XRCC5_HUMAN - dbPTM
XRCC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID XRCC5_HUMAN
UniProt AC P13010
Protein Name X-ray repair cross-complementing protein 5
Gene Name XRCC5
Organism Homo sapiens (Human).
Sequence Length 732
Subcellular Localization Nucleus . Nucleus, nucleolus . 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. [PubMed: 12145306]
Protein Sequence MVRSGNKAAVVLCMDVGFTMSNSIPGIESPFEQAKKVITMFVQRQVFAENKDEIALVLFGTDGTDNPLSGGDQYQNITVHRHLMLPDFDLLEDIESKIQPGSQQADFLDALIVSMDVIQHETIGKKFEKRHIEIFTDLSSRFSKSQLDIIIHSLKKCDISLQFFLPFSLGKEDGSGDRGDGPFRLGGHGPSFPLKGITEQQKEGLEIVKMVMISLEGEDGLDEIYSFSESLRKLCVFKKIERHSIHWPCRLTIGSNLSIRIAAYKSILQERVKKTWTVVDAKTLKKEDIQKETVYCLNDDDETEVLKEDIIQGFRYGSDIVPFSKVDEEQMKYKSEGKCFSVLGFCKSSQVQRRFFMGNQVLKVFAARDDEAAAVALSSLIHALDDLDMVAIVRYAYDKRANPQVGVAFPHIKHNYECLVYVQLPFMEDLRQYMFSSLKNSKKYAPTEAQLNAVDALIDSMSLAKKDEKTDTLEDLFPTTKIPNPRFQRLFQCLLHRALHPREPLPPIQQHIWNMLNPPAEVTTKSQIPLSKIKTLFPLIEAKKKDQVTAQEIFQDNHEDGPTAKKLKTEQGGAHFSVSSLAEGSVTSVGSVNPAENFRVLVKQKKASFEEASNQLINHIEQFLDTNETPYFMKSIDCIRAFREEAIKFSEEQRFNNFLKALQEKVEIKQLNHFWEIVVQDGITLITKEEASGSSVTAEEAKKFLAPKDKPSGDTAAVFEEGGDVDDLLDMI
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
7Methylation-MVRSGNKAAVVLCM
-CCCCCCCEEEEEEE
41.0523748837
35UbiquitinationESPFEQAKKVITMFV
CCHHHHHHHHHHHHH
47.4723000965
36UbiquitinationSPFEQAKKVITMFVQ
CHHHHHHHHHHHHHH
41.7223000965
39PhosphorylationEQAKKVITMFVQRQV
HHHHHHHHHHHHHHH
13.9320068231
40SulfoxidationQAKKVITMFVQRQVF
HHHHHHHHHHHHHHH
1.8121406390
51SumoylationRQVFAENKDEIALVL
HHHHHCCCCEEEEEE
48.52-
84SulfoxidationITVHRHLMLPDFDLL
EEEEEECCCCCCCHH
4.1128183972
102PhosphorylationESKIQPGSQQADFLD
HHHCCCCCHHHHHHH
26.2925159151
125UbiquitinationIQHETIGKKFEKRHI
HCCHHCCHHHHHHHH
50.9021906983
126UbiquitinationQHETIGKKFEKRHIE
CCHHCCHHHHHHHHH
54.2522817900
129UbiquitinationTIGKKFEKRHIEIFT
HCCHHHHHHHHHHHH
53.0322817900
136PhosphorylationKRHIEIFTDLSSRFS
HHHHHHHHCHHHHCC
41.5123403867
140PhosphorylationEIFTDLSSRFSKSQL
HHHHCHHHHCCHHHH
44.6423403867
141MethylationIFTDLSSRFSKSQLD
HHHCHHHHCCHHHHH
36.16115481507
143PhosphorylationTDLSSRFSKSQLDII
HCHHHHCCHHHHHHH
30.2228152594
144AcetylationDLSSRFSKSQLDIII
CHHHHCCHHHHHHHH
39.2419608861
144UbiquitinationDLSSRFSKSQLDIII
CHHHHCCHHHHHHHH
39.2423000965
145PhosphorylationLSSRFSKSQLDIIIH
HHHHCCHHHHHHHHH
34.4722617229
153PhosphorylationQLDIIIHSLKKCDIS
HHHHHHHHHCCCCEE
31.3228102081
1552-HydroxyisobutyrylationDIIIHSLKKCDISLQ
HHHHHHHCCCCEEEE
55.13-
155AcetylationDIIIHSLKKCDISLQ
HHHHHHHCCCCEEEE
55.1325825284
155SuccinylationDIIIHSLKKCDISLQ
HHHHHHHCCCCEEEE
55.1323954790
155UbiquitinationDIIIHSLKKCDISLQ
HHHHHHHCCCCEEEE
55.1322817900
