFTVPMLKEACRAYG CCHHHHHHHHHHHCC	36.69	-
588	Phosphorylation	LKEACRAYGLKSGLK HHHHHHHCCCCCCCC	12.02	22817900
591	Acetylation	ACRAYGLKSGLKKQE HHHHCCCCCCCCHHH	37.81	25953088
591	Ubiquitination	ACRAYGLKSGLKKQE HHHHCCCCCCCCHHH	37.81	-
592	Phosphorylation	CRAYGLKSGLKKQEL HHHCCCCCCCCHHHH	55.17	29214152
595	Malonylation	YGLKSGLKKQELLEA CCCCCCCCHHHHHHH	56.80	32601280
595	Ubiquitination	YGLKSGLKKQELLEA CCCCCCCCHHHHHHH	56.80	-
596	Acetylation	GLKSGLKKQELLEAL CCCCCCCHHHHHHHH	54.79	26051181
596	Ubiquitination	GLKSGLKKQELLEAL CCCCCCCHHHHHHHH	54.79	21906983
604	Phosphorylation	QELLEALTKHFQD-- HHHHHHHHHHHCC--	29.53	21406692
605	2-Hydroxyisobutyrylation	ELLEALTKHFQD--- HHHHHHHHHHCC---	43.18	-
605	Acetylation	ELLEALTKHFQD--- HHHHHHHHHHCC---	43.18	21466224
605	Ubiquitination	ELLEALTKHFQD--- HHHHHHHHHHCC---	43.18	21906983