156AcetylationIIIHSLKKCDISLQF
HHHHHHCCCCEEEEE
42.2926051181
156UbiquitinationIIIHSLKKCDISLQF
HHHHHHCCCCEEEEE
42.2921906983
171UbiquitinationFLPFSLGKEDGSGDR
EEEECCCCCCCCCCC
58.90-
175PhosphorylationSLGKEDGSGDRGDGP
CCCCCCCCCCCCCCC
50.2520873877
191PhosphorylationRLGGHGPSFPLKGIT
CCCCCCCCCCCCCCC
44.0523403867
195SumoylationHGPSFPLKGITEQQK
CCCCCCCCCCCHHHH
48.80-
195AcetylationHGPSFPLKGITEQQK
CCCCCCCCCCCHHHH
48.8019608861
195NeddylationHGPSFPLKGITEQQK
CCCCCCCCCCCHHHH
48.8032015554
195SumoylationHGPSFPLKGITEQQK
CCCCCCCCCCCHHHH
48.8028112733
195UbiquitinationHGPSFPLKGITEQQK
CCCCCCCCCCCHHHH
48.8023000965
198PhosphorylationSFPLKGITEQQKEGL
CCCCCCCCHHHHHHH
36.0920860994
2022-HydroxyisobutyrylationKGITEQQKEGLEIVK
CCCCHHHHHHHHHEE
54.14-
202AcetylationKGITEQQKEGLEIVK
CCCCHHHHHHHHHEE
54.1426051181
202UbiquitinationKGITEQQKEGLEIVK
CCCCHHHHHHHHHEE
54.1422817900
225PhosphorylationEDGLDEIYSFSESLR
CCCHHHHHHHCHHHH
11.13-
233AcetylationSFSESLRKLCVFKKI
HHCHHHHHHHHHHCC
52.0827178108
233UbiquitinationSFSESLRKLCVFKKI
HHCHHHHHHHHHHCC
52.0821906983
235S-nitrosocysteineSESLRKLCVFKKIER
CHHHHHHHHHHCCHH
3.66-
235S-nitrosylationSESLRKLCVFKKIER
CHHHHHHHHHHCCHH
3.6619483679
238AcetylationLRKLCVFKKIERHSI
HHHHHHHHCCHHCCC
32.2325953088
238UbiquitinationLRKLCVFKKIERHSI
HHHHHHHHCCHHCCC
32.2322817900
239UbiquitinationRKLCVFKKIERHSIH
HHHHHHHCCHHCCCC
38.03-
244PhosphorylationFKKIERHSIHWPCRL
HHCCHHCCCCCCEEE
23.5230108239
249S-nitrosocysteineRHSIHWPCRLTIGSN
HCCCCCCEEEEECCC
4.74-
249S-nitrosylationRHSIHWPCRLTIGSN
HCCCCCCEEEEECCC
4.7422178444
252PhosphorylationIHWPCRLTIGSNLSI
CCCCEEEEECCCHHH
12.1623403867
255PhosphorylationPCRLTIGSNLSIRIA
CEEEEECCCHHHHHH
30.6530266825
258PhosphorylationLTIGSNLSIRIAAYK
EEECCCHHHHHHHHH
17.6730266825
265AcetylationSIRIAAYKSILQERV
HHHHHHHHHHHHHHH
26.7119608861
265MalonylationSIRIAAYKSILQERV
HHHHHHHHHHHHHHH
26.7126320211
265UbiquitinationSIRIAAYKSILQERV
HHHHHHHHHHHHHHH
26.7123000965
266PhosphorylationIRIAAYKSILQERVK
HHHHHHHHHHHHHHH
18.8226546556
273UbiquitinationSILQERVKKTWTVVD
HHHHHHHHHCEEEEE
51.1923000965
274UbiquitinationILQERVKKTWTVVDA
HHHHHHHHCEEEEEC
46.5723000965
275PhosphorylationLQERVKKTWTVVDAK
HHHHHHHCEEEEECH
22.2023312004
277PhosphorylationERVKKTWTVVDAKTL
HHHHHCEEEEECHHC
18.8423312004
282AcetylationTWTVVDAKTLKKEDI
CEEEEECHHCCHHHC
50.3423236377
282UbiquitinationTWTVVDAKTLKKEDI
CEEEEECHHCCHHHC
50.3427667366
285AcetylationVVDAKTLKKEDIQKE
EEECHHCCHHHCCCC
60.3925953088
285SumoylationVVDAKTLKKEDIQKE
EEECHHCCHHHCCCC
60.39-
285UbiquitinationVVDAKTLKKEDIQKE
EEECHHCCHHHCCCC
60.3932015554
286UbiquitinationVDAKTLKKEDIQKET
EECHHCCHHHCCCCE
64.8322817900
291UbiquitinationLKKEDIQKETVYCLN
CCHHHCCCCEEEECC
56.5433845483
295NitrationDIQKETVYCLNDDDE
HCCCCEEEECCCCCC
9.91-
295PhosphorylationDIQKETVYCLNDDDE
HCCCCEEEECCCCCC
9.9127642862
296S-nitrosocysteineIQKETVYCLNDDDET
CCCCEEEECCCCCCC
2.19-
296S-nitrosylationIQKETVYCLNDDDET
CCCCEEEECCCCCCC
2.1919483679
307SumoylationDDETEVLKEDIIQGF
CCCCHHHHHHHHHCC
59.52-
307UbiquitinationDDETEVLKEDIIQGF
CCCCHHHHHHHHHCC
59.5221906983
316PhosphorylationDIIQGFRYGSDIVPF
HHHHCCCCCCCCCCH
20.7928152594
318PhosphorylationIQGFRYGSDIVPFSK
HHCCCCCCCCCCHHH
18.4125159151
324PhosphorylationGSDIVPFSKVDEEQM
CCCCCCHHHCCHHHH
26.2120873877
325SumoylationSDIVPFSKVDEEQMK
CCCCCHHHCCHHHHH
54.83-
325AcetylationSDIVPFSKVDEEQMK
CCCCCHHHCCHHHHH
54.8326051181
325NeddylationSDIVPFSKVDEEQMK
CCCCCHHHCCHHHHH
54.8332015554
325SumoylationSDIVPFSKVDEEQMK
CCCCCHHHCCHHHHH
54.83-
325UbiquitinationSDIVPFSKVDEEQMK
CCCCCHHHCCHHHHH
54.8323000965
332SumoylationKVDEEQMKYKSEGKC
HCCHHHHHHCCCCCE
49.58-
332AcetylationKVDEEQMKYKSEGKC
HCCHHHHHHCCCCCE
49.5819608861
332MethylationKVDEEQMKYKSEGKC
HCCHHHHHHCCCCCE
49.587713937
332SumoylationKVDEEQMKYKSEGKC
HCCHHHHHHCCCCCE
49.5819608861
332UbiquitinationKVDEEQMKYKSEGKC
HCCHHHHHHCCCCCE
49.5823000965
333PhosphorylationVDEEQMKYKSEGKCF
CCHHHHHHCCCCCEE
17.8828176443
334MethylationDEEQMKYKSEGKCFS
CHHHHHHCCCCCEEE
36.1924797987
334UbiquitinationDEEQMKYKSEGKCFS
CHHHHHHCCCCCEEE
36.1923000965
335PhosphorylationEEQMKYKSEGKCFSV
HHHHHHCCCCCEEEE
48.7929214152
338SumoylationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.23-
3382-HydroxyisobutyrylationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.23-
338AcetylationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.2323954790
338MalonylationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.2326320211
338SumoylationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.2319608861
338UbiquitinationMKYKSEGKCFSVLGF
HHHCCCCCEEEEEHH
28.2323000965
339S-nitrosocysteineKYKSEGKCFSVLGFC
HHCCCCCEEEEEHHH
4.52-
339S-nitrosylationKYKSEGKCFSVLGFC
HHCCCCCEEEEEHHH
4.5219483679
341PhosphorylationKSEGKCFSVLGFCKS
CCCCCEEEEEHHHCC
26.3821712546
346S-nitrosocysteineCFSVLGFCKSSQVQR
EEEEEHHHCCHHHHH
3.87-
346S-nitrosylationCFSVLGFCKSSQVQR
EEEEEHHHCCHHHHH
3.8719483679
347AcetylationFSVLGFCKSSQVQRR
EEEEHHHCCHHHHHH
51.3725953088
347UbiquitinationFSVLGFCKSSQVQRR
EEEEHHHCCHHHHHH
51.3721906983
348PhosphorylationSVLGFCKSSQVQRRF
EEEHHHCCHHHHHHH
27.4723882029
357SulfoxidationQVQRRFFMGNQVLKV
HHHHHHHCCHHHEEE
4.5321406390
363AcetylationFMGNQVLKVFAARDD
HCCHHHEEEEECCCH
36.1326051181
363UbiquitinationFMGNQVLKVFAARDD
HCCHHHEEEEECCCH
36.1323000965
378PhosphorylationEAAAVALSSLIHALD
HHHHHHHHHHHHHHC
17.2318452278