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
6	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
27	S	Phosphorylation	Kinase	ATM	Q13315	PSP
27	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
33	S	Phosphorylation	Kinase	ATM	Q13315	PSP
33	S	Phosphorylation	Kinase	PRKDC	P78527	GPS
51	S	Phosphorylation	Kinase	DNAPK	P78527	PSP
455	T	Phosphorylation	Kinase	CDK2	P24941	PSP
477	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
530	Y	Phosphorylation	Kinase	SRC	P12931	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF146	Q9NTX7	PMID:21825151
-	K	Ubiquitination	E3 ubiquitin ligase	MDM2	Q00987	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
51	S	Phosphorylation		9362500
Phosphorylation of Ser-51 does not affect DNA repair.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of XRCC6_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CHK1_HUMAN	CHEK1	physical	12756247
KAT2A_HUMAN	KAT2A	physical	9488450
XRCC5_HUMAN	XRCC5	physical	9488450
XRCC5_HUMAN	XRCC5	physical	10219089
ATP23_HUMAN	XRCC6BP1	physical	10219089
CLUS_HUMAN	CLU	physical	10219089
RFA2_HUMAN	RPA2	physical	10064605
TDT_HUMAN	DNTT	physical	10570175
HXC4_HUMAN	HOXC4	physical	11279128
HXD4_HUMAN	HOXD4	physical	11279128
DLX2_HUMAN	DLX2	physical	11279128
PO2F2_HUMAN	POU2F2	physical	11279128
TERF2_HUMAN	TERF2	physical	10984620
XRCC5_HUMAN	XRCC5	physical	10984620
XRCC5_HUMAN	XRCC5	physical	10446239
ABL1_HUMAN	ABL1	physical	9798959
PO2F1_HUMAN	POU2F1	physical	17213819
P53_HUMAN	TP53	physical	15782130
BARD1_HUMAN	BARD1	physical	15782130
MSX2_HUMAN	MSX2	physical	12145306
RUNX2_HUMAN	RUNX2	physical	12145306
NAA15_HUMAN	NAA15	physical	12145306
XRCC5_HUMAN	XRCC5	physical	12145306
H2AX_HUMAN	H2AFX	physical	15613478
PRKDC_HUMAN	PRKDC	physical	15520013
DNLI4_HUMAN	LIG4	physical	15520013
XRCC4_HUMAN	XRCC4	physical	15520013
XRCC5_HUMAN	XRCC5	physical	15520013
PARP1_HUMAN	PARP1	physical	10400681
XRCC5_HUMAN	XRCC5	physical	15023334
CBP_HUMAN	CREBBP	physical	15023334
CAF1A_HUMAN	CHAF1A	physical	21209461
BAZ1A_HUMAN	BAZ1A	physical	21172662
PRKDC_HUMAN	PRKDC	physical	8422676
K0408_HUMAN	KIAA0408	physical	21900206
EID1_HUMAN	EID1	physical	21900206
PFD3_HUMAN	VBP1	physical	21900206
XRCC5_HUMAN	XRCC5	physical	10783163
WRN_HUMAN	WRN	physical	10783163
XRCC5_HUMAN	XRCC5	physical	21454661
HXB7_HUMAN	HOXB7	physical	17308091
XRCC5_HUMAN	XRCC5	physical	15367688
TYY1_HUMAN	YY1	physical	15367688
XRCC5_HUMAN	XRCC5	physical	15910003
ORC3_HUMAN	ORC3	physical	15910003
ORC2_HUMAN	ORC2	physical	15910003
ORC6_HUMAN	ORC6	physical	15910003
ILF3_HUMAN	ILF3	physical	21969602
PRKDC_HUMAN	PRKDC	physical	21969602
MSH6_HUMAN	MSH6	physical	21075794
MSH2_HUMAN	MSH2	physical	21075794
XRCC5_HUMAN	XRCC5	physical	11493912
HXC4_HUMAN	HOXC4	physical	12672812
PO2F1_HUMAN	POU2F1	physical	12672812
PARP1_HUMAN	PARP1	physical	16490787
CFLAR_HUMAN	CFLAR	physical	22322857
DNLI4_HUMAN	LIG4	physical	10757784
XRCC5_HUMAN	XRCC5	physical	10757784
HDAC6_HUMAN	HDAC6	physical	21847364
HD_HUMAN	HTT	physical	15383276
TADA3_HUMAN	TADA3	physical	15383276
TCPG_HUMAN	CCT3	physical	15383276
XRCC5_HUMAN	XRCC5	physical	19177010
BAX_HUMAN	BAX	physical	19177010
CLUS_HUMAN	CLU	physical	19177010
BAX_HUMAN	BAX	physical	19118032
CLUS_HUMAN	CLU	physical	19118032
XRCC5_HUMAN	XRCC5	physical	19118032
XRCC5_HUMAN	XRCC5	physical	22939629
PRKDC_HUMAN	PRKDC	physical	22939629
RHG05_HUMAN	ARHGAP5	physical	22939629
PRGR_HUMAN	PGR	physical	10750018
XRCC6_HUMAN	XRCC6	physical	10750018
XRCC5_HUMAN	XRCC5	physical	10750018
PRKDC_HUMAN	PRKDC	physical	10750018
GRAA_HUMAN	GZMA	physical	16440001
XRCC5_HUMAN	XRCC5	physical	17159921
HMGA1_HUMAN	HMGA1	physical	18850631
HMGA2_HUMAN	HMGA2	physical	18850631
ARAP1_HUMAN	ARAP1	physical	16169070
CTNA1_HUMAN	CTNNA1	physical	22863883
CUL2_HUMAN	CUL2	physical	22863883
CSDE1_HUMAN	CSDE1	physical	22863883
SYFB_HUMAN	FARSB	physical	22863883
GANAB_HUMAN	GANAB	physical	22863883
PUR2_HUMAN	GART	physical	22863883
IMDH1_HUMAN	IMPDH1	physical	22863883
PLAK_HUMAN	JUP	physical	22863883
DPYL3_HUMAN	DPYSL3	physical	22863883
MSH6_HUMAN	MSH6	physical	22863883
PLOD2_HUMAN	PLOD2	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SAMH1_HUMAN	SAMHD1	physical	22863883
SET_HUMAN	SET	physical	22863883
F10A1_HUMAN	ST13	physical	22863883
SPT5H_HUMAN	SUPT5H	physical	22863883
SWP70_HUMAN	SWAP70	physical	22863883
XRCC5_HUMAN	XRCC5	physical	18809223
PPARG_HUMAN	PPARG	physical	18809223
KC1A_HUMAN	CSNK1A1	physical	26496610
DYN2_HUMAN	DNM2	physical	26496610
DNLI4_HUMAN	LIG4	physical	26496610
PRKDC_HUMAN	PRKDC	physical	26496610
TERF2_HUMAN	TERF2	physical	26496610
WRN_HUMAN	WRN	physical	26496610
XRCC4_HUMAN	XRCC4	physical	26496610
XRCC5_HUMAN	XRCC5	physical	26496610
BAG2_HUMAN	BAG2	physical	26496610
ANR28_HUMAN	ANKRD28	physical	26496610
POTE1_HUMAN	POT1	physical	26496610
TINF2_HUMAN	TINF2	physical	26496610
TE2IP_HUMAN	TERF2IP	physical	26496610
TNC18_HUMAN	TNRC18	physical	26496610
CCD57_HUMAN	CCDC57	physical	26496610
PAXX_HUMAN	C9orf142	physical	26496610
HDAC6_HUMAN	HDAC6	physical	25299772
BAX_HUMAN	BAX	physical	25299772
AP2A_HUMAN	TFAP2A	physical	19906305
XRCC5_HUMAN	XRCC5	physical	19906305
WRN_HUMAN	WRN	physical	28514442
PARP2_HUMAN	PARP2	physical	28514442
XPC_HUMAN	XPC	physical	28514442
DNLI3_HUMAN	LIG3	physical	28514442
XRCC5_HUMAN	XRCC5	physical	28514442
SP16H_HUMAN	SUPT16H	physical	28514442
PARP1_HUMAN	PARP1	physical	28514442
XRCC1_HUMAN	XRCC1	physical	28514442
H2AY_HUMAN	H2AFY	physical	28514442
SSRP1_HUMAN	SSRP1	physical	28514442
SPTA1_HUMAN	SPTA1	physical	16889989

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of XRCC6_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-31; LYS-331; LYS-338;LYS-461 AND LYS-468, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455 AND SER-520, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC."; Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.; Proteomics 5:3589-3599(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-222, AND MASSSPECTROMETRY.	16097034 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27, AND MASSSPECTROMETRY.	15302935 [Abstract]
"DNA-dependent protein kinase phosphorylation sites in Ku 70/80heterodimer."; Chan D.W., Ye R., Veillette C.J., Lees-Miller S.P.; Biochemistry 38:1819-1828(1999). Cited for: PHOSPHORYLATION AT SER-6.	10026262 [Abstract]
"Double-strand break repair by Ku70 requires heterodimerization withKu80 and DNA binding functions."; Jin S., Weaver D.T.; EMBO J. 16:6874-6885(1997). Cited for: PHOSPHORYLATION AT SER-51.	9362500 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-455, AND MASSSPECTROMETRY.	19413330 [Abstract]

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