379PhosphorylationAAAVALSSLIHALDD
HHHHHHHHHHHHHCC
31.9918452278
389SulfoxidationHALDDLDMVAIVRYA
HHHCCCCHHHHHHHH
2.5930846556
399AcetylationIVRYAYDKRANPQVG
HHHHHHHCCCCCCCE
40.5126051181
399UbiquitinationIVRYAYDKRANPQVG
HHHHHHHCCCCCCCE
40.51-
413UbiquitinationGVAFPHIKHNYECLV
EEECCCCCCCEEEEE
23.8216196087
416PhosphorylationFPHIKHNYECLVYVQ
CCCCCCCEEEEEEEE
14.03-
433PhosphorylationFMEDLRQYMFSSLKN
CHHHHHHHHHHHHCC
8.1623312004
436PhosphorylationDLRQYMFSSLKNSKK
HHHHHHHHHHCCCCC
20.4530108239
437PhosphorylationLRQYMFSSLKNSKKY
HHHHHHHHHCCCCCC
31.9030108239
439AcetylationQYMFSSLKNSKKYAP
HHHHHHHCCCCCCCC
62.2125953088
439UbiquitinationQYMFSSLKNSKKYAP
HHHHHHHCCCCCCCC
62.2121906983
442UbiquitinationFSSLKNSKKYAPTEA
HHHHCCCCCCCCCHH
60.2322817900
443SumoylationSSLKNSKKYAPTEAQ
HHHCCCCCCCCCHHH
46.60-
443AcetylationSSLKNSKKYAPTEAQ
HHHCCCCCCCCCHHH
46.607709569
443SumoylationSSLKNSKKYAPTEAQ
HHHCCCCCCCCCHHH
46.60-
443UbiquitinationSSLKNSKKYAPTEAQ
HHHCCCCCCCCCHHH
46.6022817900
460PhosphorylationAVDALIDSMSLAKKD
HHHHHHHHHHHCCCC
11.8623532336
461SulfoxidationVDALIDSMSLAKKDE
HHHHHHHHHHCCCCC
3.1828183972
462PhosphorylationDALIDSMSLAKKDEK
HHHHHHHHHCCCCCC
29.1823532336
4652-HydroxyisobutyrylationIDSMSLAKKDEKTDT
HHHHHHCCCCCCCCC
67.08-
465UbiquitinationIDSMSLAKKDEKTDT
HHHHHHCCCCCCCCC
67.0821906983
4662-HydroxyisobutyrylationDSMSLAKKDEKTDTL
HHHHHCCCCCCCCCH
66.56-
466AcetylationDSMSLAKKDEKTDTL
HHHHHCCCCCCCCCH
66.5625953088
466SuccinylationDSMSLAKKDEKTDTL
HHHHHCCCCCCCCCH
66.5623954790
466UbiquitinationDSMSLAKKDEKTDTL
HHHHHCCCCCCCCCH
66.5622817900
4692-HydroxyisobutyrylationSLAKKDEKTDTLEDL
HHCCCCCCCCCHHHH
62.93-
469AcetylationSLAKKDEKTDTLEDL
HHCCCCCCCCCHHHH
62.9325953088
469UbiquitinationSLAKKDEKTDTLEDL
HHCCCCCCCCCHHHH
62.9321906983
470PhosphorylationLAKKDEKTDTLEDLF
HCCCCCCCCCHHHHC
31.9729214152
472PhosphorylationKKDEKTDTLEDLFPT
CCCCCCCCHHHHCCC
36.9629214152
480PhosphorylationLEDLFPTTKIPNPRF
HHHHCCCCCCCCHHH
27.4924719451
481AcetylationEDLFPTTKIPNPRFQ
HHHCCCCCCCCHHHH
59.6625953088
481UbiquitinationEDLFPTTKIPNPRFQ
HHHCCCCCCCCHHHH
59.6623000965
493S-nitrosocysteineRFQRLFQCLLHRALH
HHHHHHHHHHHHHHC
3.23-
493S-nitrosylationRFQRLFQCLLHRALH
HHHHHHHHHHHHHHC
3.2322178444
515SulfoxidationIQQHIWNMLNPPAEV
HHHHHHHHCCCCCCC
1.9928183972
523PhosphorylationLNPPAEVTTKSQIPL
CCCCCCCCCCCCCCH
21.7321406692
524PhosphorylationNPPAEVTTKSQIPLS
CCCCCCCCCCCCCHH
33.6021406692
525UbiquitinationPPAEVTTKSQIPLSK
CCCCCCCCCCCCHHH
30.8821906983
526PhosphorylationPAEVTTKSQIPLSKI
CCCCCCCCCCCHHHH
31.1120860994
531PhosphorylationTKSQIPLSKIKTLFP
CCCCCCHHHHHHHHH
27.2924719451
532SumoylationKSQIPLSKIKTLFPL
CCCCCHHHHHHHHHH
56.77-
532AcetylationKSQIPLSKIKTLFPL
CCCCCHHHHHHHHHH
56.7719608861
532MalonylationKSQIPLSKIKTLFPL
CCCCCHHHHHHHHHH
56.7726320211
532SumoylationKSQIPLSKIKTLFPL
CCCCCHHHHHHHHHH
56.7728112733
532UbiquitinationKSQIPLSKIKTLFPL
CCCCCHHHHHHHHHH
56.7723000965
534SumoylationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.80-
5342-HydroxyisobutyrylationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.80-
534AcetylationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.8026051181
534SuccinylationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.8023954790
534SumoylationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.8028112733
534UbiquitinationQIPLSKIKTLFPLIE
CCCHHHHHHHHHHHH
42.8023000965
535PhosphorylationIPLSKIKTLFPLIEA
CCHHHHHHHHHHHHH
36.7821712546
543SumoylationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.79-
5432-HydroxyisobutyrylationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.79-
543AcetylationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.7925953088
543MalonylationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.7926320211
543SumoylationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.79-
543UbiquitinationLFPLIEAKKKDQVTA
HHHHHHHHHHCCCCH
47.7923000965
544AcetylationFPLIEAKKKDQVTAQ
HHHHHHHHHCCCCHH
69.5025953088
544UbiquitinationFPLIEAKKKDQVTAQ
HHHHHHHHHCCCCHH
69.5023000965
545UbiquitinationPLIEAKKKDQVTAQE
HHHHHHHHCCCCHHH
53.3223000965
549PhosphorylationAKKKDQVTAQEIFQD
HHHHCCCCHHHHHCC
19.5928555341
563PhosphorylationDNHEDGPTAKKLKTE
CCCCCCCCCCCCEEC
57.5528555341
565AcetylationHEDGPTAKKLKTEQG
CCCCCCCCCCEECCC
62.2023954790
565SumoylationHEDGPTAKKLKTEQG
CCCCCCCCCCEECCC
62.20-
565UbiquitinationHEDGPTAKKLKTEQG
CCCCCCCCCCEECCC
62.2021906983
566AcetylationEDGPTAKKLKTEQGG
CCCCCCCCCEECCCC
53.40155623
566SumoylationEDGPTAKKLKTEQGG
CCCCCCCCCEECCCC
53.4028112733
566UbiquitinationEDGPTAKKLKTEQGG
CCCCCCCCCEECCCC
53.4022817900
568SumoylationGPTAKKLKTEQGGAH
CCCCCCCEECCCCCE
59.92-
568SumoylationGPTAKKLKTEQGGAH
CCCCCCCEECCCCCE
59.9228112733
568UbiquitinationGPTAKKLKTEQGGAH
CCCCCCCEECCCCCE
59.9233845483
569PhosphorylationPTAKKLKTEQGGAHF
CCCCCCEECCCCCEE
43.9328464451
577PhosphorylationEQGGAHFSVSSLAEG
CCCCCEEEHHHHCCC
15.9515941674
579PhosphorylationGGAHFSVSSLAEGSV
CCCEEEHHHHCCCCC
20.5928857561
580PhosphorylationGAHFSVSSLAEGSVT
CCEEEHHHHCCCCCC
29.4621712546
585PhosphorylationVSSLAEGSVTSVGSV
HHHHCCCCCCCCCCC
17.4622817901
587PhosphorylationSLAEGSVTSVGSVNP
HHCCCCCCCCCCCCH
21.2827080861
588PhosphorylationLAEGSVTSVGSVNPA
HCCCCCCCCCCCCHH
23.4827080861
603UbiquitinationENFRVLVKQKKASFE
HHHHHEEECCCCCHH
52.8427667366
608PhosphorylationLVKQKKASFEEASNQ
EEECCCCCHHHHHHH
41.9122115753
613PhosphorylationKASFEEASNQLINHI
CCCHHHHHHHHHHHH
28.5222115753
629PhosphorylationQFLDTNETPYFMKSI
HHHCCCCCCCHHHHH
25.9225159151
633SulfoxidationTNETPYFMKSIDCIR
CCCCCCHHHHHHHHH
2.4830846556
640MethylationMKSIDCIRAFREEAI
HHHHHHHHHHHHHHH
33.72115481513
648AcetylationAFREEAIKFSEEQRF
HHHHHHHHCCHHHHH
50.3023749302
648UbiquitinationAFREEAIKFSEEQRF
HHHHHHHHCCHHHHH
50.3023000965
660SumoylationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.80-
6602-HydroxyisobutyrylationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.80-
660AcetylationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.8019608861
660MethylationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.8022631769
660SumoylationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.8019608861
660UbiquitinationQRFNNFLKALQEKVE
HHHHHHHHHHHHHHH
42.8023000965
6652-HydroxyisobutyrylationFLKALQEKVEIKQLN
HHHHHHHHHHHHHCC
32.01-
665AcetylationFLKALQEKVEIKQLN
HHHHHHHHHHHHHCC
32.0119608861
665UbiquitinationFLKALQEKVEIKQLN
HHHHHHHHHHHHHCC
32.0123000965
669SumoylationLQEKVEIKQLNHFWE
HHHHHHHHHCCCHHE
34.9228112733
669UbiquitinationLQEKVEIKQLNHFWE
HHHHHHHHHCCCHHE
34.9233845483
688SumoylationDGITLITKEEASGSS
CCEEEEECCCCCCCC
46.7128112733
692PhosphorylationLITKEEASGSSVTAE
EEECCCCCCCCCCHH
42.3521815630
694PhosphorylationTKEEASGSSVTAEEA
ECCCCCCCCCCHHHH
21.0930108239
695PhosphorylationKEEASGSSVTAEEAK
CCCCCCCCCCHHHHH
27.3230576142
697PhosphorylationEASGSSVTAEEAKKF
CCCCCCCCHHHHHHH
30.2430576142
702AcetylationSVTAEEAKKFLAPKD
CCCHHHHHHHHCCCC
47.5423749302
702MethylationSVTAEEAKKFLAPKD
CCCHHHHHHHHCCCC
47.54-
702SuccinylationSVTAEEAKKFLAPKD
CCCHHHHHHHHCCCC
47.5423954790
702SumoylationSVTAEEAKKFLAPKD
CCCHHHHHHHHCCCC
47.54-
702UbiquitinationSVTAEEAKKFLAPKD
CCCHHHHHHHHCCCC
47.5427667366
703AcetylationVTAEEAKKFLAPKDK
CCHHHHHHHHCCCCC
53.2926051181
703UbiquitinationVTAEEAKKFLAPKDK
CCHHHHHHHHCCCCC
53.2922817900
710UbiquitinationKFLAPKDKPSGDTAA
HHHCCCCCCCCCCCH
47.40-
712PhosphorylationLAPKDKPSGDTAAVF
HCCCCCCCCCCCHHH
55.8521712546
715PhosphorylationKDKPSGDTAAVFEEG
CCCCCCCCCHHHCCC
21.7528112733
731SulfoxidationDVDDLLDMI------
CHHHHHHCC------
3.8521406390

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
577SPhosphorylationKinaseDNAPKP78527
PSP
579SPhosphorylationKinasePRKDCP78527
Uniprot
580SPhosphorylationKinaseDNAPKP78527
PSP
715TPhosphorylationKinaseDNAPKP78527
PSP
-KUbiquitinationE3 ubiquitin ligaseFBXL12Q9NXK8
PMID:24658274
-KUbiquitinationE3 ubiquitin ligaseRNF138Q8WVD3
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseRNF8O76064
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of XRCC5_HUMAN !!

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 XRCC5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XRCC6_HUMANXRCC6physical
10446239
KAT2A_HUMANKAT2Aphysical
9488450
VAV_HUMANVAV1physical
10673353
TYK2_HUMANTYK2physical
10673353
PRKDC_HUMANPRKDCphysical
9312071
XRCC6_HUMANXRCC6physical
10207052
PO2F1_HUMANPOU2F1physical
12393188
DPOLA_HUMANPOLA1physical
12393188
PCNA_HUMANPCNAphysical
12393188
TOP2A_HUMANTOP2Aphysical
12393188
PRI1_HUMANPRIM1physical
12393188
RPAB1_HUMANPOLR2Ephysical
12393188
RPB4_HUMANPOLR2Dphysical
12393188
ORC2_HUMANORC2physical
12393188
ORC1_HUMANORC1physical
12393188
PRKDC_HUMANPRKDCphysical
12393188
RFC1_HUMANRFC1physical
12393188
PRKDC_HUMANPRKDCphysical
10446239
BRCA1_HUMANBRCA1physical
18936166
BARD1_HUMANBARD1physical
18936166
MSX2_HUMANMSX2physical
12145306
RUNX2_HUMANRUNX2physical
12145306
NAA15_HUMANNAA15physical
12145306
XRCC6_HUMANXRCC6physical
12145306
PRKDC_HUMANPRKDCphysical
15520013
DNLI4_HUMANLIG4physical
15520013
XRCC4_HUMANXRCC4physical
15520013
XRCC6_HUMANXRCC6physical
15520013
PARP1_HUMANPARP1physical
10400681
CAF1A_HUMANCHAF1Aphysical
21209461
BAZ1A_HUMANBAZ1Aphysical
21172662
SMCA5_HUMANSMARCA5physical
21172662
CHRC1_HUMANCHRAC1physical
21172662
DPOE3_HUMANPOLE3physical
21172662
XRCC6_HUMANXRCC6physical
21172662
APLF_HUMANAPLFphysical
17396150
XRCC6_HUMANXRCC6physical
10783163
WRN_HUMANWRNphysical
10783163
XRCC6_HUMANXRCC6physical
21070772
COIL_HUMANCOILphysical
21070772
RPB1_HUMANPOLR2Aphysical
12391174
HXB7_HUMANHOXB7physical
17308091
XRCC6_HUMANXRCC6physical
15367688
TYY1_HUMANYY1physical
15367688
PRKDC_HUMANPRKDCphysical
15758953
ATM_HUMANATMphysical
15758953
ATR_HUMANATRphysical
15758953
NBN_HUMANNBNphysical
15758953
XRCC6_HUMANXRCC6physical
15910003
ORC3_HUMANORC3physical
15910003
ORC2_HUMANORC2physical
15910003
ORC6_HUMANORC6physical
15910003
ORC4_HUMANORC4physical
15910003
HXC4_HUMANHOXC4physical
12672812
PARP1_HUMANPARP1physical
16490787
DHX9_HUMANDHX9physical
14704337
DNLI4_HUMANLIG4physical
10757784
XRCC6_HUMANXRCC6physical
10757784
SP16H_HUMANSUPT16Hphysical
21679440
XRCC6_HUMANXRCC6physical
21679440
WRN_HUMANWRNphysical
21679440
DHX9_HUMANDHX9physical
21679440
SSRP1_HUMANSSRP1physical
21679440
H2AX_HUMANH2AFXphysical
21679440
PRKDC_HUMANPRKDCphysical
21679440
LAP2A_HUMANTMPOphysical
21679440
LAP2B_HUMANTMPOphysical
21679440
TOP1_HUMANTOP1physical
21679440
PARP1_HUMANPARP1physical
21679440
DDX17_HUMANDDX17physical
21679440
WRN_HUMANWRNphysical
12937274
TFAP4_HUMANTFAP4physical
22939629
PAF1_HUMANPAF1physical
22939629
PTER_HUMANPTERphysical
22939629
SYYC_HUMANYARSphysical
22939629
PRGR_HUMANPGRphysical
10750018
XRCC6_HUMANXRCC6physical
10750018
XRCC5_HUMANXRCC5physical
10750018
PRKDC_HUMANPRKDCphysical
10750018
GRAA_HUMANGZMAphysical
16440001
DCR1C_HUMANDCLRE1Cphysical
16857680
PRKDC_HUMANPRKDCphysical
16857680
XRCC6_HUMANXRCC6physical
11196700
C1QBP_HUMANC1QBPphysical
22863883
CUL2_HUMANCUL2physical
22863883
CSDE1_HUMANCSDE1physical
22863883
DNMBP_HUMANDNMBPphysical
22863883
EIF3J_HUMANEIF3Jphysical
22863883
IF4B_HUMANEIF4Bphysical
22863883
GANAB_HUMANGANABphysical
22863883
HSP74_HUMANHSPA4physical
22863883
PLAK_HUMANJUPphysical
22863883
MSH2_HUMANMSH2physical
22863883
SYNC_HUMANNARSphysical
22863883
NUCL_HUMANNCLphysical
22863883
PLCB3_HUMANPLCB3physical
22863883
ANM3_HUMANPRMT3physical
22863883
RL24_HUMANRPL24physical
22863883
SAMH1_HUMANSAMHD1physical
22863883
SF01_HUMANSF1physical
22863883
TRM1_HUMANTRMT1physical
22863883
XRCC6_HUMANXRCC6physical
22863883
BRCA1_HUMANBRCA1physical
23344954
PRKDC_HUMANPRKDCphysical
26344197
XRCC6_HUMANXRCC6physical
26344197
CBL_HUMANCBLphysical
26496610
CX6B1_HUMANCOX6B1physical
26496610
DC1I2_HUMANDYNC1I2physical
26496610
ERF_HUMANERFphysical
26496610
XRCC6_HUMANXRCC6physical
26496610
NDST1_HUMANNDST1physical
26496610
MPRI_HUMANIGF2Rphysical
26496610
LIMS1_HUMANLIMS1physical
26496610
MSH5_HUMANMSH5physical
26496610
NFIB_HUMANNFIBphysical
26496610
PCDH7_HUMANPCDH7physical
26496610
PPM1A_HUMANPPM1Aphysical
26496610
PRKDC_HUMANPRKDCphysical
26496610
ABCE1_HUMANABCE1physical
26496610
ROCK1_HUMANROCK1physical
26496610
WRN_HUMANWRNphysical
26496610
BRPF1_HUMANBRPF1physical
26496610
NCOA3_HUMANNCOA3physical
26496610
MPDZ_HUMANMPDZphysical
26496610
M3K6_HUMANMAP3K6physical
26496610
GOGA5_HUMANGOLGA5physical
26496610
SPN1_HUMANSNUPNphysical
26496610
SMYD5_HUMANSMYD5physical
26496610
WWP1_HUMANWWP1physical
26496610
ZZEF1_HUMANZZEF1physical
26496610
RTEL1_HUMANRTEL1physical
26496610
LTOR1_HUMANLAMTOR1physical
26496610
ASAP3_HUMANASAP3physical
26496610
PEAK1_HUMANPEAK1physical
26496610
NAA15_HUMANNAA15physical
26496610
BAP18_HUMANC17orf49physical
26496610
MITD1_HUMANMITD1physical
26496610
MIB2_HUMANMIB2physical
26496610
CE128_HUMANCEP128physical
26496610
AP2A_HUMANTFAP2Aphysical
19906305
XRCC6_HUMANXRCC6physical
19906305
SPTA1_HUMANSPTA1physical
16889989
EP300_HUMANEP300physical
29049411
DDB2_HUMANDDB2physical
28035050
DDB1_HUMANDDB1physical
28035050
XRCC6_HUMANXRCC6physical
28035050

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 XRCC5_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-144; LYS-195; LYS-265;LYS-332; LYS-660 AND LYS-665, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 SER-258, AND MASSSPECTROMETRY.
"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-577; SER-579; SER-580 AND THR-715.

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